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1-L-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
?
-
-
-
-
?
1-L-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O
?
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
2-glycerophosphate + H2O
glycerate + phosphate
2-naphthyl phosphate + H2O
2-naphthol + phosphate
2-phosphoglycerate + H2O
glyceric acid + phosphate
-
-
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
5'-ATP + H2O
?
-
250% of the activity with myo-inositol hexakisphosphate
-
?
6-phosphogluconate + H2O
gluconate + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
alpha-glycerophosphate + H2O
glycerol + phosphate
-
78% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
AMP + phosphate
adenosine + phosphate
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
ADP + phosphate
beta-glycerophosphate + H2O
glycerol + phosphate
CTP + H2O
CDP + phosphate
-
352% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-fructose 6-phosphate + H2O
fructose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 3-phosphate + H2O
glucose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
glucose + phosphate
-
reaction is nearly as efficient as on phytate
-
?
D-ribose 5-phosphate + H2O
?
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
dATP + H2O
? + phosphate
-
31% of the activity with 4-nitrophenylphosphate
-
-
?
dATP + H2O
dADP + phosphate
-
338% relative activity compared to myo-inositol hexakisphosphate
-
-
?
dCTP + H2O
? + phosphate
-
35% of the activity with 4-nitrophenylphosphate
-
-
?
dCTP + H2O
dCDP + phosphate
-
367% relative activity compared to myo-inositol hexakisphosphate
-
-
?
dGTP + H2O
? + phosphate
-
52% of the activity with 4-nitrophenylphosphate
-
-
?
dGTP + H2O
dGDP + phosphate
-
189% relative activity compared to myo-inositol hexakisphosphate
-
-
?
di-sodium phenyl phosphate dihydrate + H2O
?
-
111.85% activity compared to myo-inositol hexakisphosphate
-
-
?
diphosphate + H2O
2 phosphate
dTTP + H2O
? + phosphate
-
37% of the activity with 4-nitrophenylphosphate
-
-
?
dTTP + H2O
dTDP + phosphate
-
389% relative activity compared to myo-inositol hexakisphosphate
-
-
?
fructose 1,6-bisphosphate + H2O
?
-
-
-
?
fructose 1,6-diphosphate + H2O
?
glucose 1-phosphate + H2O
glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
glycerol 2-phosphate + H2O
glycerol + phosphate
glycerol 3-phosphate + H2O
glycerol + phosphate
GTP + H2O
GDP + phosphate
-
271% relative activity compared to myo-inositol hexakisphosphate
-
-
?
inositol 1-monophosphate + H2O
inositol + phosphate
-
58% activity compared to myo-inositol hexakisphosphate
-
-
?
inositol 2-monophosphate + H2O
inositol + phosphate
-
84% activity compared to myo-inositol hexakisphosphate
-
-
?
inositol bisphosphate + H2O
?
inositol monophosphate + H2O
inositol + phosphate
inositol pentaphosphate + H2O
?
-
-
-
-
?
inositol tetraphosphate + H2O
?
inositol triphosphate + H2O
?
L-tyrosine phosphate + H2O
L-tyrosine + phosphate
-
142% relative activity compared to myo-inositol hexakisphosphate
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
myo-inositol 2,4,5,6-tetrakisphosphate + H2O
myo-inositol 2,4,6-trisphosphate + phosphate
myo-inositol hexakisphosphate + 3 H2O
myo-inositol 2,4,6-trisphosphate + 3 phosphate
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
? + phosphate
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
1D-myo-inositol-1,2,4,5,6-pentakisphosphate + phosphate
although the PhyK homolog AppA is biochemically characterized as a 6-phytase, a co-crystal structure shows the phytate 3-phosphate as scissile group in a similar position to in the active site of PhyK
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,4,5,6-pentakisphosphate + phosphate
although the PhyK homolog AppA is biochemically characterized as a 6-phytase, a co-crystal structure shows the phytate 3-phosphate as scissile group in a similar position to in the active site of PhyK
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
58.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
O-phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
28% of the activity with 4-nitrophenylphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phenyl phosphate
phenol + phosphate
phenyl phosphate + H2O
phenol + phosphate
phosphoenolpyruvate + H2O
pyruvate + phosphate
phytate + H2O
? + phosphate
polyphosphate + H2O
?
-
-
-
-
?
pyridoxal phosphate + H2O
pyridoxal + phosphate
-
-
-
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
-
-
-
-
?
rice bran + H2O
? + phosphate
soybean meal + H2O
? + phosphate
-
-
-
-
?
tetrasodium diphosphate + H2O
?
-
6% of the activity with myo-inositol hexakisphosphate
-
?
UTP + H2O
UDP + phosphate
-
350% relative activity compared to myo-inositol hexakisphosphate
-
-
?
additional information
?
-
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
74% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
2.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
89.6% of the activity with myo-inositol hexakisphosphate
-
?
2-glycerophosphate + H2O
glycerate + phosphate
-
127% of the activity with myo-inositol hexakisphosphate
-
-
?
2-glycerophosphate + H2O
glycerate + phosphate
-
19.8% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
2-glycerophosphate + H2O
glycerate + phosphate
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
4.9% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
97.1% of the activity with myo-inositol hexakisphosphate
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
69% of the activity with 4-nitrophenylphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
95% activity compared to myo-inositol hexakisphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
95% activity compared to myo-inositol hexakisphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
168% relative activity compared to myo-inositol hexakisphosphate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
phytase activity detection using 4-methylumbelliferyl phosphate as substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
254% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
254% 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
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
39.8% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
11% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
101% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
7.6% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
23.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
7.6% of the activity with myo-inositol hexakisphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
0.65% 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
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
59.6% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is nearly as efficient as on phytate
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
ADP + H2O
?
-
-
-
-
?
ADP + H2O
?
-
25.6% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
?
-
75% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
?
-
75% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
?
-
7.5% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ADP + H2O
?
-
7.5% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ADP + H2O
?
-
14.2% of the activity with myo-inositol hexakisphosphate
-
?
ADP + H2O
? + phosphate
-
50% of the activity with 4-nitrophenylphosphate
-
-
?
ADP + H2O
? + phosphate
-
177% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
80% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
80% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
103% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
-
0.02% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
? + phosphate
-
130% of the activity with myo-inositol hexakisphosphate
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
120% activity compared to myo-inositol hexakisphosphate
-
-
?
ADP + H2O
AMP + phosphate
-
206% relative activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
173% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
173% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
no activity
-
-
?
AMP + H2O
adenosine + phosphate
10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
50% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
50% activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
9.6% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
AMP + H2O
adenosine + phosphate
143% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
30% relative activity compared to myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
25.0% of the activity with myo-inositol hexakisphosphate
-
?
AMP + H2O
adenosine + phosphate
-
195% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
-
-
-
?
ATP + H2O
?
-
38.8% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
50% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
50% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
?
-
5.6% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
ATP + H2O
?
-
22.3% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
reaction is nearly as efficient as on phytate
-
?
ATP + H2O
? + phosphate
-
256% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
97% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
97% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
208% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
-
0.26% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
-
256% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
133% activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
365% relative activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
76.67% activity compared to myo-inositol hexakisphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
76.67% activity compared to myo-inositol hexakisphosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
146% of the activity with myo-inositol hexakisphosphate
-
?
D-fructose 1,6-diphosphate + H2O
?
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
202.19% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
202.19% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
poor substrate
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
228% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
228% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
35% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
35% activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
8.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
8.1% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
158% of the activity with myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
229% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
5% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
poor substrate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
strong preference for glucose 1-phosphate over phytate, under physiological conditions glucose 1-phosphate is its most likely substrate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
76.72% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
92.0% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
20% of the activity with 4-nitrophenylphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
190% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
190% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
78.5% of the activity with myo-inositol hexakisphosphate
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
82% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
128% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
57% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
poor substrate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
73.75% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
73.75% activity compared to myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
0.39% of the activity with myo-inositol hexakisphosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
217% of the activity with myo-inositol hexakisphosphate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
50% of the activity with myo-inositol hexakisphosphate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
75% relative activity compared to myo-inositol hexakisphosphate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
poor substrate
-
-
?
diphosphate + H2O
2 phosphate
-
95% of the activity with 4-nitrophenylphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
Na-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
Na-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
438.5% of the activity with myo-inositol hexakisphosphate
-
?
diphosphate + H2O
2 phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
-
12.3% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
fructose 1,6-diphosphate + H2O
?
-
12.3% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
fructose 1,6-diphosphate + H2O
?
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
2.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
2.7% of the activity with myo-inositol hexakisphosphate, recombinant enzyme
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
50.8% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
less than 10% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
98% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
85.6% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
141% of the activity with myo-inositol hexakisphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
43% of the activity with 4-nitrophenylphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
GTP + H2O
?
-
-
-
?
inositol bisphosphate + H2O
?
-
-
-
-
?
inositol bisphosphate + H2O
?
-
-
-
-
?
inositol monophosphate + H2O
inositol + phosphate
-
-
-
-
?
inositol monophosphate + H2O
inositol + phosphate
-
-
-
-
?
inositol tetraphosphate + H2O
?
-
almost the same activity as with myo-inositol hexakisphosphate
-
-
?
inositol tetraphosphate + H2O
?
-
-
-
-
?
inositol triphosphate + H2O
?
-
40% of the activity with myo-inositol hexakisphosphate
-
-
?
inositol triphosphate + H2O
?
-
-
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
myo-inositol-2,4,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol 2,4,5,6-tetrakisphosphate + H2O
myo-inositol 2,4,6-trisphosphate + phosphate
-
-
-
-
?
myo-inositol 2,4,5,6-tetrakisphosphate + H2O
myo-inositol 2,4,6-trisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + 3 H2O
myo-inositol 2,4,6-trisphosphate + 3 phosphate
-
enzyme efficiently hydrolyzes Ca2+-phytate salts and yields myo-inositol 2,4,6-trisphosphate and three phosphate groups as final products
-
-
?
myo-inositol hexakisphosphate + 3 H2O
myo-inositol 2,4,6-trisphosphate + 3 phosphate
-
enzyme efficiently hydrolyzes Ca2+-phytate salts and yields myo-inositol 2,4,6-trisphosphate and three phosphate groups as final products
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
a mixture of two pentaphosphates: the major component is 1-myo-inositol 1,2,4,5,6-pentakisphosphate and the other is 1-myo-inositol 1,2,3,4,5-pentakisphosphate
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
about 85% of myo-inositol hexakisphosphate in soybean meal is hydrolyzed by the enzyme whereas only 67% of the myo-inositol hexakisphosphate in cottonseed meal is hydrolyzed by the same enzyme treatment
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
94776, 114252, 114253, 114257, 114258, 114264, 114273, 114279, 134797, 677690, 677774, 678749, 679568 -
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
calcium myo-inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
dodecasodium myo-inositol hexakisphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
100% relative activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
preferred substrate, 100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
preferred substrate, 100% activity
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Schwanniomyces castellii
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
Torulopsis candida
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
sodium salt
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
best substrate is calcium phytate, sodium phytate results in 60% activity compared to calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
best substrate is calcium phytate, sodium phytate results in 60% activity compared to calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
highest activity at 2.05 mM substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
highest activity at 2.05 mM substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid, sodium phytate is preferred compared to calcium phytate and potassium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytic acid, sodium phytate is preferred compared to calcium phytate and potassium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
KM873028
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
KM873028
highly preferred substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
substrate is calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
substrates are sodium phytate, potassium phytate, and calcium phytate. Highest activity with calcium phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytase
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytase
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
i.e. phytate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
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
-
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, 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
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
absolutely specific for the substrate, the phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol pentakisphosphate + phosphate
-
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
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + 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
-
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
Aspergillus syndowi
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
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
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
very specific for, no activity on other phosphate esters
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
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
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
step-wise hydrolysis of myo-inositol hexakisphosphate
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
hydrolyzes phytate in a stepwise manner
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Penicillium caseoicolum
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + 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
-
-
-
?
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 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
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
Schwanniomyces castellii
-
constitutive
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
after 10 min D-myo-inositol 1,2,4,5,6-pentakisphosphate is the major degradation product, accompanied by small amounts of D-myo-inositol 1,2,3,4,6-pentakisphosphate, D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate. After 30 min, the quantity of D-myo-inositol 1,2,4,5,6-pentakisphosphate decreases and the levels of D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate increases. After 90 min the major products are Ins(1,3,5) P3 and Ins(2,4,6)P3
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
after 10 min D-myo-inositol 1,2,4,5,6-pentakisphosphate is the major degradation product, accompanied by small amounts of D-myo-inositol 1,2,3,4,6-pentakisphosphate, D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate. After 30 min, the quantity of D-myo-inositol 1,2,4,5,6-pentakisphosphate decreases and the levels of D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate increases. After 90 min the major products are Ins(1,3,5) P3 and Ins(2,4,6)P3
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
step-wise dephosphorylation occurs via 1. D-myo-inositol 1,2,4,5,6-pentakisphosphate, 2. D-myo-inositol 1,2,5,6-tetrakisphosphate or D-myo-inositol 2,4,5,6-tetrakisphosphate, 3. D-myo-inositol 1,2,6-trisphosphate, D-myo-inositol 1,2,3-trisphosphate or D-myo-inositol 1,4,5-trisphosphate, 4. myo-inositol 1,2-bisphosphate or myo-inositol 2,5-bisphosphate, myo-inositol 4,5-bisphosphate or myo-inositol 2,4-bisphosphate. Myo-inositol 2-monophosphate is the final product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
DL-inositol 1,2,4,5,6-pentaphosphate + phosphate
-
10-14% of product
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
7% of the activity with 4-nitrophenylphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
sodium salt
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate disodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol hexakisphosphate sodium salt + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + sodium phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
cleavage initiation in the dephosphorylation of myo-inositol hexakisphosphate at C3
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
substrate Na-phytate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
substrate Na-phytate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
-
25% of the activity with 4-nitrophenylphosphate
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
135% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
135% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the enzyme shows 22.5% activity towards p-nitrophenyl phosphate compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
311% relative activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
152.95% activity compared to myo-inositol hexakisphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
152.95% activity compared to myo-inositol hexakisphosphate
-
-
?
phenyl phosphate
phenol + phosphate
-
-
-
?
phenyl phosphate
phenol + phosphate
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
84% of the activity with myo-inositol hexakisphosphate
-
?
phenyl phosphate + H2O
phenol + phosphate
-
188% relative activity compared to myo-inositol hexakisphosphate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
89.2% of the activity with myo-inositol hexakisphosphate
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
92% of the activity with 4-nitrophenylphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
130% activity compared to myo-inositol hexakisphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
130% activity compared to myo-inositol hexakisphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
328% relative activity compared to myo-inositol hexakisphosphate
-
-
?
phytate + H2O
?
-
-
-
-
?
phytate + H2O
?
-
-
-
-
?
phytate + H2O
?
-
Na- and Ca-phytate, the first results in higher activity, substrate binding analysis by molecular modelling of phytate inside the active site, residue K77 is able to form two hydrogen bonds with the two phosphate groups on the phytate, whereas in case of K77R, the guanidinium group of arginine is able to form up to 4 H-bonds with the two phosphate groups
-
-
?
phytate + H2O
?
-
-
-
-
?
phytate + H2O
?
-
Na- and Ca-phytate, the first results in higher activity, substrate binding analysis by molecular modelling of phytate inside the active site, residue K77 is able to form two hydrogen bonds with the two phosphate groups on the phytate, whereas in case of K77R, the guanidinium group of arginine is able to form up to 4 H-bonds with the two phosphate groups
-
-
?
phytate + H2O
?
-
-
-
-
?
phytate + H2O
? + phosphate
-
-
-
-
?
phytate + H2O
? + phosphate
-
-
-
?
phytate + H2O
? + phosphate
-
-
-
?
phytate + H2O
? + phosphate
-
-
-
?
rice bran + H2O
? + phosphate
-
natural phytate source
-
-
?
rice bran + H2O
? + phosphate
-
natural phytate source
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
high levels of phosphorous in the growth medium inhibit phytase synthesis, effect is larger in semisolid medium than in liquid medium
-
-
?
additional information
?
-
-
the enzyme exhibits a broad substrate selectivity, substrate are e.g. ATP, ADP, AMP, glucose-6-phosphate, fructose-6-phosphate, 4-nitrophenyl phosphate, and beta-glycerophosphate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme exhibits a broad substrate selectivity, substrate are e.g. ATP, ADP, AMP, glucose-6-phosphate, fructose-6-phosphate, 4-nitrophenyl phosphate, and beta-glycerophosphate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.1 per mM and s
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.1 per mM and s
-
-
?
additional information
?
-
-
enzyme exhibits phytase and acid phosphatase activity
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
to reduce phytates in dried grains with solubles (DDGS) and corn gluten feed (CGF), a phytase from Aspergillus niger, PhyA, is investigated regarding its capability to catalyze the hydrolysis of phytates in light steep water and whole stillage. Dephosphorylation of phytates in light steep water and whole stillage proceeds via the formation of InsP5, InsP4, InsP3, and InsP2 intermediates with phosphate and InsP1 as the end products. During the process, the amount of phosphate in the substrates is increased from 54% to 66% in the whole stillage, and from 20% to 90% in the light steep water, suggesting to a substantial dephosphorylation of the phytates in the light steep water and whole stillage via PhyA catalyzed hydrolysis. The most effective period of degradation is during the first 2 h for whole stillage and 6 h for light steep water
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.04 per mM and s
-
-
?
additional information
?
-
-
substrate specificity with substrates Na-phytate, i.e. myo-inositol-1,2,3,4,5,6-hexakisphosphate, naphtyl-1 phosphate, 4-nitrophenylphosphate, ATP, and ADP, overview
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl phosphate, catalytic efficiency is about 0.04 per mM and s
-
-
?
additional information
?
-
-
substrate specificity with substrates Na-phytate, i.e. myo-inositol-1,2,3,4,5,6-hexakisphosphate, naphtyl-1 phosphate, 4-nitrophenylphosphate, ATP, and ADP, overview
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with highest activity for calcium phytate, the enzyme is also active with ADP, ATP, glycerol beta-phosphate, glucose 6-phosphate, and 4-nitrophenyl phosphate. Among all the feed samples, mustard oil cake is dephytinized more efficiently than otherfeed samples, e.g. cotton oil cake
-
-
?
additional information
?
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay
-
-
?
additional information
?
-
usage of chromogenic agent containing 1:3 mixture of 100 g/l ammonium molybdate, and 0.785 g/l ammonium metavanadate in 15% HNO3 for the phosphate product detection in enzyme assay
-
-
?
additional information
?
-
the enzyme is also able to dephosphorylate ATP and ADP with 95 and 29% of the activity compared to phytic acid, respectively
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0
-
-
?
additional information
?
-
-
substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, beta-glycerophosphate, glucose 6-phosphate, sodium glycerophosphate, AMP, ADP and ATP
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP
-
-
?
additional information
?
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
-
the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP
-
-
?
additional information
?
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
the purified enzyme shows specificity to different salts of phytic acid, it also shows phosphomonoesterase activity with ADP and ATP (high activity), while not with 4-nitrophenyl phosphate and glucose 6-phosphate
-
-
?
additional information
?
-
the purified enzyme shows specificity to different salts of phytic acid, it also shows phosphomonoesterase activity with ADP and ATP (high activity), while not with 4-nitrophenyl phosphate and glucose 6-phosphate
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
-
phytases from bifidobacteria could be partly active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
effect of sourdough on the myo-inositol phosphates levels, overview
-
-
?
additional information
?
-
ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively
-
-
?
additional information
?
-
-
phytases from bifidobacteria partly could be active in human gut and could contribute to phytic acid degradation during food processing
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, but the highest activity is observed with phytic acid. Other substrates are 4-nitrophenyl phosphate, ATP, glucose-6-phosphate, and glycerol-3-phosphate. Phosphate detection by ammonium heptamolybdate reagent
-
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
-
less than 5% of the activity with myo-inositol hexakisphosphate with: ATP, ADP, glycerophosphate, glucose 1-phosphate, glucose 6-phosphate, fructose 6-phosphate and mannose 6-phosphate
-
?
additional information
?
-
KM873028
enzyme rPhysXT52 shows nonspecific phosphohydrolytic activity with 4-nitrophenyl phosphate, 1-naphthyl phosphate, 2-naphthyl phosphate, phenyl phosphate, 2-glycerophosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-diphosphate, AMP, ADP, ATP, and NADP+, overview
-
-
?
additional information
?
-
-
hydrolysis of insoluble metal-phytates, overview. The enzyme is also active with 4-nitrophenyl phosphate, sodium diphosphate, glucose-1-phosphate, and glucose-6-phosphate
-
-
?
additional information
?
-
-
the enzyme also performs unspecific phosphomonoesterase (PME) activity with substrate 4-nitrophenyl phosphate. Phytase and PME activities in Evernia prunastri strongly co-vary among sites of sample collection with contrasting N deposition
-
-
?
additional information
?
-
enzyme is a 6-phytase, EC 3.1.3.26. Major degradation product is DL-inositol 1,2,3,4,5-pentaphosphate
-
-
?
additional information
?
-
-
HcBPP preferentially recognizes its substrate and selectively hydrolyzes insoluble Ca2+-phytate salts at three phosphate group sites, yielding the final product, myo-inositol 2,4,6-trisphosphate, exhibiting also the 1- and 5-phytase activities. Ins(2,4,6)P3 is unable to bind Ca2+ or any other cation tested, including Co2+, Cu2+, Fe3+, Mg2+, Mn2+, Sr2+, and Zn2+
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
the enzyme also shows phosphate-monoester phosphohydrolase activity, EC 3.1.3.2
-
-
?
additional information
?
-
-
no activity with GTP and diphosphate
-
?
additional information
?
-
-
inducible enzyme
-
-
?
additional information
?
-
phytase ASr1 acts primarily as a scavenger of phosphate groups locked in the phytic acid molecule
-
-
?
additional information
?
-
substrate binding structure modelling, all six phosphate groups of phytate are involved in a hydrogen bond network connecting the substrate with PhyK, induced conformational changes upon substrate binding, overview
-
-
?
additional information
?
-
-
no activity with GTP and diphosphate
-
?
additional information
?
-
-
inducible enzyme
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP. The recombinant LlALP2 expressed in Pichia pastoris hydrolyzes phytate and 4-nitrophenyl phosphate and exhibits no activity towards ATP. Activity against 4-nitrophenyl phosphate is nearly 2.5fold higher than against phytate, similar to what is observed with the native enzyme
-
-
?
additional information
?
-
the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP. The recombinant LlALP2 expressed in Pichia pastoris hydrolyzes phytate and 4-nitrophenyl phosphate and exhibits no activity towards ATP. Activity against 4-nitrophenyl phosphate is nearly 2.5fold higher than against phytate, similar to what is observed with the native enzyme
-
-
?
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
-
the enzyme is also active with glucose 6-phosphate, but not with NADP+, ATP, and diphosphate
-
-
?
additional information
?
-
the enzyme also shows moderate activity with 4-nitrophenyl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1,6-bisphosphate, and glucose 6-phosphate, and low activity with AMP, ADP, and ATP. The enzyme cleaves phytate in soybean meal, rapeseed meal, and corn meal
-
-
?
additional information
?
-
the enzyme also shows moderate activity with 4-nitrophenyl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1,6-bisphosphate, and glucose 6-phosphate, and low activity with AMP, ADP, and ATP. The enzyme cleaves phytate in soybean meal, rapeseed meal, and corn meal
-
-
?
additional information
?
-
high substrate specificity for sodium phytate. No substrates: 4-nitrophenyl phosphate, D-glucose 1-phosphate, ATP, D-fructose-1,6-diphosphate, glycerol 2-phosphate
-
-
?
additional information
?
-
high substrate specificity for sodium phytate. No substrates: 4-nitrophenyl phosphate, D-glucose 1-phosphate, ATP, D-fructose-1,6-diphosphate, glycerol 2-phosphate
-
-
?
additional information
?
-
-
no activity towards 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate and 1-L-myo-inositol 1,2,5,6-tetrakisphosphate
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10
-
-
?
additional information
?
-
glucose-1-phosphatase enzymes and, specifically, Agp phytases are known to have a broad substrate specificity. The bifunctional enzyme from Pantoea sp. 3.5.1 exhibits 3-phytase activity, and also glucose-1-phosphatase, cf. EC 3.1.3.10. Broad substrate specificity, substrates are phytate and many other phosphate-containing substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview
-
-
?
additional information
?
-
-
determination of phytase activity of bacteriocins producing lactic acid bacteria previously isolated from spontaneous rye sourdough. The results show that the highest extracellular phytase activity produces Pediococcus pentosaceus KTU05-8 and KTU05-9 strains, as compared to Lactobacillus sakei strain KTU05-6, Pediococcus acidilactici strain KTU05-7, and Pediococcus pentosaceus KTU05-10, with a volumetric phytase activity of 32 and 54 U/ml, respectively, under conditions similar to leavening of bread dough (pH 5.5 and 30°C). In vitro studies in simulated gastrointestinal tract media pH provide that bioproducts prepared with Pediococcus pentosaceus strains used in wholemeal wheat bread preparation increase solubility of iron, zinc, manganese, calcium, and phosphorus average 30%
-
-
?
additional information
?
-
-
the enzyme catalyzes phosphate release from cereals such as corn, soybean, and wheat
-
-
?
additional information
?
-
-
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
?
-
enzyme PhyA efficiently releases phosphate from feedstuffs such as soybean, rich bran, and corn meal. The enzyme shows significant substrate specificity for phytate and only low activity with 4-nitrophenyl phosphate, diphosphate, 2-naphthyl phosphate, alpha-glyceryl phosphate, beta-glycerylphosphate, glucose 1-phosphate, fructose 1-phosphate, fructose 6-phosphate, AMP, ADP, and ATP
-
-
?
additional information
?
-
among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
no considerable activity with other phosphorylated substrates like ATP, ADP, dSPP, pNPP, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
-
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
the C-terminal domain is catalytically active, while the N-terminal domain exhibits no measurable myo-inositol hexakisphosphate phosphohydrolase activity
-
-
?
additional information
?
-
-
the enzyme is inducible under carbon limitation in the presence of myo-inositol hexakisphosphate
-
-
?
additional information
?
-
-
the phytase demonstrates high substrate specificity for sodium phytate. The enzyme also hydrolyzes 4-nitrophenyl phosphate, ATP, AMPc, glucose 6-phosphate, glucose 1-phosphate, and UDPG
-
-
?
additional information
?
-
-
the phytase isozymes exhibit a broad affinity for various phosphorylated compounds, i.e. 4-nitrophenyl phosphate 1-naphthyl phosphate, 2-naphthyl phosphate, AMP, ATP, GTP, fructose-1, 6-bisphosphate, fructose-6-phosphate, glucose-6-phosphate, and pyridoxal phosphate, substrate specificities, overview
-
-
?
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
-
color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
-
degradation of phytate by high-phytase Saccharomyces cerevisiae strains during simulated gastrointestinal digestion. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
phytase activity is determined using the ferrous sulfate-molybdenum blue method
-
-
?
additional information
?
-
the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate
-
-
?
additional information
?
-
-
phytase hydrolyzes and liberates inorganic phosphate from Ca2+, Mg2+, and Co2+ phytates more efficiently than those of Al3+, Fe2+, Fe3+, and Zn2+
-
-
?
additional information
?
-
enzyme rSt-Phy also shows haloperoxidase activity with KBr, metavanadate, and H2O2, only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, overview
-
-
?
additional information
?
-
-
the recombinant enzyme displayed broad substrate specificity. Molecular modeling and docking of phytase with various substrates show differential binding patterns, overview. Strong binding affinity with ATP and phytic acid, while the lowest with AMP and phosphoenol pyruvate. The enzyme is also active with ATP and 4-nitrophenyl phosphate
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
substrate specificity of recombinant isozymes, overview
-
-
?
additional information
?
-
-
lower activity with 4-nitrophenyl phosphate, no or poor activity with AMP, ADP, ATP, GTP, NADP+, glucose 1-phosphate, and glucose 6-phosphate
-
-
?
additional information
?
-
-
role of phytase in Ca2+ mobilization during germination of mung bean seed via a salvage pathway that involves allosteric activation by myo-inositol triphosphate
-
?
additional information
?
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
additional information
?
-
-
the cell-bound phytase is able to effectively dephytinize wheat flour, wheat bran, rice flour, and soybean flour, or soymilk, to varied extents
-
-
?
additional information
?
-
the enzyme catalyzes the dephytinization of soymilk
-
-
?
additional information
?
-
-
the enzyme catalyzes the dephytinization of soymilk
-
-
?
additional information
?
-
the phytase exhibits broad substrate specificity since it hydrolyses 4-nitrophenyl phosphate, ATP, ADP, and glucose-6-phosphate besides phytic acid. The enzyme hydrolyzes insoluble calcium and magnesium phytates efficiently, but not iron phytate
-
-
?
additional information
?
-
-
the phytase exhibits broad substrate specificity since it hydrolyses 4-nitrophenyl phosphate, ATP, ADP, and glucose-6-phosphate besides phytic acid. The enzyme hydrolyzes insoluble calcium and magnesium phytates efficiently, but not iron phytate
-
-
?
additional information
?
-
vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
enzyme is a 6-phytase, EC 3.1.3.26. Major degradation product is DL-inositol 1,2,3,4,5-pentaphosphate
-
-
?
additional information
?
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
-
the ferrous sulfate-molybdenum blue method is used for enzyme activity detection
-
-
?
additional information
?
-
substrate specificity of the recombinant isozyme, overview
-
-
?
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0.49
1-L-myo-inositol 1,2,3,4,5-pentakisphosphate
-
pH 5.5, 37°C
0.51
1-L-myo-inositol 1,2,3,5,6-pentakisphosphate
-
pH 5.5, 37°C
0.49 - 250
1-naphthyl phosphate
0.667 - 0.881
2-glycerophosphate
0.512 - 230
2-naphthyl phosphate
1.562 - 3.495
4-methylumbelliferyl phosphate
0.04 - 120
4-nitrophenyl phosphate
0.703
4-nitrophenylphosphate
-
37°C, pH 4.5
2.2
D-fructose 1,6-bisphosphate
-
pH 5.5, 37°C
0.14 - 1.1
D-fructose 1,6-diphosphate
1.9
D-Fructose 1-phosphate
-
pH 5.5, 37°C
0.478 - 0.676
D-fructose 6-phosphate
0.26 - 0.28
D-glucose 1-phosphate
0.27 - 2.3
D-glucose 6-phosphate
1.2 - 9.8
D-ribose 5-phosphate
0.17
di-sodium phenyl phosphate dihydrate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.229 - 18
fructose 1,6-diphosphate
56
fructose 6-phosphate
-
-
20
glucose 6-phosphate
-
-
110
Glycerol 2-phosphate
-
-
2
inositol bisphosphate
-
-
2
inositol monophosphate
-
-
2
inositol pentaphosphate
-
-
2
inositol tetraphosphate
-
-
2
inositol triphosphate
-
-
0.0104 - 114.8
myo-inositol hexakisphosphate
0.14 - 0.15
myo-inositol hexakisphosphate disodium salt
0.08 - 0.16
myo-inositol hexakisphosphate sodium salt
0.035 - 8.442
myo-inositol-1,2,3,4,5,6-hexakisphosphate
0.74 - 11
O-phospho-L-serine
0.52 - 18.16
p-nitrophenyl phosphate
0.801
phosphoenolpyruvate
-
37°C, pH 4.5
0.776 - 0.915
pyridoxal phosphate
additional information
additional information
-
0.49 - 2
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP2
0.516
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP11
0.718
1-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP12
1.6
1-naphthyl phosphate
-
-
3.8
1-naphthyl phosphate
-
pH 5.5, 50°C
250
1-naphthyl phosphate
-
-
0.667
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP11
0.704
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP2
0.881
2-glycerophosphate
-
pH 5.0, 35°C, phytase LP12
0.512
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP2
0.634
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP12
0.653
2-naphthyl phosphate
-
pH 5.0, 35°C, phytase LP11
230
2-naphthyl phosphate
-
-
1.562
4-methylumbelliferyl phosphate
recombinant mutant T44V/K45E, pH 6.6, 37°C
1.598
4-methylumbelliferyl phosphate
recombinant mutant T44I/K45E, pH 6.6, 37°C
3.495
4-methylumbelliferyl phosphate
recombinant wild-type enzyme, pH 6.6, 37°C
0.04
4-nitrophenyl phosphate
-
pH 5.0, 45°C
0.123
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP12
0.152
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP11
0.176
4-nitrophenyl phosphate
-
pH 5.0, 35°C, phytase LP2
0.265
4-nitrophenyl phosphate
-
-
0.93
4-nitrophenyl phosphate
-
pH 5.5, 50°C
1.38
4-nitrophenyl phosphate
-
-
1.38
4-nitrophenyl phosphate
-
pH 2.5
2.2
4-nitrophenyl phosphate
-
pH 5.6
4.3
4-nitrophenyl phosphate
-
-
10.1
4-nitrophenyl phosphate
-
pH 5.5, 50°C
120
4-nitrophenyl phosphate
-
-
0.398
ADP
-
pH 5.0, 35°C, phytase LP12
0.403
ADP
-
pH 5.0, 35°C, phytase LP11
0.451
ADP
-
pH 5.0, 35°C, phytase LP2
0.315
AMP
-
pH 5.0, 35°C, phytase LP12
0.319
AMP
-
pH 5.0, 35°C, phytase LP2
0.365
AMP
-
pH 5.0, 35°C, phytase LP11
0.07
ATP
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.412
ATP
-
pH 5.0, 35°C, phytase LP12
0.531
ATP
-
pH 5.0, 35°C, phytase LP11
0.596
ATP
-
pH 5.0, 35°C, phytase LP2
0.14
D-fructose 1,6-diphosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.359
D-fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP2
0.731
D-fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP12
1.1
D-fructose 1,6-diphosphate
-
-
0.478
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP11
0.531
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP2
0.676
D-fructose 6-phosphate
-
pH 5.0, 35°C, phytase LP12
0.26
D-glucose 1-phosphate
-
pH 5.5, 37°C
0.26
D-glucose 1-phosphate
-
37°C, pH 4.5
0.28
D-glucose 1-phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.27
D-glucose 6-phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.302
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP2
0.401
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP11
0.634
D-glucose 6-phosphate
-
pH 5.0, 35°C, phytase LP12
1.3
D-glucose 6-phosphate
-
pH 5.5, 37°C
2.3
D-glucose 6-phosphate
-
-
1.2
D-ribose 5-phosphate
-
-
9.8
D-ribose 5-phosphate
-
pH 5.5, 37°C
0.445
diphosphate
-
pH 5.0, 35°C, phytase LP11
0.691
diphosphate
-
pH 5.0, 35°C, phytase LP12
0.812
diphosphate
-
pH 5.0, 35°C, phytase LP2
0.229
fructose 1,6-diphosphate
-
pH 5.0, 35°C, phytase LP11
18
fructose 1,6-diphosphate
-
-
0.217
GTP
-
pH 5.0, 35°C, phytase LP2
0.398
GTP
-
pH 5.0, 35°C, phytase LP11
0.423
GTP
-
pH 5.0, 35°C, phytase LP12
0.0104
myo-inositol hexakisphosphate
-
pH 5.5
0.01073
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
0.0139
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
0.0147
myo-inositol hexakisphosphate
-
in 50 mM NaOAc (pH 5.0) or 100 mM Tris-HCl buffer (pH 8.0), at 37°C
0.01547
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
0.016
myo-inositol hexakisphosphate
-
-
0.01794
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
0.01927
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
0.02075
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
0.021
myo-inositol hexakisphosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
0.02189
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
0.027
myo-inositol hexakisphosphate
-
-
0.027
myo-inositol hexakisphosphate
-
native fungal enzyme
0.027
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, native enzyme
0.02769
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
0.03
myo-inositol hexakisphosphate
-
pH 5.0, 58°C
0.03073
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
0.034
myo-inositol hexakisphosphate
-
pH 3.5, 37°C
0.038
myo-inositol hexakisphosphate
-
-
0.04
myo-inositol hexakisphosphate
-
-
0.04
myo-inositol hexakisphosphate
-
-
0.04
myo-inositol hexakisphosphate
Schwanniomyces castellii
-
-
0.04
myo-inositol hexakisphosphate
-
strain NRRL 3135
0.04
myo-inositol hexakisphosphate
strain NRRL 3135
0.04
myo-inositol hexakisphosphate
-
pH 5.0, 58°C
0.045
myo-inositol hexakisphosphate
mutant C435G, pH 2.5, 42°C
0.05
myo-inositol hexakisphosphate
-
pH 7.0
0.05
myo-inositol hexakisphosphate
-
at pH 7.5
0.05
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, recombinant enzyme
0.056
myo-inositol hexakisphosphate
mutant C264G, pH 6.0, 37°C
0.06
myo-inositol hexakisphosphate
-
at pH 6.5
0.061
myo-inositol hexakisphosphate
-
-
0.062
myo-inositol hexakisphosphate
-
high molecular weight form
0.065
myo-inositol hexakisphosphate
-
recombinant enzyme
0.07
myo-inositol hexakisphosphate
wild-type, pH 5.0, 58°C
0.074
myo-inositol hexakisphosphate
-
pH 3.5, 37°C
0.078
myo-inositol hexakisphosphate
-
pH 4.5, 55°C
0.08
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP11
0.0827
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 4.0
0.0864
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 4.0
0.0934
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 4.0
0.1
myo-inositol hexakisphosphate
-
-
0.1
myo-inositol hexakisphosphate
-
at pH 6
0.1
myo-inositol hexakisphosphate
-
at pH 5.3
0.1064
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1076
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 5.5
0.1083
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 5.5
0.11
myo-inositol hexakisphosphate
-
-
0.114
myo-inositol hexakisphosphate
-
low molecular weight form
0.114
myo-inositol hexakisphosphate
in 200 mM sodium acetate buffer (pH 5.5), at 37°C
0.1224
myo-inositol hexakisphosphate
-
wild type enzyme, at pH 4.0
0.124
myo-inositol hexakisphosphate
-
pH 5.0, 58°C, recombinant enzyme
0.13
myo-inositol hexakisphosphate
-
-
0.13
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP2
0.1304
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.135
myo-inositol hexakisphosphate
-
-
0.135
myo-inositol hexakisphosphate
-
immobilized enzyme
0.1363
myo-inositol hexakisphosphate
wild-type, pH 9.0, temperature not specified in the publication
0.138
myo-inositol hexakisphosphate
wild-type, pH 7.0, temperature not specified in the publication
0.143
myo-inositol hexakisphosphate
wild-type, pH 8.0, temperature not specified in the publication
0.143
myo-inositol hexakisphosphate
recombinant enzyme, pH 5.0, 60°C
0.145
myo-inositol hexakisphosphate
mutant C215S, pH 5.0, 37°C
0.146
myo-inositol hexakisphosphate
wild-type, pH 6.0, temperature not specified in the publication
0.147
myo-inositol hexakisphosphate
calcium phytate, pH 5.0, 60°C
0.15
myo-inositol hexakisphosphate
-
-
0.15
myo-inositol hexakisphosphate
-
at pH 5.5
0.151
myo-inositol hexakisphosphate
wild-type, pH 5.0, temperature not specified in the publication
0.154
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.156
myo-inositol hexakisphosphate
mutant D308E, pH 7.0, temperature not specified in the publication
0.156
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
0.156
myo-inositol hexakisphosphate
native enzyme, pH 5.0, 60°C
0.159
myo-inositol hexakisphosphate
wild-type, pH 4.0, temperature not specified in the publication
0.159
myo-inositol hexakisphosphate
-
substrate sodium phytate, pH 5.0, 60°C, recombinant enzyme
0.16
myo-inositol hexakisphosphate
-
pH 5.0
0.16
myo-inositol hexakisphosphate
-
pH 5.0, 50°C
0.1623
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R/T271R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.167
myo-inositol hexakisphosphate
mutant D308A, pH 7.0, temperature not specified in the publication
0.1675
myo-inositol hexakisphosphate
-
wild type enzyme, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.17
myo-inositol hexakisphosphate
-
pH 5.0, 37°C
0.1719
myo-inositol hexakisphosphate
-
wild type enzyme, at pH 5.5
0.18
myo-inositol hexakisphosphate
mutant C31G, pH 5.5, 53°C
0.18
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli
0.189
myo-inositol hexakisphosphate
mutant D56E, pH 7.0, temperature not specified in the publication
0.196
myo-inositol hexakisphosphate
pH 4.5, 37°C
0.196
myo-inositol hexakisphosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
0.2
myo-inositol hexakisphosphate
-
-
0.2
myo-inositol hexakisphosphate
-
-
0.2
myo-inositol hexakisphosphate
-
at pH 2.5
0.206
myo-inositol hexakisphosphate
pH 4.5, 37°C
0.208
myo-inositol hexakisphosphate
-
substrate potassium phytate, pH 5.0, 60°C, recombinant enzyme
0.21
myo-inositol hexakisphosphate
-
pH 2.5, 60°C
0.218
myo-inositol hexakisphosphate
mutant D56L, pH 7.0, temperature not specified in the publication
0.22
myo-inositol hexakisphosphate
pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris
0.24
myo-inositol hexakisphosphate
native enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
0.247
myo-inositol hexakisphosphate
-
pH 5.0, 37°C
0.248
myo-inositol hexakisphosphate
mutant D56A, pH 7.0, temperature not specified in the publication
0.25
myo-inositol hexakisphosphate
-
-
0.25
myo-inositol hexakisphosphate
-
-
0.25
myo-inositol hexakisphosphate
-
-
0.252
myo-inositol hexakisphosphate
-
pH 5.0, 37°C
0.262
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 52.5°C
0.278
myo-inositol hexakisphosphate
-
37°C, pH 4.5
0.28
myo-inositol hexakisphosphate
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.293
myo-inositol hexakisphosphate
pH 7.0, 50°C, sodium phytate
0.3
myo-inositol hexakisphosphate
-
-
0.3
myo-inositol hexakisphosphate
-
pH 5.0, 35°C, phytase LP12
0.3
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.32
myo-inositol hexakisphosphate
-
sodium phytate, pH 5.0, 60°C
0.326
myo-inositol hexakisphosphate
KM873028
recombinant enzyme, pH 3.9, 37°C
0.33
myo-inositol hexakisphosphate
-
-
0.34
myo-inositol hexakisphosphate
-
0.34
myo-inositol hexakisphosphate
-
pH 5.5, 37°C
0.34
myo-inositol hexakisphosphate
-
37°C, pH 4.5
0.35
myo-inositol hexakisphosphate
-
-
0.36
myo-inositol hexakisphosphate
pH 7.4, 37°C, presence of Ca2+
0.38
myo-inositol hexakisphosphate
-
pH 5.5, 40°C
0.382
myo-inositol hexakisphosphate
-
recombinant wild-type enzyme, pH 2.5, 40°C
0.3847
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 5.5
0.39
myo-inositol hexakisphosphate
-
-
0.39
myo-inositol hexakisphosphate
37°C, pH 7.0
0.39
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
0.405
myo-inositol hexakisphosphate
-
recombinant mutant enzyme, pH 2.5, 40°C
0.42
myo-inositol hexakisphosphate
pH 4.5, 50°C
0.43
myo-inositol hexakisphosphate
-
mutant Q258N/Q349N, pH 4.5, 37°C
0.44
myo-inositol hexakisphosphate
-
-
0.44
myo-inositol hexakisphosphate
-
strain 92
0.44
myo-inositol hexakisphosphate
strain 92
0.45
myo-inositol hexakisphosphate
-
-
0.46
myo-inositol hexakisphosphate
-
pH 4, 37°C
0.48
myo-inositol hexakisphosphate
-
strain IIIAn/8
0.48
myo-inositol hexakisphosphate
-
wild-type, pH 4.5, 37°C
0.48 - 0.545
myo-inositol hexakisphosphate
pH 5.5, 55°C, sodium phytate
0.49
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
0.5
myo-inositol hexakisphosphate
-
Bacillus subtilis var. natto
0.51
myo-inositol hexakisphosphate
-
pH 2.0, 37°C, recombinant enzyme
0.52
myo-inositol hexakisphosphate
pH 7.5, 55°C
0.52
myo-inositol hexakisphosphate
-
mutant Q258N, pH 4.5, 37°C
0.532
myo-inositol hexakisphosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0 at 37°C
0.532
myo-inositol hexakisphosphate
recombinant enzyme, in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0, at 37°C
0.54
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
0.545
myo-inositol hexakisphosphate
pH 4.5, 55°C
0.55
myo-inositol hexakisphosphate
-
-
0.58
myo-inositol hexakisphosphate
-
sodium salt, pH 5.5, 50°C
0.59
myo-inositol hexakisphosphate
-
calcium salt, pH 5.5, 50°C
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
0.63
myo-inositol hexakisphosphate
-
-
0.667
myo-inositol hexakisphosphate
-
substrate calcium phytate, pH 5.0, 60°C, recombinant enzyme
0.7
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.72
myo-inositol hexakisphosphate
-
pH 4.5, 45°C
0.757
myo-inositol hexakisphosphate
pH 5.0, 55°C, recombinant His-tagged enzyme
0.78
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
0.8
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pGAPZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.856
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged C-terminal domain
0.858
myo-inositol hexakisphosphate
pH 6.0, 40°C, recombinant His-tagged full-length enzyme
0.91
myo-inositol hexakisphosphate
-
-
0.98
myo-inositol hexakisphosphate
-
-
1
myo-inositol hexakisphosphate
-
immobilized enzyme
1.073
myo-inositol hexakisphosphate
pH 7.0, 65°C
1.125
myo-inositol hexakisphosphate
pH 7.5, 70°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
1.4
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
1.45
myo-inositol hexakisphosphate
-
5.0 mM myo-inositol hexakisphosphate in 0.2 M sodium acetate, pH 5.0, at 60°C
1.5
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
1.77
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
1.8
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Pichia pastoris (pGAPZalphaA) or Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2
myo-inositol hexakisphosphate
-
-
2.1
myo-inositol hexakisphosphate
-
-
2.1
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.19
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
2.8
myo-inositol hexakisphosphate
-
-
2.84
myo-inositol hexakisphosphate
-
-
2.84
myo-inositol hexakisphosphate
-
pH 5.5
3
myo-inositol hexakisphosphate
-
pH 2.5, 15°C
114.8
myo-inositol hexakisphosphate
-
potassium salt, pH 5.5, 50°C
0.14
myo-inositol hexakisphosphate disodium salt
pH 5.5, 50°C
0.15
myo-inositol hexakisphosphate disodium salt
pH 5.5, 50°C
0.08
myo-inositol hexakisphosphate sodium salt
pH 5.5, 50°C
0.16
myo-inositol hexakisphosphate sodium salt
pH 5.5, 50°C
0.035
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a1, pH 5.0, 36°C
0.036
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme a, pH 5.0, 36°C
0.045
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
0.045
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b1, pH 5.0, 36°C
0.046
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b2, pH 5.0, 36°C
0.048
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant isozyme b, pH 5.0, 36°C
0.056
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 6.0, 37°C, recombinant mutant C264G
0.07
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 58°C, recombinant wild-type enzyme
0.13
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
isozyme RO2, pH 4.5, 40°C
0.145
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 37°C, recombinant mutant C215S
0.18
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.5, 53°C, recombinant mutant C31G
0.19
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
0.191
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C
0.2
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 4.0, 60°C
0.24
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase 168PhyA, pH 7.0, 55°C
0.42
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
pH 7.0, 37°C
0.45
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79L, pH 4.5, 37°C
0.5
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
dual domain phytase PhyH, pH 7.0, 35°C
0.52
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
pH 5.5, 50°C
0.55
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79S, pH 4.5, 37°C
0.69
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant R79G, pH 4.5, 37°C
1.086
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C
1.28
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
beta-propeller phytase PhyP, pH 7.0, 37°C
1.432
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
phytase domain Phy-DII, pH 7.0, 35°C
1.6
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
isozyme RO1, pH 4.5, 40°C
1.98
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
3.024
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
8.442
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
0.74
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP12
0.8 - 11
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP2
0.891
O-phospho-L-serine
-
pH 5.0, 35°C, phytase LP11
0.52
p-nitrophenyl phosphate
-
at 62°C, in 50 mM sodium acetate buffer (pH 5)
2.27
p-nitrophenyl phosphate
-
in 200 mM sodium acetate buffer, 1 mM CaCl2, pH 4.0 at 37°C
12.4
p-nitrophenyl phosphate
-
37°C, pH 4.5
18.16
p-nitrophenyl phosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
0.087 - 0.324
phytate
-
pH 2.5, 55°C
0.138
phytate
-
wild-type enzyme
0.14
phytate
pH 5.0, 37°C
0.25 - 0.425
phytate
pH 4.0, 55°C
0.67
phytate
pH 7.5, 37°C
0.747
phytate
-
mutant enzyme E227A
0.914
phytate
-
mutant enzyme D55A
0.934
phytate
-
mutant enzyme Y159H
0.967
phytate
-
mutant enzyme K76E
2.505
phytate
-
mutant enzyme R122E
3.046
phytate
-
mutant enzyme R122K
3.542
phytate
-
mutant enzyme D258A
8.661
phytate
-
mutant enzyme Y159A
11.99
phytate
-
mutant enzyme K76R
0.776
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP11
0.876
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP12
0.915
pyridoxal phosphate
-
pH 5.0, 35°C, phytase LP2
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
KM873028
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
thermodynamics
-
additional information
additional information
kinetics and thermodynamics, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
substrate specificity and kinetics of recombinant isozymes, overview
-
additional information
additional information
-
typical Michaelis-Menten kinetics
-
additional information
additional information
typical Michaelis-Menten kinetics
-
additional information
additional information
-
typical Michaelis-Menten kinetics
-
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk plots
-
additional information
additional information
enzyme kinetics, also with other substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview
-
additional information
additional information
kinetics and thermodynamics of recombinant full-length enzyme and C-terminal domain, overview
-
additional information
additional information
-
kinetics and thermodynamics of recombinant full-length enzyme and C-terminal domain, overview
-
additional information
additional information
Line-Weaver Burk plot
-
additional information
additional information
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
additional information
additional information
-
Michealis-Menten kinetics
-
additional information
additional information
thermodynamics of the recombinant enzyme
-
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-
-
-
brenda
isolated from soil, India
-
-
brenda
isolated from soil, India
-
-
brenda
gene phyA
-
-
brenda
gene phyA
-
-
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
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
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
3-phytase A precursor
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
gene phyI1s
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
SwissPRot
brenda
isolated from soil samples collected in Northeast Parana State in Brazil
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
SwissPRot
brenda
-
UniProt
brenda
NRRL 326
-
-
brenda
NRRL 330
-
-
brenda
NRRL 372
-
-
brenda
NRRL 4361
-
-
brenda
-
-
-
brenda
NRRL337
-
-
brenda
NRRL372
-
-
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
isolated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Aspergillus syndowi
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
NRRL 4875
-
-
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
-
-
-
brenda
-
UniProt
brenda
strain DSM7
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from geother-mal soil located in Southern Tunisia
UniProt
brenda
gene phyC
UniProt
brenda
-
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
-
UniProt
brenda
gene phyH
-
-
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
-
-
-
brenda
-
UniProt
brenda
isolated from Oryza sativa phyllosphere
-
-
brenda
KCCM 90097
-
-
brenda
isolated from Dig Rostam hot mineral spring in Iran
UniProt
brenda
isolated from soil samples
UniProt
brenda
isolated from soil samples
UniProt
brenda
-
UniProt
brenda
ATCC15703
-
-
brenda
ATCC15703
-
-
brenda
ATCC 27535
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from The Halsary, Caithness, UK
-
-
brenda
isolated from Lake Kasumigaura, Japan
UniProt
brenda
isolated from Lake Kasumigaura, Japan
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
genes phyG1 and phyG51
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from Migneit, Gwynedd, UK
-
-
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
-
KM873028
GenBank
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from a rhizosphere
-
-
brenda
isolated from rabbit ceca
-
-
brenda
collected from the Derwent Valley, Derbyshire, UK, and from other sites subject to different rates of wet inorganic N (NO3- + NH4+) deposition, overview
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
L. Merr.. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from Derwent Valley, Derbyshire, UK
-
-
brenda
symbiotic bacterial strain isolated from the gut contents of Batocera horsfieldi larvae, gene phyA115
UniProt
brenda
symbiotic bacterial strain isolated from the gut contents of Batocera horsfieldi larvae, gene phyA115
UniProt
brenda
No. PG-2
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Nostoc sp. is the Lobaria pulmonaria (5183) cyanobiont; collected from Lairg, Sutherland, UK
UniProt
brenda
isolated from Lor cheese samples
-
-
brenda
isolated from Lor cheese samples
-
-
brenda
-
-
-
brenda
var. amiga. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
UniProt
brenda
-
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
-
-
-
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
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
isolated from soil collected from four different ecological and geographical habitats of the Republic of Tatarstan, Russia, forest near the village Agerze, Aznakaevo District
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from Derwent Valley, Derbyshire, UK
-
-
brenda
var. carotovota ACCC 10276
-
-
brenda
strain DSMZ 18074
-
-
brenda
strains KTU05-8 and KTU05-9, isolated from spontaneous Lithuanian rye sourdoughs
-
-
brenda
Nostoc sp. is the Peltigera membranacea cyanobiont N6; collected from Beddgelert, Gwynedd, UK
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Penicillium caseoicolum
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
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
-
-
-
brenda
-
-
-
brenda
collected from Derwent Valley, Derbyshire, UK
-
-
brenda
-
-
-
brenda
Bacteroides ruminicola, isolated from Mehsani buffalo rumen
UniProt
brenda
isolated from chickpea (Cicer arietinum) rhizosphere
-
-
brenda
isolated from chickpea (Cicer arietinum) rhizosphere
-
-
brenda
collected from The Halsary, Caithness, UK
-
-
brenda
-
-
-
brenda
isolated from foreshore soil on the coast of Busan, Korea
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
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
-
-
-
brenda
-
-
-
brenda
collected from Lairg, Sutherland, UK
-
-
brenda
collected from Derwent Valley, Derbyshire, UK
-
-
brenda
collected from Kildonan, Sutherland, UK
-
-
brenda
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
var. microsporus, isolated from Brazilian soil
-
-
brenda
NRRL 2710
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from Antarctic deep-sea sediment
-
-
brenda
isolated from Antarctic deep-sea sediment
-
-
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
-
-
-
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
-
-
-
brenda
-
-
-
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
isolated from wheat rhizosphere
UniProt
brenda
isolated from Tunisian soils
UniProt
brenda
isolated from Tunisian soils
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
-
-
-
brenda
solated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
Torulopsis candida
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
collected from Derwent Valley, Derbyshire, UK
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
isozyme b; isozyme b
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
purple acid phosphatase with phytase activity
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced. The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
-
-
-
brenda
ATCC 11382 and ATCC 11358
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
var. awamorii ATCC 38854. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
NRRL 4875 and PCC 104
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
94776, 114248, 114249, 114254, 114264, 114270, 114271, 114272, 114274, 114275, 649616, 678975, 707770 -
-
brenda
-
UniProt
brenda
-
-
-
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
-
-
-
brenda
3-phytase A precursor
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
-
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
-
-
-
brenda
-
SwissPRot
brenda
-
114252, 114253, 114257, 114258, 114273, 114279, 134797, 654003, 665282, 665283, 666691, 666692, 677690, 677774, 679568, 680395 -
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
SwissPRot
brenda
-
UniProt
brenda
-
UniProt
brenda
3-phytase A precursor
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.
-
-
brenda
gene phyA
SwissPRot
brenda
gene phyA
-
-
brenda
gene phyI1s
-
-
brenda
isolated from soil samples collected in Northeast Parana State in Brazil
-
-
brenda
japonicus saito ATCC 1034
-
-
brenda
NRRL 3135
-
-
brenda
NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
NRRL 326
-
-
brenda
NRRL 330
-
-
brenda
NRRL 372
-
-
brenda
NRRL 4361
-
-
brenda
NRRL337
-
-
brenda
NRRL372
-
-
brenda
recombinant enzyme from strain van Tieghem
-
-
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 ATCC 10864
-
-
brenda
strain ATCC 9142
-
-
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
strain van Teighem
-
-
brenda
strain van Tieghem
-
-
brenda
The enzyme exhibits phytase and acid phosphatase activity. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced.The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
-
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
van Teighem
-
-
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
var. cinnamoneum NRRL 348
-
-
brenda
variant ficuum
-
-
brenda
-
-
-
brenda
gene phyA
SwissPRot
brenda
NRRL 3135
-
-
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
-
-
-
brenda
The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
isolated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
ATCC 11362
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
NRRL 4875
-
-
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
-
-
-
brenda
-
UniProt
brenda
isolated from geother-mal soil located in Southern Tunisia
UniProt
brenda
strain DSM7
-
-
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
gene phyC
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (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
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
gene phyH
-
-
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
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
3-phytase
UniProt
brenda
isolated from Dig Rostam hot mineral spring in Iran
UniProt
brenda
isolated from Oryza sativa phyllosphere
-
-
brenda
isozymes FTE, FTEII, and FBA
UniProt
brenda
KCCM 90097
-
-
brenda
subsp. spizizenii
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
var. natto
-
-
brenda
-
-
-
brenda
3-phytase
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
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
-
-
-
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
-
-
-
brenda
-
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
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
bifunctional enzyme with acid phosphatase and phytase activities
-
-
brenda
gene APPA
-
-
brenda
gene AppA2
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
-
UniProt
brenda
isozyme a; Golden Promise, isozyme a
UniProt
brenda
isozyme b2; Golden Promise, isozyme b2
UniProt
brenda
ssp. spontaneum, ssp. agriocrithum, and ssp. vulgare
-
-
brenda
a low molecular weight form and a high molecular weight form
-
-
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
-
-
-
brenda
MO-3
-
-
brenda
strainMO-3. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
-
-
-
brenda
MO-3
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
ASR1
-
-
brenda
No. PG-2
-
-
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
-
-
-
brenda
ASR1
-
-
brenda
-
-
-
brenda
fragment
UniProt
brenda
-
-
-
brenda
fragment
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
SwissProt
brenda
LIALP1
SwissProt
brenda
tassi
-
-
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
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
gene phyA; protease-resistance phytase gene phyA
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
-
-
-
brenda
isolated from foreshore soil on the coast of Busan, Korea
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
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
i.e. Rhizopus microsporus var. oligosporus, isozymes RO1 and RO2
-
-
brenda
NRRL 2710
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
brenda
acidic histidine acid phosphatase PhyH49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
alkaline beta-propeller phytase PhyB49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
acidic histidine acid phosphatase PhyH49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
alkaline beta-propeller phytase PhyB49; isolated from the gut of Batocera horsfieldi (Coleoptera) larvae
UniProt
brenda
-
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.
SwissProt
brenda
-
-
-
brenda
i.e. Myceliophthora thermophila or Sporotrichum thermophile strain BJTLR50
-
-
brenda
i.e. Sporotrichum thermophile or Myceliophthora thermophila
UniProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SWissProt
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
-
brenda
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SWissProt
brenda
i.e. Myceliophthora thermophila
UniProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
solated from a soil sample collected from Rohtak, Haryana (India)
UniProt
brenda
i.e. Myceliophthora thermophila
UniProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
i.e. Myceliophthora thermophila
UniProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
i.e. Myceliophthora thermophila
UniProt
brenda
i.e. Sporotrichum thermophile or Thielavia heterothallica
UniProt
brenda
cv. DBW17
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-
brenda
isozyme a1
UniProt
brenda
isozyme a1; isozyme a1
UniProt
brenda
isozyme a2
UniProt
brenda
isozyme b1; isozyme b1
UniProt
brenda
isozyme a1; isozyme a1
UniProt
brenda
isozyme b1; isozyme b1
UniProt
brenda
isolated from a soil metagenome
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-
brenda
metagenome-derived phytase, metagenome derived from subsurface groundwater
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-
brenda
-
-
-
brenda
i.e. Pichia anomala or Hansenula anomala
UniProt
brenda
i.e. Wickerhamomyces anomalus or Hansenula anomala
UniProt
brenda
isolated from dried flower buds of Woodfordia fruticosa
UniProt
brenda
single copy gene PPHY
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
-
UniProt
brenda
gene YeappA
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
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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
Q27N
-
1.7fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity is almost constant over entire pH-range, pH 4-8
Q27P
-
1.7fold decrease in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Mutant enzyme has a pronounced tendency to aggregate and precipitate
Q27S
-
1.9fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
Q27T
-
2.8fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity over the entire pH-range, pH 4-8
Q27V
-
1.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme
R151L
-
mutation has no effect on specific activity
R151L/S152N
-
mutant protein with reduced susceptibility to proteolysis
S140Y/D141G
-
mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity
Y282H
-
mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3
K186G/R187Q
mutant protein with reduced susceptibility to proteolysis
A35E/P42S/Q168R/T248R
thermostable mutant. Molecular dynamics simulation and comparison with wild-type show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly
A58E/P65S
-
increased activity at pH 5.5
A58E/P65S/Q191R/T271R/E228K
-
pH-activity profile-improved mutant, optimum shift to pH 4.0, 64% increased specific activity at pH 3.5
A58E/P65S/Q191R/T271R/E228K/K300E
-
pH-activity profile-improved mutant, eliminates the activity dip at pH 3.5 shown in the wild type
A58E/P65S/Q191R/T271R/E228K/S149P
-
improved thermostability
A58E/P65S/Q191R/T271R/E228K/S149P/F131L
-
improved thermostability
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R
-
Although the substitution of K112R is supposed to create a new hydrogen bond with Y113 at a distance of 2.56 A, it does not offer extra benefit to thermostability
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R
-
27% increased specific activity at pH 5.5, 100% increased specific activity at pH 3.5
A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R/K300E
-
33% decreased activity at pH 5.5, wild type specific activity at pH 3.5
A58E/Q191R
-
increased activity at pH 5.5
A58E/Q191R/T271R
-
increased activity at pH 5.5
C345G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C435G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
D461N
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
E121F
-
random mutagenesis, the mutant shows 3.1fold increased activity and 3.24fold reduced affinity for sodium phytate compared to the wild-type enzyme
E35A/R168A
-
no activity and decreased thermostability
E35A/R168A/R248A
-
no activity and 25% loss of thermostability
E35A/R248A
-
no activity and decreased thermostability
E89D
-
mutant enzyme from strain T213, slight decrease in activity
E89D/H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
E89D/R297Q
-
mutant enzyme from strain T213, 2.6fold increase in activity
F376Y
random mutagenesis, the mutant has an altered thermostability compared to wild-type
G377T
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
H292N
-
mutant enzyme from strain T213, as active as wild-type enzyme
H292N/R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
K300D
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.71
K300E
-
mutation results in an increase of the hydrolysis of phythic acid of 56% and 19% at pH 4.0 and pH 5.0 at 37°C respectively. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.74
K300R
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.81
K300T
-
specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.68
K41E
-
random mutagenesis, the mutant shows 2.5fold increased activity and 1.78fold reduced affinity for sodium phytate compared to the wild-type enzyme
K432R
random mutagenesis, the mutant has an altered thermostability compared to wild-type
Q172R
random mutagenesis, the mutant has an altered thermostability compared to wild-type
Q172R/K432R
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
Q368E
random mutagenesis, the mutant has an altered thermostability compared to wild-type
Q368E/K432R
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
R168A/R248A
-
no activity and decreased thermostability
R297Q
-
mutant enzyme from strain T213, about 3fold increase in activity
S238D
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
T195L
random mutagenesis, the mutant has an altered thermostability compared to wild-type
T195L/Q368E/F376Y
site-directed mutagenesis, the mutant has an altered thermostability compared to wild-type
T255E
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.0 and pH 6.0
E121F
-
random mutagenesis, the mutant shows 3.1fold increased activity and 3.24fold reduced affinity for sodium phytate compared to the wild-type enzyme
-
K41E
-
random mutagenesis, the mutant shows 2.5fold increased activity and 1.78fold reduced affinity for sodium phytate compared to the wild-type enzyme
-
K432R
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
Q172R
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
Q368E
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
T195L
-
random mutagenesis, the mutant has an altered thermostability compared to wild-type
-
D461N
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
-
S238D
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.5 and pH 6.0
-
T255E
-
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 2.0 and pH 6.0
-
C345G
-
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
-
C435G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
A68S/A72E/A73E/S77N
-
t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme
E41A/D42G
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme
H61E
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme
D148E
site-directed mutagenesis, mutation on the surface, the specific activity of mutant D148E increases by about 35% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
D258A
-
turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme
D314A
-
inactive mutant enzyme
D52E
site-directed mutagenesis, mutation in the active site, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme, probably because that the side chain of residue D52 is involved in formation of octahedral coordination shells with bridging water molecules in the active site
D55A
-
turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme
E211A
-
inactive mutant enzyme
E227A
-
turnover number of mutant enzyme is 9.29% of that of the wild-type enzyme
E260A
-
inactive mutant enzyme
K76E
-
turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme
K76R
-
turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme
N156E
site-directed mutagenesis, mutation on the surface, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme. The mutation site N156 is in the vicinity of residue Y159 which coordinates with Ca2+ by its hydroxyl group. The substitution of Glu for N156 may indirectly change the micro-environment around residue Y159, leading to the reduction in activity of phytase
R122E
-
turnover number of mutant enzyme is 48.81% of that of the wild-type enzyme
R122K
-
turnover number of mutant enzyme is 17.11% of that of the wild-type enzyme
S197E
site-directed mutagenesis, mutation on the surface, the specific activity of mutant S197E increases by about 13% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
Y159F
-
inactive mutant enzyme
D148E
-
site-directed mutagenesis, mutation on the surface, the specific activity of mutant D148E increases by about 35% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
-
D52E
-
site-directed mutagenesis, mutation in the active site, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme, probably because that the side chain of residue D52 is involved in formation of octahedral coordination shells with bridging water molecules in the active site
-
N156E
-
site-directed mutagenesis, mutation on the surface, the mutation leads to significant loss of specific activity of the mutant compared to wild-type enzyme. The mutation site N156 is in the vicinity of residue Y159 which coordinates with Ca2+ by its hydroxyl group. The substitution of Glu for N156 may indirectly change the micro-environment around residue Y159, leading to the reduction in activity of phytase
-
S197E
-
site-directed mutagenesis, mutation on the surface, the specific activity of mutant S197E increases by about 13% over a temperature range of 40-75°C at pH 7.0 compared to wild-type. The mutant enzyme shows a much higher thermostability than the wild-type phytase
-
G117A/G266A
-
mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at G177 and G266 results in a substantial stabilization of PhyL compared to wild-type (DELTAG value of 8 kJ/mol) with an elevated DELTAG value of 20 kJ/mol
H32P/S256P/K304P/K324P/S353P
-
mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at 5 consensus positions only slightly enhances stabilization compared to wild-type (DELTAG value of 8 kJ/mol) with a DELTAG value of 8.8 kJ/mol
D308A
50% of wild-type activity, significant decrease in melting temperature and optimum temperature
D308E
94% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56A
0.4% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56E
20% of wild-type activity, significant decrease in melting temperature and optimum temperature
D56L
0.6% of wild-type activity, significant decrease in melting temperature and optimum temperature
E180N
-
site-directed mutagenesis, cell surface residue, the mutant shows activity similar to the wild-type enzyme
E227S
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
E229V
-
site-directed mutagenesis, cell surface residue, the mutant shows 19% increased activity compared to the wild-type enzyme
K179R
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
K77R
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
K77R/K179R
-
site-directed mutagenesis, mutation of residues not directly involved in the catalysis but involved in substrate binding, the double mutant phytase shows higher stability at pH 2.6-3.0 compared to the wild-type enzyme. The mutant retains over 80% of its initial activity after 3 h incubation at pH 2.6 while the wild-type phytase retains only about 40% of its original activity. The mutant shows highly reduced activity compared to the wild-type enzyme
P257R
-
site-directed mutagenesis, cell surface residue, the mutant shows reduced activity compared to the wild-type enzyme
S283R
-
site-directed mutagenesis, cell surface residue, the mutant shows 13% increased activity compared to the wild-type enzyme
D308A
-
50% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D308E
-
94% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56A
-
0.4% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56E
-
20% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
D56L
-
0.6% of wild-type activity, significant decrease in melting temperature and optimum temperature
-
E180N
-
site-directed mutagenesis, cell surface residue, the mutant shows activity similar to the wild-type enzyme
-
E227S
-
site-directed mutagenesis, active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
-
E229V
-
site-directed mutagenesis, cell surface residue, the mutant shows 19% increased activity compared to the wild-type enzyme
-
P257R
-
site-directed mutagenesis, cell surface residue, the mutant shows reduced activity compared to the wild-type enzyme
-
S283R
-
site-directed mutagenesis, cell surface residue, the mutant shows 13% increased activity compared to the wild-type enzyme
-
D24G/K111E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/N121S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A
site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/S51P
site-directed mutagenesis, inactive mutant
E378A/D128A/D71A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,3,6,7 with loss of four salt bridges
E378A/D178A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,5 with loss of two salt bridges
E378A/R56A/D128A/D267A/D178A/D71A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1-7 with loss of seven salt bridges
E378A/R56A/D267A/E443A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB1,2,4,7 with loss of four salt bridges
R56A/D128A
KM873028
site-directed mutagenesis, mutant rPhyXT52:DELTASB2,3 with loss of two salt bridges
Q258N
-
substitution introduced to enhance the glycosylation activity upon expression in Pichia pastoris
Q258N/Q349N
-
substitutions introduced to enhance the glycosylation activity upon expression in Pichia pastoris. Mutant displays 40% enhancement in thermostability compared to wild-type
T308A
5% of the specific activity of wild-type
L151S
the mutation enhances the activity in the range of 37-70°C and pH 2.5-7.0 by facilitating the interaction between the substrate and the catalytic centre
N354D
the substitution influences the pH profile by weakening the bondage with the side chain of D353, which causes a pKa shift of the catalytic centre
T11A/G56E/L65F/Q144H/L151S
mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin
T11A/H37Y/G56E/L65F/Q144H/L151S/N354D
mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin
D344A
site-directed mutagenesis
H71A
site-directed mutagenesis
R70A
site-directed mutagenesis
R74A
site-directed mutagenesis
T101C/A229C/S307C/V352C/M364C/F398C
-
enhancing the thermal resistance of the acidobacteria-derived phytase by engineering of disulfide bridges, construction of engineered mutant rPhyA6DB by site-directed mutagenesis, overview
E230G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230P
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230R
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162V
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G/L230G
site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
R79G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R79L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R79S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S51A
-
optimum temperature and pH similar to wild-type
S51D
-
optimum temperature and pH similar to wild-type
S51I
-
shift in optimal pH to 5.0. Compared with wild-type, mutant S51T shows higher specific activity, greater activity over pH 2.0-5.5, and increased thermal and acid stability
S51K
-
optimum temperature and pH similar to wild-type
S51T
-
shift in optimal pH to 4.5. Specific activity of S51T at pH 4.5 is 5.5fold higher than the corresponding specific activity of wild-type
E153R
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230D
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230K
site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme
E230P
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230S
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
E230T
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L162V
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
L99A/L162G/L230G
site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme
I15T
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15T/R162G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15V/P62S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15Y/P94S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K45E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L398S/C342G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
M1T/H146R
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44I/K45E
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
T44M
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44R/K45M
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45D
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45E
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
T44V/K45S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45W
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T44V/K45Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y27C/K45E/K306E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
I15T
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
K45E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T44I/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
T44V/K45E
-
site-directed mutagenesis, the active site loop mutant shows increased activity compared to the wild-type enzyme, hybrid homology modeling
-
Q27L
-
3.4fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27
Q27L
-
mutation increases the specific activity mainly around pH 6.5, while the increase is much smaller in the pH range 2 to 5, the pH that seems most relevant for maximal performance of the enzyme in animals. Decreasing the negative surface charge of the Aspergillus fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowers the pH-optimum by ca. 0.5 unit but also results in 70-75% inactivation of the enzyme
S152N
-
mutant protein with reduced susceptibility to proteolysis
S152N
-
mutation has no effect on specific activity
A58E/P65S/Q191R/T271R
-
increased activity and improved thermostability retaining 20% greater activity after being heated at 80°C for 10 min and has a 7°C higher melting temperature than that of wild type PhyA
A58E/P65S/Q191R/T271R
-
retains 20% greater activity after being heated at 80°C for 10 min and has 7°C higher melting temperature than that of the wild type enzyme
C215S
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C215S
site-directed mutagenesis, the mutant shows altered temperature optimum compared to the wild-type enzyme
C264G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C264G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C31G
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C31G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C71S
site-directed mutagenesis, inactive mutant
C71S
removal of disulfide bridge results in loss of activity
P212H
site-directed mutagenesis, the mutant exhibits a two-peak ppH profile with optima at pH 3.2 and pH 5.5. The substitution of histidine at position 212 has remarkable effect on pH and temperature properties of the enzyme
P212H
site-directed mutagenesis, the mutant shows altered the pH optimum shifted from pH 2.5 to pH 3.2 and a decrease in thermostability compared to wild-type enzyme, the mutant exhibits a two-peak pH profile with optima at pH 3.2 and pH 5.5
C215S
-
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
-
C215S
-
site-directed mutagenesis, the mutant shows altered temperature optimum compared to the wild-type enzyme
-
C264G
-
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
-
C264G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
C31G
-
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
-
C31G
-
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
-
C71S
-
removal of disulfide bridge results in loss of activity
-
C71S
-
site-directed mutagenesis, inactive mutant
-
Y159A
-
turnover number of mutant enzyme is 0.19% of that of the wild-type enzyme
Y159A
-
turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme
D24G
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G shows 62.7, 68.3, and 17.9% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. The specific activity of the Escherichia coli-expressed D24G at pH 7.0 and 37°C is improved by 40.3 % as compared with that of the wild-type, while the improvement is 91.9% in Bacillus subtilis and 82.2% in Pichia pastoris, respectively. Overall, the mutant's activity is increased compared to the wild-type
D24G
site-directed mutagenesis, the mutant shows 29.7% activity compared to the wild-type at pH 7.0, 60°C, and 76.6% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows 42.7% activity compared to the wild-type at pH 7.0, 60°C, and 84.2% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R/K111E/N121S
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G/K70R/K111E/N121S shows 54.1, 42.6, and 10.8% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. Overall, the mutant's activity is significantly increased compared to the wild-type
D24G/K70R/K111E/N121S
site-directed mutagenesis, the mutant shows 42.8% activity compared to the wild-type at pH 7.0, 60°C, and 121.1% at pH 4.5, 37°C
K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
K265E
site-directed mutagenesis, the mutant shows similar activity compared to wild-type
S51A
site-directed mutagenesis, the mutant shows 13.5% activity compared to the wild-type at pH 7.0, 60°C, and 79.5% at pH 4.5, 37°C
S51A
site-directed mutagenesis. Overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G
-
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G shows 62.7, 68.3, and 17.9% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. The specific activity of the Escherichia coli-expressed D24G at pH 7.0 and 37°C is improved by 40.3 % as compared with that of the wild-type, while the improvement is 91.9% in Bacillus subtilis and 82.2% in Pichia pastoris, respectively. Overall, the mutant's activity is increased compared to the wild-type
-
D24G
-
site-directed mutagenesis, the mutant shows 29.7% activity compared to the wild-type at pH 7.0, 60°C, and 76.6% at pH 4.5, 37°C
-
D24G/K70R/K111E/N121S
-
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G/K70R/K111E/N121S shows 54.1, 42.6, and 10.8% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. Overall, the mutant's activity is significantly increased compared to the wild-type
-
D24G/K70R/K111E/N121S
-
site-directed mutagenesis, the mutant shows 42.8% activity compared to the wild-type at pH 7.0, 60°C, and 121.1% at pH 4.5, 37°C
-
K265E
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type
-
K265E
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
-
S51A
-
site-directed mutagenesis. Overall, the mutant's activity is increased compared to the wild-type
-
S51A
-
site-directed mutagenesis, the mutant shows 13.5% activity compared to the wild-type at pH 7.0, 60°C, and 79.5% at pH 4.5, 37°C
-
additional information
construction of three recombinant phyA mutant strains, i.e. PP-NPm-8, PP-NPep-6A and I44E/T252RPhyA, that show improved catalytic efficiency or thermostability compared to the wild-type strain. Variations of bond and electrostatic energy before and after substitution at Q172, T195, Q368, F376, and K432, half-life of thermal inactivation and kinetic parameters of PP-NPep-6A phytase and its mutants, predictions of residue interactions, overview
additional information
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
-
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
-
construction of three recombinant phyA mutant strains, i.e. PP-NPm-8, PP-NPep-6A and I44E/T252RPhyA, that show improved catalytic efficiency or thermostability compared to the wild-type strain. Variations of bond and electrostatic energy before and after substitution at Q172, T195, Q368, F376, and K432, half-life of thermal inactivation and kinetic parameters of PP-NPep-6A phytase and its mutants, predictions of residue interactions, overview
-
additional information
-
protein engineering is carried out to shift the pH optimum of a thermostable Aspergillus fumigatus phytase to acidic range. The wild enzyme exhibits enhanced activities at pH 2.5 and pH 5.5. Mutants D461N, G377T, T255E, and S238D retain bi-peak pH profiles, but there is an observed enhancement in activity at pH 6.0 compared to pH 5.5. Mutant P212H exhibits enhancement in activity at pH 3.0-3.5 compared to the wild-type enzyme
-
additional information
-
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
-
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
-
additional information
directed evolution and library screening, pH and tempearture profiles of the mutant enzymes compared to the wild-type enzyme, detailed overview
additional information
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
additional information
-
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
additional information
-
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
-
additional information
-
directed evolution and library screening, pH and tempearture profiles of the mutant enzymes compared to the wild-type enzyme, detailed overview
-
additional information
KM873028
construction of mutants that lose salt bridges through the mutations, the combinations of the disabled salt bridges are randomly selected. The mutants show reduced melting temperatures and reduced optimum reaction temperature compared to wild-type rPhyXT52, overview
additional information
the HvPAPhy_a-transformed barley plants with high phytase activities possess triple potential utilities for the improvement of phosphate bioavailability. First of all, the utilization of the mature grains as feed to increase the release of bio-available phosphate and minerals bound to the phytate of the grains, secondly, the utilization of the powdered straw either directly or phytase extracted hereof as a supplement to high phytate feed or food, and finally, the use of the stubble to be ploughed into the soil for mobilizing phytatebound phosphate for plant growth
additional information
replacements of G56E, L65F, Q144H, and L151S improved the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
-
replacements of G56E, L65F, Q144H, and L151S improved the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
entrapment of permeabilized cells in 3% w/v alginate resulting in a 10% loss of enzyme activity, corresponding to 90% immobilization yield. The immobilized cells can be successfully reused in four consecutive assays with sustained phytase activity, overview
additional information
-
entrapment of permeabilized cells in 3% w/v alginate resulting in a 10% loss of enzyme activity, corresponding to 90% immobilization yield. The immobilized cells can be successfully reused in four consecutive assays with sustained phytase activity, overview
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
-
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
-
engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview
additional information
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
additional information
-
directed evolution identifies the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic effect on activity with a broadened pH spectrum. Kinetic characterization of the improved variants, YmPh-M10 (T44I/K45E) and YmPh-M16 (T44V/K45E), show up to sevenfold increased specific activity and up to 2.2fold reduced KM at pH 6.6 under screening conditions compared to Yersinia mollaretii phytase wild-type (YmPhWT). pH-Dependence of wild-type and mutant enzymes, overview
-
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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
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Schwanniomyces castellii
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Penicillium caseoicolum
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
Aspergillus syndowi
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
agriculture
-
enzyme is used in animal feed to reduce phosphate pollution
agriculture
-
since monogastric animals virtually lack phytase activity in their digestive tract, phytic acid phosphorus is metabolically unavailable to these animals. The problem can be circumvented by supplementation of the feed with a recombinantly produced phytase that has a pH activity profile ideally suited for maximal activity in the digestive tract of either pigs or poultry
agriculture
-
the enzyme is suitable for supplementing animal feeds to improve the availability of phosphate from phytate
agriculture
-
feedstuffs studied contains only small amounts of soluble protein-phytate complexes. Insoluble protein-phytate complexes are formed at low pH, as found in the stomach of monogastric animals. Dietary phytase supplementation prevents the formation of protein-phytate complexes or aids in dissolving them faster. Therefore, phytase may improve protein digestibility
agriculture
-
the ability of the enzyme to liberate phytate-phosphate is similar when included in low Ca2+ and nonphytate phosphorus diets for broilers. Either source can be fed to commercial broilers to aid improving phytate-bound phosphate use
agriculture
-
over-expression of phyA2 gene in maize seeds using a construct driven by the maize embryo-specific globulin-1 promoter. Phytase activity in transgenic maize seeds reaches approximately 2,200 units per kg seed, about a 50fold increase compared to non-transgenic maize seeds. The phytase expression is stable across four generations. The transgenic seeds germinate normally
agriculture
-
the dry weight and inorganic phosphate contents of wheat plants are high when supplemented with phytase or fungal spores. The plants provided with 5 mg phytate per plant exhibit enhanced growth and inorganic phosphate. With increase in the dosage of phytase, there is an increase in growth and inorganic phosphate of plants, the highest being at 20 U per plant. The compost made employing the combined native microflora of the wheat straw and Sporotrichum. Thermophile promots growth of the plants. The plant-growth-promoting effect is higher with the compost made using Sporotricum thermophile than that from only the native microflora
agriculture
-
the presence of rhizosphere microorganisms reduces the dependence of plants on extracellular secretion of phytase from roots when grown in a phosphate-deficient soil. The expression of phytase in transgenic plants has little or no impact on the microbial community structure as compared with control plant lines, whereas soil treatments, such as the addition of phosphate, has large effects. Soil microorganisms are explicitly involved in the availability of phosphate to plants and the microbial community in the rhizosphere appears to be resistant to the impacts of single-gene changes in plants designed to alter rhizosphere biochemistry and nutrient cycling
agriculture
-
the presence of rhizosphere microorganisms reduces the dependence of plants on extracellular secretion of phytase from roots when grown in a phosphate-deficient soil. The expression of phytase in transgenic plants has little or no impact on the microbial community structure as compared with control plant lines, whereas soil treatments, such as the addition of phosphate, has large effects. Soil microorganisms are explicitly involved in the availability of phosphate to plants and the microbial community in the rhizosphere appears to be resistant to the impacts of single-gene changes in plants designed to alter rhizosphere biochemistry and nutrient cycling
agriculture
-
transgenic expression of phytase in Solanum tuberosum leads to stable expression levels over several cycles of propagation. Field tests show that tuber size, number and yield increase in transgenic potato. Improved phosphorus acquisition when phytate is provided as a sole phosphorus source and enhanced microtuber formation in cultured transgenic potato seedlings when phytate is provided as an additional phosphorus source are observed. The potato-produced phytase supplement is as effective as a commercially available microbial phytase in increasing the availability of phytate-phosphorus to weanling pigs
agriculture
-
the phytase has the potential to be useful as an animal feed supplement
agriculture
-
seed-specific overexpression of Aspergillus niger phytase in corn leads to transgenic corn with bioavailable phosphate. Maximal phytase activity of 125 FTU/g kernels can be obtained, 1000fold above that of the wild type, with 1000 g of kernels containing up to 67 times the feed industry requirement. An animal feeding trial demonstrated that the recombinant enzyme has similar nutritional effects on broiler chickens to a commercially available phytase product in terms of reducing inorganic phosphorus addition to feed and phosphate excretion in animal manure
agriculture
enzyme PHY US42 can be used as feed additive in combination with an acid phytase for monogastric animals
agriculture
enzyme rSt-Phy is useful in the dephytinization of broiler feeds efficiently in simulated gut conditions of chick leading to the liberation of soluble inorganic phosphate with concomitant mitigation in anti-nutrient effects of phytates
agriculture
neutral phytase is used as a feed additive for degradation of anti-nutritional phytate in aquatic feed industry. Mutant phytases D148E and S197E with increased activities and thermostabilities have application potential as additives in aquaculture feed
agriculture
phytase is used as a feed additive for degradation of anti-nutritional phytate, the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive
agriculture
since the enzyme degrades phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, it might be a promising candidate as a feed additive enzyme
agriculture
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
agriculture
the phytase has the potential to be useful as an animal feed supplement. Among all the feed samples, mustard oil cake is dephytinized more efficiently than other feed samples
agriculture
the RPHY1 gene mined from rumen proves its promising candidature as a feed supplement enzyme in animal farming
agriculture
-
the phytase has the potential to be useful as an animal feed supplement
-
agriculture
-
neutral phytase is used as a feed additive for degradation of anti-nutritional phytate in aquatic feed industry. Mutant phytases D148E and S197E with increased activities and thermostabilities have application potential as additives in aquaculture feed
-
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
agriculture
-
supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture
-
agriculture
-
the phytase has the potential to be useful as an animal feed supplement. Among all the feed samples, mustard oil cake is dephytinized more efficiently than other feed samples
-
agriculture
-
since the enzyme degrades phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, it might be a promising candidate as a feed additive enzyme
-
agriculture
-
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
-
agriculture
-
enzyme PHY US42 can be used as feed additive in combination with an acid phytase for monogastric animals
-
analysis
-
comparison of assay methods and the impact of assay conditions on activity estimate using the molybdenum blue method, the molybdovanadate method, and the acetone phosphomolybdate method. Nearly identical activity of PhyA is determined from the molybdenum blue method and the acetone phosphomolybdate method. The molybdenum blue method and the molybdovanadate method give only 22% difference in PhyA activity
analysis
-
comparison of assay methods and the impact of assay conditions on activity estimate using the molybdenum blue method, the molybdovanadate method, and the acetone phosphomolybdate method. The activity values of AppA2 are more variable with the three assay methods than those of Aspergillus niger PhyA. The molybdenum blue method and the molybdovanadate method produce nearly a 3fold disparity for AppA2. Overall, the pH value, the type of buffers, and the inclusion of ancillary chemicals such as the detergents Triton X-100 and BSA each account for approximately one-third of the variations of AppA2
analysis
-
screening method to elucidate the ability of different yeast strains to utilize phytic acid as sole phosphorus source. The growth test in liquid culture in a microtiter plate with phytic acid as sole phosphorus source is a reliable, fast and easy-to-use screening method
analysis
-
screening method to elucidate the ability of different yeast strains to utilize phytic acid as sole phosphorus source. The growth test in liquid culture in a microtiter plate with phytic acid as sole phosphorus source is a reliable, fast and easy-to-use screening method
analysis
-
gain of function mutants of the enzyme can be instrumental for the structure-function study of the enzyme and for industrial application
analysis
-
gain of function mutants of the enzyme can be instrumental for the structure-function study of the enzyme and for industrial application
-
biotechnology
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a 20fold increase in total root phytase activity in transgenic lines expressing Aspergillus niger phytase results in improved phosphorus nutrition, such that the growth and phosphorus content of the plants is equivalent to control plants supplied with inorganic phosphate. Use of gene technology to improve the ability of plants to utilize accumulated forms of soil organic phosphorus
biotechnology
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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
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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
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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
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a cross-linked enzyme aggregate (CLEA) of 3-phytase is synthesised, which is incubated with vanadate and tested as a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide as the oxidant. The results show that the 3-phytase-CLEA demonstrates a similar efficiency (ca. 95% conversion) and asymmetric induction (ca. 60%) as the free enzyme. Moreover, the 3-phytase-CLEA can be reused at least three times without significant loss of activity
biotechnology
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to evaluate the ability of EDTA to improve phytate P utilization and the possible synergistic effect between EDTA and microbial phytase an experiment is conducted using 360 Ross 308 broiler chicks. The experiment is carried out using a completely randomized design. Four replicate of 15 chicks per each are fed dietary treatments. Phytase supplementation of P-deficient diets significantly improves weight gain and feed efficiency, but it has no effect on feed consumption. Microbial phytase supplementation significantly decreases alkaline phosphatase concentration. Results obtained suggest no synergistic effect between phytase and EDTA in broiler chicks
biotechnology
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Pichia pastoris containing cell-surface phytase releases phosphorus from feedstuff at a level similar to secreted phytase
biotechnology
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synthesis of a modified phytase gene with 1256 bp in length with optimal codons for expression in Pichia pastoris. A Pichia pastoris strain that expresses the modified phytase gene phyA-mod shows a 50% increase in phytase activity level
biotechnology
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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
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food industry
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Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
food industry
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the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview
food industry
the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive, applicability of recombinant PPHY in dephytinization of wheat bread, overview
food industry
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
food industry
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the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
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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
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food industry
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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
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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
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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
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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
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the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
-
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid
-
food industry
-
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes
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nutrition
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addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
nutrition
-
improves the nutrient utilization as additives in fish feed
nutrition
-
may be considered for application as an animal feed additive to assist in the hydrolysis of phytate complexes to improve the bioavailability of phosphorus in plant feedstuff
nutrition
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complete removal of inorganic phosphate from growing pig diets coupled with phytase supplementation improves digestibility and retention of phosphor and nitrogen, thus reducing manure phosphor excretion without any negative effect on pig performance
nutrition
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
nutrition
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
nutrition
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Pichia pastoris containing cell-surface phytase releases phosphorus from feedstuff at a level similar to secreted phytase. Pichia pastoris with phytase displayed on its surface has a great potential as a whole-cell supplement to animal feed
nutrition
use of Yersinia rohdei phytase as an attractive additive to animal feed. Compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and a potential commercial phytase from Yersinia intermedia, the Yersinia rohdei phytase is more resistant to pepsin, retains more activity under gastric conditions, and releases more inorganic phosphorus from soybean meal under simulated gastric conditions
nutrition
isozymes LlALP1 and LlALP2 have the potential to be useful as feed and food supplements
nutrition
-
the phytase has the potential to be useful as an animal feed supplement
nutrition
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seed-specific overexpression of Aspergillus niger phytase in corn leads to transgenic corn with bioavailable phosphate. Maximal phytase activity of 125 FTU/g kernels can be obtained, 1000fold above that of the wild type, with 1000 g of kernels containing up to 67 times the feed industry requirement. An animal feeding trial demonstrated that the recombinant enzyme has similar nutritional effects on broiler chickens to a commercially available phytase product in terms of reducing inorganic phosphorus addition to feed and phosphate excretion in animal manure
nutrition
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due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
nutrition
the enzyme is useful to reduced phytate in tandoori and naan dough for flat Indian bread, The enzymatic reduction of phytic acid will lead to the retention of the nutrients, and thus, result in a significant improvement in mineral absorption. The addition of rPPHY resulted in 67.5% and 23.2 % reduction in phytic acid content in tandoori and naan, respectively. The texture of the test breads remains as good as the control breads
nutrition
-
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
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nutrition
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addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
may be considered for application as an animal feed additive to assist in the hydrolysis of phytate complexes to improve the bioavailability of phosphorus in plant feedstuff
-
nutrition
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the phytase has the potential to be useful as an animal feed supplement
-
nutrition
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due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
addition of Aspergillus niger phytase to the flour containing wheat bran increases iron absorption in humans
-
nutrition
-
enzyme is at least as efficient as commercial phytase for hydrolyzing phytate in corn-based animal feed
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synthesis
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
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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
-
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
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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
Penicillium caseoicolum
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
synthesis
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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
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
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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
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expression of phytase in a Medicago truncatula cell suspension line. Recombinant phytase accumulates to at least 25 mg/l and remaines stable along the growth curve, and an enriched fraction with high enzymatic activity is easily obtained
synthesis
expression of phytase in Glycine max under control of a root-specific promoter. The phytase activity and phosphate levels in transgenic soybean root secretions are 4.7 U/mg protein and 439 microM, respectively, compared to 0.8 U/mg protein and 120 microM, respectively, in control soybeans
synthesis
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expression of phytase in Lactobacillus casei. The highest phytase activities in the supernatant and cells are 22.12 and 4.49 U per ml at the fourth day of incubation
synthesis
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immobilization of enzyme via a cross-linked enzyme aggregate. The immobilized enzyme incubated with vanadate shows a similar efficiency and asymmetric induction as the free enzyme and can be used at least three times without significant loss of activity. In presence of organic solvents, the activtiy is still limited. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate
synthesis
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immobilization of phytase on Sepabead EC-EP and use in the biodegradation of soymilk phytate. The immobilized enzyme exhibits an activity of 0.1 U per g of carrier and activity yield of 70.83%. Optimum temperature is 55°C, optimum pH for the immobilized enzyme is 5.5. Enzyme is stable between pH 3.0-8.0 and below 70°C. The immobilized enzyme hydrolyzes 65% of soymilk phytate in 8 h at 60°C, as compared with 56% hydrolysis observed for the native enzyme over the same period of time
synthesis
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the optimal medium for phytase production contains oat 10.0 g/l, ammonium sulfate 15.0 g/l, glucose 30 g/l, and NaCl 20.0 g/l, while the optimal cultivation conditions for phytase production are pH 5.0, a temperature of 28°C, and a shaking speed of 170 rpm. Under the optimal conditions, over 557.9 mU/ml of phytase activity is produced within 72 h of fermentation at the shake flask level
synthesis
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a maximal level of phytase of 113.7 U/g of dry substrate is obtained in wheat bran based medium containing 5% sucrose, 50% humidity, 7.5% of biomass at 33°C, pH 7.0 during 72 h and a 285% improvement in enzyme titre is achieved
synthesis
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a maximal level of phytase of 113.7 U/g of dry substrate is obtained in wheat bran based medium containing 5% sucrose, 50% humidity, 7.5% of biomass at 33°C, pH 7.0 during 72 h and a 285% improvement in enzyme titre is achieved
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synthesis
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
-
synthesis
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the optimal medium for phytase production contains oat 10.0 g/l, ammonium sulfate 15.0 g/l, glucose 30 g/l, and NaCl 20.0 g/l, while the optimal cultivation conditions for phytase production are pH 5.0, a temperature of 28°C, and a shaking speed of 170 rpm. Under the optimal conditions, over 557.9 mU/ml of phytase activity is produced within 72 h of fermentation at the shake flask level
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synthesis
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preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
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additional information
PhyA115 is a beta-propeller phytase that has application potential in aquaculture feed
additional information
phytase has great potential applications not only in the areas of animal nutrition and resource conservation, but also in environmental protection and public health
additional information
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phytases show great potential for application in different sectors such as in animal nutrition, human nutrition, aquaculture, and pharmacology. These enzymes are considered as a green feed additive that can be used to neutralize the antinutritional effects of phytate, thereby increasing the bioavailability of phosphorus and other minerals. They also contribute to the reduction of environmental pollution by phosphorus
additional information
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the enzyme is useful as animal feed additive, in dephytinization of food ingredients, and bioremediation of phosphorous pollution in the environment
additional information
-
phytase has great potential applications not only in the areas of animal nutrition and resource conservation, but also in environmental protection and public health
-
additional information
-
PhyA115 is a beta-propeller phytase that has application potential in aquaculture feed
-
additional information
-
the enzyme is useful as animal feed additive, in dephytinization of food ingredients, and bioremediation of phosphorous pollution in the environment
-