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Information on EC 3.1.3.8 - 3-phytase
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3.1.3.8 3-phytaseSpecify your search results
Word Map
- 3.1.3.8
- phosphorus
- meal
-
broiler
- ash
- phytases
-
corn-soybean
- agriculture
- synthesis
-
phytic
-
barrows
- tibia
-
allotted
-
housed
-
meal-based
-
digesta
-
quadratic
-
nonphytate
-
phytase-supplemented
-
equivalency
-
growing-finishing
- nutrition
-
monogastric
-
excreta
-
indigestible
- ficuum
-
dicalcium
-
chromic
-
manure
-
p-deficient
-
corn-based
-
gain:feed
-
phytate-p
-
grower
-
crates
-
maize-soybean
-
low-phosphorus
-
t-cannulas
- 6-phytase
-
phosphorus-deficient
-
monocalcium
-
phytate-degrading
- food industry
-
as-fed
- biotechnology
-
feedstuffs
-
cornstarch
-
wheat-based
- analysis
-
metabolisable
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
microbial phytase, natuphos, alkaline phytase, 3-phytase, phytase a, beta-propeller phytase, atpap15, cell-bound phytase, appa2, acid phytase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-phytase
-
-
-
-
168phyA
3-phytase
3-phytase A
3-phytase B
acid phytase
acidic histidine acid phosphatase
alkaline beta-propeller phytase
alkaline phytase
AppA
AppA2
AppA2 phytase
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Aspergillus niger N25 phytase
beta-propeller phytase
BPP
cysteine phytase
dual-domain BPP
HAP phytase
histidine acid phosphatase
histidine acid phosphatase phytase
histidine acid phytase
MiPhyA
MOK1 phytase
MYCTH_2306203
myo-inositol 1,2,3,4,5,6-hexakisphosphate phosphohydrolase
myo-inositol hexakiphosphate phosphohydrolase
myo-inositol hexakisphosphate 3-phosphohydrolase
myo-inositol hexakisphosphate phosphohydrolase
myo-inositol hexaphosphate phosphohydrolase
MYO-inositol-hexaphosphate 3-phosphohydrolase
-
-
-
-
Natuphos
neutral phytase
PAP
PAP type I
PAPhy
PAPhys
pH 2.5 optimum acid phosphatase
-
-
-
-
Phy
PHY US42
PHY US573
phy168
PhyA
PhyA115
PhyB
PhyB49
PhyC
PhyCm
PhyH
PhyH49
PhyK
phytase
phytase A
phytase C
phytate 1-phosphatase
-
-
-
-
Phytate 3-phosphatase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
PSphy
purple acid phosphatase
St-Phy
YmPh
additional information
beta-propeller phytase
-
beta-propeller phytase has substrate specificity for myo-inositol hexakisphosphate and yields a myo-inositol trisphosphate and three phosphate groups as the final products
beta-propeller phytase
-
beta-propeller phytase has substrate specificity for myo-inositol hexakisphosphate and yields a myo-inositol trisphosphate and three phosphate groups as the final products
-
phytase
-
-
-
-
additional information
phytase ASR1 is a member of the histidine-acid-phosphatase family, that shares two conserved active-site motifs, RHGXRXP and HD, and hydrolyzes metal-free phytate with pH optima in the acidic range
additional information
PPHY is a phytase belonging to histidine acid phosphatases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 3-phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
37288-11-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-ATP + H2O
?
-
250% of the activity with myo-inositol hexakisphosphate
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
78% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + phosphate
adenosine + phosphate
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
CTP + H2O
CDP + phosphate
-
352% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 3-phosphate + H2O
glucose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
glucose + phosphate
-
reaction is nearly as efficient as on phytate
-
?
dATP + H2O
? + phosphate
-
31% of the activity with 4-nitrophenylphosphate
-
-
?
dATP + H2O
dADP + phosphate
-
338% relative activity compared to myo-inositol hexakisphosphate
-
-
?
dCTP + H2O
? + phosphate
-
35% of the activity with 4-nitrophenylphosphate
-
-
?
dCTP + H2O
dCDP + phosphate
-
367% relative activity compared to myo-inositol hexakisphosphate
-
-
?
dGTP + H2O
? + phosphate
-
52% of the activity with 4-nitrophenylphosphate
-
-
?
dGTP + H2O
dGDP + phosphate
-
189% relative activity compared to myo-inositol hexakisphosphate
-
-
?
di-sodium phenyl phosphate dihydrate + H2O
?
-
111.85% activity compared to myo-inositol hexakisphosphate
-
-
?
dTTP + H2O
? + phosphate
-
37% of the activity with 4-nitrophenylphosphate
-
-
?
dTTP + H2O
dTDP + phosphate
-
389% relative activity compared to myo-inositol hexakisphosphate
-
-
?
GTP + H2O
GDP + phosphate
-
271% relative activity compared to myo-inositol hexakisphosphate
-
-
?
inositol 1-monophosphate + H2O
inositol + phosphate
-
58% activity compared to myo-inositol hexakisphosphate
-
-
?
inositol 2-monophosphate + H2O
inositol + phosphate
-
84% activity compared to myo-inositol hexakisphosphate
-
-
?
L-tyrosine phosphate + H2O
L-tyrosine + phosphate
-
142% relative activity compared to myo-inositol hexakisphosphate
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
1D-myo-inositol-1,2,4,5,6-pentakisphosphate + phosphate
although the PhyK homolog AppA is biochemically characterized as a 6-phytase, a co-crystal structure shows the phytate 3-phosphate as scissile group in a similar position to in the active site of PhyK
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,4,5,6-pentakisphosphate + phosphate
although the PhyK homolog AppA is biochemically characterized as a 6-phytase, a co-crystal structure shows the phytate 3-phosphate as scissile group in a similar position to in the active site of PhyK
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
58.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
O-phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
28% of the activity with 4-nitrophenylphosphate
-
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
UTP + H2O
UDP + phosphate
-
350% relative activity compared to myo-inositol hexakisphosphate
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
74% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
2.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.6% of the activity with myo-inositol hexakisphosphate
-
?
2-glycerophosphate + H2O
glycerate + phosphate
-
127% of the activity with myo-inositol hexakisphosphate
-
-
?
2-glycerophosphate + H2O
glycerate + phosphate
-
19.8% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
4.9% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
97.1% of the activity with myo-inositol hexakisphosphate
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
69% of the activity with 4-nitrophenylphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
95% activity compared to myo-inositol hexakisphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
95% activity compared to myo-inositol hexakisphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
168% relative activity compared to myo-inositol hexakisphosphate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
254% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
254% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
39.8% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
101% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
7.6% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
23.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
7.6% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
0.65% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
59.6% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is nearly as efficient as on phytate
-
?
ADP + H2O
?
-
25.6% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
?
-
75% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
?
-
7.5% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ADP + H2O
?
-
7.5% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ADP + H2O
?
-
14.2% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
? + phosphate
-
50% of the activity with 4-nitrophenylphosphate
-
-
?
ADP + H2O
? + phosphate
-
177% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
80% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
80% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
103% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
-
0.02% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
AMP + phosphate
-
120% activity compared to myo-inositol hexakisphosphate
-
-
?
ADP + H2O
AMP + phosphate
-
206% relative activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
173% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
173% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
50% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
50% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
9.6% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
AMP + H2O
adenosine + phosphate
143% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
30% relative activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
25.0% of the activity with myo-inositol hexakisphosphate
-
?
AMP + H2O
adenosine + phosphate
-
195% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
38.8% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
50% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
5.6% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ATP + H2O
?
-
22.3% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
reaction is nearly as efficient as on phytate
-
?
ATP + H2O
? + phosphate
-
256% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
97% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
97% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
208% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
-
0.26% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
-
256% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
133% activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
365% relative activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
76.67% activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
76.67% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
146% of the activity with myo-inositol hexakisphosphate
-
?
D-fructose 1,6-diphosphate + H2O
?
-
202.19% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
202.19% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
poor substrate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
228% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
228% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
35% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
35% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
8.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
8.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
158% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
229% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
5% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
poor substrate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
strong preference for glucose 1-phosphate over phytate, under physiological conditions glucose 1-phosphate is its most likely substrate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
76.72% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
92.0% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
20% of the activity with 4-nitrophenylphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
190% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
190% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
78.5% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
82% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
128% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
57% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
poor substrate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
73.75% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
73.75% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
0.39% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
217% of the activity with myo-inositol hexakisphosphate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
50% of the activity with myo-inositol hexakisphosphate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
poor substrate
-
-
?
diphosphate + H2O
2 phosphate
-
95% of the activity with 4-nitrophenylphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
438.5% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
fructose 1,6-diphosphate + H2O
?
-
12.3% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
fructose 1,6-diphosphate + H2O
?
-
12.3% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
2.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
2.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
50.8% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
98% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
85.6% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
141% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
43% of the activity with 4-nitrophenylphosphate
-
-
?
inositol tetraphosphate + H2O
?
-
almost the same activity as with myo-inositol hexakisphosphate
-
-
?
inositol triphosphate + H2O
?
-
40% of the activity with myo-inositol hexakisphosphate
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol 2,4,5,6-tetrakisphosphate + H2O
myo-inositol 2,4,6-trisphosphate + phosphate
-
-
-
-
?
myo-inositol 2,4,5,6-tetrakisphosphate + H2O
myo-inositol 2,4,6-trisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + 3 H2O
myo-inositol 2,4,6-trisphosphate + 3 phosphate
-
enzyme efficiently hydrolyzes Ca2+-phytate salts and yields myo-inositol 2,4,6-trisphosphate and three phosphate groups as final products
-
-
?
myo-inositol hexakisphosphate + 3 H2O
myo-inositol 2,4,6-trisphosphate + 3 phosphate
-
enzyme efficiently hydrolyzes Ca2+-phytate salts and yields myo-inositol 2,4,6-trisphosphate and three phosphate groups as final products
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
a mixture of two pentaphosphates: the major component is 1-myo-inositol 1,2,4,5,6-pentakisphosphate and the other is 1-myo-inositol 1,2,3,4,5-pentakisphosphate
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
about 85% of myo-inositol hexakisphosphate in soybean meal is hydrolyzed by the enzyme whereas only 67% of the myo-inositol hexakisphosphate in cottonseed meal is hydrolyzed by the same enzyme treatment
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
94776, 114252, 114253, 114257, 114258, 114264, 114273, 114279, 134797, 677690, 677774, 678749, 679568
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
calcium myo-inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
dodecasodium myo-inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
100% relative activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
preferred substrate, 100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
preferred substrate, 100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Schwanniomyces castellii
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Thermothelomyces heterothallicus BJTLR50
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Torulopsis candida
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Bacillus sp. (in: Bacteria) DECSR1
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
sodium salt
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Aspergillus niger NII 08121
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
best substrate is calcium phytate, sodium phytate results in 60% activity compared to calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Aspergillus oryzae SBS50
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Aspergillus oryzae SBS50
best substrate is calcium phytate, sodium phytate results in 60% activity compared to calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
highest activity at 2.05 mM substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis B.S.46
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis B.S.46
-
highest activity at 2.05 mM substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis DR8886
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis DR8886
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid, sodium phytate is preferred compared to calcium phytate and potassium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid, sodium phytate is preferred compared to calcium phytate and potassium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
KM873028
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
KM873028
highly preferred substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Morchella importuna SCYDJ1A1
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Pseudomonas sp. FB15
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
substrate is calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
substrates are sodium phytate, potassium phytate, and calcium phytate. Highest activity with calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytase
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BJTLR50
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BJTLR50
i.e. phytase
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Loigolactobacillus coryniformis MH121153
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for the substrate, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Bacillus sp. (in: Bacteria) KHU-10
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
step-wise hydrolysis of myo-inositol hexakisphosphate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
hydrolyzes phytate in a stepwise manner
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
after 10 min D-myo-inositol 1,2,4,5,6-pentakisphosphate is the major degradation product, accompanied by small amounts of D-myo-inositol 1,2,3,4,6-pentakisphosphate, D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate. After 30 min, the quantity of D-myo-inositol 1,2,4,5,6-pentakisphosphate decreases and the levels of D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate increases. After 90 min the major products are Ins(1,3,5) P3 and Ins(2,4,6)P3
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
after 10 min D-myo-inositol 1,2,4,5,6-pentakisphosphate is the major degradation product, accompanied by small amounts of D-myo-inositol 1,2,3,4,6-pentakisphosphate, D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate. After 30 min, the quantity of D-myo-inositol 1,2,4,5,6-pentakisphosphate decreases and the levels of D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate increases. After 90 min the major products are Ins(1,3,5) P3 and Ins(2,4,6)P3
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
step-wise dephosphorylation occurs via 1. D-myo-inositol 1,2,4,5,6-pentakisphosphate, 2. D-myo-inositol 1,2,5,6-tetrakisphosphate or D-myo-inositol 2,4,5,6-tetrakisphosphate, 3. D-myo-inositol 1,2,6-trisphosphate, D-myo-inositol 1,2,3-trisphosphate or D-myo-inositol 1,4,5-trisphosphate, 4. myo-inositol 1,2-bisphosphate or myo-inositol 2,5-bisphosphate, myo-inositol 4,5-bisphosphate or myo-inositol 2,4-bisphosphate. Myo-inositol 2-monophosphate is the final product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
7% of the activity with 4-nitrophenylphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
sodium salt
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
cleavage initiation in the dephosphorylation of myo-inositol hexakisphosphate at C3
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
substrate Na-phytate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
substrate Na-phytate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
-
25% of the activity with 4-nitrophenylphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
135% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
135% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
311% relative activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
152.95% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
152.95% activity compared to myo-inositol hexakisphosphate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
84% of the activity with myo-inositol hexakisphosphate
-
?
phenyl phosphate + H2O
phenol + phosphate
-
188% relative activity compared to myo-inositol hexakisphosphate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
89.2% of the activity with myo-inositol hexakisphosphate
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
92% of the activity with 4-nitrophenylphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
130% activity compared to myo-inositol hexakisphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
130% activity compared to myo-inositol hexakisphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
328% relative activity compared to myo-inositol hexakisphosphate
-
-
?
phytate + H2O
?
-
Na- and Ca-phytate, the first results in higher activity, substrate binding analysis by molecular modelling of phytate inside the active site, residue K77 is able to form two hydrogen bonds with the two phosphate groups on the phytate, whereas in case of K77R, the guanidinium group of arginine is able to form up to 4 H-bonds with the two phosphate groups
-
-
?
phytate + H2O
?
-
Na- and Ca-phytate, the first results in higher activity, substrate binding analysis by molecular modelling of phytate inside the active site, residue K77 is able to form two hydrogen bonds with the two phosphate groups on the phytate, whereas in case of K77R, the guanidinium group of arginine is able to form up to 4 H-bonds with the two phosphate groups
-
-
?
additional information
?
-
-
high levels of phosphorous in the growth medium inhibit phytase synthesis, effect is larger in semisolid medium than in liquid medium
-
-
?
additional information
?
-
-
the enzyme exhibits a broad substrate selectivity, substrate are e.g. ATP, ADP, AMP, glucose-6-phosphate, fructose-6-phosphate, 4-nitrophenyl phosphate, and beta-glycerophosphate
-
-
?
additional information
?
-
-
the enzyme exhibits a broad substrate selectivity, substrate are e.g. ATP, ADP, AMP, glucose-6-phosphate, fructose-6-phosphate, 4-nitrophenyl phosphate, and beta-glycerophosphate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.1 per mM and s
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.1 per mM and s
-
-
?
additional information
?
-
-
enzyme exhibits phytase and acid phosphatase activity
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
to reduce phytates in dried grains with solubles (DDGS) and corn gluten feed (CGF), a phytase from Aspergillus niger, PhyA, is investigated regarding its capability to catalyze the hydrolysis of phytates in light steep water and whole stillage. Dephosphorylation of phytates in light steep water and whole stillage proceeds via the formation of InsP5, InsP4, InsP3, and InsP2 intermediates with phosphate and InsP1 as the end products. During the process, the amount of phosphate in the substrates is increased from 54% to 66% in the whole stillage, and from 20% to 90% in the light steep water, suggesting to a substantial dephosphorylation of the phytates in the light steep water and whole stillage via PhyA catalyzed hydrolysis. The most effective period of degradation is during the first 2 h for whole stillage and 6 h for light steep water
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.04 per mM and s
-
-
?
additional information
?
-
-
substrate specificity with substrates Na-phytate, i.e. myo-inositol-1,2,3,4,5,6-hexakisphosphate, naphtyl-1 phosphate, 4-nitrophenylphosphate, ATP, and ADP, overview
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.04 per mM and s
-
-
?
additional information
?
-
-
substrate specificity with substrates Na-phytate, i.e. myo-inositol-1,2,3,4,5,6-hexakisphosphate, naphtyl-1 phosphate, 4-nitrophenylphosphate, ATP, and ADP, overview
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
Aspergillus oryzae SBS50
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay
-
-
?
additional information
?
-
usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay
-
-
?
additional information
?
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0
-
-
?
additional information
?
-
-
substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) KHU-10
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP
-
-
?
additional information
?
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
-
the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP
-
-
?
additional information
?
-
Bacillus subtilis DR8886
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
the purified enzyme shows specificity to different salts of phytic acid, it also shows phosphomonoesterase activity with ADP and ATP (high activity), while not with 4-nitrophenyl phosphate and glucose 6-phosphate
-
-
?
additional information
?
-
the purified enzyme shows specificity to different salts of phytic acid, it also shows phosphomonoesterase activity with ADP and ATP (high activity), while not with 4-nitrophenyl phosphate and glucose 6-phosphate
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
-
phytases from bifidobacteria could be partly active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
Burkholderia sp. a13(2014) JCM 30421
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
KM873028
enzyme rPhysXT52 shows nonspecific phosphohydrolytic activity with 4-nitrophenyl phosphate, 1-naphthyl phosphate, 2-naphthyl phosphate, phenyl phosphate, 2-glycerophosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-diphosphate, AMP, ADP, ATP, and NADP+, overview
-
-
?
additional information
?
-
-
hydrolysis of insoluble metal-phytates, overview. The enzyme is also active with 4-nitrophenyl phosphate, sodium diphosphate, glucose-1-phosphate, and glucose-6-phosphate
-
-
?
additional information
?
-
-
the enzyme also performs unspecific phosphomonoesterase (PME) activity with substrate 4-nitrophenyl phosphate. Phytase and PME activities in Evernia prunastri strongly co-vary among sites of sample collection with contrasting N deposition
-
-
?
additional information
?
-
enzyme is a 6-phytase, EC 3.1.3.26. Major degradation product is DL-inositol 1,2,3,4,5-pentaphosphate
-
-
?
additional information
?
-
-
HcBPP preferentially recognizes its substrate and selectively hydrolyzes insoluble Ca2+-phytate salts at three phosphate group sites, yielding the final product, myo-inositol 2,4,6-trisphosphate, exhibiting also the 1- and 5-phytase activities. Ins(2,4,6)P3 is unable to bind Ca2+ or any other cation tested, including Co2+, Cu2+, Fe3+, Mg2+, Mn2+, Sr2+, and Zn2+
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
the enzyme also shows phosphate-monoester phosphohydrolase activity, EC 3.1.3.2
-
-
?
additional information
?
-
phytase ASr1 acts primarily as a scavenger of phosphate groups locked in the phytic acid molecule
-
-
?
additional information
?
-
substrate binding structure modelling, all six phosphate groups of phytate are involved in a hydrogen bond network connecting the substrate with PhyK, induced conformational changes upon substrate binding, overview
-
-
?
additional information
?
-
-
no activity with GTP and diphosphate
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP. The recombinant LlALP2 expressed in Pichia pastoris hydrolyzes phytate and 4-nitrophenyl phosphate and exhibits no activity towards ATP. Activity against 4-nitrophenyl phosphate is nearly 2.5fold higher than against phytate, similar to what is observed with the native enzyme
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP. The recombinant LlALP2 expressed in Pichia pastoris hydrolyzes phytate and 4-nitrophenyl phosphate and exhibits no activity towards ATP. Activity against 4-nitrophenyl phosphate is nearly 2.5fold higher than against phytate, similar to what is observed with the native enzyme
-
-
?
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
Loigolactobacillus coryniformis MH121153
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
the enzyme also shows moderate activity with 4-nitrophenyl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1,6-bisphosphate, and glucose 6-phosphate, and low activity with AMP, ADP, and ATP. The enzyme cleaves phytate in soybean meal, rapeseed meal, and corn meal
-
-
?
additional information
?
-
Morchella importuna SCYDJ1A1
the enzyme also shows moderate activity with 4-nitrophenyl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1,6-bisphosphate, and glucose 6-phosphate, and low activity with AMP, ADP, and ATP. The enzyme cleaves phytate in soybean meal, rapeseed meal, and corn meal
-
-
?
additional information
?
-
high substrate specificity for sodium phytate. No substrates: 4-nitrophenyl phosphate, D-glucose 1-phosphate, ATP, D-fructose-1,6-diphosphate, glycerol 2-phosphate
-
-
?
additional information
?
-
Niallia nealsonii ZJ0702
high substrate specificity for sodium phytate. No substrates: 4-nitrophenyl phosphate, D-glucose 1-phosphate, ATP, D-fructose-1,6-diphosphate, glycerol 2-phosphate
-
-
?
additional information
?
-
-
no activity towards 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate and 1-L-myo-inositol 1,2,5,6-tetrakisphosphate
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10
-
-
?
additional information
?
-
glucose-1-phosphatase enzymes and, specifically, Agp phytases are known to have a broad substrate specificity. The bifunctional enzyme from Pantoea sp. 3.5.1 exhibits 3-phytase activity, and also glucose-1-phosphatase, cf. EC 3.1.3.10. Broad substrate specificity, substrates are phytate and many other phosphate-containing substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview
-
-
?
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
?
additional information
?
-
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
?
additional information
?
-
Penicillium chrysogenum CCT 1273
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
?
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
Penicillium oxalicum KCTC6440
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
-
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
Pseudomonas sp. FB15
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
-
the enzyme is inducible under carbon limitation in the presence of myo-inositol hexakisphosphate
-
-
?
additional information
?
-
-
the phytase demonstrates high substrate specificity for sodium phytate. The enzyme also hydrolyzes 4-nitrophenyl phosphate, ATP, AMPc, glucose 6-phosphate, glucose 1-phosphate, and UDPG
-
-
?
additional information
?
-
-
the phytase isozymes exhibit a broad affinity for various phosphorylated compounds, i.e. 4-nitrophenyl phosphate 1-naphthyl phosphate, 2-naphthyl phosphate, AMP, ATP, GTP, fructose-1, 6-bisphosphate, fructose-6-phosphate, glucose-6-phosphate, and pyridoxal phosphate, substrate specificities, overview
-
-
?
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
Rhodotorula mucilaginosa JMUY14
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
-
-
?
additional information
?
-
enzyme rSt-Phy also shows haloperoxidase activity with KBr, metavanadate, and H2O2, only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, overview
-
-
?
additional information
?
-
-
the recombinant enzyme displayed broad substrate specificity. Molecular modeling and docking of phytase with various substrates show differential binding patterns, overview. Strong binding affinity with ATP and phytic acid, while the lowest with AMP and phosphoenol pyruvate. The enzyme is also active with ATP and 4-nitrophenyl phosphate
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
-
lower activity with 4-nitrophenyl phosphate, no or poor activity with AMP, ADP, ATP, GTP, NADP+, glucose 1-phosphate, and glucose 6-phosphate
-
-
?
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
additional information
?
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
additional information
?
-
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
additional information
?
-
the enzyme catalyzes the dephytinization of soymilk
-
-
?
additional information
?
-
-
the enzyme catalyzes the dephytinization of soymilk
-
-
?
additional information
?
-
the phytase exhibits broad substrate specificity since it hydrolyses 4-nitrophenyl phosphate, ATP, ADP, and glucose-6-phosphate besides phytic acid. The enzyme hydrolyzes insoluble calcium and magnesium phytates efficiently, but not iron phytate
-
-
?
additional information
?
-
-
the phytase exhibits broad substrate specificity since it hydrolyses 4-nitrophenyl phosphate, ATP, ADP, and glucose-6-phosphate besides phytic acid. The enzyme hydrolyzes insoluble calcium and magnesium phytates efficiently, but not iron phytate
-
-
?
additional information
?
-
vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
enzyme is a 6-phytase, EC 3.1.3.26. Major degradation product is DL-inositol 1,2,3,4,5-pentaphosphate
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
strong preference for glucose 1-phosphate over phytate, under physiological conditions glucose 1-phosphate is its most likely substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,4,5,6-pentakisphosphate + phosphate
although the PhyK homolog AppA is biochemically characterized as a 6-phytase, a co-crystal structure shows the phytate 3-phosphate as scissile group in a similar position to in the active site of PhyK
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Aspergillus niger NII 08121
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Aspergillus oryzae SBS50
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis B.S.46
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Bacillus subtilis DR8886
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
KM873028
highly preferred substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Morchella importuna SCYDJ1A1
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Pseudomonas sp. FB15
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus BJTLR50
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Loigolactobacillus coryniformis MH121153
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
cleavage initiation in the dephosphorylation of myo-inositol hexakisphosphate at C3
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
additional information
?
-
-
high levels of phosphorous in the growth medium inhibit phytase synthesis, effect is larger in semisolid medium than in liquid medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
-
phytases from bifidobacteria could be partly active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
HcBPP preferentially recognizes its substrate and selectively hydrolyzes insoluble Ca2+-phytate salts at three phosphate group sites, yielding the final product, myo-inositol 2,4,6-trisphosphate, exhibiting also the 1- and 5-phytase activities. Ins(2,4,6)P3 is unable to bind Ca2+ or any other cation tested, including Co2+, Cu2+, Fe3+, Mg2+, Mn2+, Sr2+, and Zn2+
-
-
?
additional information
?
-
phytase ASr1 acts primarily as a scavenger of phosphate groups locked in the phytic acid molecule
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10
-
-
?
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
?
additional information
?
-
-
the enzyme is inducible under carbon limitation in the presence of myo-inositol hexakisphosphate
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
additional information
?
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
additional information
?
-
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
CaCl2
CaCl2 is required for activity, and the optimal concentration of CaCl2 for the full-length enzyme is 4 mM, the isolated C-terminal domain is most active at 3 mM
Cd2+
Co2+
Cu2+
Fe2+
Hg2+
Iron
-
the Fe ion is coordinated by the oxygen atom of Tyr224, N-atom of His 399 and the carboxylate group of Asp 194
K+
Li+
Mg2+
Mn2+
Na+
vanadate
-
incubation with vanadate to obtain a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate
Zinc
-
the Zn ion is coordinated by the N-atom of His 360, the N-atom of His 397 and the amide oxygen of Asn 278
Zn2+
additional information
Ba2+
-
53% activation at 1 mM, 46% activation at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Ca2+
-
45% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Ca2+
-
rapid equilibrium ordered mechanism in which binding of ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phytate complex. 4 mol of Ca2+ bind to 1 mol of phytate
Ca2+
-
the purified recombinant enzyme domains PhyH and PhyH-DII require Ca2+ for phytase activity, optimal at 1 mM
Ca2+
enzyme requires excess Ca2+ for its enzymatic activity as the pH decreases
Ca2+
-
the crystal structure of the enzyme in complex with inorganic phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site
Ca2+
required, assay in presence of 1.5 mM. The removal of Ca2+ causes a change in the CD-spectrum. The addition of Ca2+ to the apoenzyme results in an increase in the mean residue ellipticity, indicating a recovery of beta-sheet elements
Ca2+
KM873028
slightly elevates the phytase activity at 20 mM but inhibits the activity at a higher concentration of 50 mM
Ca2+
activates, required, optimal at 1.5-2.5 mM, activity profile, overview
Ca2+
-
required for activity. Activation of the enzyme involves a minimum of four Ca2+-binding sites and enzyme activation is mediated by cooperative interactions between Ca2+ and the enzyme or phytate. The apparent Km increases as the Ca2+ concentration is increased, and the apparent Vmax also increases
Ca2+
the activity is calcium-dependent, best at 1 mM. Four Ca2+ ions bind to the active Ca2+ binding sites (C3, C5, C6, C7) and create an ideal conformation and charge distribution for the substrate
Ca2+
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
Co2+
-
35% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Co2+
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
Fe2+
-
13% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Hg2+
-
13% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
K+
-
40% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Mg2+
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
Zn2+
-
13% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
additional information
-
no or poor effect by Mn2+ and Zn2+ at 10 mM
additional information
-
no activation or inhibition by cations K+, Ca2+, Mg2+, Mn2+, Zn2+, Cd2+, Cu2+, Pb2+, Hg2+, Fe3+, and Al3+
additional information
-
no effect is observed after addition of 200 mM Fe2+ or Fe3+
additional information
enzyme refolded in presence of Cu2+, Fe2+, Mg2+, Co2+, Zn2+ or Mn2+, fails to show any enzyme activity even in the presence of Ca2+ in the reaction mix
additional information
-
the enzyme is inhibited by metal ions Mn2+, Zn2+, Ca2+, Cu2+, Fe2+, Mg2+, and Co2+
additional information
poor effect by Mg2+ and Sr2+ at 1 mM
additional information
-
not affected at concentrations up to 10 mM by: Cd2+, Ca2+, K+, Mg2+, Mn2+, Ni2+ and Na+
additional information
-
Ca2+, Ag+, Mg2+, Co2+, Zn2+, and Ni2+ have poor effects at 1-5 mM
additional information
-
Li+, Na+, K+ and Mg2+ do not significantly affect the phytase activity
additional information
-
the enzyme shows no requirement for metal ions
additional information
no requirement of metal ions for the activity
additional information
-
no requirement of metal ions for the activity
additional information
no effect by KI, Mn2+, and Na+ at 1-10 mM, poor effect by Co2+ at 1-10 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
guanidinium-HCl
-
6 M, 92% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
LiCl
enzyme PHY US573 is extremely salt-tolerant preserving 80% and 95% of activity in the presence of 20 g/l of NaCl and LiCl, respectively
myo-inositol-1,2,3,4,5,6-hexakissulfate
-
potent inhibition, the compound is isosteric and isoelectronic with respect to substrate myo-inositol-1,2,3,4,5,6-hexakisphosphate
NaCl
enzyme PHY US573 is extremely salt-tolerant preserving 80% and 95% of activity in the presence of 20 g/l of NaCl and LiCl, respectively
pancreatin
-
34.2% residual activity after 1 h incubation with pancreatin at 40°C
-
1,2-Cyclohexanedione
-
about 7 Arg of the total 19 are modified, partially reversed by 0.2 M hydroxylamine
2,3-Butanedione
-
strong inhibition, interacts with arginine residues
2,3-Butanedione
strong inhibition at 1-5 mM, complete inhibition at 10 mM
Al3+
-
98% inhibition at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
arsenate
-
the enzyme of Pteris vittata shows partial resistance to arsenate in contrast to enzymes from other ferns, e.g. Pteris ensiformis and Nephrolepis exaltata
Ca2+
-
5 mM, 10% decreased activity, although calcium has no direct influence on enzymatic activity, it plays a crucial protective role, since in the absence of calcium, the denaturation of the enzyme is complete after 1 h at 66.5°C
Ca2+
KM873028
slightly elevates the phytase activity at 20 mM but inhibits the activity at a higher concentration of 50 mM
Co2+
-
60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Cu2+
-
effect on the ability of phytase to hydrolyze phytate phosphorus is dependent on pH. At pH 2.5 (gastric pH), no inhibition is noted among the treatments (copper citrate, copper chloride, copper lysinate, cupper sulfate, tribasic copper chloride) except that the addition of 250 and 500 mg Cu/kg diet from copper chloride and 500 mg Cu/kg from copper sulfate slightly inhibits phytate phosphorus hydrolysis. When pH is increased to 5.5-6.5 (small intestinal digesta) phytate phosphorus hydrolysis is greatly inhibited
Cu2+
-
70% inhibition at 5 mM, 95% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Fe2+
-
59% inhibition at 5-15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Fe2+
-
30% inhibition at 1 mM, complete inhibition at 2 mM; complete inhibition
Fe2+
-
stronger inhibition at 10 mM of isozyme RO2 compared to isozyme RO1
Fe3+
-
stronger inhibition at 10 mM of isozyme RO2 compared to isozyme RO1
Hg2+
-
48% inhibition at 10 mM, 87% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
K+
-
16% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
KI
-
6 M, 95% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
metavanadate
-
50% inhibition at 0.0011 and pH 2.5, or at 0.0053 mM and pH 5.0
-
metavanadate
50% inhibition at 0.00075 mM and pH 5.0 or at 0.00090 mM and pH 3.0
-
Mg2+
-
61% inhibition at 5 mM, 92% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Mg2+
KM873028
has no significant influence at low concentrations of 1 and 5 mM and inhibits the phytase activity at high concentrations of 20 and 50 mM
Mn2+
-
73% inhibition at 4 mM, 97% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Mn2+
-
92% inhibition at 1 mM, complete inhibition at 5 mM; complete inhibition
Mn2+
-
activates at 1 mM by 15%, inhibits 16% at 5 mM, 49% at 10 mM, and 85% at 50 mM
molybdate
-
almost complete inhibition of isozymes RO1 and RO2 at 1-10 mM
myo-inositol hexakisphosphate
-
inhibition at substrate concentrations above 2.5 mM
myo-inositol hexakisphosphate
-
completely inhibited by 5 mM myo-inositol hexakisphosphate
myo-inositol hexasulfate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
myo-inositol hexasulfate
-
a potent competitive inhibitor for phytase
N-bromosuccinimide
strong inhibition at 1-5 mM, complete inhibition at 10 mM
orthovanadate
-
50% inhibition at 0.0004 and pH 2.5, or at 0.040 mM and pH 5.0
orthovanadate
50% inhibition at 0.0022 mM and pH 5.0 or at 0.000072 mM and pH 3.0
Pb2+
KM873028
94% inhibition at 1 mM, almost complete inhibition at 5 mM
Pepsin
-
40.8% residual activity after 1 h incubation with pepsin at 40°C
-
Pepsin
-
loses 65% of the initial activity in the presence of 3000 units pepsin
-
Pepsin
-
32.4% residual activity after 1 h incubation with pepsin at 40°C
-
Phenylglyoxal
-
interacts with arginine residues. Phenylglyoxal does not show any inhibition under acidic pH 5.0
PMSF
-
80% inhibition at 2.0 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
SDS
-
0.1%, 92% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
SDS
KM873028
73% inhibition at 0.1% w/v, 85% at 0.5% w/v, and 94% at 2% w/v
SDS
90% inhibition at 1%, complete inhibition at 10%, 10% inhibition at 0.1%
Urea
-
in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Urea
-
8 M, 65% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
vanadate
-
51V-NMR studies show that vanadate is incorporated in the active site. Enzyme shows higher affinity for vanadate at pH 5.0 than at pH 7.6. vanadium is covalently coordinated in the active site of the enzyme to an apical histidine and to oxygen donors. Two sites are available for coordination. Upon addition of H2O2 two peroxide-vanadate-phytase complexes are formed at pH 5.0 in the case of 3-phytase
vanadate
meta-vanadate and ortho-vanadate, exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with substrate phytate, molecular docking study and inhibition mechanism, overview. The active site of haloperoxidase shows close similarity with histidine acid phytases. Inhibition of phytase by vanadate can make the enzyme behave as a vanadate-dependent haloperoxidase provided phosphoesterase activity of the enzyme is shut down by the vanadate. The vanadate exists as an anion at pH 3.0 and possibly binds to the active site cleft of phytase, which has a cluster of positively charged amino acids arginine, lysine, and histidine below the isoelectric point (pI) of the enzyme. Upon molecular docking of metavanadate with the rPPHY, it was observed to interact with the same amino acid residues of the catalytic site, with which substrate interacts. Both inhibitor and substrate might sit into the catalytic cleft of the enzyme which is placed between conserved alpha/beta-domain and a variable alpha-domain of rPPHY. When bonding of the substrate/inhibitor was analyzed, it is found to form bonds with arginine (R70), arginine (R74), and aspartate (D344). Inhibition kinetics of phytase by metavanadate
additional information
-
neither inhibitory nor stimulating: Mn2+, Mg2+, Ni2+, SO4-, and NO3-
-
additional information
-
recombinant enzyme is inhibited by antibody raised against a 20-mer internal peptide
-
additional information
the phytase of Aspergillus oryzae shows protease resistance. Poor effect by urea at 1-2 M and by EDTA at 1-5 mM
-
additional information
-
the phytase of Aspergillus oryzae shows protease resistance. Poor effect by urea at 1-2 M and by EDTA at 1-5 mM
-
additional information
the enzyme is resistant to bovine bile extract
-
additional information
-
the enzyme is resistant to bovine bile extract
-
additional information
-
no inhibition by myo-inositol hexasulfate up to 2 mM, no inhibition by F- up to 10 mM
-
additional information
the purified enzyme is resistant to proteases trypsin and pepsin
-
additional information
-
not affected at concentrations up to 10 mM by: EDTA, Cd2+, Ca2+, K+, Mg2+, Mn2+, Ni2+ and Na+
-
additional information
-
the enzyme is fairly stable in the presence of pepsin under physiological conditions
-
additional information
-
no substrate inhibition by 4-nitrophenyl phosphate up to 10 mM
-
additional information
phytase enzymes in general possess a native resistance towards proteolytic degradation
-
additional information
-
not inhibited by 1 mM EDTA and 5 mM 1,10-phenanthroline
-
additional information
poor inhibition by Co2+ and Al3+ at 5 mM
-
additional information
-
no or poor inhibition of isozymes RO1 and RO2 by EDTA
-
additional information
-
the enzyme shows strong protease resistance, after being incubated with 0.1 mg/ml of pepsin and trypsin at 37°C for 1 h, the residual activity is 92.2% and 75.6%, respectively
-
additional information
the recombinant enzyme shows resistance to trypsin
-
additional information
enzyme PHYUS42 exhibits high stability after incubation at 37°C for 1 h in the presence of bovine bile and digestive proteases like pepsin, trypsin, and chymotrypsin. PHY US42 maintains 90% of its activity after incubation for 1 h in the presence of 0.5% bovine bile
-
additional information
-
inhibitor docking study, overview. The enzyme is protease resistant
-
additional information
the enzyme rStPhy shows very low sensitivity to pepsin
-
additional information
the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy
-
additional information
the enzyme is resistent against pepsin and trypsin, 95% of initial activity is retrieved after 1.0-h incubation in pepsin/trypsin. Poor inhibition by acetone, EDTA and 2-mercaptoethanol
-
additional information
no inhibition by sodium azide, DTT, 2-mercaptoethanol, EDTA, toluene, glycerol, and PMSF
-
additional information
-
no inhibition by sodium azide, DTT, 2-mercaptoethanol, EDTA, toluene, glycerol, and PMSF
-
additional information
when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutant E230R of YeAPPA retains less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230
-
additional information
-
when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutant E230R of YeAPPA retains less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230
-
additional information
when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutants E230K and E230R of YkAPPA retain less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230
-
additional information
-
when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutants E230K and E230R of YkAPPA retain less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
activates, dependent on, best at 1 mM, required for thermal stability
cetyl trimethyl ammonium bromide
-
1%, 80% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
iodoacetic acid
-
0.1 mM, 28% acti1vation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
L-Tartaric acid
-
0.1 mM, 34% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
oxalate
-
0.1 mM, 52% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
p-hydroxymercuribenzoate
-
0.1 mM, 22% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Phosphomycin
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
PMSF
-
0.1 mM, 63% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Sodium azide
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Tween-20
-
1%, 80% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Tween-80
-
1%, 77% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2-mercaptoethanol
-
0.1 mM, 59% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
citrate
-
0.1 mM, 45% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
EDTA
-
0.1 mM, 54% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
isoamyl alcohol
slightly stimulates the phytase activity
Triton X-100
-
5%, 75% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Tween 20
KM873028
about 22% and 30% activation at 0.5% and 1% v/v, respectively
Tween 80
KM873028
about 27% and 35% activation at 0.5% and 1% v/v, respectively
additional information
no effect by EDTA and EGTA at up to 20 mM
-
additional information
the chelating agent EDTA has no discernible effect on the activity of rSt-Phy
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bone Resorption
Formulating diets based on digestible calcium instead of total calcium does not affect growth performance or carcass characteristics, but microbial phytase ameliorates bone resorption caused by low calcium in diets fed to pigs from 11 to 130 kg.
Colorectal Neoplasms
A novel mechanism underlying phytate-mediated biological action-phytate hydrolysates induce intracellular calcium signaling by a Galphaq protein-coupled receptor and phospholipase C-dependent mechanism in colorectal cancer cells.
Malnutrition
Effects of nutritional deficiencies during neonatal and post-weaning period on rat intestinal phytase and phosphatase activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
di-sodium phenyl phosphate dihydrate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
1.562
4-methylumbelliferyl phosphate
recombinant mutant T44V/K45E, pH 6.6, 37°C
1.598
4-methylumbelliferyl phosphate
recombinant mutant T44I/K45E, pH 6.6, 37°C
3.495
4-methylumbelliferyl phosphate
recombinant wild-type enzyme, pH 6.6, 37°C
0.14
D-fructose 1,6-diphosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.28
D-glucose 1-phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.27
D-glucose 6-phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.01073
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
0.0139
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
0.0147
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
0.01547
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
0.01794
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
0.01927
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
0.02075
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
0.021
myo-inositol hexakisphosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.02189
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
0.02769
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
0.03073
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
0.0827
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 4.0
0.0864
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 4.0
0.0934
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 4.0
0.1064
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1076
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 5.5
0.1083
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 5.5
0.114
myo-inositol hexakisphosphate
in 200 mM sodium acetate buffer (pH 5.5), at 37°C
0.1304
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1363
myo-inositol hexakisphosphate
wild-type, pH 9.0, temperature not specified in the publication
0.138
myo-inositol hexakisphosphate
wild-type, pH 7.0, temperature not specified in the publication
0.143
myo-inositol hexakisphosphate
wild-type, pH 8.0, temperature not specified in the publication
0.143
myo-inositol hexakisphosphate
recombinant enzyme, pH 5.0, 60°C
0.146
myo-inositol hexakisphosphate
wild-type, pH 6.0, temperature not specified in the publication
0.147
myo-inositol hexakisphosphate
calcium phytate, pH 5.0, 60°C
0.151
myo-inositol hexakisphosphate
wild-type, pH 5.0, temperature not specified in the publication
0.154
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.156
myo-inositol hexakisphosphate
mutant D308E, pH 7.0, temperature not specified in the publication
0.156
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
0.156
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
0.159
myo-inositol hexakisphosphate
wild-type, pH 4.0, temperature not specified in the publication
0.159
myo-inositol hexakisphosphate
-
substrate sodium phytate, pH 5.0, 60°C, recombinant enzyme
0.1623
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R/T271R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.167
myo-inositol hexakisphosphate
mutant D308A, pH 7.0, temperature not specified in the publication
0.1675
myo-inositol hexakisphosphate
-
wild type enzyme, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.18
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
0.189
myo-inositol hexakisphosphate
mutant D56E, pH 7.0, temperature not specified in the publication
0.196
myo-inositol hexakisphosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
0.208
myo-inositol hexakisphosphate
-
substrate potassium phytate, pH 5.0, 60°C, recombinant enzyme
0.218
myo-inositol hexakisphosphate
mutant D56L, pH 7.0, temperature not specified in the publication
0.22
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
0.24
myo-inositol hexakisphosphate
native enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
0.248
myo-inositol hexakisphosphate
mutant D56A, pH 7.0, temperature not specified in the publication
0.262
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 52.5°C
0.28
myo-inositol hexakisphosphate
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.293
myo-inositol hexakisphosphate
pH 7.0, 50°C, sodium phytate
0.3
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.32
myo-inositol hexakisphosphate
-
sodium phytate, pH 5.0, 60°C
0.326
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 37°C
0.382
myo-inositol hexakisphosphate
-
recombinant wild-type enzyme, pH 2.5, 40°C
0.3847
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 5.5
0.39
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
0.405
myo-inositol hexakisphosphate
-
recombinant mutant enzyme, pH 2.5, 40°C
0.48 - 0.545
myo-inositol hexakisphosphate
pH 5.5, 55°C, sodium phytate
0.49
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
0.532
myo-inositol hexakisphosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0 at 37°C
0.532
myo-inositol hexakisphosphate
recombinant enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
0.54
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
0.606
myo-inositol hexakisphosphate
-
pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.667
myo-inositol hexakisphosphate
-
substrate calcium phytate, pH 5.0, 60°C, recombinant enzyme
0.7
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.757
myo-inositol hexakisphosphate
pH 5.0, 55°C, recombinant His-tagged enzyme
0.78
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
0.8
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pGAPZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.856
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged C-terminal domain
0.858
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged full-length enzyme
1.2
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.4
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
1.45
myo-inositol hexakisphosphate
-
5.0 mM myo-inositol hexakisphosphate in 0.2 M sodium acetate, pH 5.0, at 60°C
1.5
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
1.77
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
1.8
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Pichia pastoris (pGAPZalphaA) or Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.1
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.19
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
0.035
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a1, pH 5.0, 36°C
0.036
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a, pH 5.0, 36°C
0.045
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
0.045
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b1, pH 5.0, 36°C
0.046
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b2, pH 5.0, 36°C
0.048
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
0.056
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 6.0, 37°C, recombinant mutant C264G
0.07
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 58°C, recombinant wild-type enzyme
0.13
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
isozyme RO2, pH 4.5, 40°C
0.145
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 37°C, recombinant mutant C215S
0.18
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.5, 53°C, recombinant mutant C31G
0.19
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
0.191
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C
0.24
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase 168PhyA, pH 7.0, 55°C
0.45
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79L, pH 4.5, 37°C
0.5
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
dual domain phytase PhyH, pH 7.0, 35°C
0.55
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79S, pH 4.5, 37°C
0.69
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79G, pH 4.5, 37°C
1.086
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C
1.28
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase PhyP, pH 7.0, 37°C
1.432
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DII, pH 7.0, 35°C
1.6
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
isozyme RO1, pH 4.5, 40°C
1.98
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
3.024
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
8.442
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
0.52
p-nitrophenyl phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
2.27
p-nitrophenyl phosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0 at 37°C
18.16
p-nitrophenyl phosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
KM873028
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
thermodynamics
-
additional information
additional information
kinetics and thermodynamics, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
-
typical Michaelis-Menten kinetics
-
additional information
additional information
typical Michaelis-Menten kinetics
-
additional information
additional information
-
typical Michaelis-Menten kinetics
-
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk plots
-
additional information
additional information
enzyme kinetics, also with other substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview
-
additional information
additional information
kinetics and thermodynamics of recombinant full-length enzyme and C-terminal domain, overview
-
additional information
additional information
-
kinetics and thermodynamics of recombinant full-length enzyme and C-terminal domain, overview
-
additional information
additional information
Line-Weaver Burk plot
-
additional information
additional information
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
additional information
additional information
-
Michealis-Menten kinetics
-
additional information
additional information
thermodynamics of the recombinant enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.33
4-methylumbelliferyl phosphate
recombinant wild-type enzyme, pH 6.6, 37°C
10.18
4-methylumbelliferyl phosphate
recombinant mutant T44V/K45E, pH 6.6, 37°C
10.42
4-methylumbelliferyl phosphate
recombinant mutant T44I/K45E, pH 6.6, 37°C
0.07
myo-inositol hexakisphosphate
mutant D56A, pH 7.0, temperature not specified in the publication
0.1
myo-inositol hexakisphosphate
mutant D56L, pH 7.0, temperature not specified in the publication
0.422
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
0.476
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
0.496
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
0.548
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
0.553
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
0.557
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
0.576
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
0.71
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
0.93
myo-inositol hexakisphosphate
-
5.0 mM myo-inositol hexakisphosphate in 0.2 M sodium acetate, pH 5.0, at 60°C
1.67
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged C-terminal domain
3.34
myo-inositol hexakisphosphate
mutant D56E, pH 7.0, temperature not specified in the publication
8.33
myo-inositol hexakisphosphate
mutant D308A, pH 7.0, temperature not specified in the publication
15.55
myo-inositol hexakisphosphate
mutant D308E, pH 7.0, temperature not specified in the publication
16.55
myo-inositol hexakisphosphate
wild-type, pH 7.0, temperature not specified in the publication
20.39
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged full-length enzyme
37.8
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
51.2
myo-inositol hexakisphosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
51.2
myo-inositol hexakisphosphate
recombinant enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
59.2
myo-inositol hexakisphosphate
native enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
398
myo-inositol hexakisphosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
720
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
908
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
1300
myo-inositol hexakisphosphate
calcium phytate, pH 5.0, 60°C
1837.8
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
2056
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
2230
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
2450.5
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
2510.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
2527.8
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
4965.7
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
5100
myo-inositol hexakisphosphate
recombinant enzyme, pH 5.0, 60°C
7367.6
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
7860
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
8430.1
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
284600
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 37°C
300000
myo-inositol hexakisphosphate
-
pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
375200
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 52.5°C
3 - 6
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 6.0, 37°C, recombinant mutant C264G
4.17
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DII, pH 7.0, 35°C
5.92
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase 168PhyA, pH 7.0, 55°C
12.28
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C
27.72
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
dual domain phytase PhyH, pH 7.0, 35°C
44.94
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase PhyP, pH 7.0, 37°C
59.83
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
62
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 37°C, recombinant mutant C215S
83.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
90
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
94.4
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C
161
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
234
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.5, 53°C, recombinant mutant C31G
248
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
253
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b2, pH 5.0, 36°C
260
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a, pH 5.0, 36°C
270
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b1, pH 5.0, 36°C
279
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a1, pH 5.0, 36°C
350
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 58°C, recombinant wild-type enzyme
370
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH not specified in the publication, temperature not specified in the publication
1.9
p-nitrophenyl phosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
44.2
p-nitrophenyl phosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
additional information
additional information
-
turnover number of immobilized enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency, fusion of domain PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies
-
1.53
4-methylumbelliferyl phosphate
recombinant wild-type enzyme, pH 6.6, 37°C
6.2
4-methylumbelliferyl phosphate
recombinant mutant T44I/K45E, pH 6.6, 37°C
6.52
4-methylumbelliferyl phosphate
recombinant mutant T44V/K45E, pH 6.6, 37°C
0.27
myo-inositol hexakisphosphate
mutant D56A, pH 7.0, temperature not specified in the publication
0.44
myo-inositol hexakisphosphate
mutant D56E, pH 7.0, temperature not specified in the publication
1.95
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged C-terminal domain
16.14
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
17.67
myo-inositol hexakisphosphate
mutant D56L, pH 7.0, temperature not specified in the publication
20.08
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
23.76
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged full-length enzyme
24.7
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
25.26
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
32.11
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
34.22
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
35.42
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
39.33
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
49.9
myo-inositol hexakisphosphate
mutant D308A, pH 7.0, temperature not specified in the publication
99.7
myo-inositol hexakisphosphate
mutant D308E, pH 7.0, temperature not specified in the publication
119.9
myo-inositol hexakisphosphate
wild-type, pH 7.0, temperature not specified in the publication
242.3
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
242.3
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
2267.5
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
2368.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
3272.7
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
4695.6
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
4767.2
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
5080.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
5231.8
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
5258.8
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
6235.5
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
8843.5
myo-inositol hexakisphosphate
calcium phytate, pH 5.0, 60°C
12389
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
37207.6
myo-inositol hexakisphosphate
recombinant enzyme, pH 5.0, 60°C
873006
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 37°C
1432060
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 52.5°C
0.00043
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 37°C, recombinant mutant C215S
0.00072
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 6.0, 37°C, recombinant mutant C264G
0.0013
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.5, 53°C, recombinant mutant C31G
0.002
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
0.005
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 58°C, recombinant wild-type enzyme
2.9
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DII, pH 7.0, 35°C
19.17
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
27.83
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
30
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
30.5
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
35
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase PhyP, pH 7.0, 37°C
54
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
dual domain phytase PhyH, pH 7.0, 35°C
87
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C
134
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79L, pH 4.5, 37°C
250
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase 168PhyA, pH 7.0, 55°C
517
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
550
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b2, pH 5.0, 36°C
600
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b1, pH 5.0, 36°C
640
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C
682
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79S, pH 4.5, 37°C
722
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a, pH 5.0, 36°C
796
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a1, pH 5.0, 36°C
4605
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79G, pH 4.5, 37°C
7900
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0046
myo-inositol-1,2,3,4,5,6-hexakissulfate
-
pH 5.0-5.5, temperature not specified in the publication
2.3
phytate
-
free, not complexed with Ca2+, competitive inhibitor
0.97
Ca2+
-
free, not complexed with phytate, competitive inhibitor
4.5
Ca2+
wild-type, pH 9.0, temperature not specified in the publication
5.2
Ca2+
wild-type, pH 8.0, temperature not specified in the publication
7.4
Ca2+
wild-type, pH 7.0, temperature not specified in the publication
17.6
Ca2+
wild-type, pH 6.0, temperature not specified in the publication
43.6
Ca2+
wild-type, pH 5.0, temperature not specified in the publication
738
Ca2+
wild-type, pH 4.0, temperature not specified in the publication
additional information
additional information
-
vanadate inhibition kinetics
-
additional information
additional information
vanadate inhibition kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000083
0.0000167
0.000133
0.23
recombinant alkaline beta-propeller phosphatase PhyH49, pH 7.5, 37°C, in a strain grown under phosphate limitation in the presence of phytate
0.58
recombinant acidic histidine phosphatase PhyH49, pH 4.5, 37°C, in a strain grown under phosphate limitation in the presence of phytate
1.82
-
functional domain Phyd-DII, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 35°C
13.01
-
beta-propeller phytase 168PhyA, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 55°C
13.82
purified recombinant His-tagged wild-type enzyme, pH 7.0, 60°C
1350
-
native enzyme from Penicillium chrysogenum strain CCT 1273, pH 5.0, 50°C
14.87
-
incomplete domain Phyd-DI fused to beta-propeller phytase 168PhyA, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 55°C
144
purified recombinant acidic histidine phosphatase PhyH49, pH 4.5, 37°C, substrate phytate
15.3
about, purified recombinant His-tagged wild-type PhyC, pH 7.0, 65°C
17.24
purified recombinant His-tagged mutant S51A/K265E, pH 7.0, 60°C
17.88
purified recombinant His-tagged mutant S197E, pH 7.0, 65°C
18.14
purified recombinant His-tagged mutant D24G/S51A, pH 7.0, 60°C
18.17
purified recombinant His-tagged mutant D24G/N121S, pH 7.0, 60°C
18.88
purified recombinant His-tagged mutant D24G/K111E, pH 7.0, 60°C
19.27
purified recombinant His-tagged mutant D24G/K265E, pH 7.0, 60°C
19.33
purified recombinant His-tagged mutant D24G/S51A/K265E, pH 7.0, 60°C
19.67
purified recombinant His-tagged mutant D24G/K70R, pH 7.0, 60°C
19.7
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Escherichia coli, pH 7.0, 60°C
19.72
purified recombinant His-tagged mutant D24G/K265N, pH 7.0, 60°C
19.73
purified recombinant His-tagged mutant D24G/K70R/K111E/N121S, pH 7.0, 60°C
20.64
purified recombinant His-tagged mutant D148E, pH 7.0, 65°C
21.61
-
beta-propeller phytase PhyP, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 37°C
22.7
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Pichia pastoris, pH 7.0, 60°C
2860
-
recombinant enzyme from Penicillium griseoroseum strain T73, pH 5.0, 50°C
286923
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
29.82
-
incomplete domain Phyd-DI fused to beta-propeller phytase PhyP, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 37°C
2982
purified recombinant nonglycosylated enzyme expressed from Escherichia coli, pH 5.5, 37°C
30.4
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Bacillus subtilis, pH 7.0, 60°C
4.43
-
dual domain PhyH, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 35°C
5.92
purified recombinant His-tagged enzyme, pH and temperature not specified in the publication, substrate alpha-D-glucose 1-phosphate
52.4
8.9
recombinant enzyme secreted from heterologously expressing Pichia pastoris, pH 5.5, 37°C
9.5
purified recombinant alkaline beta-propeller phosphatase PhyH49, pH 7.5, 37°C, substrate phytate
967
purified recombinant glycosylated enzyme expressed from Pichia pastoris, pH 5.5, 37°C
additional information
additional information
-
10 phytase units per gram dry matter at pH 4.5 and 37°C for recombinant enzyme expressed in Chlamydomonas rheinhardtii
additional information
-
phytase activity and phytic acid and total protein contents in grains of cultivated and tibetan wild barleys, overview
additional information
no activity of purified recombinant domain N
additional information
activity during recycling of immobilized permeabilized cells, overview
additional information
-
activity during recycling of immobilized permeabilized cells, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2
2.5
3.2
3.5
4 - 4.5
4 - 5
4 - 5.5
4.4
4.5
4.8
4.9
and a local pH-optimum at pH 3.4, substrate: myo-inositol hexakisphosphate
5 - 5.5
5 - 6
5.5
5.6
6 - 6.5
6.5
7 - 7.5
7.5
3.5
-
recombinant enzyme. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
3.5
substrate: D-glucose 1-phosphate, D-glucose 6-phosphate and D-fructose 1-phosphate
4
-
and a second lower optimum at pH 2.5, reaction with 4-nitrophenyl phosphate, native and recombinant enzyme
5
-
Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate, mutant enzyme Q27T/K68A with phytate as substrate
5.5
-
Y27T/K68A mutant enzyme, phytate as substrate, mutant enzyme Q27T with phytate as substrate
5.5
-
and a second lower optimum (60% of the activity at pH 5.5) at pH 2.5 for NRRL 3135 phytase. Specific activity for the T213 phytase is 3fold lower than for the NRRL 3135 phytase
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5 - 3
-
pH 1.5: about 50% of maximal activity, pH 3.0: about 55% of maximal activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5 - 6.5
activity range, enzyme mutant R79G, profile, overview
1.8 - 6
-
pH 1.8: about 45% of maximal activity, pH 6.0: about 45% of maximal activity
2 - 12
-
pH 2.0: about 45% of maximal activity, 12.0: about 25% of maximal activity
2 - 5.5
2 - 5.7
-
pH 2.0: about 10% of maximal activity, pH 5.7: about 40% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
2 - 6
2 - 7.5
2 - 9
2.5 - 5
2.5 - 5.5
2.5 - 6
-
pH 2.5: about 35% of maximal activity, pH 6.0: about 25% of maximal activity, recombinant enzyme
2.5 - 8
activity range, profile overview, narrow optimum, over 50% activity only at pH 4.0-5.0
2.5 - 8.5
activity range, profile overview, over 50% of activity at pH 3.5-6.5
3 - 5.5
3 - 7
3 - 8
3 - 9
3.5 - 5.5
3.5 - 6
3.5 - 7
3.5 - 9
pH profiles of wild-type and mutant enzymes, no activity of mutant enzymes above pH 7.5, overview
3.8 - 5.8
-
pH 3.8: about 55% of maximal activity, pH 5.8: about 70% of maximal activity
4 - 5
-
pH 3.0: nearly no activity, pH 4.0: optimum, pH 5.0: about 60% of maximal activity, pH 6.0: about 10% of maximal activity, reaction with 4-nitrophenyl phosphate
4 - 6
4 - 7
4 - 7.5
-
pH 4.0: about 45% of maximal activity, pH 7.5: about 45% of maximal activitry, Q27T mutant enzyme, phytate as substrate
4 - 8
-
pH 4.0: about 50% of maximal activity, pH 8.0: about 25% of maximal activity
4.2 - 6.5
-
pH 4.2: about 80% of maximal activity, pH 6.5: about 70% of maximal activity
4.5 - 5.5
4.5 - 6.5
-
pH 4.5: about 40% of maximal activity, pH 6.5: about 70% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
4.5 - 7
4.5 - 8
-
pH 4.5: about 55% of maximal activity, pH 8.5: about 25% of maximal activity
4.5 - 8.5
5 - 10
-
pH 5.0: about 50% of maximal activity, pH 10.0: about 80% of maximal activity, presence of 10 mM CaCl2
5 - 7
-
pH 5.0: about 90% of maximal activity, pH 7.0: about 50% of maximal activity, at 37°C
5 - 7.5
-
pH 5.0: about 70% of maximal activity, pH 7.5: about 50% of maximal activity
5.5 - 7.5
-
pH 5.5: about 35% of maximal activity, pH 7.5: about 95% of maximal activity
5.6 - 7.4
the activity of the wild-tyype enzyme YmPhWT decreases drastically by 14fold from pH 5.6 to pH 7.4
6 - 8
6 - 9
additional information
2 - 5.5
-
pH 2.0: about 70% of maximal activity, pH 5.5: 40-50% of maximal activity enzyme, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2 - 6
-
pH 2.0: about 65% of maximal activity, pH 6.0: about 85% of maximal activity
2 - 6
-
2.0: about 55% of maximal activity, pH 6.0: 85% of maximal activity
2 - 6
pH 2.0: about 45% of maximal activiry, pH 6.0: about 50% of maximal activity, substrate: myo-inositol hexakisphosphate
2 - 6
-
maximal activity at pH 5.0 followed by pH 2.0 (73% of maximal activity), no activity at pH 7.0-8.0
2 - 7.5
activity range, profile overview. sharp drop in activity above pH 6.5
2 - 9
-
the pH profile of the enzyme contains peaks at pH 3.0 and pH 7.0, with the activity at pH 3.0 being approximately 70% of the peak activity at pH 7.0
2 - 9
-
over 70% of maximal activity within this range, profile overview
2.5 - 5
-
pH 2.5: about 45% of maximal activity, pH 5.0: about 20% of maximal activity, reaction with 4-nitrophenyl phosphate, recombinant enzyme
2.5 - 5
-
pH 2.5: about 60% of maximal activity, pH 5.0: optimum, pH 6.0: no activity, reaction with phytate, recombinant enzyme
2.5 - 5.5
-
pH-activity profile, with optima at pH 2.5 with 60% of maximal activity, and at pH 5.0-5.5 with maximal activity, and a local minimum at pH 3.5
3 - 5.5
-
pH 3.0: about 55% of maximal activity, pH 5.5: about 50% of maximal activity, hydrolysis of 4-nitrophenyl phosphate
3 - 5.5
-
optimum pH 5.0, over 80% of maximal activity at pH 3.0-5.5, dramatical loss of activity above pH 5.5
3 - 7
activity range, profile overview. Over 70% of maximal activity at pH 4.5-6.5
3 - 8
-
enzyme is virtually inactive below pH 3.0 and above pH 8.0, phytase LP11, LP12 and LP2
3.5 - 5.5
-
pH 3.5: about 65% of maximal activity, pH 5.5: about 60% of maximal activity, Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate
3.5 - 5.5
-
pH 3.5: about 75% of maximal activity, pH 5.5: about 45% of maximal activity, Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate
3.5 - 6
pH 3.5: about 40% of maximal activity, pH 6.0: about 80% of maximal activity, pH 6.5: about 30% of maximal activity. enzyme expressed in Saccharomyces cerevisiae
3.5 - 6
-
pH 3.5: about 50% of maximal activity, pH 6.0: about 30% of maximal activity
3.5 - 7
-
pH 3.5: about 35% of maximal activity, pH 7.0: about 70% of maximal activity
3.5 - 7
-
pH 3.5: about 35% of maximal activity, pH 7.0: about 70% of maximal activity, reaction with phytate
4 - 6
-
pH 3.0: no activity, pH 4.0: optimum, pH 5.0: about 60% of maximal activity, pH 6.0: about 10% of maximal activity, 4-nitrophenyl phosphate as substrate
4 - 6
-
pH 4.0: about 35% of maximal activity, pH 6.0: about 50% of maximal activity, myo-inositol hexakisphosphate as substrate
4 - 6
-
pH 4.0: about 40% of maximal activity, pH 6.0: about 50% of maximal activity, reaction with phytate
4 - 7
-
pH 4.0: about 50% of maximal activity, pH 7.0: about 45% of maximal activity, Y27T/K68A mutant enzyme, phytate as substrate
4.5 - 7
-
pH 4.5: about 40% of maximal activity, pH 7.0: about 30% of maximal activity
4.5 - 7
-
pH 4.5: about 30% of maximal activity, pH 8.5: about 40% of maximal activity
4.5 - 7
-
pH 4.5: about 70% of maximal activity, pH 7.0: about 45% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
4.5 - 8.5
-
pH 4.5: about 30% of maximal activity, pH 6.0: about 80% of maximal activity, pH 8.5: about 75% of maximal activity
6 - 9
activity range of recombinant isozyme LlALP2. Maximum activity at pH 8.0, 10% of maximal activity at pH 6.0, 60% of maximal activity at pH 9. The pH activity profile is similar to that of wild-type alkaline phytase isolated from lily pollen
additional information
-
enzyme is able to retain almost complete phytase activity in the presence of commercial livestock feed even after 48 h over various pH tested
additional information
-
pH profiles of wild-type and mutant phytases PhyA, overview
additional information
pH profiles of wild-type and mutant phytases PhyA, overview
additional information
mutants D461N, G377T, T255E and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
-
mutants D461N, G377T, T255E and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
the two types of phytases are complementary in phytate degradation over the pH range of pH 2.0-9.0
additional information
the two types of phytases are complementary in phytate degradation over the pH range of pH 2.0-9.0
additional information
pH-dependence of wild-type and mutant enzymes, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
36
37
40
42
45
50
50 - 55
53
55
58
60
65
70
75 - 80
additional information
-
the hydrolysis rate is higher at 60°C as compared to 26°C
55
-
domain Phy-DI fused to beta-propeller phytases PhyP and 168PhyA
55
-
recombinant enzyme. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
over 85% of maximal activity at 15-25°C, maximal activity at 25°C, sharp drop inactivity at above 30°C, over 50% of maximal activity at 0-5°C
10 - 40
-
the enzyme exhibits markedly higher activity at low temperature with retention of 65% and 43% of the optimum activity at reaction temperature 25°C and 10°C, respectively
20 - 50
-
20°C: about 30% of maximal activity, 50°C: about 45% of maximal activity
20 - 75
25 - 55
25 - 60
-
25°C: about 45% of maximal activity, 60°C: about 35% of maximal activity
25 - 70
30 - 45
-
30°C: about 55% of maximal activity, 45°C: about 35% of maximal activity
30 - 65
30 - 70
30 - 80
-
30°C: about 40% of maximal activity, 80°C: about 55% of maximal activity, presence of 10 mM CaCl2
34 - 62
-
34°C: about 55% of maximal activity, 62°C: about 75% of maximal activity
35 - 58
-
35°C: about 50% of maximal activity, 58°C: optimum, 68°C: enzyme is completely inactive, recombinant enzyme
35 - 70
-
30°C: about 45% of maximal activity, 70°C: about 55% of maximal activity
37 - 50
37 - 60
temperature profiles of wild-type and mutant enzymes, overview
37 - 62
-
37°C: about 40% of maximal activity, 62°C: about 45% of maximal activity
37 - 65
37 - 75
-
37°C: about 65% of maximal activity, 75°C: about 45% of maximal activity
38 - 58
-
38°C: about 40% of maximal activity, 58°Coptimal activity, 70°C: no activity, reaction with phytate, recombinant enzyme
40 - 75
-
activity profiles of isozymes RO1 and RO2, almost no activity at 75°C for both RO1 and RO2
40 - 80
45 - 65
45 - 70
45°C: 45% of maximal activity, 70°C: about 55% of maximal activity
45 - 75
-
45°C: about 45% of maximal activity, 75°C: about 50% of maximal activity
additional information
20 - 75
-
20°C: about 30% of maximal activity, 75°C: about 40% of maximal activity
20 - 75
-
20°C: about 30% of maximal activity, 75°C: about 40% of maximal activity, reaction with phytate
25 - 55
more than 40% of the maximal activity at temperatures 25-55°C
25 - 55
-
over 50% of maximal activity within this range, maximal activity at 50°C, inactive at 60°C
30 - 65
30°C: about 55% of maximal activity, 65°C: about 40% of maximal activity, substrate: myo-inositol hexakisphosphate
30 - 65
-
over 50% of maximal activity within this range, profile overview
30 - 70
activity range of recombinant isozyme LlALP2, sharp decrease in activity at temperatures above 55°C, consistent with the observations with the native LlALP
30 - 70
-
activity range, recombinant enzyme, maximal activity at 50°C, 64% at 40°C
37 - 65
-
37°C: about 40% of maximal activity, 65°C: about 40% of maximal activity
37 - 65
-
37°C: about 35% of maximal activity, 65°C: 60-80% of maximal activity, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
45 - 65
-
45°C: about 40% of maximal activity, 60°C: about 60% of maximal activity
45 - 65
-
45°C: about 65% of maximal activity, 65°C: about 30% of maximal activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
additional information
the highest activities of wild-type and D24G expressed in Pichia pastoris are achieved at 50°C and 55°C, decreased by 10°C and 5°C compared to those expressed in Escherichia coli, respectively. Temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis, overview
additional information
-
the highest activities of wild-type and D24G expressed in Pichia pastoris are achieved at 50°C and 55°C, decreased by 10°C and 5°C compared to those expressed in Escherichia coli, respectively. Temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis, overview
additional information
activation of phytase up to 60°C followed by inactivation at higher temperatures, kinetics overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from soil samples collected in Northeast Parana State in Brazil
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
Aspergillus oryzae SBS50
isolated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Aspergillus syndowi
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from geother-mal soil located in Southern Tunisia
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Bacillus sp. (in: Bacteria) KHU-10
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from the Derwent Valley, Derbyshire, UK, and from other sites subject to different rates of wet inorganic N (NO3- + NH4+) deposition, overview
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
L. Merr.. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
symbiotic bacterial strain isolated from the gut contents of Batocera horsfieldi larvae, gene phyA115
UniProt
brenda
symbiotic bacterial strain isolated from the gut contents of Batocera horsfieldi larvae, gene phyA115
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Nostoc sp. is the Lobaria pulmonaria (5183) cyanobiont; collected from Lairg, Sutherland, UK
UniProt
brenda
var. amiga. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from soil collected from four different ecological and geographical habitats of the Republic of Tatarstan, Russia, forest near the village Agerze, Aznakaevo District
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strains KTU05-8 and KTU05-9, isolated from spontaneous Lithuanian rye sourdoughs
-
-
brenda
Nostoc sp. is the Peltigera membranacea cyanobiont N6; collected from Beddgelert, Gwynedd, UK
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Penicillium caseoicolum
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Bacteroides ruminicola, isolated from Mehsani buffalo rumen
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Schwanniomyces castellii
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Thermothelomyces thermophilus BCRC 31852
Thermothelomyces thermophilus BJTLR50
solated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
Thermothelomyces thermophilus DSM 1799
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Torulopsis candida
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced. The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
var. awamorii ATCC 38854. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
94776, 114248, 114249, 114254, 114264, 114270, 114271, 114272, 114274, 114275, 649616, 678975, 707770
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
ATCC 130703. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
-
114252, 114253, 114257, 114258, 114273, 114279, 134797, 654003, 665282, 665283, 666691, 666692, 677690, 677774, 679568, 680395
-
-
brenda
ATCC 9142. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from soil samples collected in Northeast Parana State in Brazil
-
-
brenda
NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strain 92 and strain NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissPRot
brenda
strain NRRL3135. The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme exhibits phytase and acid phosphatase activity. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced.The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
van Teighem. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strain NRRL3135. The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from geother-mal soil located in Southern Tunisia
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isozymes FTE, FTEII, and FBA
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
strainMO-3. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from foreshore soil on the coast of Busan, Korea
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
ATCC 22959. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
i.e. Rhizopus microsporus var. oligosporus, isozymes RO1 and RO2
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
acidic histidine acid phosphatase PhyH49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
alkaline beta-propeller phytase PhyB49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
acidic histidine acid phosphatase PhyH49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
alkaline beta-propeller phytase PhyB49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
i.e. Myceliophthora thermophila or Sporotrichum thermophile strain BJTLR50
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brenda
i.e. Sporotrichum thermophile or Myceliophthora thermophila
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SWissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SWissProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
solated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
i.e. Myceliophthora thermophila
UniProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
Thermothelomyces thermophilus BCRC 31852
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
Thermothelomyces thermophilus DSM 1799
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
metagenome-derived phytase, metagenome derived from subsurface groundwater
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-
brenda
i.e. Wickerhamomyces anomalus or Hansenula anomala
UniProt
brenda
isolated from dried flower buds of Woodfordia fruticosa
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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thermotolerant phytase is produced by Rhizopus microsporus var. microsporus biofilm on an inert support using sugarcane bagasse as carbon source. The enzyme production is strictly regulated by the phosphorus content with optimal production at 0.5 mM of sodium phytate and KH2PO4
brenda
recombinant enzyme in culture medium of Bacillus subtilis
brenda
barley plants constitutively express HvPAPhy_a, high preformed phytase levels in the mature dry vegetative material of the 35S:PAPhy_a-plant. Expression analysis in different plant tissues, overview. Positive correlation between phytase activity and plants being heterozygous or homozygous for the HvPAPhy_a cisgene (the genomic clone of HvPAPhy_a including the native promoter and terminator of the gene)
brenda
additional information
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phytase increases markedly at the late stationary phase
brenda
Bacillus sp. (in: Bacteria) KHU-10
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phytase increases markedly at the late stationary phase
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brenda
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fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml
brenda
Rhodotorula mucilaginosa JMUY14
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fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml
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brenda
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phytase synthesized early in germination persists for several days in the cotyledon
brenda
solid-state fermentation, optimization of enzyme phytase production by Sporotrichum thermophile, method, detailed overview. Maximum phytase production (1881.26 U/g dry mouldy residue) in 2.5% Tween 80, 1.0% yeast extract, and 48 h of incubation period. Phytase production in the mixed substrate (sugarcane bagasse and wheat bran) fermentation enhances 11.6fold over the initial production as a consequence of optimization. Phytase titres are sustainable in flasks, trays and column bioreactor (1796 to 2095 U/g dry mouldy residue), thus validating the model and the process for large-scale phytase production. When the yeast extract is replaced with corn steep liquor (2% w/v), a sustained enzyme titre (1890 U/g dry mouldy residue) is attained, making the process cost-effective. Among all the detergents, Tween 80 supports a higher phytase production than others. The enzyme efficiently liberates nutritional components from poultry feed (inorganic phosphate, soluble protein and reducing sugars) in a time-dependent manner
brenda
Thermothelomyces thermophilus BJTLR50
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solid-state fermentation, optimization of enzyme phytase production by Sporotrichum thermophile, method, detailed overview. Maximum phytase production (1881.26 U/g dry mouldy residue) in 2.5% Tween 80, 1.0% yeast extract, and 48 h of incubation period. Phytase production in the mixed substrate (sugarcane bagasse and wheat bran) fermentation enhances 11.6fold over the initial production as a consequence of optimization. Phytase titres are sustainable in flasks, trays and column bioreactor (1796 to 2095 U/g dry mouldy residue), thus validating the model and the process for large-scale phytase production. When the yeast extract is replaced with corn steep liquor (2% w/v), a sustained enzyme titre (1890 U/g dry mouldy residue) is attained, making the process cost-effective. Among all the detergents, Tween 80 supports a higher phytase production than others. The enzyme efficiently liberates nutritional components from poultry feed (inorganic phosphate, soluble protein and reducing sugars) in a time-dependent manner
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brenda
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strong expression in the early stages of seedling growth and pollen germination
brenda
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both phytase and acid phosphatase enzyme activities in the root increase substantially in response to phosphorus-sufficient condition. The lowest enzyme activity is observed in the absence of any phosphorus source in the media. The level of acid phosphatase and phytase activities is more or less the same under various growth conditions
brenda
quantitative reverse transcription PCR enzyme expression analysis in developing grains
brenda
grain, the enzyme is expressed during barley seed development
brenda
quantitative reverse transcription PCR enzyme expression analysis in developing grains
brenda
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quantitative reverse transcription PCR enzyme expression analysis in developing grains
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brenda
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strong expression in the early stages of seedling growth and pollen germination
brenda
additional information
enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus source. Phytase production by strain a13 is induced by the presence of phytic acid and repressed by the addition of glucose
brenda
additional information
Burkholderia sp. a13(2014) JCM 30421
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enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus source. Phytase production by strain a13 is induced by the presence of phytic acid and repressed by the addition of glucose
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brenda
additional information
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optimization of process parameters for phytase production by Enterobacter sp. ACSS leads to a 4.6fold improvement in submerged fermentation, which is enhanced further in fed-batch fermentation
brenda
additional information
ability of the Pantoea sp. 3.5.1 isolate to grow with insoluble Ca-phytate as the sole source of phosphorus, not due to the secretion of an extracellular phytase. Growth dynamics and extracellular and intracellular phytate-hydrolyzing activities of Pantoea sp. 3.5.1 culture, overview
brenda
additional information
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growth on rice flour suspension or on potato dextrose agar
brenda
additional information
the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations
brenda
additional information
identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
brenda
additional information
identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
brenda
additional information
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identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
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brenda
additional information
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among 10 yeast strains analyzed, Arxula adeninivorans and Pichia anomala display highest volumetric phytase activities
brenda
additional information
optimization of fermentation for production of cell-bound phytase, overview
brenda
additional information
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optimization of fermentation for production of cell-bound phytase, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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recombinant protein, localization to cell suface of Pichia pastoris with a glycosylphosphatidylinositiol anchoring system
brenda
additional information
about 78% of the enzyme is cell wall bound
brenda
recombinant protein, expressed in Pichia pastoris
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brenda
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recombinant protein, expressed in Pichia pastoris
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brenda
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brenda
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the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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brenda
recombinant protein, expressed in Pichia pastoris
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brenda
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recombinant protein, expressed in Pichia pastoris
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brenda
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among 10 yeast strains analyzed, Arxula adeninivorans and Pichia anomala display highest volumetric phytase activities and Arxula adeninivorans shows the highest intra- and extracellular specific activities
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brenda
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the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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brenda
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the phytase might be a secreted enzyme located in the extracellular or periplasmic space of the host, residues 1-25 from the N-terminus are predicted to be a putative signal peptide of this phytase
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brenda
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among 10 yeast strains analyzed, Arxula adeninivorans and Pichia anomala display highest volumetric phytase activities and Arxula adeninivorans shows the highest intra- and extracellular specific activities
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recombinant enzyme expressed in Escherichia coli
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recombinant enzyme expressed in Escherichia coli
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brenda
integral membrane protein
brenda
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integral membrane protein
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brenda
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integral membrane protein
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brenda
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integral membrane protein
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brenda
additional information
the enzyme contains a signal peptide
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brenda
additional information
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the enzyme sequence contains a signal peptide and a signal peptide cleavage site
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brenda
additional information
Penicillium chrysogenum CCT 1273
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the enzyme sequence contains a signal peptide and a signal peptide cleavage site
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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release of phosphate by stepwise hydrolysis of phosphomonoester bonds in phytate. Phytate is the major storage form of phosphate and inositol, predominantly occurring in cereal grains, legumes, and oilseeds
physiological function
additional information
evolution
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dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together
evolution
the two phytases, an acidic histidine acid phosphatase, PhyH49, and an alkaline beta-propeller phytase, PhyB49, share low identities with known phytases, 61% at most
evolution
enzyme rStPhy belongs to the histidine acid phosphatase (HAP) phytases family
evolution
molecular modeling of PHY US42 indicates that this phytase belongs to the group of beta-propeller phytases that are usually calcium-dependent
evolution
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on the basis of the site at which phytate dephosphorization begins, phytases can be grouped into three classes: 3-phytases (EC 3.1.3.8), 6-phytases (EC 3.1.3.26), and 5-phytases (EC 3.1.3.72). The fungal phytases are included in the 3-phytases class, in which the dephosphorization starts at the third phosphate group. Because of their catalytic mechanism, the fungal phytases belong to the histidine acid phosphatase class
evolution
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the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
evolution
the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity. The amino acid sequence of the Pantoea sp. 3.5.1 AgpP phytase harbors an N-terminal RHNLRAP motif (where the italicized residues are variable) and a C-terminal HD motif, which are the structural hallmarks of the highly conserved catalytic core of histidine acid phosphatases (HAPs) [consensus sequence RH(G/N)XRXP/HD, where the slash separates the N- and C-terminal sequences]
evolution
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the enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
-
the enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
KM873028
the enzyme belongs to the histidine acid phosphatase (HAP) family phytases present in insect-cultivated fungus gardens
evolution
the enzyme belongs to the histidine acid phosphatase (HAP) family, it possesses typical conserved motifs of HAP phytases: RHGERFP in AA125-131 and HD in AA394-395
evolution
the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP
evolution
the enzyme sequence contains histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family
evolution
the phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids
evolution
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the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP
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evolution
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dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together
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evolution
Burkholderia sp. a13(2014) JCM 30421
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the enzyme sequence contains histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family
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evolution
Penicillium chrysogenum CCT 1273
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the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
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evolution
Loigolactobacillus coryniformis MH121153
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the enzyme belongs to the histidine acid phosphatase (HAP) family
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evolution
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the two phytases, an acidic histidine acid phosphatase, PhyH49, and an alkaline beta-propeller phytase, PhyB49, share low identities with known phytases, 61% at most
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evolution
Morchella importuna SCYDJ1A1
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the enzyme belongs to the histidine acid phosphatase (HAP) family, it possesses typical conserved motifs of HAP phytases: RHGERFP in AA125-131 and HD in AA394-395
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evolution
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molecular modeling of PHY US42 indicates that this phytase belongs to the group of beta-propeller phytases that are usually calcium-dependent
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malfunction
activity and catalytic efficiency at low temperature are reduced in a recombinant protein from which the N-terminal domain is removed
malfunction
Pseudomonas sp. FB15
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activity and catalytic efficiency at low temperature are reduced in a recombinant protein from which the N-terminal domain is removed
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physiological function
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gene disruption mutants show a lower phytase and phophatase activity in seedlings and germinating pollen and lower pollen germination rate
physiological function
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cysteine phytase is the major phytate-degrading enzyme in the anaerobic ruminal environment
physiological function
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cysteine phytase is the major phytate-degrading enzyme in the anaerobic ruminal environment
physiological function
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importance of enzyme domain PhyH-DI in phytate degradation
physiological function
phytase activity in grain is essential to make phosphate available to cell metabolism, and in food and feed
physiological function
-
phytate is an antinutritional factor that influences the bioavailability of essential minerals by forming complexes with them and converting them into insoluble salts. beta-Propeller phytase hydrolyzes insoluble Ca2+-phytate salts and completely abrogates the ability of phytate to chelate metal ions, stoichiometry, affinity, and thermodynamics of these interactions by isothermal titration calorimetry, overview. Ins(2,4,6)P3 is unable to bind Ca2+ or any other cation tested, including Co2+, Cu2+, Fe3+, Mg2+, Mn2+, Sr2+, and Zn2+
physiological function
transgenic expression in Brassica napus with a signal peptide sequence. Transgenic lines exhibit significantly higher exuded phytase activity when compared to wild-type controls. Transgenic Brassica napus has significantly improved phosphate uptake and plant biomass. Seed yields of transgenic increase by 20.9% when compared to wild-type. When phytate is used as the sole phosphate source, phosphate accumulation in seeds increases by 20.6. Phytase activities in transgenic canola seeds range from 1,138 to 1,605 U/kg seeds, while no phytase activity is detected in wild-type seeds. Phytic acid content in seeds is significantly lower than in wild-type
physiological function
AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria
physiological function
-
phytase degrades phytates to release phosphate and other essential ions. It is widespread in nature, found in plants, animals and microorganisms. The use of phytase reduces phosphate excretion in monogastric animals and avoids supplementation of feeds with inorganic phosphate. Animal stomach is the main functional site for phytase-mediated dephosphorylation in the gastrointestinal tract
physiological function
phytase hydrolyzes phytate (myo-inositol 1,2,3,4,5,6-hexakisphosphate, IP6) and its salts present in cereals and legumes to release inorganic phosphate. It contributes to the removal of phytate, an anti-nutritional factor in feed, and thereby increases the bioavailability of phosphate, minerals, protein, and starch
physiological function
phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops
physiological function
-
phytases (myo-inositol hexakisphosphate phosphohydrolases) are enzymes that compose a special class of phosphatases. Phytases catalyze the hydrolysis of the phosphomonoester bonds of phytate (salts of myo-inositol 1,2,3,4,5,6-hexakis dihydrogen phosphate), releasing lower forms of myo-inositol and inorganic phosphates. Regulation of enzymatic synthesis by phosphate is coordinated by the PHO pathwa
physiological function
phytases are a special class of phosphatases that sequentially hydrolyse phytic acid to less-phosphorylated myo-inositol which release inorganic phosphates. This class of enzyme is widely distributed in nature and has been isolated from several sources, including plants, animals, and microorganisms
physiological function
phytate present in cereals lowers bioavailability of minerals. The reduction of phytic acid content can lead to improvement in mineral availability, and thus mitigate antinutrient effects of phytic acid
physiological function
-
the enzyme promotes plant growth showing a significant effect, with an increase of 10% of root and 25% of shoot length, resulting in a 2.2fold increase in biomass
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
-
phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops
-
physiological function
-
phytase hydrolyzes phytate (myo-inositol 1,2,3,4,5,6-hexakisphosphate, IP6) and its salts present in cereals and legumes to release inorganic phosphate. It contributes to the removal of phytate, an anti-nutritional factor in feed, and thereby increases the bioavailability of phosphate, minerals, protein, and starch
-
physiological function
-
importance of enzyme domain PhyH-DI in phytate degradation
-
physiological function
Burkholderia sp. a13(2014) JCM 30421
-
phytases are a special class of phosphatases that sequentially hydrolyse phytic acid to less-phosphorylated myo-inositol which release inorganic phosphates. This class of enzyme is widely distributed in nature and has been isolated from several sources, including plants, animals, and microorganisms
-
physiological function
-
the enzyme promotes plant growth showing a significant effect, with an increase of 10% of root and 25% of shoot length, resulting in a 2.2fold increase in biomass
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additional information
catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
additional information
-
catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
additional information
-
conformational dynamics of the active site loop, structure analysis, overview. Molecular dynamic studies indicate that the movement in the active site is mainly confined by the active site loop resulted in wider opening of the loop in absence of phytate, possible role of loop residues as prerequisite for highly active phytases
additional information
phytase ASR1 is a member of the histidine-acid-phosphatase family, that shares two conserved active-site motifs, RHGXRXP and HD, and hydrolyzes metal-free phytate with pH optima in the acidic range. Histidine-acid-phosphatases share a common two-step mechanism for catalysis. The reaction starts with a nucleophilic attack on the phosphoester bond by a conserved histidine in the long active-site motif. The histidine side chain from the conserved HD motif protonates the leaving group. The second step comprises hydrolysis of the resulting covalent phospho-histidine intermediate. Comparison of substrate binding of Klebsiella sp. ASR1 PhyK with Escherichia coli AppA phytase
additional information
replacements of G56E, L65F, Q144H, and L151S improve the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
-
replacements of G56E, L65F, Q144H, and L151S improve the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
-
the enzyme adsorbs to and interacts with pure minerals and oxisol clays also releasing orthophosphate from InsP6-saturated minerals, overview
additional information
-
the enzyme can also act as a vanadate haloperoxidase, EC 1.11.1.10
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP- , near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP- , near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
-
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
-
the enzyme shows strong resistance toward pepsin and trypsin
additional information
-
the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency. The intact domain is responsible for phytate hydrolysis. Enzyme domain PhyH-DI also hydrolyzes the phytate intermediate D-Ins(1,4,5,6)P4, and acts synergistically, causing a 1.2-2.5fold increase in phosphate release, with domain PhyH-DII, other beta-propeller phytases, PhyP and 168PhyA, and a histidine acid phosphatase. Fusion of PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies
additional information
amino acid sequence analysis and homology structure modeling
additional information
Bacillus phytases exhibit their desirable activity profile at neutral pH. They have higher thermal stability, and strict substrate specificity for the calcium-phytate complex than that of acidic phytase. Molecular model of phytase constructed by homology modeling method using the structure with PDB ID 2POO as template, overview
additional information
catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are catalytic sites R44, R48, D115, R119, H333, and D334, overview
additional information
-
catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are catalytic sites R44, R48, D115, R119, H333, and D334, overview
additional information
homology modeling and computational analysis of Penicillium oxalicum strain KCTC6440 PhyA, comparison to the structure of phytase PhyA from Penicillium oxalicum strain PJ3
additional information
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
additional information
molecular docking of wild-type and mutant enzymes, homology modelling using the enzyme structure of the phytase from Bacillus amyloliquefaciens (PDB ID 2POO) as the template, overview. Residues D24, S51 and K70 have a relatively large influence on the catalytic activity probably because they are adjacent to the active site cleft. The enzyme is composed of six beta-sheets and possesses six calcium binding sites. The 25 amino acid residues except V60, involved in calcium binding, are highly conserved
additional information
requirement of a thiol group for the activity
additional information
KM873028
structural model of rPhyXT52 is deduced by homology modeling using the Yersinia kristensenii phytase (PDB ID 4ARV) structure as template, overview
additional information
-
structure of the active site pocket of phytase protein, homology modeling of HAP-phytase, overview
additional information
the catalytically important amino acids Arg74, His75, Arg78, His368, and Asp369 are identified by docking and site-directed mutagenesis, molecular surface analysis, and three-dimensional modeling
additional information
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
additional information
-
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
additional information
the enzyme has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis
additional information
the enzyme structure possesses a phosphate-binding pocket with residues R54, H55, R58, I61, R146, W272, H315, E316, and V317 involved in phosphate ligand binding
additional information
the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
additional information
-
the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
additional information
-
the phytase seems to possess improved adaptability to the low pH condition caused by the gastric acid in livestock and poultry stomachs
additional information
three-dimensional model of recombinant PPHY by homology modeling using the crystal structure of phytase chain A from Debaryomyces castellii (PDB ID 2gfiA) as template, inhibitor docking of sodium phytate, vanadate, and tartrate
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
-
additional information
-
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
-
additional information
-
molecular docking of wild-type and mutant enzymes, homology modelling using the enzyme structure of the phytase from Bacillus amyloliquefaciens (PDB ID 2POO) as the template, overview. Residues D24, S51 and K70 have a relatively large influence on the catalytic activity probably because they are adjacent to the active site cleft. The enzyme is composed of six beta-sheets and possesses six calcium binding sites. The 25 amino acid residues except V60, involved in calcium binding, are highly conserved
-
additional information
-
the enzyme shows strong resistance toward pepsin and trypsin
-
additional information
-
Bacillus phytases exhibit their desirable activity profile at neutral pH. They have higher thermal stability, and strict substrate specificity for the calcium-phytate complex than that of acidic phytase. Molecular model of phytase constructed by homology modeling method using the structure with PDB ID 2POO as template, overview
-
additional information
-
the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency. The intact domain is responsible for phytate hydrolysis. Enzyme domain PhyH-DI also hydrolyzes the phytate intermediate D-Ins(1,4,5,6)P4, and acts synergistically, causing a 1.2-2.5fold increase in phosphate release, with domain PhyH-DII, other beta-propeller phytases, PhyP and 168PhyA, and a histidine acid phosphatase. Fusion of PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies
-
additional information
-
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
-
additional information
-
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
-
additional information
-
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
-
additional information
Pseudomonas sp. FB15
-
the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
-
additional information
Penicillium oxalicum KCTC6440
-
homology modeling and computational analysis of Penicillium oxalicum strain KCTC6440 PhyA, comparison to the structure of phytase PhyA from Penicillium oxalicum strain PJ3
-
additional information
Aspergillus niger NII 08121
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
-
additional information
-
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
-
additional information
Bacillus subtilis DR8886
-
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
-
additional information
-
amino acid sequence analysis and homology structure modeling
-
Show AA Sequence and Transmembrane Helices (4030 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
214000
36500
37000
-
6 * 37000, gel filtration of the enzyme in a 6 M guanidine hydrochloride solution
39200
-
x * 54600, native enzyme, x * 39200, recombinant enzyme expressed in Lactobacillus casei, SDS-PAGE
40000
42000
43000
44000
45000
45900
46000
47000
48159
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
48423
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
490000
50524
1 * 50524, calculation from nucleotide sequence
51000
52980
53000
53800
2 * 53800, about, isozyme LlALP1, sequence calculation
54600
-
x * 54600, native enzyme, x * 39200, recombinant enzyme expressed in Lactobacillus casei, SDS-PAGE
56000
56200
2 * 56200, about, isozyme LlALP2, sequence calculation
60000
60000 - 81000
64000
65000
65500
66000
70000
700000
74460
76000
77000
80000
84000
85000 - 100000
92000
47000
-
x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
60000
-
x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
66000
-
x * 66000, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
6 * 37000, gel filtration of the enzyme in a 6 M guanidine hydrochloride solution
homodimer
monomer
additional information
?
-
x * 54600, native enzyme, x * 39200, recombinant enzyme expressed in Lactobacillus casei, SDS-PAGE
?
-
x * 66000, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified, SDS-PAGE
?
-
x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
?
x * 41000, about, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 41000, about, recombinant His6-tagged enzyme, SDS-PAGE
-
?
x * 45000, Pichia pastoris-expressed Phy168 after deglycosylation, SDS-PAGE
?
x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE
?
-
x * 45000, Pichia pastoris-expressed Phy168 after deglycosylation, SDS-PAGE
-
?
Bacillus subtilis DR8886
-
x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE
-
?
x * 63000, recombinant His-tagged enzyme, SDS-PAGE, x * 47750, sequence calculation
?
x * 59000-65000, recombinant glycosylated enzyme from Pichia pastoris, SDS-PAGE, x * 45000, recombinant deglycosylated enzyme from Pichia pastoris, SDS-PAGE
?
x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
?
x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
?
-
x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
-
?
Thermothelomyces thermophilus BCRC 31852
-
x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
-
?
Thermothelomyces thermophilus DSM 1799
-
x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
-
homodimer
2 * 53800, about, isozyme LlALP1, sequence calculation
homodimer
2 * 56200, about, isozyme LlALP2, sequence calculation
monomer
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
monomer
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
monomer
-
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
-
monomer
-
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
-
monomer
-
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
-
monomer
-
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
-
monomer
-
1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
monomer
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
monomer
-
1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
-
monomer
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
-
monomer
-
1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
-
monomer
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
-
monomer
1 * 43000, SDS-PAGE, 1 * 46000, about, sequence calculation
monomer
Burkholderia sp. a13(2014) JCM 30421
-
1 * 43000, SDS-PAGE, 1 * 46000, about, sequence calculation
-
monomer
1 * 61090, sequence calculation, 1 * 61089, mass spectrometry, 1 * 60000, SDS-PAGE
monomer
Morchella importuna SCYDJ1A1
-
1 * 61090, sequence calculation, 1 * 61089, mass spectrometry, 1 * 60000, SDS-PAGE
-
monomer
1 * 50524, calculation from nucleotide sequence
monomer
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
monomer
-
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
-
additional information
-
peptide mass fingerprinting, MALDI-TOF mass spectrometry
additional information
-
peptide mass fingerprinting, MALDI-TOF mass spectrometry
-
additional information
-
a broad protein band of 85000-100000 Da is observed after SDS-PAGE
additional information
-
SDS-PAGE gives two broad bands in the regions 73000 Da and 100000 Da
additional information
-
a broad proptein band of 85000-100000 Da is observed after SDS-PAGE
additional information
-
structural model of the wild type and mutant enzymes, overview
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
structural model of the wild type and mutant enzymes, overview
-
additional information
Aspergillus niger NII 08121
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
-
additional information
molecular model of phytase constructed by homology modeling method, overview
additional information
-
molecular model of phytase constructed by homology modeling method, overview
-
additional information
-
the dual-domain beta-propeller phytase PhyH from Bacillus sp. HJB17 contains an incomplete N-terminal beta-propeller phytase domain, PhyH-DI, residues 41-318, and a typical beta-propeller phytase domain, PhyH-DII, residues 319-644, at the C-terminus. Modelling of the three-dimensional structures of domains PhyH-DI and PhyH-DII, PhyH-DI is predicted to have a five-blade propeller structure and PhyH-DII a six-blade beta-propeller containing five four-stranded sheets and one five-stranded sheet
additional information
-
the dual-domain beta-propeller phytase PhyH from Bacillus sp. HJB17 contains an incomplete N-terminal beta-propeller phytase domain, PhyH-DI, residues 41-318, and a typical beta-propeller phytase domain, PhyH-DII, residues 319-644, at the C-terminus. Modelling of the three-dimensional structures of domains PhyH-DI and PhyH-DII, PhyH-DI is predicted to have a five-blade propeller structure and PhyH-DII a six-blade beta-propeller containing five four-stranded sheets and one five-stranded sheet
-
additional information
the enzyme contains an N-terminal incomplete domain, residues 29-297, i.e. domain N, and a typical beta-propeller phytase domain at the C terminus
additional information
-
the enzyme contains an N-terminal incomplete domain, residues 29-297, i.e. domain N, and a typical beta-propeller phytase domain at the C terminus
-
additional information
the ASR1 phytase polypeptide chain is organized into an alpha and an alpha,beta domain, and the active site is located in a positively charged cleft between the domains
additional information
AppAS contains three potential sites of N-glycosylation, a putative signal peptide of 22 amino acids at N-terminal end and 8 cysteine residues among which 99-130, 200-210, 404-413 are the most possible disulfide bond pairs. The calculated molecular mass of the protein with and without the signal sequence are about 47 and 45 kDa, respectively
additional information
the recombinant enzyme StPhy is composed of 26.65% alpha-helices, 5.26% beta-sheets and 68.09% random coils at pH 5.0 and 60°C. The three-dimensional structure of rStPhy displays characteristic signature sequences, RHGXRXP and HD, of HAP phytases, three-dimensional modeling, overview. Tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy
additional information
amino acid sequence analysis and molecular modeling, overview
additional information
-
amino acid sequence analysis and molecular modeling, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no modification
proteolytic modification
side-chain modification
additional information
phytase enzymes in general possess a native resistance towards proteolytic degradation
glycoprotein
-
the recombinant enzyme expressed in potato leaves is 15% less glycosylated than the native enzyme
glycoprotein
-
six predicted N-glycosylation sites are observed to be glycosylated from the experimental electron density
glycoprotein
recombinant enzyme expressed in yeast is highly glycosylated
glycoprotein
two potential N-glycosylated sites within the Asn-Xaa-Ser/Thr sequence are found in the phy168 phytase. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115
glycoprotein
-
two potential N-glycosylated sites within the Asn-Xaa-Ser/Thr sequence are found in the phy168 phytase. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115
-
glycoprotein
-
after treatment with EndoH, protein gives one band of 50 kDa in SDS-PAGE
glycoprotein
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 8 N-glycosylation sites
glycoprotein
sequence contains six conserved putative N-glycosylation sites
glycoprotein
-
the enzyme sequence harbors putative N-linked glycosylation sites
glycoprotein
Penicillium chrysogenum CCT 1273
-
the enzyme sequence harbors putative N-linked glycosylation sites
-
glycoprotein
glycosylation of six potential N-glycosylation sites
glycoprotein
-
analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide
glycoprotein
enzyme AppAS contains three potential sites of N-glycosylation, recombinant nontagged enzyme from Pichia pastoris strain GS115(his4) is glycosylated, deglycosylation of rAppAP is carried out using Endo H deglycosylase
glycoprotein
in silico analysis reveals 4 potential N-glycosylation sites, Asp165,Asp200, Asp275 and Asp346, and 3 potential O-glycosylation sites, Thr185, Thr274, and Thr321, in the enzyme
glycoprotein
the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C
glycoprotein
seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consisted of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview
glycoprotein
seven N-linked glycosylation sites, three of these sites are dominated by variant forms of the XylMan3FucGlcNAc2, i.e. the HRP-type of glycan. Complex-type glycans with one or two additional GlcNAc occur, but in trace amounts only. At four sites, the glycan consists of a single GlcNAc residue, mass spectrometric isozyme glycan analysis, overview
glycoprotein
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 9 N-glycosylation sites
glycoprotein
-
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 9 N-glycosylation sites
-
glycoprotein
-
sequence contains a putative N-glycosylation site at residue R198, molecular mass decreases after treatment with Endo H
glycoprotein
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 7 N-glycosylation sites
proteolytic modification
the mature peptide sequence lacked RHGXRXP, a conserved motif at the catalytic site of acidic phytases. The enzyme contains a signal peptide
proteolytic modification
Bacillus subtilis DR8886
-
the mature peptide sequence lacked RHGXRXP, a conserved motif at the catalytic site of acidic phytases. The enzyme contains a signal peptide
-
proteolytic modification
sequence contains a putative signal peptide of 15 amino acids
proteolytic modification
-
sequence contains a putative signal peptide of 15 amino acids
-
proteolytic modification
-
sequence contains a putative signal sequence of 27 amino acids
proteolytic modification
-
sequence contains a signal peptide of 24 amino acids
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
side-chain modification
-
glycosylation is moderate in Aspergillus niger, it is excessive and highly variable in Hansenula polymorpha and Saccharomyces cerevisiae
side-chain modification
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
side-chain modification
-
glycoprotein contains mannose, galactose and N-acetylglucosamine, ten potential N-glycosylation sites
side-chain modification
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
side-chain modification
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
side-chain modification
-
enzyme from strain NRRL 3135 and recombinant enzyme from Aspergillus niger van Tieghem are 35.29% glycosylated, only N-linked oligosaccharides, released mannose residues are (alpha1-2,3,6) linked, the trisaccharide core structure is nonfucosylated, the structure of N-linked oligosaccharides ranges from (Man)5(GlcNAc)2 to (Man)10(GlcNAc)2
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
-
side-chain modification
-
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
-
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
-
side-chain modification
-
glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase
-
side-chain modification
-
enzyme from strain NRRL 3135 and recombinant enzyme from Aspergillus niger van Tieghem are 35.29% glycosylated, only N-linked oligosaccharides, released mannose residues are (alpha1-2,3,6) linked, the trisaccharide core structure is nonfucosylated, the structure of N-linked oligosaccharides ranges from (Man)5(GlcNAc)2 to (Man)10(GlcNAc)2
-
side-chain modification
-
glycoprotein contains mannose, galactose and a small amount of inositol
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
-
side-chain modification
-
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
-
side-chain modification
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
side-chain modification
extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at resolution higher than 1.7 A, native enzyme and enzyme in complex with P=4 at pH 5.5 and at pH 7.5. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site
-
deglycosylated PhyA free or in complex with inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, vapour-diffusion hanging drop technique, reservoirs contain 1 ml of PEG 3350 at 15-30% w/v, and ammonium nitrate a t0.1-0.4 M, siliconized coverslips are used to suspend a drop containing 0.002 ml of phytase at 13 mg/ml protein concetration and 0.002 ml of reservoir solution over the reservoir, X-ray diffraction structure determination and analysis at 2.2-2.4 A resolution
-
molecular dynamics simulation and comparison between wild-type and thermostable mutant A35E/P42S/Q168R/T248R show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly
the crystal structure of the enzyme in complex with phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site
-
to 2.3 A resolution. The structure can be divided into two parts: a large alpha/beta-domain with a six-stranded beta-sheet and a small alpha-domain. The four active sites of the tetramer are solvent-exposed and are accessible to substrate
analysis of crystal structure of the phytate complex of Escherichia coli phytase at pH 6.6 with phytate bound via its 3-phosphate to the active site with Hg2+ as intermolecular bridge, X-ray diffraction structure at 2.28 A resolution, analysis of active site loops, overview
-
apo-enzyme, to 1.9 A resolution, and in complex with substrate analogue myo-inositiol hexakissulfate, to 1.59 A resolution. The substrate analogue is coordinated by residues Arg18, His19, Arg22, Thr25, Lys26, His128, Thr219, His306, Asp307 and a number of water molecules. The Nepsilon2 atom of the catalytic nucleophile, His19, lies 3.2 A from S6 of the analogue and is in-line with the S-O bond from the inositol ring. The OD1 atom of Asp307, the proton donor, forms an H-bond with the oxygen at position 6 of the inositol ring
native PhyK and inactive mutant H25A phytase PhyK, the latter with bound sulfate ions, hanging-drop vapor diffusion at 18°C, 5-6 weeks, for the wild-type enzyme: mixing of 6 mg/ml protein in 20 mM sodium acetate (pH 5.0), 50 mm NaCl with an equal volume of 4.0 M sodium formate, for mutant H25A: mixing of 0.0015 ml of protein in 25 mM sodium acetate pH 5.0, 60 mM NaCl and 1 mM tris-(2-carboxyethyl)phosphine with 0.0015 ml of 12% PEG 8000, 0.08 M (NH4)2SO4, 0.1 M sodium acetate and 1.5 mM phytate, 1 week, 22°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, single-wavelength anomalous-diffraction phasing
recombinant phytase contains the active site RHGXRXP and HD sequence motifs, a large alpha/beta-domain and a small alpha-domain
-
phytase in complex with persulfated phytate, determination of three different structures from three crystal forms: phytase alone, phytase bound with myo-inositol hexasulfate at a location slightly away from the active site and phytase bound with myo-inositol hexosulfate at the active site. The crystal structures reveal a phytase fold of the dual-specificity phosphatase type. The active site is locatewd near a conserved Cys241-containing P loop. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G277K
-
mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3
K68A
-
mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity
Q27A
-
1.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. The pH-activity profile resembles that of wild-type enzyme with slight increases below pH 4.0 and around pH 6.5
Q27G
-
2.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme.Increase in specific activity is almost constant over entire pH-range, pH 4-8
Q27I
-
3.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27
Q27L
Q27N
-
1.7fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity is almost constant over entire pH-range, pH 4-8
Q27P
-
1.7fold decrease in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Mutant enzyme has a pronounced tendency to aggregate and precipitate
Q27S
-
1.9fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
Q27T
-
2.8fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity over the entire pH-range, pH 4-8
Q27V
-
1.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
R151L/S152N
-
mutant protein with reduced susceptibility to proteolysis
S140Y/D141G
-
mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity
S152N
Y282H
-
mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3
K186G/R187Q
mutant protein with reduced susceptibility to proteolysis
A35E/P42S/Q168R/T248R
thermostable mutant. Molecular dynamics simulation and comparison with wild-type show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly
A58E/P65S/Q191R/T271R
A58E/P65S/Q191R/T271R/E228K
-
pH-activity profile-improved mutant, optimum shift to pH 4.0, 64% increased specific activity at pH 3.5
A58E/P65S/Q191R/T271R/E228K/K300E
-
pH-activity profile-improved mutant, eliminates the activity dip at pH 3.5 shown in the wild type
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R
-
Although the substitution of K112R is supposed to create a new hydrogen bond with Y113 at a distance of 2.56 A, it does not offer extra benefit to thermostability
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R
-
27% increased specific activity at pH 5.5, 100% increased specific activity at pH 3.5
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R/K300E
-
33% decreased activity at pH 5.5, wild type specific activity at pH 3.5
C215S
C264G
C31G
C345G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C435G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C71S
D461N
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
E121F
-
random mutagenesis, the mutant shows 3.1fold increased activity and 3.24fold reduced affinity for sodium phytate compared to the wild-type enzyme
E89D/H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
F376Y
random mutagenesis, the mutant has an altered thermostability compared to wild-type
G377T
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
K300D
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.71
K300E
-
mutation results in an increase of the hydrolysis of phythic acid of 56% and 19% at pH 4.0 and pH 5.0 at 37°C respectively. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.74
K300R
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.81
K300T
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.68
K41E
-
random mutagenesis, the mutant shows 2.5fold increased activity and 1.78fold reduced affinity for sodium phytate compared to the wild-type enzyme
K432R
random mutagenesis, the mutant has an altered thermostability compared to wild-type
P212H
Q172R
random mutagenesis, the mutant has an altered thermostability compared to wild-type
Q172R/K432R
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
Q368E
random mutagenesis, the mutant has an altered thermostability compared to wild-type
Q368E/K432R
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
S238D
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
T195L
random mutagenesis, the mutant has an altered thermostability compared to wild-type
T195L/Q368E/F376Y
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
T255E
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.0 and pH 6.0
E121F
-
random mutagenesis, the mutant shows 3.1fold increased activity and 3.24fold reduced affinity for sodium phytate compared to the wild-type enzyme
-
K41E
-
random mutagenesis, the mutant shows 2.5fold increased activity and 1.78fold reduced affinity for sodium phytate compared to the wild-type enzyme
-
K432R
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
Q172R
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
Q368E
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
T195L
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
D461N
Aspergillus niger NII 08121
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
-
S238D
Aspergillus niger NII 08121
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
-
T255E
Aspergillus niger NII 08121
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.0 and pH 6.0
-
C215S
C264G
C31G
C345G
-
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
-
C435G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
C71S
A68S/A72E/A73E/S77N
-
t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme
E41A/D42G
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme
H61E
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme
D148E
site-directed mutagenesis, mutation on the surface, the specific activity of mutant D148E increases by about 35% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
D258A
-
turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme
D52E
site-directed mutagenesis, mutation in the active site, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme, probably because that the side chain of residue D52 is involved in formation of octahedral coordination shells with bridging water molecules in the active site
D55A
-
turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme
E227A
-
turnover number of mutant enzyme is 9.29% of that of the wild-type enzyme
K76E
-
turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme
K76R
-
turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme
N156E
site-directed mutagenesis, mutation on the surface, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme. The mutation site N156 is in the vicinity of residue Y159 which coordinates with Ca2+ by its hydroxyl group. The substitution of Glu for N156 may indirectly change the micro-environment around residue Y159, leading to the reduction in activity of phytase
R122E
-
turnover number of mutant enzyme is 48.81% of that of the wild-type enzyme
R122K
-
turnover number of mutant enzyme is 17.11% of that of the wild-type enzyme
S197E
site-directed mutagenesis, mutation on the surface, the specific activity of mutant S197E increases by about 13% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
Y159A
D148E
-
site-directed mutagenesis, mutation on the surface, the specific activity of mutant D148E increases by about 35% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
-
D52E
-
site-directed mutagenesis, mutation in the active site, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme, probably because that the side chain of residue D52 is involved in formation of octahedral coordination shells with bridging water molecules in the active site
-
N156E
-
site-directed mutagenesis, mutation on the surface, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme. The mutation site N156 is in the vicinity of residue Y159 which coordinates with Ca2+ by its hydroxyl group. The substitution of Glu for N156 may indirectly change the micro-environment around residue Y159, leading to the reduction in activity of phytase
-
S197E
-
site-directed mutagenesis, mutation on the surface, the specific activity of mutant S197E increases by about 13% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
-
G117A/G266A
-
mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at G177 and G266 results in a substantial stabilization of PhyL compared to wild-type (DELTAG value of 8 kJ/mol) with an elevated DELTAG value of 20 kJ/mol
H32P/S256P/K304P/K324P/S353P
-
mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at 5 consensus positions only slightly enhances stabilization compared to wild-type (DELTAG value of 8 kJ/mol) with a DELTAG value of 8.8 kJ/mol
D308A
50% of wild-type activity, significant decrease in melting temperature and optimum temperature
D308E
94% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56A
0.4% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56E
20% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56L
0.6% of wild-type activity, significant decrease in melting temperature and optimum temperature
E180N
-
site-directed mutagenesis, cell surface residue, the mutant shows activity similar to the wild-type enzyme
E227S
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
E229V
-
site-directed mutagenesis, cell surface residue, the mutant shows 19% increased activity compared to the wild-type enzyme
K179R
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
K77R
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
K77R/K179R
-
site-directed mutagenesis, mutation of residues not directly involved in the catalysis but involved in substrate binding, the double mutant phytase shows higher stability at pH 2.6-3.0 compared to the wild-type enzyme. The mutant retains over 80% of its initial activity after 3 h incubation at pH 2.6 while the wild-type phytase retains only about 40% of its original activity. The mutant shows highly reduced activity compared to the wild-type enzyme
P257R
-
site-directed mutagenesis, cell surface residue, the mutant shows reduced activity compared to the wild-type enzyme
S283R
-
site-directed mutagenesis, cell surface residue, the mutant shows 13% increased activity compared to the wild-type enzyme
D308A
-
50% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D308E
-
94% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56A
-
0.4% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56E
-
20% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56L
-
0.6% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
E180N
-
site-directed mutagenesis, cell surface residue, the mutant shows activity similar to the wild-type enzyme
-
E227S
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
-
E229V
-
site-directed mutagenesis, cell surface residue, the mutant shows 19% increased activity compared to the wild-type enzyme
-
P257R
-
site-directed mutagenesis, cell surface residue, the mutant shows reduced activity compared to the wild-type enzyme
-
S283R
-
site-directed mutagenesis, cell surface residue, the mutant shows 13% increased activity compared to the wild-type enzyme
-
D24G
D24G/K111E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K265N
D24G/K70R
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R/K111E/N121S
D24G/N121S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A
site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
K265E
S51A
S51A/K265E
D24G
D24G/K70R/K111E/N121S
K265E
S51A
E378A/D128A/D71A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,3,6,7 with loss of four salt bridges
E378A/D178A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,5 with loss of two salt bridges
E378A/R56A/D128A/D267A/D178A/D71A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1-7 with loss of seven salt bridges
E378A/R56A/D267A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,2,4,7 with loss of four salt bridges
R56A/D128A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB2,3 with loss of two salt bridges
Q258N
-
substitution introduced to enhance the glycosylation activity upon expression in Pichia pastoris
Q258N/Q349N
-
substitutions introduced to enhance the glycosylation activity upon expression in Pichia pastoris. Mutant displays 40% enhancement in thermostability compared to wild-type
L151S
the mutation enhances the activity in the range of 37-70°C and pH 2.5-7.0 by facilitating the interaction between the substrate and the catalytic centre
N354D
the substitution influences the pH profile by weakening the bondage with the side chain of D353, which causes a pKa shift of the catalytic centre
T11A/G56E/L65F/Q144H/L151S
mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin
T11A/H37Y/G56E/L65F/Q144H/L151S/N354D
mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin
T101C/A229C/S307C/V352C/M364C/F398C
-
enhancing the thermal resistance of the acidobacteria-derived phytase by engineering of disulfide bridges, construction of engineered mutant rPhyA6DB by site-directed mutagenesis, overview
E230G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230P
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230R
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162V
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G/L230G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
R79G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R79L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R79S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S51I
-
shift in optimal pH to 5.0. Compared with wild-type, mutant S51T shows higher specific activity, greater activity over pH 2.0-5.5, and increased thermal and acid stability
S51T
-
shift in optimal pH to 4.5. Specific activity of S51T at pH 4.5 is 5.5fold higher than the corresponding specific activity of wild-type
E153R
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230D
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230K
site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme
E230P
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230S
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230T
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162V
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G/L230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
I15T
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15T/R162G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15V/P62S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15Y/P94S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K45E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L398S/C342G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
M1T/H146R
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44I/K45E
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
T44M
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44R/K45M
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45D
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45E
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
T44V/K45S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45W
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y27C/K45E/K306E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
additional information
Q27L
-
3.4fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27
Q27L
-
mutation increases the specific activity mainly around pH 6.5, while the increase is much smaller in the pH range 2 to 5, the pH that seems most relevant for maximal performance of the enzyme in animals. Decreasing the negative surface charge of the Aspergillus fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowers the pH-optimum by ca. 0.5 unit but also results in 70-75% inactivation of the enzyme
A58E/P65S/Q191R/T271R
-
increased activity and improved thermostability retaining 20% greater activity after being heated at 80°C for 10 min and has a 7°C higher melting temperature than that of wild type PhyA
A58E/P65S/Q191R/T271R
-
retains 20% greater activity after being heated at 80°C for 10 min and has 7°C higher melting temperature than that of the wild type enzyme
C215S
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C215S
site-directed mutagenesis, the mutant shows altered temperature optimum compared to the wild-type enzyme
C264G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C264G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C31G
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C31G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
P212H
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 3.2 and pH 5.5. The substitution of histidine at position 212 has remarkable effect on pH and temperature properties of the enzyme
P212H
site-directed mutagenesis, the mutant shows altered the pH optimum shifted from pH 2.5 to pH 3.2 and a decrease in thermostability compared to wild-type enzyme, the mutant exhibits a two-peak pH profile with optima at pH 3.2 and pH 5.5
C215S
-
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
-
C215S
-
site-directed mutagenesis, the mutant shows altered temperature optimum compared to the wild-type enzyme
-
C264G
-
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
-
C264G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
C31G
-
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
-
C31G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
Y159A
-
turnover number of mutant enzyme is 0.19% of that of the wild-type enzyme
Y159A
-
turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme
D24G
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G shows 62.7, 68.3, and 17.9% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. The specific activity of the Escherichia coli-expressed D24G at pH 7.0 and 37°C is improved by 40.3 % as compared with that of the wild-type, while the improvement is 91.9% in Bacillus subtilis and 82.2% in Pichia pastoris, respectively. Overall, the mutant's activity is increased compared to the wild-type
D24G
site-directed mutagenesis, the mutant shows 29.7% activity compared to the wild-type at pH 7.0, 60°C, and 76.6% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows 42.7% activity compared to the wild-type at pH 7.0, 60°C, and 84.2% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R/K111E/N121S
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G/K70R/K111E/N121S shows 54.1, 42.6, and 10.8% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. Overall, the mutant's activity is significantly increased compared to the wild-type
D24G/K70R/K111E/N121S
site-directed mutagenesis, the mutant shows 42.8% activity compared to the wild-type at pH 7.0, 60°C, and 121.1% at pH 4.5, 37°C
K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
K265E
site-directed mutagenesis, the mutant shows similar activity compared to wild-type
S51A
site-directed mutagenesis, the mutant shows 13.5% activity compared to the wild-type at pH 7.0, 60°C, and 79.5% at pH 4.5, 37°C
S51A
site-directed mutagenesis. Overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G
-
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G shows 62.7, 68.3, and 17.9% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. The specific activity of the Escherichia coli-expressed D24G at pH 7.0 and 37°C is improved by 40.3 % as compared with that of the wild-type, while the improvement is 91.9% in Bacillus subtilis and 82.2% in Pichia pastoris, respectively. Overall, the mutant's activity is increased compared to the wild-type
-
D24G
-
site-directed mutagenesis, the mutant shows 29.7% activity compared to the wild-type at pH 7.0, 60°C, and 76.6% at pH 4.5, 37°C
-
D24G/K70R/K111E/N121S
-
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G/K70R/K111E/N121S shows 54.1, 42.6, and 10.8% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. Overall, the mutant's activity is significantly increased compared to the wild-type
-
D24G/K70R/K111E/N121S
-
site-directed mutagenesis, the mutant shows 42.8% activity compared to the wild-type at pH 7.0, 60°C, and 121.1% at pH 4.5, 37°C
-
K265E
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type
-
K265E
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
-
S51A
-
site-directed mutagenesis. Overall, the mutant's activity is increased compared to the wild-type
-
S51A
-
site-directed mutagenesis, the mutant shows 13.5% activity compared to the wild-type at pH 7.0, 60°C, and 79.5% at pH 4.5, 37°C
-
additional information
construction of three recombinant phyA mutant strains, i.e. PP-NPm-8, PP-NPep-6A and I44E/T252RPhyA, that show improved catalytic efficiency or thermostability compared to the wild-type strain. Variations of bond and electrostatic energy before and after substitution at Q172, T195, Q368, F376, and K432, half-life of thermal inactivation and kinetic parameters of PP-NPep-6A phytase and its mutants, predictions of residue interactions, overview
additional information
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
-
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
construction of three recombinant phyA mutant strains, i.e. PP-NPm-8, PP-NPep-6A and I44E/T252RPhyA, that show improved catalytic efficiency or thermostability compared to the wild-type strain. Variations of bond and electrostatic energy before and after substitution at Q172, T195, Q368, F376, and K432, half-life of thermal inactivation and kinetic parameters of PP-NPep-6A phytase and its mutants, predictions of residue interactions, overview
-
additional information
Aspergillus niger NII 08121
-
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
-
additional information
Aspergillus niger NII 08121
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
-
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
-
additional information
directed evolution and library screening, pH and tempearture profiles of the mutant enzymes compared to the wild-type enzyme, detailed overview
additional information
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
additional information
-
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
additional information
-
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
-
additional information
-
directed evolution and library screening, pH and tempearture profiles of the mutant enzymes compared to the wild-type enzyme, detailed overview
-
additional information
KM873028
construction of mutants that lose salt bridges through the mutations, the combinations of the disabled salt bridges are randomly selected. The mutants show reduced melting temperatures and reduced optimum reaction temperature compared to wild-type rPhyXT52, overview
additional information
the HvPAPhy_a-transformed barley plants with high phytase activities possess triple potential utilities for the improvement of phosphate bioavailability. First of all, the utilization of the mature grains as feed to increase the release of bio-available phosphate and minerals bound to the phytate of the grains, secondly, the utilization of the powdered straw either directly or phytase extracted hereof as a supplement to high phytate feed or food, and finally, the use of the stubble to be ploughed into the soil for mobilizing phytatebound phosphate for plant growth
additional information
replacements of G56E, L65F, Q144H, and L151S improved the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
-
replacements of G56E, L65F, Q144H, and L151S improved the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
entrapment of permeabilized cells in 3% w/v alginate resulting in a 10% loss of enzyme activity, corresponding to 90% immobilization yield. The immobilized cells can be successfully reused in four consecutive assays with sustained phytase activity, overview
additional information
-
entrapment of permeabilized cells in 3% w/v alginate resulting in a 10% loss of enzyme activity, corresponding to 90% immobilization yield. The immobilized cells can be successfully reused in four consecutive assays with sustained phytase activity, overview
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
-
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
-
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 7
purified recombinant His-tagged enzyme, over 50% activity remaining
751361
1.5 - 8
37°C, 0.2 M buffer solution, no significant change in activity after 24 h
664984
11
purified enzyme, 25°C, about 50% activity remaining after about 50 min, inactivation after 180 min
751308
2 - 12
-
purified native enzyme, over 65% activity remains after 96 h
751544
2 - 6
-
half-life of the enzyme at pH 2.0, 3.0, 4.0, 5.0 and 6.0 is 577.5, 433.1, 770.0, 247.5 and 91.2 min, respectively
750074
2 - 8
2 - 9
37°C, 1 h, over 80% activity remaining of the purified recombinant PhyCm within the range of pH 5.0-9.0, profile, overveiw
717000
2.5
3 - 10
3 - 5
3 - 7
3 - 8
3 - 9
3.5 - 9
pH profiles of wild-type and mutant enzymes, no activity of mutant enzymes above pH 7.5, overview
715678
4
purified enzyme, 25°C, about 50% activity remaining after about 50 min, inactivation after 180 min
751308
4 - 10
purified recombinant enzyme, over 60% activity remaining within this range
750437
4 - 8
4 - 9
1 h, 4°C, the purified native phytase does not show any significant decline in activity at pH 4.0-5.5, almost 80% of the activity is lost at pH 9.0. At the optimum pH 4.5, the enzyme retains over 90% of its initial activity even after 10 days of incubation
749654
5 - 7
5 - 8
purified recombinant enzyme, stable at pH 5.0-8.0, retaining more than 70% of the initial activity at 37°C for 1 h
714791
5.5 - 10.5
purified recombinant enzyme, stable, profile overview
713922
6
-
purified enzyme, loss of 60% activity after 120 min, and of all activity after 240 min
750074
6 - 7
-
partially purified enzyme, 30 min, completely stable at, 85% activity remains after 24 h
750883
6.5
7 - 10
purified recombinant enzyme, stable in neutral to alkaline buffers, retaining more than 70% of its activity at pH 7.0-10.0 and 37°C for 1 h
714791
8 - 10
-
partially purified enzyme, 30 min, 1.16fold activation, completely stable for 24 h
750883
additional information
supplemental Ca2+ upgrades both the thermostability and pH stability of recombinant PhyCm
717000
2
very stable at the low pH, losing no activity when incubated at pH 2.0 for 4 h
679389
2.5
-
Allzyme phytase can keep more than 60% of activity when pH reaches below 2.5
679568
2.5
-
72 h, 55°C, 90-95% residual activity in presence of different commercial feeds
707761
2.5
-
purified recombinant His-tagged wild-type enzyme, 37°C, half-life is 2 h (for mutant rPhyA6DB 5.4 h)
751304
3 - 10
-
the enzyme retains more than 65% of the maximal activity in the pH range of pH 3.0-9.0. In addition, it is stable over the broad pH range of pH 3.0-10.0
714177
3 - 5
purified extracellular enzyme, 120 min, 50°C, loss of 20% activity
750764
3 - 7
-
no denaturation is observed for pH values between 5.0 and 7.0 after 67 days of storage at -20°C, whereas the phytase is denatured for pH values lower than 5.0, for pH values ranging from 3.0 to 7.0, the enzyme retains 80 to 100% of its activity after incubation at 40°C for 1 h
677788
3 - 8
-
purified recombinant enzyme, 2 h at room temperature, completely stable
751491
3 - 8
-
isozyme RO1 is most stable at pH 4.0-4.5 with 102-103% retained activity after 10 days. Above pH 5.0, the stability of RO1 decreases significantly. RO2, on the other hand, is stable over the pH range pH 3.0-5.5 retaining between 72% and 95% activity after 10 days. Less than 20% activity is retained above pH 6.0
715777
3 - 9
-
more than 94.0% of the residual activity is maintained after treatment at pH from 3.0 to 9.0
681737
4 - 8
-
purified native enzyme, the activity remains fairly stable over pH range of pH 4.0 to pH 8.0, 83% of maxcimal activity remain after 6 h, pH profile, overview
715310
5 - 7
-
the enzyme retains nearly 100% of their activities after 1 h incubation at 37°C and pH 5.0-7.0
714848
5 - 7
-
the enzyme retains nearly 100% of their activities after 1 h incubation at 37°C and pH 5.0-7.0
714848
6.5
-
Allzyme phytase can keep more than 60% of activity when pH reaches above 6.5
679568
7
displays a sharp decline in the activity as the pH moves toward the neutral range, and maintains negligible activity beyond pH 7.0
679389
7
purified extracellular enzyme, 120 min, 50°C, loss of 60% activity
750764
7
-
purified recombinant His-tagged wild-type enzyme, at 60°C the half-life is 5.2 min (for mutant rPhyA6DB 14.5 min), at 80°C the half-life is 2.3 min (for mutant rPhyA6DB 7.0 min)
751304
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 15
purified recombinant His-tagged enzyme, over 50% activity remaining
10 - 50
-
purified enzyme, 30 min, pH 6.5, in presence of 20 mM Ca2+, completely stable, 40% activity is retained at 10°C. The enzyme is more thermostable in presence of CaCl2 and exhibits almost 100% residual activity at temperature range 20-50°C and 63% activity at 70°C after 30 min of preincubation, followed by sharp decline in thermostability
10 - 65
purified AgpP phytase remains stable for 1 h at a temperature interval of 10-45°C losing only up to 20% of activity at 45°C, only 40% and 12% of its maximum activity are retained at 55°C and 65°C, respectively
10 - 80
-
purified native enzyme, over 70% activity remains after 180 h
100
20 - 45
-
purified recombinant enzyme domains PhyH and PhyH-DII, stable up to for 30 min
22
25 - 40
purified recombinant enzyme, over 80% activity remaining within this range, thermal stability of recobinant enzyme PSphy decreases sharply above 40°C in the presence of CaCl2, whereas it remains stable up to 60°C in its absence
30
37
37 - 60
temperature profiles of wild-type and mutant enzymes, overview
40
40 - 100
-
thermal inactivation profile of the purified enzyme, 20-25% of maximal activity at 75°C, below 20% of maximal activity remaining at 80°C, inactivation at 100°C, overview
45
45 - 50
-
there are two phases in thermal inactivation: when the temperature is between 45°C and 50°C, the thermal inactivation can be characterized as an irreversible inactivation which has some residual activity and when the temperature is above 55°C the thermal inactivation can be characterized as an irreversible process which has no residual activity
48.6
mutant D308A, melting temperature, presence of 5 mM Ca2+
48.8
wild-type, melting temperature, presence of EDTA, mutant D56A, melting temperature, presence of 5 mM Ca2+
49
49.6
mutant D56L, melting temperature, presence of 5 mM Ca2+
50
50 - 70
50 - 75
-
the purified phytase retains 73.6% of its activity after being incubated at 50°C for 10 min, while its activity is quickly lost after incubation at 65°C or 70°C for 10 min
50 - 80
-
half-life of the enzyme at 50, 60, 70 and 80°C is 866.2, 693.0, 37.8 and 11.3 min, respectively. The activity is lost completely at 80°C after 55 min incubation
54.8
mutant D308E, melting temperature, presence of 5 mM Ca2+
55
55 - 60
-
the enzyme is stable at or below 55°C exhibiting at least 80% of residual activity, and is completely denatured at 60°C or above
55 - 65
-
the enzyme is stable at temperatures up to 55°C in the presence of 5 mM Ca2+, but the stability decreases dramatically above 65°C
55.5
mutant D56E, melting temperature, presence of 5 mM Ca2+
60
60 - 100
KM873028
purified recombinant enzyme, half-life at 60, 80, and 100°C is approximate 5.6 h, 2.1 h, and 27 min, respectively. At 80°C, recombinant PhyXT52 retains about 90% residual activity after 20 min, and at 100°C more than 93% residual activity are retained after 15 min and over 83% after 20 min. Melting temperatures of wild-type rPhyXT52 and mutant enzymes rPhyXT52:DELTASB1,5, rPhyXT52:DELTASB2,3, rPhyXT52:DELTASB1,2,4,7, rPhyXT52:DELTASB1,3,6,7, rPhyXT52:DELTASB1-7 are 60.5°C, 58.2°C; 59.7°C; 54.6°C, 55.2°C, and 52.8°C. Half-lifes of mutants are determined at 60-100°C, overview
60 - 70
63
-
10 min, 10% loss of the activity of the recombinant phytase, 25% loss of the activity of the fungal enzyme
65
70
70 - 73
melting temperature of the native phytase is 73°C, while that of the recombinant phytase is 70°C
70 - 90
-
approximately 40% of the original activity is lost after exposure to 70°C for 180 min, with no residual activity being seen after exposure to 80°C for 60 min or 90°C for 5 min
75
80
85
90
90 - 100
50% and 62% activity remaining after 10 min at 100°C and 90°C, respectively
95
additional information
100
-
heat treatment at 100°C for 10 min results in loss of all phytase activity
100
5 min, mutant T11A/G56E/L65F/Q144H/L151S retains 72,81% of initial activity, and mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D retains 92.43% of initial activity
100
-
purified recombinant enzyme, pH 2.0, after 20 min inactivation, loss of 50% activity after 4 min
30
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
37
-
20 min, less than 5% of activity of enzyme in 0.01 M sodium citrate buffer, about 5% loss of activity in 0.2 M sodium citrate buffer, about 10% loss of activity in 0.2 M sodium acetate buffer, about 15% loss of activity in 0.01 sodium acetate bugffer
37
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
37
-
purified recombinant His-tagged wild-type enzyme, pH 2.5, half-life is 2 h, and for mutant rPhyA6DB 5.4 h
45
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
45
-
90 min, no significant loss of activity at temperatures up ro, phytase LP11, LP12 and LP2
45
purified enzyme, pH 6.5, 50% activity remaining after 120 min, 20% after 180 min
50
30 min, enzyme is highly resistant but loses its activity very rapidly under further increase of the temperature
50
the thermal stability of recombinant PhyB49 is affected by the concentration of Ca2+, the recombinant enzyme is stable at 50°C for 30 min at 5 mM Ca2+, but loses activity rapidly under the same conditions in presence of 1 mM Ca2+
50 - 70
-
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C
50 - 70
-
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C
50 - 70
-
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C
55
-
irreversible conformational change with loss in enzymatic activity of 70-80%
55
-
there are two phases in thermal inactivation: when the temperature is between 45°C and 50°C, the thermal inactivation can be characterized as an irreversible inactivation which has some residual activity and when the temperature is above 55°C the thermal inactivation can be characterized as an irreversible process which has no residual activity
55
-
24 h, 11% loss of activity in absence of stabilizing agent, 7% loss of activity in presence of 10 mM CaCl2, 3% loss of activity in presence of 10 mM glycine. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
55
30 min, stable, enzyme expressed in Saccharomyces cerevisiae or Pichia pastoris
55
-
72 h, pH 2.5, 90-95% residual activity in presence of different commercial feeds
55
-
10 min, stable, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
55
purified recombinant enzyme, PhyA115 is unstable without Ca2+, losing about 90% of the activity after incubation at 55°C for 4 min. At high concentrations of Ca2+ of 5-10 mM, PhyA115 retains more than 70% of the activity at 55°C for 30 min. Profiles, overview
60
-
purified native extracellular enzyme, completely stable up to
60
-
purified enzyme, residual activity of 86.0%, 68.4%, and 48.2% after 10, 20 or 40 min, respectively
60
-
purified recombinant enzyme domains PhyH and PhyH-DII, about 80% of maximal activity remaining after 30 min in presence of 10 mM Ca2+, 50% at 1 mM Ca2+, and 20% without Ca2+
60
recombinant and native enzymes, 5 mM CaCl2, pH 5.5 or pH 7.5, stable
60
-
partially purified enzyme, retains 83% and 60% of its initial activity after 90 and 120 min, respectively
60
-
90 min, 90 min, 79% loss of activity of phytase LP22, 92% loss of activity of phytase LP12 and 85% loss of activity of phytase LP2
60
purified enzyme, pH 5.0, half-life of recombinant enzyme is 6 h and of native enzyme 16 h
60
purified native enzyme, pH 5.0, has a half-life of 16 h
60
purified recombinant His-tagged enzyme, pH 5.0, has a half-life of 4 h. Purified native enzyme, pH 5.0, has a half-life of 16 h
60
-
purified recombinant enzyme, pH 2.0, after 30 min inactivation, loss of 50% activity after 15 min
60
-
purified recombinant His-tagged wild-type enzyme, pH 7.0, half-life is 5.2 min, and for mutant rPhyA6DB 14.5 min
60
phytase from permeabilized cells, pH 4.0, half-life is 5 h
60
-
2 min, pH 2.5, complete loss of activity for wild-type. Mutants S51I and S51T retain about 80% of activity
60 - 70
-
purified native enzyme, stable at 60°C, no obvious loss of activity upon incubation at 70°C for 20 min
60 - 70
-
the residual phytase activity still maintains 96.3% of the control after treatment at 60°C for 1 h, the enzyme is inactivated rapidly at temperatures higher than 60°C and is almost inactivated at 70°C within 1 h
65
-
20 min, about 35% loss of activity in 0.01 M sodium acetate buffer, about 40% loss of activity in 0.2 M acetate buffer, about 45% loss of activity in 0.01 M sodium citrate buffer, about 65% loss of activity in 0.2 M sodium citrate buffer
65
30 min, enzyme expressed in Saccharomyces cerevisiae loses about 30% of initial activity, enzyme expressed in Pichia pastoris loses about 45% of initial activity
65
-
half-life: 30 min in absence of stabilizing agent, 6 h in presence of 20 mM glycine, 2 h in presence of 10 mM CaCl2. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
65
-
10 min, 55-70% loss of activity, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
65
purified enzyme, pH 6.5, 50% activity remaining after about 20 min, 10% after 60 min, inactivation after 120 min
70
10 min, about 15% loss of activity, in presence of 1 mM Ca2+
70
purified native enzyme, 10 min, about 75% activity is maintained
70
-
the enzyme retains more than 30% of its activity following incubation at 70°C for 30 min
70
-
at 70°C the activity of the immobilized enzyme remains around 45%, whereas no activity is detected for the free enzyme
75
10 min, about 35% loss of activity, in presence of 1 mM Ca2+
75
-
10 min, 10-20% loss of activity, recombinant enzyme from different expression systems. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
75
enzyme PHY US42 maintains 80% activity after 10 min in the presence of 5 mM CaCl2, whereas in the absence of calcium, PHY US42 activity is completely abolished after 2 min of incubation
75
phytase from permeabilized cells, pH 4.0, half-life is 15 min
80
10 min, about 35% loss of activity, in presence of 1 mM Ca2+
80
deglycosylated native enzyme, 5 mM CaCl2, 10 min, 68% of initial activity remaining at pH 7.5, 36% at pH 5.5
80
deglycosylated recombinant enzyme, 5 mM CaCl2, 10 min, 85% of initial activity remaining at pH 7.5, 11% at pH 5.5
80
-
purified native enzyme, 40% of original activity remaining after 30 min
80
pH 7.0, 37°C, 70% activity remains for the purified recombinant enzyme mutant expressed from Bacillus subtilis, 25% activity remains for the purified recombinant enzyme mutant expressed from Pichia pastoris, and 50% activity remains for the purified recombinant enzyme mutant expressed from Escherichia coli
80
purified native enzyme, 10 min, about 20% activity is maintained
80
-
isozyme r-PhyG1 loses over 80% of its activity after incubation at 50°C for 15 min, whereas isozyme r-phyG51 is not affected by these conditions
80
-
about 25% loss of activity after 1 min, about 50% loss of activity after 2 min, about 65% loss of activity after 3 min
80
purified enzyme, pH 5.0, half-life of recombinant enzyme is 1 h and of native enzyme 1.5 h
80
purified native enzyme, pH 5.0, has a half-life of 1.5 h
80
purified recombinant His-tagged enzyme, pH 5.0, has a half-life of 38 min. Purified native enzyme, pH 5.0, has a half-life of 1.5 h
80
-
purified recombinant enzyme, pH 2.0, after 25 min inactivation, loss of 50% activity after 7 min
80
-
purified recombinant His-tagged wild-type enzyme, pH 7.0, half-life is 2.3 min, and for mutant rPhyA6DB 7.0 min
85
10 min, about 30% loss of activity, in presence of 1 mM Ca2+
85
-
10 min, 60% residual activity for mutant Q258N/Q349N, 5 min, 30% residual activiy for wild-type
90
-
purified native extracellular enzyme, loss of about 90% activity
90
-
20 min, about 35% loss of activity in 0.01 M sodium acetate buffer, about 40% loss of activity in 0.2 M acetate buffer, about 45% loss of activity in 0.01 M sodium citrate buffer, about 65% loss of activity in 0.2 M sodium citrate buffer
90
high ability to resist heat inactivation, after being exposed to 90°C for 15 min, the recombinant enzyme in crude and purified form retains 42% and 43.7% of the initial enzyme activity, respectively
90
-
retains 28.7% of the initial activity after incubation at 90°C for 15 min
90
retains 70% activity after exposure to 90°C for 5 min and 65% activity after 30 min
90
10 min, about 30% loss of activity, in presence of 1 mM Ca2+
95
about 40% loss of activity after 15 min, about 60% loss of activity after 30 min, in presence of 5 mM ca2+
95
-
about 55% loss of activity after 15 min, about 75% loss of activity after 30 min, with 5 mM Ca2+
additional information
-
immobilized enzyme has higher thermal stability as the untreated enzyme
additional information
-
better thermostability at 65°C and at 90°C when sodium acetate is used as the buffer, pH 5.5, than that of sodium citrate at either low, 10 mM or high, 0.2 M, concentration
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
additional information
supplemental Ca2+ upgrades both the thermostability and pH stability of recombinant PhyCm
additional information
temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis
additional information
-
temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis
additional information
-
thermal stability of the high molecular weight form and the low molecular weight form
additional information
-
analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide
additional information
the temperature stability is increased by Ca2+
additional information
the cell-bound phytase exhibits better thermostability than the pure enzyme
additional information
-
the cell-bound phytase exhibits better thermostability than the pure enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at protein concentrations below 0.05 mg/ml a rapid loss of stability occurs
-
denaturation in urea, in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
enzyme is resistant to pepsin
incubated with pepsin at 37°C for 2 h at the ratio (pepsin/phytase, wt/wt) of 0.1, the enzyme still retains 90.1% residual activity
substrate calcium phytate stablizes the enzyme, while sucrose, glycerol, and starch do not
supplemental Ca2+ upgrades both the thermostability and pH stability of recombinant PhyCm, overview
the enzyme is resistant to proteases such as trypsin or pepsin when incubated for 2 h at 37°C. Papain, elastase and pancreatin slightly decrease activity to 85%, 80% and 70%, respectively, of the original activity
-
tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
-
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
-
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,2-dimethoxyethane
-
presence of 30% increases the alpha-helical content of the phytase
Ethanol
-
presence of 30% increases the alpha-helical content of the phytase
additional information
-
high resistance to the denaturing effect of organic solvents
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 4.3, 5% v/v glycerol, 2 mM 2-mercaptoethanol, 1.7 mg/ml protein, stable for months
-
4°C, 0.05 M Tris-HCL buffer, pH 8.2,36% loss of activity after 2 weeks
-
4°C, best shelf life, maintaining 38% of its initial activity after 112 days
-
4°C, protein concentration 0.1 mg/ml or greater, half-life is approximately 6 months
-
4°C, purified native enzyme, after 30 days, 88.9% activity are remaining, after 60 days the remaining activity is 84.25% of initial activity, and after 180 days 57.5%
-
60°C, phytase from permeabilized cells, pH 4.0, 1 month, fully stable
66°C, in sodium acetate buffer (125 mM, pH 4.0), 1 h, remains stable
-
PHY produced by Penicllium griseoroseum strain T73 retains 75%, 66% and 68% of the initial activity after four weeks of storage at -20°C, 8°C, and 25°C, respectively
-
purified enzyme, shelf life is 6 months at 4°C, no loss in the activity on lyophilization
room temperature, protein concentration 0.1 mg/ml or greater, half-life is 10 days
-
stabilization by PEG 3350 results in 109% of phytase activity from the initial crude extract remaining after 90 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 1.5fold higher enzyme yield in the presence of sucrose in both submerged and solid-state fermentations, while peptone is found to be a favorable nitrogen source for submerged fermentations. NaH2PO4 favors 34% higher enzyme yield than the control, which is followed by 19% higher activity in KH2PO4 in solid-state fermentation at 0.015% w/v. The addition of Tween-20 in submerged fermentations shows a maximum yield of 12.6 U/ml while, SDS suppresses the growth of the fungus. None of the surfactants favors the enzyme yield in solid-state fermentation. CaCl2 is extensively efficient in stimulating more than 55% higher phytase production in submerged fermentation at 0.01% v/v. In solid-state fermentation, none of the metal salts stimulates phytase production
-
ammonium sulfate fractionation, Sephadex G-75 gel filtration, and DEAE Sepharose Fast Flow column chromatography
-
native enzyme 10.1fold by cationic exchange chromatography, anionic exchange chromatography, and chromatofocusing
-
native enzyme 14.22fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration, to homogeneity
-
native enzyme 24fold by ethanol precipitation, anion exchange chromatography, and gel filtration
-
native enzyme 35.87fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography, lyophilization, and gel filtration
native enzyme 71.5fold by anion exchange chromatography, cation exchange chromatography, and gel filtration
-
native enzyme 9.53fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme by dialysis, anion exchange chromatography, and gel filtration, recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli by nickel affinity chromatography. Native extracellular enzyme 528fold by dialysis, anion and cation exchange chromatography, and gel filtration
native enzyme from cell culture medium 4.2fold by ammonium sulfate frcationation and dialysis
native enzyme PhyA 427fold from strain PJ3 by ammonium sulfate fractionation, dialysis, gel filtration, and cation exchange chromatography, and again dialysis, to homogeneity
native extracellular enzyme 10.68fold by ammonium sulfate fractionation, cation exchange chromatography, and gel filtration to homogeneity
native extracellular enzyme 15.2fold by ammonium sulfate fractionation, anion and cation exchange chromatography, and gel filtration, to homogeneity
-
native extracellular enzyme 20.84fold from cell culture supernatant by ethanol precipitation, gel filtration, and anion exchange chromatography
-
native extracellular enzyme 6fold from cell culture medium of strain US573 by heat treatment and ammonium sulfate fractionation
native extracellular enzyme from culture medium 486.41fold by ammonium sulfate fractionation, cation and anion exchange chromatography, and dialysis
native extracellular enzyme from culture medium 5.51fold by ammonium sulfate fractionation, dialysis, and anion exchange chromatography, and gel filtration, to near homogeneity
-
Ni-NTA superflow resin column chromatography and HiLoad 16/10 phenyl Sepharose column chromatography
-
nickel-nitrilotriacetic acid metal affinity chromatography, DEAE cation-exchange chromatography, and Sephadex-100 gel filtration
-
partial
partial purification of native enzyme by ammonium sulfate fractionation
recombinant enzyme
recombinant enzyme 3.3fold from culture supernatant of Pichia pastoris strain GS115 by ammonium sulfate fractionation and gel filtration
recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration
recombinant extracellular enzyme from Pichia pastoris strain X33 cell culture medium by lyophilization, anion exchange chromatography, and gel filtration, to homogeneity
recombinant extracellular phytase from Pichia pastoris strain X-33 culture medium by lyophilization, dialysis, and anion exchange chromatography
-
recombinant His-tagged enzyme domains PhyH, PhyH-DI, and PhyH-DII from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography followed by two steps of gel filtration to 95% purity
-
recombinant His-tagged full-length enzyme and its N- and C-terminal domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged phytase from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant His-tagged wild-type PhyK and of mutant H25A PhyK from Escherichia coli strain C41 (DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3)
recombinant His6-tagged phytase PhyB49 from Escherichia coli strain BL21(DE3)
recombinant His6-tagged phytase PhyH49 from Escherichia coli strain BL21(DE3)
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant isozyme LlALP2-Ala, with the c-myc and (His)6 tags at the C-terminus, from Pichia pastoris strains X-33 and KM71H by cobalt, not nickel, affinity chromatography
recombinant mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography
recombinant N-terminally His6-tagged wild-type and mutant enzymes by nickel affinity chromatography
-
recombinant nonglycosylated His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant glycosylated nontagged enzyme from Pichia pastoris strain GS115(his4) by cation exchange chromatography
recombinant protein
recombinant refolded His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant refolded His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis to homogeneity
recombinant thioredoxin-His-tagged enzyme and His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 by gel filtration to homogeneity
recombinant wild-type enzyme mutant enzymes from Pichia pastoris strain X33 by ammonium sulfate fractionation, and two different steps of ion exchange chromatography
secreted recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 culture supernatant
Sephadex G-100 gel filtration and DEAE-Sepharose CL-6B anion exchange column chromatography
-
soluble screted recombinant enzyme from Pichia pastoris culture supernatant by gel filtration
soluble screted recombinant isozyme from Pichia pastoris culture supernatant by gel filtration
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
the native enzyme is purified to near homogeneity by acetone precipitation and anion exchange chromatography
two native isozymes RO1 and RO2, 75fold and 46fold, respectively, by acetone fractionation, cation exchange chromatography, gel filtration, and again cation exchange chromatography followed by anion exchange chromatography to homogeneity
-
partial purification of native enzyme by ammonium sulfate fractionation
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
soluble screted recombinant isozyme from Pichia pastoris culture supernatant by gel filtration
soluble screted recombinant isozyme from Pichia pastoris culture supernatant by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, quantitative realtime PCR expression analysis
-
concerted action of endogenous phytase, EC 3.1.3.26, and heterologous phytase from Aspergillus niger, EC 3.1.3.8, on phytic acid degradation in seed of transgenic Triticum aestivum L.
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of the His-tagged full-length enzyme and its N- and C-terminal domains in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
engineering of Escherichia coli appA phytase gene into the chloroplast genome of the model microalga, Chlamydomonas reinhardtii strain CC-125, and isolation of homoplasmic plastid transformants. Catalytic activity of the recombinant AppA can be directly detected in the whole-cell lysate with 10 phytase units per gram dry matter at pH 4.5 and 37°C, method optimization, overview
-
expreession in Solanum tuberosum under control of sweet potato sporamin promoter
-
expressed in Pichia pastoris strain GS115
expressed in Pichia pastoris strain X33
expressed in the cytoplasm of developing cotyledons from Glycine max line CAPPA
-
expression in Arabidopsis thliana. The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
expression in Aspergillus niger, Saccharomyces cerevisiae or Hansenula polymorpha
-
expression in Escherichia coli
expression in Glycine max, inserted into soybean transformation plasmid under control of constitutive and seed-specific promoters
-
expression in Nicotiana tabacum
expression in Pichia pastoris
expression in Pichia pastoris (constitutive or inducible) and Saccharomyces cerevisiae (inducible)
expression in Pichia pastoris strain GS115, methanol induction, the recombinant enzyme is secreted
expression of a truncated enzyme form, with a deletion of the 20 amino acid residues from the N-terminus of the protein
-
expression of His-tagged enzyme domains PhyH, PhyH-DI, and PhyH-DII in Escherichia coli strain BL21 (DE3)
-
expression of His-tagged wild-type PhyK and of mutant H25A PhyK in Escherichia coli strain C41 (DE3)
expression of the enzyme in three inducible yeast systems: Saccharomyces cerevisiae (pYES2), Schizosaccharomyces pombe (pDS472a), and Pichia pastoris (pPICZalphaA), and one constitutive system: Pichia pastoris (pGAPTalphaA). During 8-day batch fermentation in shaking flasks, the inducible Pichia system produces the highest activity whereas the Schizosaccharomyces pombe system produces the lowest activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene agpP, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli
gene appA or phyS, cloning from library, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of extracellular His-tagged enzyme in Escherichia coli strain BL21(DE3) as nonglycosylated protein and of extracellular nontagged enzyme in Pichia pastoris strain GS115(his4) under control of the AOX1 promoter as glycosylated protein
gene appA, random YmPh mutant libraries generation and screening, recombinant expression in Escherichia coli strain BL21 Gold (DE3)lacIQ
gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene appA_Gw, DNA and amino acid sequence determination and analysis, cloning from metagenome, recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene Blon_0263, recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, but the Bifidobacterium longum enzyme is not expressed or it is expressed at a low level
gene encoding PhyB49 PCR-amplified from the genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of the phytase as N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
gene encoding PhyH49 PCR-amplified from the genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of the phytase as N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
gene LlAlp2, functional heterologous expression of isozyme LlALP2-Ala, with the c-myc and (His)6 tags at the C-terminus, from lily pollen in Pichia pastoris strains X-33 and KM71H, optimization of expression by varying the cDNA coding for LlALP2, host strain and growth conditions, overview
gene MYCTH_2306203, construction of rSt-Phy gene using overlap extension PCR for removal of an intron, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH5alpha
gene PAPhy, recombinant expression in transgenic Hordeum vulgare plants using transfection via Agrobacterium tumefaciens strain AGL0, T1-plants are transformed with 35S:PAPhy_a showing mature grain phytase activity, in green leaves and mature dry straw, phytase activities are increased significantly by 110fold (52000 FTU/kg) and 57fold (51000 FTU/kg), respectively
gene phy, DNA and amino acid sequence determination and analysis, sequence comparisons
gene phy, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Penicillium griseoroseum strain PG63 protoplasts from vectorpAN-52-1-phy. Transformant T73 contains the phy gene integrated in at least three sitesof the genome and shows the highest, 5.1fold increase in phytase activity in comparison to the host strain
-
gene phy, DNA and amino acid sequence determination, analysis, and comparisons, cloning and expression in Escherichia coli strain DH5alpha
gene phy, functional recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, the Bifidobacterium pseudocatenulatum is efficiently expressed
gene phy, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
gene phy168, recombinant expression of wild-type and mutant enzymes in Bacillus subtilis strain WB800N, Escherichia coli TOP10 cells or strain BL21, and Pichia pastoris strain GS115, subcloning in Escherichia coli, evaluation of the best expression systems, overview. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115, when the expression host is changed from Escherichia coli to Pichia pastoris, deglycosylation is conducted. The enzyme expressed in Pichia pastoris is secreted. Wild-type enzyme and the mutants D24G, D24G/K70R/K111E/N121S secreted by Pichia pastoris show decreased thermostability compared with those expressed in Escherichia coli, correspondingly. This reduction in residual activity might be ascribed to the N-glycosylation of phy168 in Pichia pastoris
gene PHYA, construction of rSt-Phy gene using overlap extension PCR for removal of an intron, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH5alpha
gene phyA, DNA and amino acid sequence determination and analysis
gene phyA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression in Pichia pastoris strain GS115
gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination
gene phyA, DNA and amino acid sequence determination and analysis, sequence comparisons
gene phyA, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Escherichia coli
gene phyA, expression in Pichia pastoris strain X33, subcloning in Escherichia coli strain JM109 and DH5alpha
gene phyA, protease-resistance phytase gene, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 with secretion to culture supernatant
gene phyA, real-time PCR expression analysis, constitutive secretary expression of codon-optimized rStPhy under glyceraldehyde phosphate dehydrogenase (GAP) promoter in Pichia pastoris strain X-33
gene phyA, the mutants are constructed and expressed in Kluyveromyces lactis strain GG799, the enzymes are secreted
gene phyA115, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene phyC, DNA and amino acid determination and analysis, functional recombinant expression of thioredoxin-His-tagged enzyme from vector pET32a-PhyC and His-tagged enzyme from vector pET21a-PhyC in Escherichia coli cytoplasm. The concentration of the alkaline phytase expressed by pET32a is approximately 59% greater than that expressed by pET21, but its phytase activity is approximately 77% lower
gene phyC, overexpression in Pichia pastoris strain KM71
gene phyC, phylogenetic tree, expression in Pichia pastoris strain GS115 under the control of AOX1 promoter. The recombinant PhyCm, driven by the Saccharomyces cerevisiae alpha-mating factor, is secreted into culture medium
gene phyC, sequence comparisons, recombinant overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene phyI1s, DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged wild-type and mutant enzymes
-
gene phyTX52, phylogenetic analysis, recombinant overexpression of wild-type enzyme in Escherichia coli strain BL21(DE3)
KM873028
gene pphy, determination of gene copy number by quantitative real-time PCR, constitutive secretory expression of PPHY under glyceraldehyde phosphate dehydrogenase (GAP) promoter in Pichia pastoris, method optimization and evaluation, 44fold increased enzyme production
gene PPHY, DNA sequence, promoter and terminator region, and amino acid sequence determination and analysis
gene pphy, sequence comparisons, subcloning in Escherichia coli XL10-Gold cells, expression in Pichia pastoris strain X33, the recombinant enzyme is secreted
gene YeappA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
genes phyG1 and phyG51, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, quantitative realtime PCR expression analysis
-
overexpression in Bacillus subtilis using a PHI105MU331 prophage vector system
overexpression of a N-terminal His-tagged phytase in Escherichia coli
-
phylogenetic tree, functional enzyme expression in Pichia pastoris. The Pichia pastoris PHO1 phosphatase is repressed by 0.1 M phosphate buffer, and nontransformed or empty vector-transformed Pichia pastoris shows no detectable secretion or cell wall-associated phosphatase or phytase activity during 5 d of culture. Predicted endoplasmic reticulum signal peptides and potential C-terminal membrane retention signals are excised from the expression constructs, the recombinant enzyme is secreted to the culture medium
recombinant expression of wild-type and mutant enzymes in Kluyveromyces lactis strain GG799, the enzymes are secreted
recombinant overexpression in Pichia pastoris strain X-33 using inducible promoter AOX1, the enzyme is secreted
-
gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene phyA, DNA and amino acid sequence determination and analysis
phylogenetic tree, functional enzyme expression in Pichia pastoris. The Pichia pastoris PHO1 phosphatase is repressed by 0.1 M phosphate buffer, and nontransformed or empty vector-transformed Pichia pastoris shows no detectable secretion or cell wall-associated phosphatase or phytase activity during 5 d of culture. Predicted endoplasmic reticulum signal peptides and potential C-terminal membrane retention signals are excised from the expression constructs, the recombinant enzyme is secreted to the culture medium
phylogenetic tree, functional enzyme expression in Pichia pastoris. The Pichia pastoris PHO1 phosphatase is repressed by 0.1 M phosphate buffer, and nontransformed or empty vector-transformed Pichia pastoris shows no detectable secretion or cell wall-associated phosphatase or phytase activity during 5 d of culture. Predicted endoplasmic reticulum signal peptides and potential C-terminal membrane retention signals are excised from the expression constructs, the recombinant enzyme is secreted to the culture medium
phylogenetic tree, functional enzyme expression in Pichia pastoris. The Pichia pastoris PHO1 phosphatase is repressed by 0.1 M phosphate buffer, and nontransformed or empty vector-transformed Pichia pastoris shows no detectable secretion or cell wall-associated phosphatase or phytase activity during 5 d of culture. Predicted endoplasmic reticulum signal peptides and potential C-terminal membrane retention signals are excised from the expression constructs, the recombinant enzyme is secreted to the culture medium
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
phytase production by Rhizopus microsporus var. microsporus biofilm is stimulated by the phosphorus source in the medium
-
phytase production by strain a13 is induced by the presence of phytic acid
phytase production by strain a13 is repressed by the addition of glucose
phytase production by strain a13 is induced by the presence of phytic acid
phytase production by strain a13 is induced by the presence of phytic acid
Burkholderia sp. a13(2014) JCM 30421
-
-
phytase production by strain a13 is repressed by the addition of glucose
phytase production by strain a13 is repressed by the addition of glucose
Burkholderia sp. a13(2014) JCM 30421
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after heat denaturation at temperatures up to 90°C the enzyme refolds completely into a nativelike, fully active conformation. Capacity of the enzyme to refold properly after heat denaturation may favorably affect its pelleting stability
-
Ca2+ is required for refolding. Enzyme refolded in the presence of one of the divalent cations, Cu2+, Fe2+, Mg2+, Co2+, Zn2+ or Mn2+, fails to show any enzyme activity even in the presence of Ca2+ in the reaction mix
enzyme can restore its enzymatic activity in the presence of 5 mM Ca2+ to 87% of its original activity after heating to 100°C and subsequent cooling
metal-depleted apoenzyme can be restored by Ca2+, Sr2+,Co2+, Ba2+, Cu2+, La3+, Ni+, Tb2+, and Mn2+ to 44.1%, 29.8%, 36.7%, 26.9%, 1.9%, 30.0%, 34.2%, 8.3%, and 34.9% of its reference activity, respectively
phytase is unfolded by guanidinium chloride and then refolded by removing the denaturant by dialysis. The unfolded phytase when diluted in assay medium refolds as a function of timr at 25°C and 37°C, but not at higher temperature. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
purified and acetone-precipitated protein is obtained using denaturing and refolding on a nickel affinity chromatography column
recombinant enzyme from Escherichia coli inclusion bodies is solubilized by 6 M urea and 5 mM 2-mercaptoethanol in 100 mM Tris-HCl, pH 7.0. The cell-free lysate is added to the equilibrated resins and is kept for 1 h on a rocker. The recombinant protein bound to the column is refolded on the column by passing five column volumes of buffer A (6 M urea and 5 mM 2-mercaptoethanol in 100 mM Tris-HCl, pH 7.0) and buffer B (20% v/v glycerol and 5 mM 2-mercaptoethanol in 100 mM Tris-HCl, pH 7.0) in a linear gradient of 6.0 to 0.0 M urea
recombinant enzyme from Escherichia coli inclusion bodies is solubilized by 8 M urea
the enzyme denatures at temperatures of 50C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
the enzyme denatures at temperatures of 50C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
-
the enzyme denatures at temperatures of 50C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
-
the enzyme denatures at temperatures of 50C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
food industry
nutrition
synthesis
additional information
agriculture
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a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
agriculture
-
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Schwanniomyces castellii
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Penicillium caseoicolum
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Aspergillus syndowi
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
since monogastric animals virtually lack phytase activity in their digestive tract, phytic acid phosphorus is metabolically unavailable to these animals. The problem can be circumvented by supplementation of the feed with a recombinantly produced phytase that has a pH activity profile ideally suited for maximal activity in the digestive tract of either pigs or poultry
agriculture
-
the enzyme is suitable for supplementing animal feeds to improve the availability of phosphate from phytate
agriculture
-
feedstuffs studied contains only small amounts of soluble protein-phytate complexes. Insoluble protein-phytate complexes are formed at low pH, as found in the stomach of monogastric animals. Dietary phytase supplementation prevents the formation of protein-phytate complexes or aids in dissolving them faster. Therefore, phytase may improve protein digestibility
agriculture
-
the ability of the enzyme to liberate phytate-phosphate is similar when included in low Ca2+ and nonphytate phosphorus diets for broilers. Either source can be fed to commercial broilers to aid improving phytate-bound phosphate use
agriculture
-
over-expression of phyA2 gene in maize seeds using a construct driven by the maize embryo-specific globulin-1 promoter. Phytase activity in transgenic maize seeds reaches approximately 2,200 units per kg seed, about a 50fold increase compared to non-transgenic maize seeds. The phytase expression is stable across four generations. The transgenic seeds germinate normally
agriculture
-
the dry weight and inorganic phosphate contents of wheat plants are high when supplemented with phytase or fungal spores. The plants provided with 5 mg phytate per plant exhibit enhanced growth and inorganic phosphate. With increase in the dosage of phytase, there is an increase in growth and inorganic phosphate of plants, the highest being at 20 U per plant. The compost made employing the combined native microflora of the wheat straw and Sporotrichum. Thermophile promots growth of the plants. The plant-growth-promoting effect is higher with the compost made using Sporotricum thermophile than that from only the native microflora
agriculture
-
the presence of rhizosphere microorganisms reduces the dependence of plants on extracellular secretion of phytase from roots when grown in a phosphate-deficient soil. The expression of phytase in transgenic plants has little or no impact on the microbial community structure as compared with control plant lines, whereas soil treatments, such as the addition of phosphate, has large effects. Soil microorganisms are explicitly involved in the availability of phosphate to plants and the microbial community in the rhizosphere appears to be resistant to the impacts of single-gene changes in plants designed to alter rhizosphere biochemistry and nutrient cycling
agriculture
-
the presence of rhizosphere microorganisms reduces the dependence of plants on extracellular secretion of phytase from roots when grown in a phosphate-deficient soil. The expression of phytase in transgenic plants has little or no impact on the microbial community structure as compared with control plant lines, whereas soil treatments, such as the addition of phosphate, has large effects. Soil microorganisms are explicitly involved in the availability of phosphate to plants and the microbial community in the rhizosphere appears to be resistant to the impacts of single-gene changes in plants designed to alter rhizosphere biochemistry and nutrient cycling
agriculture
-
transgenic expression of phytase in Solanum tuberosum leads to stable expression levels over several cycles of propagation. Field tests show that tuber size, number and yield increase in transgenic potato. Improved phosphorus acquisition when phytate is provided as a sole phosphorus source and enhanced microtuber formation in cultured transgenic potato seedlings when phytate is provided as an additional phosphorus source are observed. The potato-produced phytase supplement is as effective as a commercially available microbial phytase in increasing the availability of phytate-phosphorus to weanling pigs
agriculture
-
the phytase has the potential to be useful as an animal feed supplement
agriculture
-
seed-specific overexpression of Aspergillus niger phytase in corn leads to transgenic corn with bioavailable phosphate. Maximal phytase activity of 125 FTU/g kernels can be obtained, 1000fold above that of the wild type, with 1000 g of kernels containing up to 67 times the feed industry requirement. An animal feeding trial demonstrated that the recombinant enzyme has similar nutritional effects on broiler chickens to a commercially available phytase product in terms of reducing inorganic phosphorus addition to feed and phosphate excretion in animal manure
agriculture
enzyme PHY US42 can be used as feed additive in combination with an acid phytase for monogastric animals
agriculture
enzyme rSt-Phy is useful in the dephytinization of broiler feeds efficiently in simulated gut conditions of chick leading to the liberation of soluble inorganic phosphate with concomitant mitigation in anti-nutrient effects of phytates
agriculture
neutral phytase is used as a feed additive for degradation of anti-nutritional phytate in aquatic feed industry. Mutant phytases D148E and S197E with increased activities and thermostabilities have application potential as additives in aquaculture feed
agriculture
phytase is used as a feed additive for degradation of anti-nutritional phytate, the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive
agriculture
since the enzyme degrades phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, it might be a promising candidate as a feed additive enzyme
agriculture
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
agriculture
the phytase has the potential to be useful as an animal feed supplement. Among all the feed samples, mustard oil cake is dephytinized more efficiently than other feed samples
agriculture
the RPHY1 gene mined from rumen proves its promising candidature as a feed supplement enzyme in animal farming
agriculture
-
the phytase has the potential to be useful as an animal feed supplement
-
agriculture
-
neutral phytase is used as a feed additive for degradation of anti-nutritional phytate in aquatic feed industry. Mutant phytases D148E and S197E with increased activities and thermostabilities have application potential as additives in aquaculture feed
-
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
agriculture
Rhodotorula mucilaginosa JMUY14
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
-
agriculture
Aspergillus oryzae SBS50
-
the phytase has the potential to be useful as an animal feed supplement. Among all the feed samples, mustard oil cake is dephytinized more efficiently than other feed samples
-
agriculture
Morchella importuna SCYDJ1A1
-
since the enzyme degrades phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, it might be a promising candidate as a feed additive enzyme
-
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
agriculture
-
enzyme PHY US42 can be used as feed additive in combination with an acid phytase for monogastric animals
-
analysis
-
comparison of assay methods and the impact of assay conditions on activity estimate using the molybdenum blue method, the molybdovanadate method, and the acetone phosphomolybdate method. Nearly identical activity of PhyA is determined from the molybdenum blue method and the acetone phosphomolybdate method. The molybdenum blue method and the molybdovanadate method give only 22% difference in PhyA activity
analysis
-
comparison of assay methods and the impact of assay conditions on activity estimate using the molybdenum blue method, the molybdovanadate method, and the acetone phosphomolybdate method. The activity values of AppA2 are more variable with the three assay methods than those of Aspergillus niger PhyA. The molybdenum blue method and the molybdovanadate method produce nearly a 3fold disparity for AppA2. Overall, the pH value, the type of buffers, and the inclusion of ancillary chemicals such as the detergents Triton X-100 and BSA each account for approximately one-third of the variations of AppA2
analysis
-
screening method to elucidate the ability of different yeast strains to utilize phytic acid as sole phosphorus source. The growth test in liquid culture in a microtiter plate with phytic acid as sole phosphorus source is a reliable, fast and easy-to-use screening method
analysis
-
screening method to elucidate the ability of different yeast strains to utilize phytic acid as sole phosphorus source. The growth test in liquid culture in a microtiter plate with phytic acid as sole phosphorus source is a reliable, fast and easy-to-use screening method
analysis
-
gain of function mutants of the enzyme can be instrumental for the structure-function study of the enzyme and for industrial application
analysis
-
gain of function mutants of the enzyme can be instrumental for the structure-function study of the enzyme and for industrial application
-
biotechnology
-
a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
biotechnology
-
the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme
biotechnology
-
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
biotechnology
-
production of phytase in laboratory-scale fermenter. Maintaining an acidic environment (pH 1.5-1.8) in the fermentation broth after the initial buildup of cell mass along with proper fragmentation of filamentous fungi results in significant improvement in phytase productivity
biotechnology
-
a cross-linked enzyme aggregate (CLEA) of 3-phytase is synthesised, which is incubated with vanadate and tested as a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide as the oxidant. The results show that the 3-phytase-CLEA demonstrates a similar efficiency (ca. 95% conversion) and asymmetric induction (ca. 60%) as the free enzyme. Moreover, the 3-phytase-CLEA can be reused at least three times without significant loss of activity
biotechnology
-
to evaluate the ability of EDTA to improve phytate P utilization and the possible synergistic effect between EDTA and microbial phytase an experiment is conducted using 360 Ross 308 broiler chicks. The experiment is carried out using a completely randomized design. Four replicate of 15 chicks per each are fed dietary treatments. Phytase supplementation of P-deficient diets significantly improves weight gain and feed efficiency, but it has no effect on feed consumption. Microbial phytase supplementation significantly decreases alkaline phosphatase concentration. Results obtained suggest no synergistic effect between phytase and EDTA in broiler chicks
biotechnology
-
Pichia pastoris containing cell-surface phytase releases phosphorus from feedstuff at a level similar to secreted phytase
biotechnology
-
synthesis of a modified phytase gene with 1256 bp in length with optimal codons for expression in Pichia pastoris. A Pichia pastoris strain that expresses the modified phytase gene phyA-mod shows a 50% increase in phytase activity level
biotechnology
-
potential of using yeast as a phytase carrier in the gastrointestinal tract. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate (i.e. myo-inositol 1,2,3,4,5-pentakisphosphate) or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
food industry
-
Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
-
the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview
food industry
the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive, applicability of recombinant PPHY in dephytinization of wheat bread, overview
food industry
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
food industry
-
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
food industry
Thermothelomyces thermophilus BCRC 31852
-
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
Thermothelomyces thermophilus DSM 1799
-
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
nutrition
-
may be considered for application as an animal feed additive to assist in the hydrolysis of phytate complexes to improve the bioavailability of phosphorus in plant feedstuff
nutrition
-
complete removal of inorganic phosphate from growing pig diets coupled with phytase supplementation improves digestibility and retention of phosphor and nitrogen, thus reducing manure phosphor excretion without any negative effect on pig performance
nutrition
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
nutrition
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
nutrition
-
Pichia pastoris containing cell-surface phytase releases phosphorus from feedstuff at a level similar to secreted phytase. Pichia pastoris with phytase displayed on its surface has a great potential as a whole-cell supplement to animal feed
nutrition
use of Yersinia rohdei phytase as an attractive additive to animal feed. Compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and a potential commercial phytase from Yersinia intermedia, the Yersinia rohdei phytase is more resistant to pepsin, retains more activity under gastric conditions, and releases more inorganic phosphorus from soybean meal under simulated gastric conditions
nutrition
isozymes LlALP1 and LlALP2 have the potential to be useful as feed and food supplements
nutrition
-
the phytase has the potential to be useful as an animal feed supplement
nutrition
-
seed-specific overexpression of Aspergillus niger phytase in corn leads to transgenic corn with bioavailable phosphate. Maximal phytase activity of 125 FTU/g kernels can be obtained, 1000fold above that of the wild type, with 1000 g of kernels containing up to 67 times the feed industry requirement. An animal feeding trial demonstrated that the recombinant enzyme has similar nutritional effects on broiler chickens to a commercially available phytase product in terms of reducing inorganic phosphorus addition to feed and phosphate excretion in animal manure
nutrition
-
due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
nutrition
the enzyme is useful to reduced phytate in tandoori and naan dough for flat Indian bread, The enzymatic reduction of phytic acid will lead to the retention of the nutrients, and thus, result in a significant improvement in mineral absorption. The addition of rPPHY resulted in 67.5% and 23.2 % reduction in phytic acid content in tandoori and naan, respectively. The texture of the test breads remains as good as the control breads
nutrition
-
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
may be considered for application as an animal feed additive to assist in the hydrolysis of phytate complexes to improve the bioavailability of phosphorus in plant feedstuff
-
nutrition
-
the phytase has the potential to be useful as an animal feed supplement
-
nutrition
Rhodotorula mucilaginosa JMUY14
-
due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
-
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Schwanniomyces castellii
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Penicillium caseoicolum
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
Aspergillus syndowi
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
-
expression of phytase in a Medicago truncatula cell suspension line. Recombinant phytase accumulates to at least 25 mg/l and remaines stable along the growth curve, and an enriched fraction with high enzymatic activity is easily obtained
synthesis
expression of phytase in Glycine max under control of a root-specific promoter. The phytase activity and phosphate levels in transgenic soybean root secretions are 4.7 U/mg protein and 439 microM, respectively, compared to 0.8 U/mg protein and 120 microM, respectively, in control soybeans
synthesis
-
expression of phytase in Lactobacillus casei. The highest phytase activities in the supernatant and cells are 22.12 and 4.49 U per ml at the fourth day of incubation
synthesis
-
immobilization of enzyme via a cross-linked enzyme aggregate. The immobilized enzyme incubated with vanadate shows a similar efficiency and asymmetric induction as the free enzyme and can be used at least three times without significant loss of activity. In presence of organic solvents, the activtiy is still limited. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate
synthesis
-
immobilization of phytase on Sepabead EC-EP and use in the biodegradation of soymilk phytate. The immobilized enzyme exhibits an activity of 0.1 U per g of carrier and activity yield of 70.83%. Optimum temperature is 55°C, optimum pH for the immobilized enzyme is 5.5. Enzyme is stable between pH 3.0-8.0 and below 70°C. The immobilized enzyme hydrolyzes 65% of soymilk phytate in 8 h at 60°C, as compared with 56% hydrolysis observed for the native enzyme over the same period of time
synthesis
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the optimal medium for phytase production contains oat 10.0 g/l, ammonium sulfate 15.0 g/l, glucose 30 g/l, and NaCl 20.0 g/l, while the optimal cultivation conditions for phytase production are pH 5.0, a temperature of 28°C, and a shaking speed of 170 rpm. Under the optimal conditions, over 557.9 mU/ml of phytase activity is produced within 72 h of fermentation at the shake flask level
synthesis
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a maximal level of phytase of 113.7 U/g of dry substrate is obtained in wheat bran based medium containing 5% sucrose, 50% humidity, 7.5% of biomass at 33°C, pH 7.0 during 72 h and a 285% improvement in enzyme titre is achieved
synthesis
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a maximal level of phytase of 113.7 U/g of dry substrate is obtained in wheat bran based medium containing 5% sucrose, 50% humidity, 7.5% of biomass at 33°C, pH 7.0 during 72 h and a 285% improvement in enzyme titre is achieved
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synthesis
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
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synthesis
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the optimal medium for phytase production contains oat 10.0 g/l, ammonium sulfate 15.0 g/l, glucose 30 g/l, and NaCl 20.0 g/l, while the optimal cultivation conditions for phytase production are pH 5.0, a temperature of 28°C, and a shaking speed of 170 rpm. Under the optimal conditions, over 557.9 mU/ml of phytase activity is produced within 72 h of fermentation at the shake flask level
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synthesis
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
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additional information
PhyA115 is a beta-propeller phytase that has application potential in aquaculture feed
additional information
phytase has great potential applications not only in the areas of animal nutrition and resource conservation, but also in environmental protection and public health
additional information
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phytases show great potential for application in different sectors such as in animal nutrition, human nutrition, aquaculture, and pharmacology. These enzymes are considered as a green feed additive that can be used to neutralize the antinutritional effects of phytate, thereby increasing the bioavailability of phosphorus and other minerals. They also contribute to the reduction of environmental pollution by phosphorus
additional information
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the enzyme is useful as animal feed additive, in dephytinization of food ingredients, and bioremediation of phosphorous pollution in the environment
additional information
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phytase has great potential applications not only in the areas of animal nutrition and resource conservation, but also in environmental protection and public health
-
additional information
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PhyA115 is a beta-propeller phytase that has application potential in aquaculture feed
-
additional information
Bacillus subtilis B.S.46
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the enzyme is useful as animal feed additive, in dephytinization of food ingredients, and bioremediation of phosphorous pollution in the environment
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Release 2023.1 (January 2023)
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