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Information on EC 3.1.3.72 - 5-phytase
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3.1.3.72 5-phytaseIUBMB Comments
The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P3.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
phyasrl, phytaseed, phytate phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline phytase
phosphatase, phytate
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-
-
-
phytase
phytase novo L
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-
-
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phytaseed
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-
-
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phytate phosphatase
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-
-
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phytase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoric ester hydrolysis
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-
-
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SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 5-phosphohydrolase
The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P3.
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CAS REGISTRY NUMBER
COMMENTARY
37341-58-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
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-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
hydrolysis of the phosphate ester at the D-5 position
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
high substrate specificity for phytic acid
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
high substrate specificity for phytic acid
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
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myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
symmetrical product, only isomer of IP5 as product
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
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enzyme activity may be regulated by the intracellular Ca2+ concentration
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
important component of phytic acid metabolism, constitutive enzyme
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
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phytic acid is a major component of seeds and pollen grains, localized in membrane-bound phytic-rich granules
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?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
myo-inositol-1,2,3,4,5,6-hexakisphosphate is identical with phytic acid
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-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
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-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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5% relative activity
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-
?
additional information
?
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myo-inositol pentakisphosphates are no good substrates, terminal hydrolysis to myo-inositol trisphosphate
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?
additional information
?
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two subsequent dephosphorylations occur adjacent to the D-5 hydroxyl group to yield myo-inositol-1,2,3-trikisphosphate as the final product, rates of removal of the second and third phosphates are significantly lower, possibly due to reduced specificity for IP5 and IP4 and inhibition by the phosphate released, IP4: only one isomer, either I-1,2,3,4-P4 or its enantiomer I-1,2,3,6-P4, no further hydrolysis of IP3
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-
?
additional information
?
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the tyrosine phosphatase (PTP)-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica dephosphorylates myo-inositol hexakisphosphate (Ins P(6)) in vitro preferentially cleaving the 5-phosphate position. Enzyme PhyAsrl has a general specificity for polyphosphorylated myo-inositol substrates, but can also dephosphorylate molecules containing high energy diphosphate bonds in vitro. It can produce Ins(2)P via a highly unique and ordered pathway of sequential dephosphorylation: Ins P(6), Ins(1,2,3,4,6)P(5), D-Ins(1,2,3,6)P(4), Ins(1,2,3)P(3), and D/L-Ins(1,2)P(2)
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?
additional information
?
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the tyrosine phosphatase (PTP)-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica dephosphorylates myo-inositol hexakisphosphate (Ins P(6)) in vitro preferentially cleaving the 5-phosphate position. Enzyme PhyAsrl has a general specificity for polyphosphorylated myo-inositol substrates, but can also dephosphorylate molecules containing high energy diphosphate bonds in vitro. It can produce Ins(2)P via a highly unique and ordered pathway of sequential dephosphorylation: Ins P(6), Ins(1,2,3,4,6)P(5), D-Ins(1,2,3,6)P(4), Ins(1,2,3)P(3), and D/L-Ins(1,2)P(2)
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-
?
additional information
?
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the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
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?
additional information
?
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no activity with riboflurin phosphate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
enzyme activity may be regulated by the intracellular Ca2+ concentration
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
-
important component of phytic acid metabolism, constitutive enzyme
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
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phytic acid is a major component of seeds and pollen grains, localized in membrane-bound phytic-rich granules
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Na+
Ca2+
-
at concentrations equimolar to the substrate: 313% activation, but inhibitory at higher concentrations
Ca2+
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activates, enzyme retains low level of activity even in Ca2+-free medium
Ca2+
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activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity, 10 mM EGTA prevents the calcium effect
Ca2+
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activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity, 10 mM EGTA prevents the calcium effect
Ca2+
-
activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity, 10 mM EGTA prevents the calcium effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
at concentrations equimolar to the substrate: 313% activation, but inhibitory at higher concentrations
Ca2+
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activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity
Ca2+
-
activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity
Ca2+
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activates at a concentration equal to the substrate, but higher concentrations result in the precipitation of the substrate as calcium phytate and strongly inhibit enzyme activity
EDTA
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at 1 mM inhibits the enzyme activity up to 90% and completely at 5 mM concentration
additional information
the recombinant enzyme shows resistance to trypsin
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additional information
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MnSO4, CaCl2, MgSO4, NaCl, KCl, BaCl2 and CoCl2 show insignificant effect on enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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sucrose poorly supports phytase production. Maximal phytase yield is obtained with 2% (v/v) inoculum, phytase activity decreases at lower and higher inoculum concentrations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant non-glycosylated enzyme expressed from Escherichia coli
0.22
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 non-glycosylated enzyme expressed from Escherichia coli
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 non-glycosylated enzyme expressed from Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2982
purified recombinant non-glycosylated enzyme expressed from Escherichia coli, pH 5.5, 37°C
967
purified recombinant glycosylated enzyme expressed from Pichia pastoris, pH 5.5, 37°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 8.5
activity range, profile overview, over 50% of activity at pH 3.5-6.5
3.5 - 8.5
-
is catalytically active under alkaline pH range 8-10, showing 90% of the optimal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
vars. Pinto, Navy, Red Kidney, Chili No. 494071, Netherlands No. 477020 and 486345, Black Beauty Turtle, Black Turtle G-0681 and T-39
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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localized in mature pollen, germination results in a rapid increase of enzyme that persists at the higher level for at least 6 h
brenda
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at the inner surfaces of storage bodies, the phytin-containing organelles in pollen, integral component of the membrane
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). Q0ZQJ3_SELRU
321
0
35729
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
?
x * 59000-65000, recombinant glycosylated enzyme from Pichia pastoris, SDS-PAGE, x * 45000, recombinant deglycosylated enzyme from Pichia pastoris, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
60
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ca. 80% activity at pH 8.0 for up to 3 h in the presence/absence of 5 mM CaCl2. In the presence/absence of 5 mM CaCl2, phytase is also stable at 80°C and shows ca. 100% of residual activity for 30 min at pH 8.0 and then declines sharply thereafter
55
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10 min, 60% loss of activity in assay containing CaCl2, compared to 40% in absence of CaCl2
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in absence of Triton X-100, very little enzyme activity is extracted from seeds
partial purification, extraction with 0.1% Triton X-100 increases recovery by nearly 4fold
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recombinant non-glycosylated 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
recovery is most complete when detergent or phospholipase C is included in extracting medium
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selective precipitation by heat and ammonium sulfate followed by anion exchange and chromatofocusing chromatography and gel filtration, purified 3300fold, to homogeneity
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in absence of Triton X-100, very little enzyme activity is extracted from seeds
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in absence of Triton X-100, very little enzyme activity is extracted from seeds
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in absence of Triton X-100, very little enzyme activity is extracted from seeds
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 non-glycosylated protein and of extracellular nontagged enzyme in Pichia pastoris strain GS115(his4) under control of the AOX1 promoter as glycosylated protein
gene phyAsrl, DNA and amino acid sequence determination and analysis, phyAsrl is constitutively expressed
recombinant extracellular expression of Lilium longiflorum alkaline phytase in Pichia pastoris strain X33. For analysis of the influence of the native signal sequences on alpha-MF-directed secretion, three expression constructs are generated by inserting three forms of rLlAlp2 downstream of the alpha-MF secretion signal in pPICZaAvectors: 1. full length optimized rLlAlp2 sequence (pPICZaA-op-rLlAlp2), 2. truncated oprLlAlp2 without QKTEL at the C-terminus (pPICZaA-op-LlAlp2DC), and 3. truncated op-rLlAlp2 without the first 19 aa at the N-terminus and without QKTEL at the C-terminus (pPICZaA-oprLlAlp2DNDC). By switching from the strong, tightly regulated promoter PAOX1 to the weaker, constitutive promoter PGAP and optimizing culture conditions, an 8 to 10fold increase in extracellular expression of rLlALP2 is achieved, optimization of culture conditions for enhanced expression, method evaluation, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
synthesis
transgenic expression in Pichia pastoris. Increasing isoform Alp2 copy number is detrimental to heterologous expression, clones with one copy of wild-type Alp2 produce the highest activity, clones with two, four and seven or more copies produce 70%, 25% and 10% respectively, of enzyme activity. Use of a sequence-optimized Alp2 gene increases the yield of the active enzyme by 25-50% in one/two copy clones. Reducing the temperature during heterologous expression leads to increases of 1.2-20fold suggesting that protein folding and post-translational processes may be the dominant factors limiting ALP2 expression
agriculture
-
partially purified enzyme shows properties that are suitable for animal feed applications
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REF.
AUTHORS
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JOURNAL
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