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Information on EC 3.1.3.26 - 4-phytase
for references in articles please use BRENDA:EC3.1.3.26
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.26 4-phytase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.1.3.26
- phosphorus
-
broiler
- meal
- aspergillus
-
phytic
- wheat
-
bird
- ash
- soybean
- phosphatases
- corn
- tibia
-
poultry
-
corn-soybean
-
starter
-
digesta
- xylanase
- bran
- cereal
-
allotted
-
monogastric
-
meal-based
-
quadratic
- flour
-
barrows
-
manure
- ileum
-
feedstuffs
-
p-deficient
- hexaphosphate
-
antinutritional
- gizzard
-
metabolizable
-
indigestible
-
grower
- synthesis
-
excreta
- agriculture
-
housed
- uteroferrin
- biotechnology
-
chromic
-
coli-derived
-
wheat-based
-
non-starch
-
equivalency
- food industry
-
cereal-based
-
insps
-
antinutrient
-
corn-based
-
sourdough
- apase
-
carbohydrase
- nutrition
Reaction Schemes
showSynonyms
phytase, purple acid phosphatase, 6-phytase, histidine acid phosphatase, ronozyme, phytase b, phya2, multiple inositol polyphosphate phosphatase, phya1, minpp, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(natto) phytase
4-phytase
6-phytase
AppA
AppA2 phytase
BIFPSEUDO_03792
Blon_0263
HAP phytase
histidine acid phosphatase
Minpp
MOK1 phytase
multiple inositol polyphosphate phosphatase
myo-inositol hexakisphosphate phosphohydrolase
myo-inositol(1,2,3,4,5,6)hexakisphosphate phosphohydrolase
myo-inositol-hexakisphosphate phosphohydrolase
myo-inositolhexakisphosphate phosphohydrolase
orf19.3727
PAP
PAP type I
PAPhys
PHO112
Phy
PhyA
PhyA2
PhyB
phytase
phytate 6-phosphatase
-
-
-
-
PJ3 phytase
purple acid phosphatase
r-PhyA170
r-PhyA86
additional information
6-phytase
-
-
-
-
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
phytase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
The product can also be designated as 1L-myo-inositol 1,2,3,4,5-pentakisphosphate when the 1L numbering is applied. Therfore the enzyme is frequently called 6-phytase.
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
phytate degradation I
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SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 4-phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-89-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phosphoglycerate + H2O
glycerate + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
5'-ATP + H2O
?
-
Substrates: 250% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
AMP + phosphate
adenosine + phosphate
-
Substrates: 43.9% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
glucose + phosphate
-
Substrates: reaction is nearly as efficient as on phytate
Products: -
Products: -
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
Substrates: 50% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
DL-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
DL-myo-inositol tetrakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
glycerol phosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol 1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
myo-inositol-2,3,4,5-tetrakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
DL-myo-inositol 1,2,3,4,5-pentakisphosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
L-myo-inositol 1,2,3,4,5-pentakisphosphate + myo-inositol 1,2,3,4,6-pentakisphosphate + myo-inositol 1,3,4,5,6-pentakisphosphate + myo-inositol 2-phosphate + D-myo-inositol 1,2-bisphosphate + L-myo-inositol 1,2-bis phosphate + L-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5 pentakisphosphate + H2O
?
-
Substrates: 12% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
Products: -
Products: -
?
myo-inositol-1,2,3,4,6 pentakisphosphate + H2O
?
-
Substrates: 22% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
Products: -
Products: -
?
myo-inositol-1,2,4,5,6 pentakisphosphate + H2O
?
-
Substrates: 16% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
Products: -
Products: -
?
myo-inositol-1,3,4,5,6 pentakisphosphate + H2O
?
-
Substrates: 27% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
Products: -
Products: -
?
myo-inositol-5-phosphate + H2O
inositol + phosphate
-
Substrates: 18% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
phenyl phosphate
phenol + phosphate
-
Substrates: -
Products: -
Products: -
?
phytate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: 74% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: 130% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: 89.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: 63.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: 97.1% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 39.8% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 11% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 11% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 101% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: 59.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: reaction is nearly as efficient as on phytate
Products: -
Products: -
?
ADP + H2O
?
-
Substrates: 25.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
ADP + H2O
?
-
Substrates: 14.2% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
alpha-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
alpha-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
-
Substrates: 9.7fold higher activity than with myo-inositol hexakisphosphate
Products: -
Products: -
?
AMP + H2O
adenosine + phosphate
-
Substrates: 25.0% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: 38.8% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: 22.3% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
ATP + H2O
?
-
Substrates: reaction is nearly as efficient as on phytate
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
beta-glycerophosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: 146% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
Substrates: 28.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
Substrates: 92.0% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: 78.5% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
diphosphate + H2O
2 phosphate
-
Substrates: 438.5% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
diphosphate + H2O
2 phosphate
-
Substrates: 735fold higher activity than with myo-inositol hexakisphosphate
Products: -
Products: -
?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
glucose 1-phosphate + H2O
glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
Substrates: -
Products: -
Products: -
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
Substrates: 50.8% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
Substrates: 19fold higher activity than with myo-inositol hexakisphosphate
Products: -
Products: -
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
Substrates: 85.6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
Substrates: 15fold higher activity than with myo-inositol hexakisphosphate
Products: -
Products: -
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
inositol pentakisphosphate + H2O
?
-
Substrates: myo-inositol pentakisphosphate
Products: -
Products: -
?
inositol-1-phosphate + H2O
inositol + phosphate
-
Substrates: -
Products: -
Products: -
?
inositol-1-phosphate + H2O
inositol + phosphate
-
Substrates: myo-inositol-1-phosphate, 6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Substrates: strong affinity for sodium phytate as substrate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Loigolactobacillus coryniformis MH121153
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Loigolactobacillus coryniformis MH121153
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
Substrates: substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: product release is the rate limiting step of the reaction
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: product release is the rate limiting step of the reaction
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: product release is the rate limiting step of the reaction
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Aspergillus syndowi
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: very specific for, no activity on other phosphate esters
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: very specific for, no activity on other phosphate esters
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: step-wise hydrolysis of myo-inositol hexakisphosphate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: removal of 5 phosphate residues from each molecule of phytate
Products: removal of 5 phosphate residues from each molecule of phytate
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: removal of 5 phosphate residues from each molecule of phytate
Products: removal of 5 phosphate residues from each molecule of phytate
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: hydrolyzes phytate in a stepwise manner
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
A0A1D7YZ01
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Penicillium caseoicolum
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: very specific for phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: very specific for phytate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
Substrates: constitutive
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: 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
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
Substrates: -
Products: major degradation product
Products: major degradation product
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
Substrates: -
Products: major degradation product, plus DL-inositol 1,2,4,5,6-pentaphosphate, DL-inositol 1,2,3,4-tetraphosphate and DL-inositol 1,2,4,6-tetraphosphate
Products: major degradation product, plus DL-inositol 1,2,4,5,6-pentaphosphate, DL-inositol 1,2,3,4-tetraphosphate and DL-inositol 1,2,4,6-tetraphosphate
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
Substrates: -
Products: activity of EC 3.1.3.8, 10-14% of product
Products: activity of EC 3.1.3.8, 10-14% of product
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
Substrates: -
Products: activity of EC 3.1.3.8, 10-14% of product
Products: activity of EC 3.1.3.8, 10-14% of product
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: the other isomers of inositol hexaphosphate are hydrolyzed at lower rate in decreasing order: myo-inositol hexakisphosphate, neo-inositol hexakisphosphate, scyllo inositol hexakisphosphate : D-chiro inositol hexakisphosphate, L-chiro inositol hexakisphosphate
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: the phosphate from position 6 is liberated first, followed by the phosphate at positions 5 and 4, or 1 and 3
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: 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.
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
Substrates: 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.
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Oryza sativa Japonica Group Himalaya
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: little activity for p-nitrophenyl phosphate above pH 4.0
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: little activity for p-nitrophenyl phosphate above pH 4.0
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: 6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
phenyl phosphate + H2O
phenol + phosphate
-
Substrates: 84% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
phenyl phosphate + H2O
phenol + phosphate
-
Substrates: 61.7fold higher activity than with myo-inositol hexakisphosphate
Products: -
Products: -
?
phenyl phosphate + H2O
phenol + phosphate
-
Substrates: 89.2% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
Substrates: -
Products: -
Products: -
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
Substrates: -
Products: -
Products: -
?
tetrasodium diphosphate + H2O
?
-
Substrates: 6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
tetrasodium diphosphate + H2O
?
-
Substrates: 6% of the activity with myo-inositol hexakisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: MINPP lacks InsP6 2-phosphohydrolase activity
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme exhibits phytase and acid phosphatase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: highest activity in cells in the late stationary phase
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Burkholderia sp. a13(2014) JCM 30421
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrolysis of insoluble metal-phytates, overview. The enzyme is also active with 4-nitrophenyl phosphate, sodium diphosphate, glucose-1-phosphate, and glucose-6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: highest activity under anaerobic conditions, during the exponential growth no activity observed
Products: -
Products: -
?
additional information
?
-
-
Substrates: undegraded phytates can cause mineral deficiencies in humans. The presence of undigested phytate in the colon may protect against the development of colonic carcinoma
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also shows phosphate-monoester phosphohydrolase activity, EC 3.1.3.2
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
Products: -
Products: -
?
additional information
?
-
Loigolactobacillus coryniformis MH121153
-
Substrates: the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of the recombinant isozyme, overview
Products: -
Products: -
?
additional information
?
-
Oryza sativa Japonica Group Himalaya
Substrates: substrate specificity of the recombinant isozyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
Products: -
Products: -
?
additional information
?
-
Penicillium chrysogenum CCT 1273
-
Substrates: the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
Products: -
Products: -
?
additional information
?
-
Substrates: among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
Products: -
Products: -
?
additional information
?
-
-
Substrates: among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Penicillium oxalicum KCTC6440
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Rhodotorula mucilaginosa JMUY14
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme hydrolyzes phytate, 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme hydrolyzes phytate, 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: lower activity with 4-nitrophenyl phosphate, no or poor activity with AMP, ADP, ATP, GTP, NADP+, glucose 1-phosphate, and glucose 6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no cleavage of myo-inositol 2-phosphate, 1,2-cyclic inositol phosphate, Na-3-glycerophosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
Products: -
Products: -
?
additional information
?
-
Substrates: the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Loigolactobacillus coryniformis MH121153
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Substrates: phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: inducible enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
Substrates: constitutive
Products: -
Products: -
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
Substrates: constitutive enzyme
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Substrates: -
Products: -
Products: -
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Oryza sativa Japonica Group Himalaya
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: highest activity in cells in the late stationary phase
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effect of sourdough on the myo-inositol phosphates levels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: highest activity under anaerobic conditions, during the exponential growth no activity observed
Products: -
Products: -
?
additional information
?
-
-
Substrates: undegraded phytates can cause mineral deficiencies in humans. The presence of undigested phytate in the colon may protect against the development of colonic carcinoma
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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%
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
Products: -
Products: -
?
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+
-
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+
Cd2+
Co2+
Cu2+
Fe2+
Hg2+
K+
Mg2+
Mn2+
Na+
Ni2+
Sr2+
Zn2+
additional information
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+
-
enhances thermal stablity and shows an impact on pH-optimum and temperature optimum
Ca2+
is found essential for both refolding and activity of the enzyme
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+
enzyme is Ca2+-dependent, drastically improves thermal stability of the enzyme
Ca2+
-
2 mM, pH 8 phytase, more than 300% activation at concentrations equimolar to the substrate, pH 8
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
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
Na+
-
a high concentration of sodium chloride affects the activity of fungal phytase in the pH 3-4 range
Na+
a high concentration of sodium chloride shifts the pH optimum to 2.0 from 5.5
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
Zn2+
-
activity rises by about 40% as the Zn2+ concentration, rises from 0.02 mM to 0.08 mM. Maximal increase in activity in 0.05 mM Zn2+
additional information
-
no effect is observed after addition of 200 mM Fe2+ or Fe3+
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
not influenced by K+, Co2+, Cr3+, Cu2+, Mg2+, Mn2+, Ag+, and Ca2+
additional information
-
not influenced by K+, Co2+, Cr3+, Cu2+, Mg2+, Mn2+, Ag+, and Ca2+
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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
p-nitrophenol
-
stronger inhibition of acid phytase than of alkaline phytase
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
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+
-
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
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 (smal intestinal digesta) phytate phosphorus hydrolysis is greatly inhibited
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 (smal intestinal digesta) phytate phosphorus hydrolysis is greatly inhibited
F-
-
10 mM NaF, pH 5 phytase is inhibited by 80%, no effect on pH 8 phytase
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
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
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
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+
-
activates at 1 mM by 15%, inhibits 16% at 5 mM, 49% at 10 mM, and 85% at 50 mM
myo-inositol hexakisphosphate
-
activity decreases with increasing concentration of myo-inositol hexakisphosphate
myo-inositol hexakissulfate
in crystal strucuture, the inhibitor is displaced from the position adopted by phytate by an average of 1.1 A over the six carbons of the inositol ring
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
PCMB
-
0.2 mM, 100% inhibition of acid phytase, 78% inhibition of alkaline phytase
Pepsin
-
loses 80% of the initial activity in the presence of 3000 units pepsin
-
phosphate
-
4.0 mM, 75.5% of phytase 1 activity, 80.2% inhibition of phytase 2 activity
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
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 of the enzyme. The 6-phytase, which is inactive in the sulfoxidation of thioanisole, show higher affinity for vanadate at pH 7.6 than at pH 5.0. 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 no peroxide-vanadate-phytase complexes are observed for the 6-phytase as seen for 3-phytase, in agreement with the inactivity of the 6-phytase for the oxidation of thioanisole
Zn2+
-
moderately inhibited by up to 2 mM ZnCl2, strongly inhibited at higher concentrations
additional information
-
inhibitory activity in decreasing order is Fe2+ > Cu2+> Mn+ > Co2+ > InS6 > Mg2+ > K+ > Zn2+ > nil addition
-
additional information
-
recombinant enzyme is inhibited by antibody raised against a 20-mer internal peptide
-
additional information
highly resistant to pepsin or trypsin treatment
-
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
poor inhibition by Co2+ and Al3+ at 5 mM
-
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
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
-
additional information
the mutant V162L shows increased sensitivity to cleavage by pepsin (loss of 73% activity) compared to the wild-type (loss of 35% activity), while the sensitivity to trypsin is unaltered. 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
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% 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
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 80
-
0.1% v/v, activates up to 167% for PI fraction and 137% for PII fraction
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
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
additional information
-
the strain shows increased phytase activity in a culture medium with 40 g/l sucrose, KH2P04 providing 5 mg/l phosphorus, and cultivation temperature of 24°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
AIDS Dementia Complex
Purple acid phosphatase of human brain macrophages in AIDS encephalopathy.
Alveolitis, Extrinsic Allergic
Hypersensitivity pneumonitis caused by occupational exposure to phytase.
Amebiasis
Structure-Function Relationship Study of a Secretory Amoebic Phosphatase: A Computational-Experimental Approach.
Asthma, Occupational
Response to a case of occupational asthma due to the enzymes phytase and beta-glucanase.
Bacterial Infections
Potential immune-modulatory effects of wheat phytase on the performance of a mouse macrophage cell line, Raw 264.7, exposed to long-chain inorganic polyphosphate.
Blepharospasm
Scientific skepticism and new discoveries: an analysis of a report of zinc/phytase supplementation and the efficacy of botulinum toxins in treating cosmetic facial rhytides, hemifacial spasm and benign essential blepharospasm.
Bone Diseases
Crystallization and preliminary X-ray diffraction studies of mammalian purple acid phosphatase.
Bone Resorption
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle.
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.
Bone Resorption
Recombinant human and mouse purple acid phosphatases: expression and characterization.
Breast Neoplasms
Differential expression of tartrate-resistant acid phosphatase isoforms 5a and 5b by tumor and stromal cells in human metastatic bone disease.
Coccidiosis
Effects of phytase supplementation in broiler diets on a natural Eimeria challenge in naive and vaccinated birds.
Coccidiosis
Impact of coccidiostat and phytase supplementation on gut microbiota composition and phytate degradation in broiler chickens.
Coccidiosis
The interactive effect of phytase and coccidia on the gross lesions as well as the absorption capacity of intestine in broilers fed with diets low in calcium and available phosphorous.
Coccidiosis
The interactive effects of Eimeria acervulina infection and phytase for broiler chicks.
Coccidiosis
Utility of Feed Enzymes and Yeast Derivatives in Ameliorating Deleterious Effects of Coccidiosis on Intestinal Health and Function in Broiler Chickens.
Dehydration
Importance of inositols and their derivatives in cowpea under root dehydration: An omics perspective.
Dermatitis
Effect of dietary calcium concentrations in low non-phytate phosphorus diets containing phytase on growth performance, bone mineralization, litter quality, and footpad dermatitis incidence in growing broiler chickens.
Enteritis
Dietary calcium, phosphorus, and phytase effects on bird performance, intestinal morphology, mineral digestibility, and bone ash during a natural necrotic enteritis episode.
Enteritis
Influence of dietary calcium level, calcium source, and phytase on bird performance and mineral digestibility during a natural necrotic enteritis episode.
Enteritis
Influence of meat and bone meal, phytase, and antibiotics on broiler chickens challenged with subclinical necrotic enteritis: 1. growth performance, intestinal pH, apparent ileal digestibility, cecal microbiota, and tibial mineralization.
Enteritis
Influence of meat and bone meal, phytase, and antibiotics on broiler chickens challenged with subclinical necrotic enteritis: 2. intestinal permeability, organ weights, hematology, intestinal morphology, and jejunal gene expression.
Enteritis
Interactive effect of 2 dietary calcium and phytase levels on broilers challenged with subclinical necrotic enteritis: part 1-broiler performance, gut lesions and pH, bacterial counts, and apparent ileal digestibility.
Enteritis
Interactive effect of dietary calcium and phytase on broilers challenged with subclinical necrotic enteritis: 3. Serum calcium and phosphorus, and bone mineralization.
Enteritis
Interactive effect of dietary calcium and phytase on broilers challenged with subclinical necrotic enteritis: part 2. Gut permeability, phytate ester concentrations, jejunal gene expression, and intestinal morphology.
Enteritis
Over-processed meat and bone meal and phytase effects on broilers challenged with subclinical necrotic enteritis: Part 1. Performance, intestinal lesions and pH, bacterial counts and apparent ileal digestibility.
Enteritis
Over-processed meat and bone meal and phytase effects on broilers challenged with subclinical necrotic enteritis: Part 2. Inositol phosphate esters hydrolysis, intestinal permeability, hematology, jejunal gene expression and intestinal morphology.
Enteritis
Over-processed meat and bone meal and phytase effects on broilers challenged with subclinical necrotic enteritis: Part 3. Bone mineralization and litter quality.
Hypersensitivity
Occupational allergy to phytase: case series of eight production workers exposed to animal feed additives.
Infections
Catalytic properties of wheat phytase that favorably degrades long-chain inorganic polyphosphate.
Infections
Effects of phytase supplementation in broiler diets on a natural Eimeria challenge in naive and vaccinated birds.
Infections
Genome-wide analysis of H3K4me3 and H3K27me3 modifications due to Lr28 for leaf rust resistance in bread wheat (Triticum aestivum).
Infections
Influence of meat and bone meal, phytase, and antibiotics on broiler chickens challenged with subclinical necrotic enteritis: 2. intestinal permeability, organ weights, hematology, intestinal morphology, and jejunal gene expression.
Infections
The effects of 1,25-dihydroxycholecalciferol and phytase on the natural phytate phosphorus utilization by laying hens.
Infections
The interactive effects of Eimeria acervulina infection and phytase for broiler chicks.
Infections
Wheat phytase can alleviate the cellular toxic and inflammatory effects of lipopolysaccharide.
Malnutrition
Effects of neonatal undernutrition and subsequent nutritional rehabilitation or administration of thyroxine and hydrocortisone on the inositol phosphatase activities in rat intestine.
Malnutrition
Effects of nutritional deficiencies during neonatal and post-weaning period on rat intestinal phytase and phosphatase activities.
Malnutrition
Effects of postweaning protein malnutrition on intestinal inositol phosphatase activities in normally weaned and neonatally undernourished rats.
Neoplasm Metastasis
Differential expression of tartrate-resistant acid phosphatase isoforms 5a and 5b by tumor and stromal cells in human metastatic bone disease.
Neoplasms
Possible relevance between prohormone convertase 2 expression and tumor growth in human adrenocorticotropin-producing pituitary adenoma.
Newcastle Disease
Effects of phytate and phytase on the performance and immune function of broilers fed nutritionally marginal diets.
Osteochondrodysplasias
Effects of phytase and 1,25-dihydroxycholecalciferol on phytate utilization and the quantitative requirement for calcium and phosphorus in young broiler chickens.
Osteochondrodysplasias
Influence of dietary phytase supplementation on incidence and severity in broilers divergently selected for tibial dyschondroplasia.
Osteochondrodysplasias
Phytase in broiler rations--effects on carcass yields and incidence of tibial dyschondroplasia.
Osteoporosis
Identification of purple acid phosphatase inhibitors by fragment-based screening: Promising new leads for osteoporosis therapeutics.
Osteoporosis
Identification of Purple Acid Phosphatase Inhibitors by Fragment-Based Screening: Promising New Leads for Osteoporosis Therapeutics.
Osteoporosis
Purple acid phosphatase inhibitors as leads for osteoporosis chemotherapeutics.
Osteoporosis
Synthesis, evaluation and structural investigations of potent purple acid phosphatase inhibitors as drug leads for osteoporosis.
Pituitary ACTH Hypersecretion
Possible relevance between prohormone convertase 2 expression and tumor growth in human adrenocorticotropin-producing pituitary adenoma.
Porcine Reproductive and Respiratory Syndrome
Effects of high inclusion of soybean meal and a phytase superdose on growth performance of weaned pigs housed under the rigors of commercial conditions.
Protein Deficiency
Effects of neonatal undernutrition and subsequent nutritional rehabilitation or administration of thyroxine and hydrocortisone on the inositol phosphatase activities in rat intestine.
Protein Deficiency
Effects of nutritional deficiencies during neonatal and post-weaning period on rat intestinal phytase and phosphatase activities.
Rhinitis
Occupational allergy to phytase: case series of eight production workers exposed to animal feed additives.
Rickets
Additive effects of 1,25-dihydroxycholecalciferol and phytase on phytate phosphorus utilization and related parameters in broiler chickens.
Rickets
Dietary 1,25-dihydroxycholecalciferol supplementation increases natural phytate phosphorus utilization in chickens.
Rickets
Effects of phytase and 1,25-dihydroxycholecalciferol on phytate utilization and the quantitative requirement for calcium and phosphorus in young broiler chickens.
Rickets
Experimental approach to optimize phytate phosphorus utilization by broiler chickens by addition of supplements.
Rickets
The effect of several organic acids on phytate phosphorus hydrolysis in broiler chicks.
Rickets
The role of vitamin D and intestinal phytase in the prevention of rickets in rats on cereal diets.
Starvation
Characterization of low phosphorus insensitive mutants reveals a crosstalk between low phosphorus-induced determinate root development and the activation of genes involved in the adaptation of Arabidopsis to phosphorus deficiency.
Starvation
Characterization of Purple Acid Phosphatase Family and Functional Analysis of GmPAP7a/7b Involved in Extracellular ATP Utilization in Soybean.
Starvation
Cloning and characterization of phosphorus starvation inducible Brassica napus PURPLE ACID PHOSPHATASE 12 gene family, and imprinting of a recently evolved MITE-minisatellite twin structure.
Starvation
Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition
Starvation
GmPAP12 Is Required for Nodule Development and Nitrogen Fixation Under Phosphorus Starvation in Soybean.
Starvation
Phytase activity in tobacco (Nicotiana tabacum) root exudates is exhibited by a purple acid phosphatase.
Starvation
The phosphorus source phytate changes the composition of the cell wall proteome in Bacillus subtilis.
Starvation
Transition state regulator AbrB inhibits transcription of Bacillus amyloliquefaciens FZB45 phytase through binding at two distinct sites located within the extended phyC promoter region.
Vitamin D Deficiency
Effect of phytate feeding with & without protein & vitamin D deficiencies on intestinal phytase activity in rat.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A, pH 4.5, 37°C
0.033
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A/T305E, pH 4.5, 37°C
0.092
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant T305E, pH 4.5, 37°C
0.161
myo-inositol 1,2,3,4,5,6-hexakisphosphate
wild-type, pH 4.5, 37°C
0.171
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304E, pH 4.5, 37°C
0.016
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 4.5, at 37°C
0.01945
myo-inositol hexakisphosphate
pH 5.0, 37°C, recombinant wild-type enzyme, substrate is sodium phytate
0.0386
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M citrate buffer at pH 5.5 and 37°C
0.09
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 3.2
0.13
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 2.5
0.17
myo-inositol hexakisphosphate
A0A1D7YZ01
Vmax: 1714 micromol/min/mg
0.1773
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M citrate buffer at pH 5.5 and 37°C
0.18
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
0.186
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 6.0, at 37°C
0.22
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
0.2278
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
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
0.3219
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
0.382
myo-inositol hexakisphosphate
-
recombinant wild-type enzyme, pH 2.5, 40°C
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
0.54
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 3.2
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
0.7
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
0.77
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 3.2
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
1
myo-inositol hexakisphosphate
recombinant enzyme, in 0.1 M sodium acetate buffer (pH 4.5) at 37°C
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
1.5
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
1.8
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
4.72
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5
4.79
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5
0.054
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
0.35
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
0.36
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73S, pH 4.5, 37°C
0.53
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73D, pH 4.5, 37°C
0.61
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73E, pH 4.5, 37°C
0.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73T, pH 4.5, 37°C
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Line-Weaver Burk plot
-
additional information
additional information
-
Michealis-Menten kinetics
-
additional information
additional information
-
Lineweaver-Burk plots
-
additional information
additional information
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
additional information
additional information
-
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
231
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
10.5
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A, pH 4.5, 37°C
12.5
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A/T305E, pH 4.5, 37°C
128
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304E, pH 4.5, 37°C
1689
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant T305E, pH 4.5, 37°C
10209
myo-inositol 1,2,3,4,5,6-hexakisphosphate
wild-type, pH 4.5, 37°C
0.52 - 0.7
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
0.63
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5
3.17
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 2.5
3.5
myo-inositol hexakisphosphate
-
mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 3.2
5.7
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
9.3
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 3.2
17
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 3.2
23.8
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5
40.67
myo-inositol hexakisphosphate
-
mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5
43.97
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
44.83
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M citrate buffer at pH 5.5 and 37°C
80.74
myo-inositol hexakisphosphate
-
mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C
88.83
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5
123.1
myo-inositol hexakisphosphate
-
wild type enzyme, in 0.2 M citrate buffer at pH 5.5 and 37°C
279.3
myo-inositol hexakisphosphate
phytic acid dipotassium salt
655
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 6.0, at 37°C
720
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
2230
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
6931
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 4.5, at 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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
320
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A, pH 4.5, 37°C
380
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304A/T305E, pH 4.5, 37°C
700
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant D304E, pH 4.5, 37°C
18000
myo-inositol 1,2,3,4,5,6-hexakisphosphate
mutant T305E, pH 4.5, 37°C
64000
myo-inositol 1,2,3,4,5,6-hexakisphosphate
wild-type, pH 4.5, 37°C
3272.7
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
12389
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
428
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
661
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73T, pH 4.5, 37°C
1199
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73E, pH 4.5, 37°C
1554
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73D, pH 4.5, 37°C
6017
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73S, pH 4.5, 37°C
6776
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
Ca2+
-
free, not complexed with phytate, competitive inhibitor
2.3
phytate
-
free, not complexed with Ca2+, competitive inhibitor
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.53
1350
-
native enzyme from Penicillium chrysogenum strain CCT 1273, pH 5.0, 50°C
2860
-
recombinant enzyme from Penicillium griseoroseum strain T73, pH 5.0, 50°C
2982
purified recombinant nonglycosylated enzyme expressed from Escherichia coli, pH 5.5, 37°C
3960
with 4 mM sodium phytate in 0.25 M sodium acetate buffer, pH 4.5, at 37°C
967
purified recombinant glycosylated enzyme expressed from Pichia pastoris, pH 5.5, 37°C
987
substrate 4-nitrophenyl phosphate, mutant L28C/W360C, pH 5.5, 37°C
additional information
additional information
-
specific activity of the purified protein: 8.7 U/mg
additional information
-
specific activity of the purified protein: 8.5-9 U/mg
additional information
-
specific activity of the purified protein: 8.7 U/mg
additional information
-
phytic acid content and phytase activity vary significantly among cultivars and market classes, ranging from 16.7 to 25.1 g/kg and from 224 to 361 phytase activity (liberation of inorganic phosphate) micromol/min/kg of sample, respectively
additional information
-
phytase activity is found intracellularly while no activity is detected in the culture liquid
additional information
-
phytase production is practically absent in the exponential phase and reaches a maximum in the late stationary phase
additional information
-
specific activity of the purified protein: 8.7 U/mg
additional information
compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and Yersinia intermedia, the Yersinia rohdei phytase is more resistant to pepsin, retains more activity under gastric conditions, and releases more inorganic phosphorus (two to ten times) from soybean meal under simulated gastric conditions
additional information
-
compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and Yersinia intermedia, the Yersinia rohdei phytase is more resistant to pepsin, retains more activity under gastric conditions, and releases more inorganic phosphorus (two to ten times) from soybean meal under simulated gastric conditions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
3.5
4 - 4.5
4 - 5
4.5
4.5 - 5
4.7
4.8
5 - 5.5
5 - 6
5.2
5.5
6.5
7 - 7.5
7.2
7.5
2
a high concentration of sodium chloride shifts the pH optimum to 2.0 from 5.5
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
4
-
and a second lower optimum at pH 2.5, reaction with 4-nitrophenyl phosphate, native and recombinant enzyme
4.5
-
enzyme expressed from synthetic gene encoding Peniophora lycii phytase and expressed in methylotrophic yeast Pichia pastoris
4.5 - 5
-
broad pH-activity profile with three maxima at pH 3, 4.5-5 and 6
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
1.8 - 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 - 4.5
2 - 5.5
2 - 6
2.5 - 5
2.5 - 6
-
pH 2.5: about 35% of maximal activity, pH 6.0: about 25% of maximal activity, recombinant enzyme
2.5 - 8.5
activity range, profile overview, over 50% of activity at pH 3.5-6.5
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 - 5.7
-
pH 3.0: about 30% of maximal activity, pH 5.7: about 70% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
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
-
pH 3.5: about 40% of maximal activity, pH 5.5: about 75% of maximal activity
3.5 - 5.5
3.5 - 6
-
pH 3.5: about 50% of maximal activity, pH 6.0: about 40% of maximal activity, enzyme expressed from synthetic gene encoding Peniophora lycii phytase and expressed in methylotrophic yeast Pichia pastoris
3.5 - 7
-
pH 3.5: about 35% of maximal activity, pH 7.0: about 70% of maximal activity, reaction with phytate
3.8 - 5.8
-
pH 3.8: about 55% of maximal activity, pH 5.8: about 70% of maximal activity
4 - 5
4 - 5.7
-
pH 4.0: about 65% of maximal activity, pH 5.7: about 75% of maximal activity
4 - 6
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 - 7.5
-
pH 4.0: about 45% of maximal activity, pH 7.5: about 45% of maximal activitry, Q27T mutant enzyme, phytate as substrate
4.2 - 5.3
-
pH 4.2: about 70% of maximal activity, pH 5.3: about 50% 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 - 6
-
pH 4.5: about 45% of maximal activity, pH 6.0: about 60% of maximal activity
4.7 - 6.5
-
at 55°C, about 90% of maximal activity at pH 6.5 and pH 6.6, at 30°C about 80% of maximal activity
5 - 10
-
pH 5.0: about 50% of maximal activity, pH 10.0: about 80% of maximal activity, presence of 10 mM CaCl2
6 - 8
6 - 9
-
about 40% of maximal activity at pH 6.0 and 9.0, hydrolysis of myo-inositol hexakisphosphate
9 - 11
-
pH 9.0: about 50% of maximal activity, pH 11.0: about 25% of maximal activity, hydrolysis of p-nitrophenyl phosphate
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
-
maximal activity at pH 5.0 followed by pH 2.0 (73% of maximal activity), no activity at pH 7.0-8.0
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
-
pH 2.5: about 45% of maximal activity, pH 5.0: about 20% of maximal activity, reaction with 4-nitrophenyl phosphate, recombinant enzyme
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 - 5.5
-
pH 3.5: about 90% of maximal activity, pH 5.5: 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
-
pH 4.0: about 35% of maximal activity, pH 6.0: about 50% of maximal activity, myo-inositol hexakisphosphate as substrate
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 40% of maximal activity, pH 6.0: about 50% of maximal activity, reaction with phytate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
40 - 45
45
50
50 - 55
55
55 - 60
58
60
65
70
75 - 80
50
-
enzyme expressed from synthetic gene encoding Peniophora lycii phytase and expressed in methylotrophic yeast Pichia pastoris
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
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 - 60
20 - 75
20 - 80
activity range of wild-type and mutant enzyme, profile overview
25 - 55
-
over 50% of maximal activity within this range, maximal activity at 50°C, inactive at 60°C
25 - 60
-
25°C: about 45% of maximal activity, 60°C: about 35% of maximal activity
25 - 70
30 - 70
30 - 80
-
30°C: about 40% of maximal activity, 80°C: about 55% of maximal activity, presence of 10 mM CaCl2
33 - 63
-
33°C: about 40% of maximal activity, 63°C: about 70% of maximal activity
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 - 60
-
35°C: enzyme from PI fraction shows about 40% of maximal activity, enzyme from PII fraction shows about 45% of maximal activity, 50°C: enzyme from PII fraction shows about 50% of maximal activity, 60°C, enzyme PI fraction shows about 40% of maximal activity, enzyme from PII fraction shows about 10% 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 - 65
-
45°C: about 45% of maximal activity, 65°C: about 45% of maximal activity, enzyme expressed from synthetic gene encoding Peniophora lycii phytase and expressed in methylotrophic yeast Pichia pastoris
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
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
57 - 65
-
57°C: maximal activity, 65°C: about 35% of maximal activity
additional information
20 - 60
-
20°C: about 55% of maximal activity, 60°C: about 75% of maximal activity
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
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.94
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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. 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
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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
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.
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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.
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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
BCC18313 (TR86), 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
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 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.
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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
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.
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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.
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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.
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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 (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; 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
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
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.
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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 (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
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
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.
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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.
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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 (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
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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
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.
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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.
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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 (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
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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 (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
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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 (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; DSMZ 18074, 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
A0A1D7YZ01
UniProt
brenda
strains KTU05-8 and KTU05-9, isolated from spontaneous Lithuanian rye sourdoughs
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-
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
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
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.
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-
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.
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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 (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
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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 (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
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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 (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
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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.
-
-
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.
-
-
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.
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brenda
Bacteroides ruminicola, isolated from Mehsani buffalo rumen
UniProt
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
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.
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-
brenda
BCC18081 (TR170), 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
UniProt
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.
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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.
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-
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
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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 (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
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-
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 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 (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.
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
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 (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; 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
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 (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
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 (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
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
recombinantly expressed in Saccharomyces cerevisiae, Pichia pastoris or Pseudomonas fluorescens
-
-
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 (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
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 (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
UniProt
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
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
Thunb. Cv. Nellie White, 2 enzyme forms pH 5 phytase and pH 8 phytase
-
-
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
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
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.
-
-
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.
-
-
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
metagenome-derived phytase, metagenome derived from subsurface groundwater
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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.
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
-
phytase increases markedly at the late stationary phase
brenda
-
phytase increases markedly at the late stationary phase
-
brenda
-
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
-
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
-
phytase synthesized early in germination persists for several days in the cotyledon
brenda
recombinant enzyme in culture medium of Bacillus subtilis
brenda
-
synthetic gene encoding Peniophora lycii phytase expressed in methylotrophic yeast Pichia pastoris
brenda
-
one of the phytases is already present in mature ungerminated lily pollen and the other one is newly synthesized during germination from a long-lived, pre-existing mRNA
brenda
phytase mRNA and phytase activity increases during seed development, consistent with the use of an embryonic promoter
brenda
grain, the enzyme is expressed during barley seed development
brenda
-
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.
brenda
-
activity is greatest in duodenum and lowest in ileum
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
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
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
-
brenda
-
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
-
brenda
-
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
-
brenda
recombinant enzyme expressed in Escherichia coli
brenda
-
recombinant enzyme expressed in Escherichia coli
-
brenda
integral membrane protein
brenda
-
integral membrane protein
-
brenda
-
integral membrane protein
-
brenda
-
integral membrane protein
-
brenda
additional information
-
the enzyme sequence contains a signal peptide and a signal peptide cleavage site
-
brenda
additional information
Penicillium chrysogenum CCT 1273
-
the enzyme sequence contains a signal peptide and a signal peptide cleavage site
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
hydrolysis leads initially to one predominant InsP5 species, presumably 1D-myo-Ins(1,2,3,4,5)P5. Further hydrolysis yields 1D-myo-Ins(2,3,4,5)P4 as the predominant InsP4 intermediate. Initial hydrolysis of phytate by AppA leads to almost complete conversion to InsP5 before breakdown of this intermediate begins. Residue D304 plays a crucial role in stereospecificity by influencing the size and polarity of specificity pockets A and B
physiological function
additional information
evolution
-
the enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
-
the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
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 enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
-
the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP
-
evolution
Burkholderia sp. a13(2014) JCM 30421
-
the enzyme sequence contains histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family
-
evolution
Loigolactobacillus coryniformis MH121153
-
the enzyme belongs to the histidine acid phosphatase (HAP) family
-
evolution
Penicillium chrysogenum CCT 1273
-
the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
-
malfunction
disruption of Candida albicans orf19.3727 leads to decreased phytase activity, reduced ability to form hyphae, attenuated in vitro adhesion, and reduced ability to penetrate human epithelium, which are the major virulence attributes of this yeast
malfunction
-
disruption of Candida albicans orf19.3727 leads to decreased phytase activity, reduced ability to form hyphae, attenuated in vitro adhesion, and reduced ability to penetrate human epithelium, which are the major virulence attributes of this yeast
-
physiological function
transgenic expression in Brassica napus. 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 59% when compared to wild-type. When phytate is used as the sole phosphate source, phosphate accumulation in seeds increases by 47. 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
the enzyme encoded by orf19.3727 of Candida albicans plays a key role in fungal pathogenesis, functional role of orf19.3727 in yeast-to-hyphal morphogenesis, adhesion, and in vitro virulence. Candida albicans orf19.3727 contributes to phytase activity and is crucial for hyphal growth, adhesion, and cellular invasion, and ultimately to its pathogenic potential
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 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
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 encoded by orf19.3727 of Candida albicans plays a key role in fungal pathogenesis, functional role of orf19.3727 in yeast-to-hyphal morphogenesis, adhesion, and in vitro virulence. Candida albicans orf19.3727 contributes to phytase activity and is crucial for hyphal growth, adhesion, and cellular invasion, and ultimately to its pathogenic potential
-
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
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
-
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
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
catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are 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 R44, R48, D115, R119, H333, and D334, overview
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 has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis
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 modeling and computational analysis of Penicillium oxalicum strain KCTC6440 PhyA, comparison to the structure of phytase PhyA from Penicillium oxalicum strain PJ3
additional information
requirement of a thiol group for the activity
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
-
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
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
Burkholderia sp. a13(2014) JCM 30421
-
requirement of a thiol group for the activity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHYA_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
461
0
51296
Swiss-Prot
-
B1GSN6_BACIU
383
0
41863
TrEMBL
other Location (Reliability: 2)
B7GTV0_BIFLS
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
623
0
66984
TrEMBL
-
C0BTR1_BIFPS
639
0
68679
TrEMBL
Secretory Pathway (Reliability: 3)
C4PKL2_HORVU
544
0
60298
TrEMBL
other Location (Reliability: 3)
H9TUK5_HAFAL
446
0
48875
TrEMBL
Secretory Pathway (Reliability: 4)
PHYA_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
465
0
50836
Swiss-Prot
-
PHYA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
463
0
51816
Swiss-Prot
-
O00096_TALTH
466
0
51451
TrEMBL
Secretory Pathway (Reliability: 3)
PHYA_THETO
487
0
52538
Swiss-Prot
Secretory Pathway (Reliability: 1)
PHYA_ASPNG
467
0
51086
Swiss-Prot
Secretory Pathway (Reliability: 3)
PHYA_ASPAW
467
0
51075
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q003Y3_CITAM
436
0
48823
TrEMBL
other Location (Reliability: 2)
Q0ZQI5_9FIRM
342
0
38475
TrEMBL
Mitochondrion (Reliability: 5)
Q6RK08_ECOLX
432
0
47042
TrEMBL
Secretory Pathway (Reliability: 3)
Q96VK8_9APHY
442
0
47552
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
40000
42000
44000
45000
46000
47000
490000
51000
x * 75000, native protein, x * 51000, deglycosylated protein, SDS-PAGE
59000
62000
64000
65000
66000
67000
71000
72000
75000
x * 75000, native protein, x * 51000, deglycosylated protein, SDS-PAGE
76000
85000 - 100000
90000
additional information
-
protein band with MW of 66000 Da and 123000 Da are detected in PI fraction. A protein band with MW 96000 Da is detected in PII fraction
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
66000
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
-
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 * 75000, native protein, x * 51000, deglycosylated protein, SDS-PAGE
?
-
x * 75000, native protein, x * 51000, deglycosylated protein, SDS-PAGE
-
?
x * 59000-65000, recombinant glycosylated enzyme from Pichia pastoris, SDS-PAGE, x * 45000, recombinant deglycosylated enzyme from Pichia pastoris, SDS-PAGE
?
x * 63000, recombinant His-tagged enzyme, SDS-PAGE, x * 47750, sequence calculation
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 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
monomer
Oryza sativa Japonica Group Himalaya
-
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
-
additional information
-
SDS-PAGE gives two broad bands in the regions 73000 Da and 100000 Da
additional information
-
a broad protein band of 85000-100000 Da is observed after SDS-PAGE
additional information
-
a broad proptein band of 85000-100000 Da is observed after SDS-PAGE
additional information
molecular modeling using the crystal structure, overview
additional information
-
molecular modeling using the crystal structure, overview
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
-
the phytase/alkaline phosphatase of the intestine contains only the complex type of N-linked oligosaccharide, the 90000 Da subunit contains O-linked oligosaccharide chains with an apparent molecular mass of 11000 Da. The 70000 Da subunit does not contain oligosaccharide chains
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
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 8 N-glycosylation sites
glycoprotein
Oryza sativa Japonica Group Himalaya
-
the monomeric enzyme is glycosylated to different degrees, the isozyme contains 8 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
-
possesses 10 N-glycosylation sites containing heterogeneous glycans, which constitute more than 20% of the total mass
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
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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
-
crystal structure of the phytase from Bacillus amyloliquefaciens DS11 demonstrate that a negatively charged active site provides a favorable electrostatic environment for the positively charged calcium-phytate complex
-
determined at 2.1 A resolution in partially and fully Ca2+-loaded states. Two calcium ions form a biocalcium center where the Asp308 carboxylate serves as a bridging arm, stabilizing the circular arrangement of the propeller structure. Three calcium ions at the active site form a triadic calcium center and neutralize an otherwise negatively charged calcium cage surrounded by a total of six aspartate and glutamate residues. The top of the molecular structure forms a shallow cleft that is lined predominantly with negatively charged side chains. The calcium-occupied cleft turns into a favorable electrostatic environment for the binding of phytate together with nearby Lys76, Lys77, Arg122, and Lys179. In addition, Ca2+ participates in catalysis directly by binding the phosphate group(s) of the substrate. Ca2+ reduces the negative charge around the active site cleft such that phytate neutralized by Ca2+ can easily fit to the active site
-
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
-
in complex with inhibitor myo-inositol hexakissulfate, to 1.72 A resolution
apo-enzyme, to 1.9 A resolution, and in complex with substrate analogue myo-inositiol hexakissulfate, to 1.59 A resolution. Te 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
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
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
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
E228K
-
shows a shift of the pH optimum to 3.8 and 266% greater hydrolysis of soy phytate at pH 3.5 than the wild type enzyme
E228K/K300R/K301E
-
shows large increase in the phytase activity ratio at pH 3.5 over pH 5.5
E272K
-
activity optimum at pH 3.2, shows improvement in substrate affinity
E89D/H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
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
K300E/K301E
-
greater improvement in relative activity at pH 3.5 and lower specific activity than the wild type enzyme
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
K94E/K300E/K301E
-
greater improvement in relative activity at pH 3.5 and lower specific activity than the wild type enzyme
E272K
-
activity optimum at pH 3.2, shows improvement in substrate affinity
-
E89D/R297Q
-
mutant enzyme from strain T213, 2.6fold increase in activity
-
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
-
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
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
-
D258A
-
turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme
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
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
Y159A
D55A
-
turnover number of mutant enzyme is 0.21% 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
-
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
-
D144N/V227A
38% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D
mutant releases 25% more inorganic phosphorus from soy phytate than the wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D/D112N
7% higher specific activity than wild-type, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S/S209G
23% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme
D144N/V227A/G344D/K46E
similar efficiency for soy phytate hydrolysis as compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/K65E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D304A
proton donor motif variant, displays exclusive 1D-1/3-phytase activity
D304E
proton donor motif variant, shows marked reduction in stereospecificity
G73D
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73E
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73L
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73S
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73T
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73Y
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
L28C/W360C
mutant contains additional disulfide bond to enhance thermal stability. Activity is similar to the wild-type
Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
-
highly active phytase with no loss of activity after heating at 62°C for 1 h and 27% of its initial activity after 10 min at 85°C, which is a significant improvement over the appA parental phytase. The mutant enzyme also shows a 3.5fold enhancement in gastric stability
S392F
site-directed mutagenesis, three-dimensional structure analysis, modeling, and comparison to wild-type structure. The mutant phytase shows 12.8%, 9.6% and 10.3% higher phytase activity at pH 6, 7 and 8, respectively, compared to wild-type enzyme, and the mutant enzymes shows thermostability improvement of 74% and 78.4% at 80°C and 90°C, respectively, compared to wild-type
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
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
V162L
site-directed mutagenesis, the mutant shows increased sensitivity to pepsin in contrast to the less sensitive wild-type enzyme
additional information
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
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
Y159A
-
turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme
Y159A
-
turnover number of mutant enzyme is 0.19% of that of the wild-type 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
-
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
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
additional information
-
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
additional information
-
construction of gene disruption null mutants of orf19.3727 of both chromosomal copies by PCR-based gene targeting method, PCR using gene-specific primers and plasmids pFA-ARG4 or pFA-HIS1. The ura3 auxotrophy in the null mutants was recovered by integrating plasmid CIp10 (carries URA3) into the RPS10 locus. Candida albicans orf19.3727 reintegrants are created by transforming full-length orf19.3727 into the null mutants. Phenotypes, overview
-
additional information
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
additional information
-
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
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
-
mutations of genes grrA and grrS, encoding GacA/GacS-like 2-component global regulatory system, or in gene rpoS encoding the sigma factor RpoS subunit of RNA polymerase, leads to a deficiency in phytase production. Introduction into mutants of the respective wild-type genes cloned into the wide-range plasmid pJFF224-NX under the control of the bacteriophage T4 gene 32 promoter complements this deficiency
additional information
-
mutations of genes grrA and grrS, encoding GacA/GacS-like 2-component global regulatory system, or in gene rpoS encoding the sigma factor RpoS subunit of RNA polymerase, leads to a deficiency in phytase production. Introduction into mutants of the respective wild-type genes cloned into the wide-range plasmid pJFF224-NX under the control of the bacteriophage T4 gene 32 promoter complements this deficiency
-
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 7
purified recombinant His-tagged enzyme, over 50% activity remaining
1.5 - 2.5
enzyme retains above 80% of activity after incubation at pH 2.5-8.0 for 60 min
2 - 12
-
purified native enzyme, over 65% activity remains after 96 h
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
2 - 8
2.5
2.5 - 8
3 - 10
3 - 5
-
after gastric incubation at pH 5.0 the phytase has retained 100% of its activity, during the gastric incubations at pH 4.0 and 3.0 phytase activity is significantly reduced
3 - 8
-
purified recombinant enzyme, 2 h at room temperature, completely stable
6
-
purified enzyme, loss of 60% activity after 120 min, and of all activity after 240 min
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)
additional information
the enzyme shows a recovery of 45% activity when it is preincubated at pH 3.0 and 37°C for 6 h prior to phytase assay
2.5
-
purified recombinant His-tagged wild-type enzyme, 37°C, half-life is 2 h (for mutant rPhyA6DB 5.4 h)
2.5 - 8
enzyme retains above 80% of activity after incubation at pH 2.5-8.0 for 60 min
2.5 - 8
enzyme retains above 80% of activity after incubation at pH 2.5-8.0 for 60 min
3 - 10
more than 85% of the total activity is retained after incubation at pH 3.0 to 10.0 for 1 h
3 - 10
A0A1D7YZ01
activity is stable over a wide range of pH, more than 80% of the total activity is retained after incubation at pH 3.0-10.0 at 37°C for 60 min
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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 - 80
-
purified native enzyme, over 70% activity remains after 180 h
100
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
40
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
49
50
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
55
60
60 - 80
enzyme activity is above 60% after treatment at 80°C for 10 min, and 54% of the activity is retained at 80°C for 15 min
62
-
1 h, no loss of activity, mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
65
70
75
75.7
-
Tm-value for mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
80
85
90
95
additional information
100
-
a minor increase of wild type enzyme activity is observed after 1 min, after 5 and 20 min at 100°C the activity is reduced to 4% and 1% of the initial activity
100
-
purified recombinant enzyme, pH 2.0, after 20 min inactivation, loss of 50% activity after 4 min
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
37
-
1 h, 90% loss of activity, 81-85% protection when heated in presence of myo-inositol hexakisphosphate, glucose 6-phosphate or phosphate
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
50
-
30 min, in presence of sodium myo-inositol hexakisphosphate or p-nitrophenyl phosphate, 1 mM Mg2+, 0.04 M Tris-succinate buffer, pH 7.0, less than 10% inactivation
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
-
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
60
-
1 min incubation at 60°C does not negatively affect the phytase activity of the wild type enzyme
60
-
60 min: 40% loss of activity of phytase IA, 30% loss of activity of phytase IB, 25% loss of activity of phytase IC, 30% loss of activity of phytase ID, 10% loss of activity of phytase II
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 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
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
-
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
20 min, almost complete loss of activity for wild-type, about 50% residual activity for mutant L28C/W360C
70
10 min, about 15% loss of activity, in presence of 1 mM Ca2+
70
-
60 min: 65% loss of activity of phytase IA, 55% loss of activity of phytase IB, 60% loss of activity of phytase IC, 58% loss of activity of phytase ID, 40% loss of activity of phytase II
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
20 min, almost complete loss of activity for wild-type, about 50% residual ativity for mutant L28C/W360C
80
10 min, about 35% loss of activity, in presence of 1 mM Ca2+
80
-
about 50% of its original activity remains after incubation at 80°C for 10 min in the presence of 10 mM CaCl2
80
-
60 min: 90% loss of activity of phytase IA, 80% loss of activity of phytase IB, 92% loss of activity of phytase IC, 88% loss of activity of phytase ID, 80% loss of activity of phytase II
80
-
enzyme expressed from synthetic gene encoding Peniophora lycii phytase expressed in methylotrophic yeast Pichia pastoris, 75% loss of activity after 10 min
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 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, 27% loss of activity,mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
85
20 min, almost complete loss of activity for wild-type, 47% residual activity for mutant L28C/W360C
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
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
more than 50% activity is retained after heating at 100°C for 10 min
additional information
more than 50% activity is retained after heating at 100°C for 10 min
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
-
phyL exhibits high thermal stability, even at a lower calcium concentration, as it is able to recover 80% of its original activity after denaturation at 95 °C for 10 min
additional information
the enzyme upon denaturation for 10 min at 75, 85 and 95°C, followed by 1 h renaturation at the room temperature (28°C) in the presence of 5 mmol/l Ca2+, restores 86%, 54%, and 37% activity
additional information
in the presence CaCl2, PHY US417 recoveres 77% of its activity after incubation at 75°C for 10 min. In the absence of calcium, even so PHY US417 is absolutely stable when incubated for 30 min at 50°C it retains only 22% of activity after 10 min at 60°C
additional information
-
in the presence CaCl2, PHY US417 recoveres 77% of its activity after incubation at 75°C for 10 min. In the absence of calcium, even so PHY US417 is absolutely stable when incubated for 30 min at 50°C it retains only 22% of activity after 10 min at 60°C
additional information
A0A1D7YZ01
enzyme retains stability when incubated at 50°C for 30 min, and over 70% activity retain. Enzyme loses activity rapidly at higher temperatures, with more than 90% activity lost after incubating at 70°C for 2 min
additional information
-
enzyme retains stability when incubated at 50°C for 30 min, and over 70% activity retain. Enzyme loses activity rapidly at higher temperatures, with more than 90% activity lost after incubating at 70°C for 2 min
additional information
-
T1/2 of 16 h at 60°C and 1.5 h at 80°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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 expressed in Pichia pastoris is not inactivated by pelleting above 80°C, enzyme expressed in Saccharomyces cerevisiae and Pseudomonas fluorescens are inactivated by pelleting above 80°C
-
strong resistance to proteases, with 90% of activity remaining after treatment with pepsin and trypsin at 37°C for 60 min
the enzyme can withstand repeated freezing and thawing without appreciable loss of acticity
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
-
the role of disulfide bridges in the folding of Aspergillus niger PhyB is investigated using dynamic light scattering. Guanidinium chloride (1 M) unfolds phytase. Its removal by dialysis refolds the protein. Tris(2-carboxyethyl)phosphine (TCEP) reduces the refolding activity by 68%. The hydrodynamic radius of PhyB phytase decreases from 5.5 to 4.14 nm when the protein is subjected to 1.0 M GuCl concentration. The active homodimer, is reduced to a monomer
-
the enzyme can withstand repeated freezing and thawing without appreciable loss of acticity
-
the enzyme can withstand repeated freezing and thawing without appreciable loss of acticity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Q Sepharose XL FPLC column chromatography and Sephacryl S-200 HR gel filtration
native enzyme 14.22fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration, to homogeneity
-
native enzyme 9.53fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
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 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 from culture medium 486.41fold by ammonium sulfate fractionation, cation and anion exchange chromatography, and dialysis
partial
purified by ultrafiltration and Macro-Prep high S-cation exchange chromatography
purified to homogeneity using acetone precipitation followed by ion-exchange and gel-filtration column chromatography
-
recombinant enzyme
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 wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange 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 wild-type and mutant enzymes from Pichia pastoris strain GS115 by gel filtration to homogeneity
soluble screted recombinant enzyme 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 optimal medium for phytase production contained oat 10.0 g/l, NH4SO4 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
-
the transformant with phy is cultivated in the bioreactor. The cell mass obtained after 9 h of cultivation is 26.81 g wet weight per litre yielding 4289 U (micromol/min) enzyme activity when compared to 1.978 g wet weight per litre mass producing 256 U (micromol/min) activity in shake-flask cultures
ultrafiltration, DEAE-cellulose column chromatography, and Sephadex G-100 gel filtration
-
using ammonium sulfate precipitation and anion exchange chromatography
using fast-performance liquid chromatography (FPLC) using a PL aquagel-OH 40 column from Agilent
using NH4SO4 precipitation and a HiTrap Q Sepharose XL FPLC column
A0A1D7YZ01
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
using ammonium sulfate precipitation and anion exchange chromatography
using ammonium sulfate precipitation and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
enzyme is expressed in a Medicago truncatula cell suspension line. Enzymatically active recombinant phytase is produced and secreted into the culture medium. Recombinant phytase accumulate to at least 25 mg/l and remains stable along the growth curve, and an enriched fraction with high enzymatic activity is easily obtained
-
expressed in Escherichia coli
expressed in Pichia pastoris
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 oryzae
expression in Pichia pastoris
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
-
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, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene appA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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 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, recombinant expression in Penicillium griseoroseum strain PG63 protoplasts from vectorpAN-52-1-phy. Transformant T73 contains the phy gene integrated in at least three sites of the genome and shows the highest, 5.1fold increase in phytase activity in comparison to the host strain
-
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 phyA, DNA and amino acid sequence determination and analysis
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 strain HMS174 (DE3), subcloning in Escherichia coli strain JM109
high level expression of a synthetic gene encoding Peniophora lycii phytase in methylotrophic yeast Pichia pastoris
-
orf19.3727 or gene PHO112, DNA and amino acid sequence determination and analysis
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability
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
phytase is heterologously expressed in the methylotrophic yeast Pichia pastoris under both the Pichia pastoris inducible alcohol oxidase (AOX1) promoter and the constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. Maximum production levels obtained are 476 U/ml, with the AOX1 expression system and 16.5 U/ml with the GAP one. These productions correspond to a 320fold and a 10fold overexpression of the protein, respectively, as compared to the homologous production
recombinantly expressed as active extracellular, glycosylated proteins in Pichia pastoris
recombinantly expressed in Pichia pastoris
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)
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability
-
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability
-
recombinantly expressed as active extracellular, glycosylated proteins in Pichia pastoris
recombinantly expressed as active extracellular, glycosylated proteins in Pichia pastoris
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
food industry
nutrition
synthesis
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
-
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
-
the enzyme is suitable for supplementing animal feeds to improve the availability of phosphate from phytate
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
-
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
-
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
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
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
-
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
actopic expressing of phytase during seed development offers an effective strategy for improving phosphorus availability in seeds. The ability to reduce the amount of phytate in seed will improve nutrient availability for animal feed
agriculture
the RPHY1 gene mined from rumen proves its promising candidature as a feed supplement enzyme in animal farming
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
-
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
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
-
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
-
ten bean cultivars are evaluated for variability in phytate, phenolic, and mineral contents, phytase activity, and antioxidant properties to elucidate the relationship of these components. Multivariate data analysis performed on 22 components analyzed in this study using principal component analysis and cluster methods demonstrate that differences in phytase, antioxidant activity, mineral contents, and bioavailability are much larger within market class than among bean cultivars
biotechnology
-
phytase from Bacillus subtilis is introduced into the cytoplasm of tobacco cells that results in equilibrium shift of inositol biosynthesis pathway, thereby making more phosphate available for primary metabolism. The transgenic line exhibit phenotypic changes like increased flowering, lower seed IP6/IP5 ratio, and enhanced growth under phosphate starvation conditions compared to wild type
biotechnology
-
phytase from Bacillus subtilis (168phyA) is constitutively expressed in tobacco and Arabidopsis to generate transgenic plants capable of utilizing exogenous phytate. In tobacco, phytase activities in transgenic leaf and root extracts are seven to eight times higher than those in wild-type extracts; whereas, the extracellular phytase activities of transgenic plants are enhanced by four to six times. Similar results are observed from the transgenic Arabidopsis. These results may offer a new perspective on mobilizing soil phytate into inorganic phosphate for plant uptake
biotechnology
-
phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract
biotechnology
Yersinia rohdei phytase is an attractive additive to animal feed
biotechnology
-
high levels of stable phytase is expressed in the culture medium of transgenic Medicago truncatula cell suspension cultures
biotechnology
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
biotechnology
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
biotechnology
-
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
-
biotechnology
-
in vitro digestibility tests show recombinantly expressed phytase is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed and is therefore suitable sources of phytase supplement
-
biotechnology
-
phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract
-
biotechnology
-
ten bean cultivars are evaluated for variability in phytate, phenolic, and mineral contents, phytase activity, and antioxidant properties to elucidate the relationship of these components. Multivariate data analysis performed on 22 components analyzed in this study using principal component analysis and cluster methods demonstrate that differences in phytase, antioxidant activity, mineral contents, and bioavailability are much larger within market class than among bean cultivars
-
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 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 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
-
phytase addition to low non-phytate phosphorus diets for broilers linearly increases the pH value and Ca and P solubilities in both digesta and diets subjected to an in vitro digestion procedure. Higher doses of microbial phytase increase Zn and Fe solubilities in both digesta and in vitro digestion procedure. Myo-inositol supplementation of the diet has no effect on mineral solubility, but decreases the pH of the in vitro digestion procedure
food industry
-
application of phytase in degrading the phytate in corn, soybean meal, and complete corn-soybean meal diet to myo-inositol phosphate esters (IP1-IP5) and completely dephosphorylated myo-inositol rings using an in vitro model of the poultry upper gastrointestinal tract. The phytase hydrolyzes phytate efficiently to small myo-inositol phosphate esters, whereas the myo-inositol level remains constant between control and phytase treatments
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
-
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
-
moderate decrease of pH by sourdough fermentation is sufficient to reduce phytate content of whole wheat flour through endogenous phytase activity
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
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
-
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
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
-
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
Aspergillus syndowi
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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
production of mutant L28C/W360C in Pichia pastoris is much lower than the wild-type enzyme due to the presence of the extra non-consecutive disulfide bond. Coexpression of protein disulfide bond isomerase increases production of the mutant protein by about 12fold
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
-
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