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Information on EC 3.1.3.26 - 4-phytase
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3.1.3.26 4-phytaseSpecify your search results
Word Map
- 3.1.3.26
- phosphorus
-
broiler
- meal
-
phytic
- aspergillus
- ash
- bone
-
bird
- wheat
-
factorial
- tract
- niger
- soybean
- phosphatases
-
poultry
-
corn-soybean
- tibia
- corn
-
chick
- bran
- cereal
-
starter
-
digesta
-
monogastric
- xylanase
-
meal-based
-
quadratic
- flour
-
barrows
-
manure
-
antinutritional
-
excreta
- gizzard
- synthesis
-
p-deficient
-
allotted
-
grower
- hexaphosphate
-
indigestible
-
feedstuffs
- agriculture
-
sourdough
-
non-starch
- uteroferrin
-
carbohydrase
-
cereal-based
-
equivalency
-
chromic
-
antinutrient
-
coli-derived
-
wheat-based
- nutrition
- food industry
- biotechnology
-
insps
The enzyme appears in viruses and cellular organisms
Synonyms
(natto) phytase, 168phyA, 4-phytase, 6'-phytase, 6-phytase, 6-phythase, AppA, appA phytase, AppA2 phytase, AppAS, 
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-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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-
-
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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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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-ATP + H2O
?
-
250% of the activity with myo-inositol hexakisphosphate
-
?
AMP + phosphate
adenosine + phosphate
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
glucose + phosphate
-
reaction is nearly as efficient as on phytate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
50% of the activity with myo-inositol hexakisphosphate
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
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
-
-
-
?
myo-inositol-1,2,3,4,5 pentakisphosphate + H2O
?
-
12% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,2,3,4,6 pentakisphosphate + H2O
?
-
22% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,2,4,5,6 pentakisphosphate + H2O
?
-
16% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-1,3,4,5,6 pentakisphosphate + H2O
?
-
27% of the activity with myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
?
myo-inositol-5-phosphate + H2O
inositol + phosphate
-
18% of the activity with myo-inositol hexakisphosphate
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
74% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.6% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
97.1% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
39.8% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
101% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
59.6% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is nearly as efficient as on phytate
-
?
ADP + H2O
?
-
25.6% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
?
-
14.2% of the activity with myo-inositol hexakisphosphate
-
?
AMP + H2O
adenosine + phosphate
-
9.7fold higher activity than with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
25.0% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
38.8% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
22.3% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
reaction is nearly as efficient as on phytate
-
?
D-fructose 1,6-diphosphate + H2O
?
-
146% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
92.0% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
78.5% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
-
438.5% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
-
735fold higher activity than with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
50.8% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
19fold higher activity than with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
85.6% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
15fold higher activity than with myo-inositol hexakisphosphate
-
-
?
inositol-1-phosphate + H2O
inositol + phosphate
-
myo-inositol-1-phosphate, 6% of the activity with myo-inositol hexakisphosphate
-
-
?
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
-
strong affinity for sodium phytate as substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Lactobacillus coryniformis MH121153
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Lactobacillus coryniformis MH121153
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, preferred substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
product release is the rate limiting step of the reaction
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Bacillus sp. (in: Bacteria) DECSR1
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Bacillus sp. (in: Bacteria) KHU-10
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
step-wise hydrolysis of myo-inositol hexakisphosphate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
removal of 5 phosphate residues from each molecule of phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
removal of 5 phosphate residues from each molecule of phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
hydrolyzes phytate in a stepwise manner
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for phytate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
-
major degradation product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,3,4,5-pentaphosphate + phosphate
-
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
-
activity of EC 3.1.3.8, 10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
activity of EC 3.1.3.8, 10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
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
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
the phosphate from position 6 is liberated first, followed by the phosphate at positions 5 and 4, or 1 and 3
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate.
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate.
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Oryza sativa Japonica Group Himalaya
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
little activity for p-nitrophenyl phosphate above pH 4.0
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
little activity for p-nitrophenyl phosphate above pH 4.0
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
6% of the activity with myo-inositol hexakisphosphate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
84% of the activity with myo-inositol hexakisphosphate
-
?
phenyl phosphate + H2O
phenol + phosphate
-
61.7fold higher activity than with myo-inositol hexakisphosphate
-
-
-
phenyl phosphate + H2O
phenol + phosphate
-
89.2% of the activity with myo-inositol hexakisphosphate
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
additional information
?
-
-
enzyme exhibits phytase and acid phosphatase activity
-
?
additional information
?
-
-
highest activity in cells in the late stationary phase
-
-
-
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
-
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
-
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) KHU-10
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
-
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
-
additional information
?
-
Burkholderia sp. a13(2014) JCM 30421
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
-
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
hydrolysis of insoluble metal-phytates, overview. The enzyme is also active with 4-nitrophenyl phosphate, sodium diphosphate, glucose-1-phosphate, and glucose-6-phosphate
-
-
-
additional information
?
-
-
highest activity under anaerobic conditions, during the exponential growth no activity observed
-
-
-
additional information
?
-
-
undegraded phytates can cause mineral deficiencies in humans. The presence of undigested phytate in the colon may protect against the development of colonic carcinoma
-
-
-
additional information
?
-
the enzyme also shows phosphate-monoester phosphohydrolase activity, EC 3.1.3.2
-
-
-
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
-
additional information
?
-
Lactobacillus coryniformis MH121153
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
-
additional information
?
-
substrate specificity of the recombinant isozyme, overview
-
-
-
additional information
?
-
Oryza sativa Japonica Group Himalaya
substrate specificity of the recombinant isozyme, overview
-
-
-
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
-
additional information
?
-
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
-
additional information
?
-
Penicillium chrysogenum CCT 1273
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
-
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
-
additional information
?
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
-
additional information
?
-
Penicillium oxalicum KCTC6440
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
-
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
-
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
-
additional information
?
-
Rhodotorula mucilaginosa JMUY14
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
-
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
-
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
-
-
-
additional information
?
-
-
lower activity with 4-nitrophenyl phosphate, no or poor activity with AMP, ADP, ATP, GTP, NADP+, glucose 1-phosphate, and glucose 6-phosphate
-
-
-
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
additional information
?
-
-
no cleavage of myo-inositol 2-phosphate, 1,2-cyclic inositol phosphate, Na-3-glycerophosphate
-
-
-
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
-
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
-
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Burkholderia sp. a13(2014) JCM 30421
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Lactobacillus coryniformis MH121153
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium chrysogenum CCT 1273
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Penicillium oxalicum KCTC6440
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
Rhodotorula mucilaginosa JMUY14
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
Oryza sativa Japonica Group Himalaya
-
-
-
?
additional information
?
-
-
highest activity in cells in the late stationary phase
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
-
additional information
?
-
-
highest activity under anaerobic conditions, during the exponential growth no activity observed
-
-
-
additional information
?
-
-
undegraded phytates can cause mineral deficiencies in humans. The presence of undigested phytate in the colon may protect against the development of colonic carcinoma
-
-
-
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
-
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
-
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
-
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
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
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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
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stronger inhibition of acid phytase than of alkaline phytase
Al3+
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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+
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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+
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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+
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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