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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
? + phosphate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-phosphoglycerate + H2O
glyceric acid + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
6-phosphogluconate + H2O
gluconate + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
no activity
-
-
?
AMP + phosphate
adenosine + phosphate
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
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
-
-
-
-
?
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
? + 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
? + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
phytate + H2O
? + phosphate
-
-
-
-
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
-
-
-
-
?
additional information
?
-
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
74% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
39.8% of the activity with myo-inositol hexakisphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
ADP + H2O
?
-
-
-
-
?
ADP + H2O
?
-
25.6% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
-
-
-
-
?
ATP + H2O
?
-
38.8% of the activity with myo-inositol hexakisphosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
50.8% of the activity with 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
-
-
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
-
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
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
-
-
-
?
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-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
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
84% of the activity with myo-inositol hexakisphosphate
-
?
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
-
-
?
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Al3+
-
98% inhibition at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Ca2+
-
200 mM, 32% inhibition
Co2+
-
60% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Fe2+
-
59% inhibition at 5-15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
goethite
-
loss of activity upon sorption on, overview
-
guanidinium-HCl
-
6 M, 92% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
haematite
-
loss of activity upon sorption on, overview
-
K+
-
16% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
kaolinite
-
loss of activity upon sorption on, overview
-
KI
-
6 M, 95% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
metavanadate
-
50% inhibition at 0.0011 and pH 2.5, or at 0.0053 mM and pH 5.0
-
Mg2+
-
61% inhibition at 5 mM, 92% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Mn2+
-
73% inhibition at 4 mM, 97% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
montmorillonite
-
loss of activity upon sorption on, overview
-
myo-inositol-1,2,3,4,5,6-hexakissulfate
-
potent inhibition, the compound is isosteric and isoelectronic with respect to substrate myo-inositol-1,2,3,4,5,6-hexakisphosphate
Ni2+
-
44% inhibition at 20 mM
orthovanadate
-
50% inhibition at 0.0004 and pH 2.5, or at 0.040 mM and pH 5.0
Pepsin
-
loses 65% of the initial activity in the presence of 3000 units pepsin
-
PMSF
-
80% inhibition at 2.0 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
SDS
-
0.1%, 92% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
vanadate
-
51V-NMR studies show that vanadate is incorporated in the active site. Enzyme shows higher affinity for vanadate at pH 5.0 than at pH 7.6. vanadium is covalently coordinated in the active site of the enzyme to an apical histidine and to oxygen donors. Two sites are available for coordination. Upon addition of H2O2 two peroxide-vanadate-phytase complexes are formed at pH 5.0 in the case of 3-phytase
Cu2+
-
-
Cu2+
-
70% inhibition at 5 mM, 95% inhibition at 15 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Cu2+
-
effect on the ability of phytase to hydrolyze phytate phosphorus is dependent on pH. At pH 2.5 (gastric pH), no inhibition is noted among the treatments (copper citrate, copper chloride, copper lysinate, cupper sulfate, tribasic copper chloride) except that the addition of 250 and 500 mg Cu/kg diet from copper chloride and 500 mg Cu/kg from copper sulfate slightly inhibits phytate phosphorus hydrolysis. When pH is increased to 5.5-6.5 (small intestinal digesta) phytate phosphorus hydrolysis is greatly inhibited
Hg2+
-
-
Hg2+
-
48% inhibition at 10 mM, 87% inhibition at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Urea
-
8 M, 65% inhibition. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Urea
-
in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Zn2+
-
-
Zn2+
-
67% inhibition at 5 mM, 96% inhibition at 20 mM
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2-mercaptoethanol
-
0.1 mM, 59% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
cetyl trimethyl ammonium bromide
-
1%, 80% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
citrate
-
0.1 mM, 45% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
EDTA
-
0.1 mM, 54% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
F-
-
200 mM, activation to 160.7% of control
iodoacetic acid
-
0.1 mM, 28% acti1vation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
L-Tartaric acid
-
0.1 mM, 34% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
oxalate
-
0.1 mM, 52% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
p-hydroxymercuribenzoate
-
0.1 mM, 22% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Phosphomycin
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
PMSF
-
0.1 mM, 63% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Sodium azide
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Triton X-100
-
5%, 75% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Tween-20
-
1%, 80% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Tween-80
-
1%, 77% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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0.045 - 0.18
myo-inositol-1,2,3,4,5,6-hexakisphosphate
3.8
1-naphthyl phosphate
-
pH 5.5, 50°C
0.93
4-nitrophenyl phosphate
-
pH 5.5, 50°C
0.01073 - 0.606
myo-inositol hexakisphosphate
0.15
myo-inositol hexakisphosphate disodium salt
pH 5.5, 50°C
0.16
myo-inositol hexakisphosphate sodium salt
pH 5.5, 50°C
0.52 - 8.442
myo-inositol-1,2,3,4,5,6-hexakisphosphate
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
additional information
additional information
-
typical Michaelis-Menten kinetics
-
0.045
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
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
0.145
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
0.01073
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
0.01547
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
0.01794
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
0.01927
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
0.02075
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
0.02189
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
0.02769
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
0.03073
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
0.034
myo-inositol hexakisphosphate
-
pH 3.5, 37°C
0.04
myo-inositol hexakisphosphate
-
strain NRRL 3135
0.04
myo-inositol hexakisphosphate
strain NRRL 3135
0.045
myo-inositol hexakisphosphate
mutant C435G, pH 2.5, 42°C
0.056
myo-inositol hexakisphosphate
mutant C264G, pH 6.0, 37°C
0.07
myo-inositol hexakisphosphate
wild-type, pH 5.0, 58°C
0.0827
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 4.0
0.0864
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 4.0
0.0934
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 4.0
0.1
myo-inositol hexakisphosphate
-
-
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
0.1224
myo-inositol hexakisphosphate
-
wild type enzyme, at pH 4.0
0.1304
myo-inositol hexakisphosphate
-
mutant enzyme A58E/P65S, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.145
myo-inositol hexakisphosphate
mutant C215S, pH 5.0, 37°C
0.154
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1623
myo-inositol hexakisphosphate
-
mutant enzyme A58E/Q191R/T271R, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1675
myo-inositol hexakisphosphate
-
wild type enzyme, at 37°C, in 0.2 M citrate buffer, pH 5.5
0.1719
myo-inositol hexakisphosphate
-
wild type enzyme, at pH 5.5
0.18
myo-inositol hexakisphosphate
mutant C31G, pH 5.5, 53°C
0.196
myo-inositol hexakisphosphate
in 1 M sodium acetate buffer pH 5.5, at 37°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
-
-
0.44
myo-inositol hexakisphosphate
-
-
0.44
myo-inositol hexakisphosphate
-
strain 92
0.44
myo-inositol hexakisphosphate
strain 92
0.45
myo-inositol hexakisphosphate
-
-
0.48
myo-inositol hexakisphosphate
-
strain IIIAn/8
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
0.52
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
pH 5.5, 50°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
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3 - 350
myo-inositol-1,2,3,4,5,6-hexakisphosphate
0.422 - 300000
myo-inositol hexakisphosphate
281
myo-inositol hexakisphosphate disodium salt
pH 5.5, 50°C
253
myo-inositol hexakisphosphate sodium salt
pH 5.5, 50°C
59.83 - 161
myo-inositol-1,2,3,4,5,6-hexakisphosphate
1.9
p-nitrophenyl phosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
1260
phytate
-
pH 2.5, 55°C
3 - 6
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 6.0, 37°C, recombinant mutant C264G
62
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 37°C, recombinant mutant C215S
90
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 2.5, 42°C, recombinant mutant C435G
234
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.5, 53°C, recombinant mutant C31G
350
myo-inositol-1,2,3,4,5,6-hexakisphosphate
pH 5.0, 58°C, recombinant wild-type enzyme
0.422
myo-inositol hexakisphosphate
recombinant mutant Q368E/K432R, pH 5.5, 37°C
0.476
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
0.496
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
0.548
myo-inositol hexakisphosphate
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
0.553
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R, pH 5.5, 37°C
0.557
myo-inositol hexakisphosphate
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
0.576
myo-inositol hexakisphosphate
recombinant mutant Q172R, pH 5.5, 37°C
0.71
myo-inositol hexakisphosphate
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
3 - 6
myo-inositol hexakisphosphate
mutant C264G, pH 6.0, 37°C
62
myo-inositol hexakisphosphate
mutant C215S, pH 5.0, 37°C
90
myo-inositol hexakisphosphate
mutant C435G, pH 2.5, 42°C
170
myo-inositol hexakisphosphate
-
pH 3.5, 37°C
234
myo-inositol hexakisphosphate
mutant C31G, pH 5.5, 53°C
350
myo-inositol hexakisphosphate
wild-type, pH 5.0, 58°C
398
myo-inositol hexakisphosphate
in 1 M sodium acetate buffer pH 5.5, at 37°C
300000
myo-inositol hexakisphosphate
-
pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
59.83
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
83.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
161
myo-inositol-1,2,3,4,5,6-hexakisphosphate
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
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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
C215S
site-directed mutagenesis, the mutant shows altered temperature optimum compared to the wild-type enzyme
C264G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C31G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C435G
site-directed mutagenesis, the mutant shows altered pH and temperature optima compared to the wild-type enzyme
C71S
site-directed mutagenesis, inactive mutant
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
C215S
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C264G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C31G
removal of disulfide bridge results in increase in Km, decrease in kcat value, loss of activity at 58°C
C345G
removal of disulfide bridge results in decrease in kcat value, loss of activity at 58°C
C71S
removal of disulfide bridge results in loss of activity
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
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
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
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
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Nayini, N.R.; Markakis, P.
Phytic acid
Phytic Acid, Chemistry and Applications (Graf, E. , ed. )
101-118
1986
Aspergillus ficuum, Aspergillus niger, Aspergillus niger NRRL 65, Aspergillus terreus, Aspergillus terreus 9A1, Bacillus subtilis, Klebsiella aerogenes, Millerozyma farinosa, Pseudomonas sp., Rhizopus microsporus var. oligosporus, Rhizopus microsporus var. oligosporus NRRL 2710, Saccharomyces sp.
-
brenda
Wyss, M.; Pasamontes, L.; Friedlein, A.; Remy, R.; Tessier, M.; Kronenberger, A.; Middendorf, A.; Lehmann, M.; Schoebelen, L.; Rthlisberger, U.; Kusznir, E.; Wahl, G.; Muller, F.; Lahm, H.W.; Vogel, K.; van Loon, A.P.G.M.
Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): molecular size, glycosylation pattern, and engineering of proteolytic resistance
Appl. Environ. Microbiol.
65
359-366
1999
Aspergillus fumigatus, Aspergillus nidulans (O00093), Aspergillus niger (P34752), Aspergillus niger CB (P34752), Aspergillus niger Naturphos (P34752), Aspergillus terreus, Aspergillus terreus 9A1, Aspergillus terreus CBS, Escherichia coli, Thermomyces dupontii (O00096), Thermothelomyces heterothallicus (O00107)
brenda
Mitchell, D.B.; Vogel, K.; Weimann, B.J.; Pasamontes, L.; van Loon, A.P.G.M.
The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila
Microbiology
143
245-252
1997
Aspergillus niger, Aspergillus terreus, Aspergillus terreus 9A1, Thermothelomyces heterothallicus
brenda
Dvorakova, J.; Volfova, O.; Kopecky, J.
Characterization of phytase produced by Aspergillus niger
Folia Microbiol. (Praha)
42
349-352
1997
Aspergillus niger
brenda
Panchal, T.; Wodzinski, R.J.
Comparison of glycosylation patterns of phytase from Aspergillus niger (A. ficuum) NRRL 3135 and recombinant phytase
Prep. Biochem. Biotechnol.
28
201-217
1998
Aspergillus niger, Aspergillus niger NRRL 3135
brenda
Van Hartingsveldt, W.; van Zeijl, C.M.J.; Harteveld, C.M.; Gouka, R.J.; Suykerbuyk, M.E.G.; Luiten, R.G.M.; van Paridon, P.A.; Selten, G.C.M.; Veenstra, A.E.; van Gorcom, R.F.M.; van den Hondel, C.A.M.J.J.
Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger
Gene
127
87-94
1993
Aspergillus niger
brenda
Shieh, T.R.; Ware, J.H.
Survey of microorganisms for the production of extracellular phytase
Appl. Microbiol.
16
1348-1351
1968
Aspergillus awamori, Aspergillus carbonarius, Aspergillus ficuum, Aspergillus ficuum K, Aspergillus ficuum NRRL 3135, Aspergillus ficuum WB 320, Aspergillus ficuum WB 364, Aspergillus ficuum WB 4016, Aspergillus ficuum WB 4541, Aspergillus ficuum WB4781, Aspergillus ficuum X, Aspergillus flavus, Aspergillus niger, Aspergillus niger NRRL 326, Aspergillus niger NRRL 330, Aspergillus niger NRRL 372, Aspergillus niger NRRL 4361, Aspergillus niger NRRL337, Aspergillus niger NRRL372, Aspergillus phoenicis, Aspergillus terreus, Aspergillus tubingensis, Aspergillus tubingensis NRRL 4875, Aspergillus versicolor
brenda
Li, J.; Hegeman, C.E.; Hanlon, R.W.; Lacy, G.H.; Denbow, D.M.; Grabau, E.A.
Secretion of active recombinant phytase from soybean cell-suspension cultures
Plant Physiol.
114
1103-1111
1997
Aspergillus niger
brenda
Dvorakova, J.
Phytase: source, preparation and exploitation
Folia Microbiol. (Praha)
43
323-338
1998
Aspergillus carbonarius, Aspergillus carneus, Aspergillus fumigatus, Aspergillus niger, Aspergillus niger 92, Aspergillus niger IIIAn/8, Aspergillus niger NRRL 3135, Aspergillus oryzae, Aspergillus sp., Aspergillus terreus, Bacillus subtilis, Candida tropicalis, Citrobacter freundii, Debaryomyces castellii, Escherichia coli, Klebsiella aerogenes, Klebsiella oxytoca, Klebsiella oxytoca MO-3, Klebsiella sp., Kluyveromyces marxianus, Mucor sp., Neurospora sp., Paramecium sp., Penicillium camemberti, Penicillium sp., Raoultella terrigena, Rhizopus microsporus var. oligosporus, Saccharomyces cerevisiae, Schwanniomyces castellii, Torulopsis candida
brenda
Wyss, M.; Pasamontes, L.; Remy, R.; Kohler, J.; Kusznir, E.; Gadient, M.; Muller, F.; van Loon, A.P.G.M.
Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger PH 2.5 acid phosphatase
Appl. Environ. Microbiol.
64
4446-4451
1998
Aspergillus fumigatus, Aspergillus niger, Aspergillus niger T213
brenda
Mullaney, E.J.; Daly, C.B.; Kim, T.; Porres, J.M.; Lei, X.G.; Sethumadhavan, K.; Ullah, A.H.
Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0
Biochem. Biophys. Res. Commun.
297
1016-1020
2002
Aspergillus niger
brenda
Casey, A.; Walsh, G.
Purification and characterization of extracellular phytase from Aspergillus niger ATCC 9142
Bioresour. Technol.
86
183-188
2003
Aspergillus niger
brenda
Vohra, A.; Satyanarayana, T.
Phytases: microbial sources, production, purification, and potential biotechnological applications
Crit. Rev. Biotechnol.
23
29-60
2003
Aspergillus amstelodami, Aspergillus awamori (P34753), Aspergillus candidus, Aspergillus carbonarius, Aspergillus carneus, Aspergillus chevalieri, Aspergillus flavus, Aspergillus fumigatus (O00092), Aspergillus nidulans, Aspergillus nidulans (O00093), Aspergillus niger (O93838), Aspergillus niger (P34752), Aspergillus niger SK57 (O93838), Aspergillus pseudoglaucus, Aspergillus syndowi, Aspergillus terreus (O00085), Aspergillus terreus CBS (O00085), Aspergillus versicolor, Aspergillus wentii, Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) DS1, Bacillus subtilis, Blastobotrys adeninivorans, Botrytis cinerea, Candida tropicalis, Clavispora lusitaniae, Cyberlindnera rhodanensis, Enterobacter sp., Escherichia coli, Geotrichum candidum, Hanseniaspora valbyensis, Klebsiella aerogenes, Klebsiella oxytoca, Kluyveromyces lactis, Lachancea kluyveri, Lachancea thermotolerans, Lactobacillus amylovorus, Metschnikowia pulcherrima, Mitsuokella multacida, Mucor piriformis, Mucor racemosus, Neurospora sp., Penicillium caseoicolum, Penicillium sp., Pseudomonas sp., Rhizopus arrhizus, Rhizopus microsporus var. oligosporus, Rhizopus stolonifer, Scheffersomyces spartinae, Schwanniomyces castellii, Schwanniomyces occidentalis, Schwanniomyces yamadae, Selenomonas ruminantium, Thermomyces dupontii (O00096), Thermomyces lanuginosus, Thermothelomyces heterothallicus, Thermothelomyces heterothallicus (O00107), Torulaspora delbrueckii, Torulaspora globosa, Torulaspora pretoriensis, Wickerhamomyces anomalus, [Candida] intermedia
brenda
Tomschy, A.; Wyss, M.; Kostrewa, D.; Vogel, K.; Tessier, M.; Hofer, S.; Burgin, H.; Kronenberger, A.; Remy, R.; van Loon, A.P.; Pasamontes, L.
Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties
FEBS Lett.
472
169-172
2000
Aspergillus niger, Aspergillus niger NRRL 3135, Aspergillus niger T213
brenda
Wang, X.Y.; Meng, F.G.; Zhou, H.M.
Unfolding and inactivation during thermal denaturation of an enzyme that exhibits phytase and acid phosphatase activities
Int. J. Biochem. Cell Biol.
36
447-459
2004
Aspergillus niger
brenda
Jermutus, L.; Tessier, M.; Pasamontes, L.; van Loon, A.P.; Lehmann, M.
Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case
J. Biotechnol.
85
15-24
2001
Aspergillus niger, Aspergillus terreus, Aspergillus terreus 9A-1
brenda
Richardson, A.E.; Hadobas, P.A.; Hayes, J.E.
Extracellular secretion of Aspergillus phytase from Arabidopsis roots enables plants to obtain phosphorus from phytate
Plant J.
25
641-649
2001
Arabidopsis thaliana, Aspergillus niger
brenda
Brinch-Pedersen, H.; Hatzack, F.; Sorensen, L.D.; Holm, P.B.
Concerted action of endogenous and heterologous phytase on phytic acid degradation in seed of transgenic wheat (Triticum aestivum L.)
Transgenic Res.
12
649-659
2003
Aspergillus niger
brenda
Wang, X.Y.; Meng, F.G.; Zhou, H.M.
The role of disulfide bonds in the conformational stability and catalytic activity of phytase
Biochem. Cell Biol.
82
329-334
2004
Aspergillus niger
brenda
Vats, P.; Sahoo, D.K.; Banerjee, U.C.
Production of phytase (myo-inositolhexakisphosphate phosphohydrolase) by Aspergillus niger van Teighem in laboratory-scale fermenter
Biotechnol. Prog.
20
737-743
2004
Aspergillus niger
brenda
Kies, A.K.; De Jonge, L.H.; Kemme, P.A.; Jongbloed, A.W.
Interaction between protein, phytate, and microbial phytase. In vitro studies
J. Agric. Food Chem.
54
1753-1758
2006
Aspergillus niger
brenda
Pang, Y.; Applegate, T.J.
Effects of copper source and concentration on in vitro phytate phosphorus hydrolysis by phytase
J. Agric. Food Chem.
54
1792-1796
2006
Aspergillus niger
brenda
Vats, P.; Banerjee, U.C.
Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem
J. Ind. Microbiol. Biotechnol.
32
141-147
2005
Aspergillus niger
brenda
Lei, X.G.; Kim, T.
Expression of microbial phytases in yeast systems and characterization of the recombinant enzymes
Methods Biotechnol.
17
209-224
2005
Aspergillus niger (P34752)
-
brenda
Silversides, F.G.; Scott, T.A.; Bedford, M.R.
The effect of phytase enzyme and level on nutrient extraction by broilers
Poult. Sci.
83
985-989
2004
Aspergillus niger
brenda
Payne, R.L.; Lavergne, T.K.; Southern, L.L.
A comparison of two sources of phytase in liquid and dry forms in broilers
Poult. Sci.
84
265-272
2005
Aspergillus niger
brenda
Zhang, W.; Mullaney, E.J.; Lei, X.G.
Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase
Appl. Environ. Microbiol.
73
3069-3076
2007
Aspergillus fumigatus, Aspergillus niger
brenda
Zhang, W.; Lei, X.G.
Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis
Appl. Microbiol. Biotechnol.
77
1033-1040
2008
Aspergillus niger
brenda
Martin, J.A.; Murphy, R.A.; Power, R.F.
Purification and physico-chemical characterisation of genetically modified phytases expressed in Aspergillus awamori
Biores. Technol.
97
1703-1708
2006
Aspergillus awamori, Aspergillus niger, Aspergillus sp.
brenda
Cao, L.; Wang, W.; Yang, C.; Yang, Y.; Diana, J.; Yakupitiyage, A.; Luo, Z.; Li, D.
Application of microbial phytase in fish feed
Enzyme Microb. Technol.
40
497-507
2007
Aspergillus niger
-
brenda
Hill, G.M.; Link, J.E.; Rincker, M.J.; Kirkpatrick, D.L.; Gibson, M.L.; Karges, K.
Utilization of distillers dried grains with solubles and phytase in sow lactation diets to meet the phosphorus requirement of the sow and reduce fecal phosphorus concentration
J. Anim. Sci.
86
112-118
2008
Aspergillus niger
brenda
Zhao, D.M.; Wang, M.; Mu, X.J.; Sun, M.L.; Wang, X.Y.
Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics
Lett. Appl. Microbiol.
45
522-528
2007
Aspergillus niger (Q6T9Z6), Aspergillus niger N-J (Q6T9Z6)
brenda
Greiner, R.; Farouk, A.E.
Purification and characterization of a bacterial phytase whose properties make it exceptionally useful as a feed supplement
Protein J.
26
467-474
2007
Aspergillus niger
brenda
Noureddini, H.; Dang, J.
Degradation of Phytates in Distillers Grains and Corn Gluten Feed by Aspergillus niger Phytase
Appl. Biochem. Biotechnol.
159
11-23
2008
Aspergillus niger
brenda
Pires, A.S.; Cabral, M.G.; Fevereiro, P.; Stoger, E.; Abranches, R.
High levels of stable phytase accumulate in the culture medium of transgenic Medicago truncatula cell suspension cultures
Biotechnol. J.
3
916-923
2008
Aspergillus niger
brenda
Promdonkoy, P.; Tang, K.; Sornlake, W.; Harnpicharnchai, P.; Kobayashi, R.S.; Ruanglek, V.; Upathanpreecha, T.; Vesaratchavest, M.; Eurwilaichitr, L.; Tanapongpipat, S.
Expression and characterization of Aspergillus thermostable phytases in Pichia pastoris
FEMS Microbiol. Lett.
290
18-24
2009
Aspergillus japonicus (B3VPB2), Aspergillus niger (B3VPB3), Aspergillus japonicus BCC18313 (B3VPB2), Aspergillus niger BCC18081 (B3VPB3)
brenda
Ebrahimnezhad, Y.; Shivazad, M.; Taherkhani, R.; Nazeradl, K.
Effects of ethylenediaminetetraacetic acid on phytate phosphorus utilization and efficiency of microbial phytase in broiler chicks
J. Anim. Physiol. Anim. Nutr. (Berl.)
92
168-172
2008
Aspergillus niger
brenda
Gunashree, B.S.; Venkateswaran, G.
Effect of different cultural conditions for phytase production by Aspergillus niger CFR 335 in submerged and solid-state fermentations
J. Ind. Microbiol. Biotechnol.
35
1587-1596
2008
Aspergillus niger
brenda
Correia, I.; Aksu, S.; Adao, P.; Pessoa, J.C.; Sheldon, R.A.; Arends, I.W.
Vanadate substituted phytase: Immobilization, structural characterization and performance for sulfoxidations
J. Inorg. Biochem.
102
318-329
2008
Aspergillus niger
brenda
Emiola, A.; Akinremi, O.; Slominski, B.; Nyachoti, C.M.
Nutrient utilization and manure P excretion in growing pigs fed corn-barley-soybean based diets supplemented with microbial phytase
Anim. Sci. J.
80
19-26
2009
Aspergillus niger
brenda
Mullaney, E.J.; Locovare, H.; Sethumadhavan, K.; Boone, S.; Lei, X.G.; Ullah, A.H.
Site-directed mutagenesis of disulfide bridges in Aspergillus niger NRRL 3135 phytase (PhyA), their expression in Pichia pastoris and catalytic characterization
Appl. Microbiol. Biotechnol.
87
1367-1372
2010
Aspergillus niger, Aspergillus niger (P34752), Aspergillus niger NRRL 3135, Aspergillus niger NRRL 3135 (P34752)
brenda
Vats, P.; Bhushan, B.; Banerjee, U.C.
Studies on the dephosphorylation of phytic acid in livestock feed using phytase from Aspergillus niger van Teighem
Biores. Technol.
100
287-291
2009
Aspergillus niger
brenda
George, T.; Richardson, A.; Li, S.; Gregory, P.; Daniell, T.
Extracellular release of a heterologous phytase from roots of transgenic plants: Does manipulation of rhizosphere biochemistry impact microbial community structure?
FEMS Microbiol. Ecol.
70
433-445
2009
Aspergillus niger, Peniophora lycii
brenda
Harnpicharnchai, P.; Sornlake, W.; Tang, K.; Eurwilaichitr, L.; Tanapongpipat, S.
Cell-surface phytase on Pichia pastoris cell wall offers great potential as a feed supplement
FEMS Microbiol. Lett.
302
8-14
2010
Aspergillus niger
brenda
Weaver, J.D.; Ullah, A.H.; Sethumadhavan, K.; Mullaney, E.J.; Lei, X.G.
Impact of assay conditions on activity estimate and kinetics comparison of Aspergillus niger PhyA and Escherichia coli AppA2 phytases
J. Agric. Food Chem.
57
5315-5320
2009
Aspergillus niger, Escherichia coli
brenda
Chen, R.; Xue, G.; Chen, P.; Yao, B.; Yang, W.; Ma, Q.; Fan, Y.; Zhao, Z.; Tarczynski, M.; Shi, J.
Transgenic maize plants expressing a fungal phytase gene
Transgenic Res.
17
633-643
2008
Aspergillus niger
brenda
Oakley, A.J.
The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic
Biochem. Biophys. Res. Commun.
397
745-749
2010
Aspergillus niger
brenda
Ullah, A.H.; Sethumadhavan, K.; Mullaney, E.J.
Vanadate inhibition of fungal PhyA and bacterial AppA2 histidine acid phosphatases
J. Agric. Food Chem.
59
1739-1743
2011
Aspergillus niger, Escherichia coli (Q6RK08)
brenda
Giaveno, C.; Celi, L.; Richardson, A.; Simpson, R.; Barberis, E.
Interaction of phytases with minerals and availability of substrate affect the hydrolysis of inositol phosphates
Soil Biol. Biochem.
42
491-498
2010
Aspergillus niger
brenda
Tian, Y.; Peng, R.; Xu, J.; Zhao, W.; Gao, F.; Fu, X.; Xiong, A.; Yao, Q.
Mutations in two amino acids in phyI1s from Aspergillus niger 113 improve its phytase activity
World J. Microbiol. Biotechnol.
26
903-907
2010
Aspergillus niger, Aspergillus niger 113
brenda
Spier, M.; Fendrich, R.; Almeida, P.; Noseda, M.; Greiner, R.; Konietzny, U.; Woiciechowski, A.; Soccol, V.; Soccol, C.
Phytase produced on citric byproducts: purification and characterization
World J. Microbiol. Biotechnol.
27
267-274
2011
Aspergillus niger, Aspergillus niger FS3
brenda
Chen, R.; Zhang, C.; Yao, B.; Xue, G.; Yang, W.; Zhou, X.; Zhang, J.; Sun, C.; Chen, P.; Fan, Y.
Corn seeds as bioreactors for the production of phytase in the feed industry
J. Biotechnol.
165
120-126
2013
Aspergillus niger
brenda
Wang, Y.; Ye, X.; Ding, G.; Xu, F.
Overexpression of phyA and appA genes improves soil organic phosphorus utilisation and seed phytase activity in Brassica napus
PLoS ONE
8
e60801
2013
Aspergillus niger (P34752)
brenda
Noorbatcha, I.A.; Sultan, A.M.; Salleh, H.M.; Amid, A.
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study
Protein J.
32
309-316
2013
Aspergillus niger (P34752), Aspergillus niger
brenda
Ushasree, M.V.; Vidya, J.; Pandey, A.
Replacement P212H altered the pH-temperature profile of phytase from Aspergillus niger NII 08121
Appl. Biochem. Biotechnol.
175
3084-3092
2015
Aspergillus niger (G8GYH6), Aspergillus niger, Aspergillus niger NII 08121 (G8GYH6)
brenda
Tang, Z.; Jin, W.; Sun, R.; Liao, Y.; Zhen, T.; Chen, H.; Wu, Q.; Gou, L.; Li, C.
Improved thermostability and enzyme activity of a recombinant phyA mutant phytase from Aspergillus niger N25 by directed evolution and site-directed mutagenesis
Enzyme Microb. Technol.
108
74-81
2018
Aspergillus niger (P34754), Aspergillus niger N25 (P34754)
brenda