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Information on EC 3.1.3.8 - 3-phytase and Organism(s) Aspergillus niger and UniProt Accession P34752

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.8 3-phytase
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This record set is specific for:
Aspergillus niger
UNIPROT: P34752 not found.
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Word Map
The taxonomic range for the selected organisms is: Aspergillus niger
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
microbial phytase, natuphos, alkaline phytase, 3-phytase, phytase a, beta-propeller phytase, atpap15, cell-bound phytase, acid phytase, appa2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phytase
-
-
-
-
3'-phytase
-
-
acid phytase
-
-
Allzyme phytase
-
commercial preparation
Aspergillus niger N25 phytase
-
histidine acid phosphatase
-
-
microbial phytase
-
-
myo-inositol hexaphosphate phosphohydrolase
-
MYO-inositol-hexaphosphate 3-phosphohydrolase
-
-
-
-
myo-inositol-hexaphosphate phosphohydrolase
-
-
Natuphos
pH 2.5 optimum acid phosphatase
-
-
-
-
phytase
phytate 1-phosphatase
-
-
-
-
Phytate 3-phosphatase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 3-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-11-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
show the reaction diagram
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
show the reaction diagram
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
show the reaction diagram
2-naphthyl phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
-
63.6% of the activity with myo-inositol hexakisphosphate
-
?
2-phosphoglycerate + H2O
glyceric acid + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
6-phosphogluconate + H2O
gluconate + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
no activity
-
-
?
AMP + phosphate
adenosine + phosphate
show the reaction diagram
-
43.9% of the activity with myo-inositol hexakisphosphate
-
?
ATP + H2O
?
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
28.6% of the activity with myo-inositol hexakisphosphate
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
glycerol 3-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
phytate + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
show the reaction diagram
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
show the reaction diagram
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
show the reaction diagram
phytate + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme production is strongly repressed by inorganic phosphates and requires a high carbon to phosphorus ratio in the medium
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
53% activation at 1 mM, 46% activation at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Cd2+
-
200 mM, activation to 156% of control
Co2+
-
35% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
Cu2+
-
200 mM, activation to 160% of control
Fe2+
-
13% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
K+
-
40% activation at 1 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
vanadate
-
incubation with vanadate to obtain a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate
additional information
-
no effect is observed after addition of 200 mM Fe2+ or Fe3+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
phosphate
-
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
2.5
ADP
-
pH 5.5, 50°C
1.75
ATP
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043 - 0.005
myo-inositol-1,2,3,4,5,6-hexakisphosphate
16.14 - 5000
myo-inositol hexakisphosphate
1874
myo-inositol hexakisphosphate disodium salt
pH 5.5, 50°C
1584
myo-inositol hexakisphosphate sodium salt
pH 5.5, 50°C
19.17 - 30.5
myo-inositol-1,2,3,4,5,6-hexakisphosphate
0.0039
phytate
-
pH 2.5, 55°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056
metavanadate
-
pH 2.5, 55°C, 0.015 mM metavanadate
-
0.0046
myo-inositol-1,2,3,4,5,6-hexakissulfate
-
pH 5.0-5.5, temperature not specified in the publication
0.0057
orthovanadate
-
pH 2.5, 55°C, 0.010 mM orthovanadate
additional information
additional information
-
vanadate inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.1
-
purified recombinant His-tagged mutant K41E, pH 5.0, 37°C
27.28
-
purified recombinant His-tagged mutant E121F, pH 5.0, 37°C
286923
recombinant mutant Q172R/K432R/Q368E/F376Y/T195L, pH 5.5, 37°C
303715
recombinant PP-NPep-6A mutant enzyme, pH 5.5, 37°C
438366
recombinant mutant Q172R/K432R, pH 5.5, 37°C
466688
recombinant mutant Q172R, pH 5.5, 37°C
467242
recombinant mutant Q172R/K432R/Q368E, pH 5.5, 37°C
478761
recombinant mutant T195L/Q368E/F376Y, pH 5.5, 37°C
493308
recombinant mutant Q172R/K432R/Q368E/F376Y, pH 5.5, 37°C
503
recombinant enzyme, at 37°C
503217
recombinant mutant Q368E/K432R, pH 5.5, 37°C
8.82
-
purified recombinant His-tagged wild-type enzyme, pH 5.0, 37°C
86.1
-
purified native enzyme, pH 5.5, 50°C, substrate phytate
870
-
pH 6.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
recombinant mutant C435G
5 - 5.5
strain NRRL 3135, an a second optimum at pH 2.2
5.5
recombinant mutant C31G
6
recombinant mutant C264G
11.5
-
and a second higher pH-optimum at pH 11.5
2
-
optimum 1
2.2
strain NRRL 3135, an a second optimum at pH 5.0-5.5
2.5 - 5
-
hydrolysis of myo-inositol hexakisphosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6
pH 3.5: about 40% of maximal activity, pH 6.0: about 80% of maximal activity, pH 6.5: about 30% of maximal activity. enzyme expressed in Saccharomyces cerevisiae
1.5 - 3
-
pH 1.5: about 50% of maximal activity, pH 3.0: about 55% of maximal activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2 - 12
-
pH 2.0: about 45% of maximal activity, 12.0: about 25% of maximal activity
2 - 5.7
-
pH 2.0: about 10% of maximal activity, pH 5.7: about 40% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
2 - 7.5
activity range, profile overview
2.5
wild-type enzyme exhibits high activity at, bi-peak profile
2.5 - 5.5
-
pH-activity profile, with optima at pH 2.5 with 60% of maximal activity, and at pH 5.0-5.5 with maximal activity, and a local minimum at pH 3.5
5.5
wild-type enzyme exhibits high activity at, bi-peak profile
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant mutants C215S and C264G
42
recombinant mutant C435G
53
recombinant mutant C31G
40
-
assay at
42
mutant C435G
63
-
at pH 5.0
66
-
at pH 4.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
activity range, profile overview
45 - 65
-
45°C: about 65% of maximal activity, 65°C: about 30% of maximal activity. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
45 - 75
-
45°C: about 45% of maximal activity, 75°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
growth on citric pulp fermentation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant protein, localization to cell suface of Pichia pastoris with a glycosylphosphatidylinositiol anchoring system
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
transgenic expression in Brassica napus with a signal peptide sequence. Transgenic lines exhibit significantly higher exuded phytase activity when compared to wild-type controls. Transgenic Brassica napus has significantly improved phosphate uptake and plant biomass. Seed yields of transgenic increase by 20.9% when compared to wild-type. When phytate is used as the sole phosphate source, phosphate accumulation in seeds increases by 20.6. Phytase activities in transgenic canola seeds range from 1,138 to 1,605 U/kg seeds, while no phytase activity is detected in wild-type seeds. Phytic acid content in seeds is significantly lower than in wild-type
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHYA_ASPNG
467
0
51086
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
Aspergillus niger CB, gel filtration
48423
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
64890
Aspergillus niger Natuphos, analytical ultracentrifugation
66360
1 * 66360, Aspergillus niger Naturphos, SDS-PAGE
71020
Aspergillus niger CB, analytical ultracentrifugation
74530
1 * 74530, Aspergillus niger CB, SDS-PAGE
82360
Aspergillus niger Natuphos, SDS-PAGE
85000 - 100000
strain NRRL 3135
100000
108000
-
x * 108000, SDS-PAGE
47000
-
x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
48800
-
x * 48800, calculation from nucleotide sequence
49200
calculated molecular weight
55000
-
1 * 55000, SDS-PAGE after deglycosylation
60000
-
x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
66000
70000
-
x * 70000, SDS-PAGE
80000
84000
85000 - 100000
-
strain NRRL3135
87000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
recombinant enzyme expressed in yeast is highly glycosylated
side-chain modification
glycoprotein
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulation and comparison between wild-type and thermostable mutant A35E/P42S/Q168R/T248R 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
deglycosylated PhyA free or in complex with inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, vapour-diffusion hanging drop technique, reservoirs contain 1 ml of PEG 3350 at 15-30% w/v, and ammonium nitrate a t0.1-0.4 M, siliconized coverslips are used to suspend a drop containing 0.002 ml of phytase at 13 mg/ml protein concetration and 0.002 ml of reservoir solution over the reservoir, X-ray diffraction structure determination and analysis at 2.2-2.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
-
no activity
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
P212H
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
-
no activity
R168A/R248A
-
no activity and decreased thermostability
R248A
-
no activity
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
-
40°C, 2 h, stable
114253
2 - 8
-
692398
6.5
-
Allzyme phytase can keep more than 60% of activity when pH reaches above 6.5
679568
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
30 min, stable, enzyme expressed in Saccharomyces cerevisiae or Pichia pastoris
65
30 min, enzyme expressed in Saccharomyces cerevisiae loses about 30% of initial activity, enzyme expressed in Pichia pastoris loses about 45% of initial activity
30
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
37
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
40
-
pH 2-7, 2 h, stable
45
-
24 h, stable. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
45 - 50
-
there are two phases in thermal inactivation: when the temperature is between 45°C and 50°C, the thermal inactivation can be characterized as an irreversible inactivation which has some residual activity and when the temperature is above 55°C the thermal inactivation can be characterized as an irreversible process which has no residual activity
49
-
t1/2: 138 min, wild-type enzyme
50
-
20 min, about 15% loss of activity
50 - 70
-
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C
63
-
10 min, 10% loss of the activity of the recombinant phytase, 25% loss of the activity of the fungal enzyme
65
-
half-life: 30 min in absence of stabilizing agent, 6 h in presence of 20 mM glycine, 2 h in presence of 10 mM CaCl2. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
66.3
-
the melting temperature of the wild type enzyme is 66.3°C
75
-
NatuPhos can maintain 75% activity under 75°C for 15 min
90
retains 70% activity after exposure to 90°C for 5 min and 65% activity after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant
denaturation in urea, in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
enzyme is resistant to pepsin
the enzyme is inactivated by pelleting above 80°C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,2-dimethoxyethane
-
presence of 30% increases the alpha-helical content of the phytase
acetonitrile
-
presence decreases the alpha-helical content of the phytase
Ethanol
-
presence of 30% increases the alpha-helical content of the phytase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified native enzyme, after 30 days, 88.9% activity are remaining, after 60 days the remaining activity is 84.25% of initial activity, and after 180 days 57.5%
-
4°C, stable for 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme mutant enzymes from Pichia pastoris strain X33 by ammonium sulfate fractionation, and two different steps of ion exchange chromatography
a 1.5fold higher enzyme yield in the presence of sucrose in both submerged and solid-state fermentations, while peptone is found to be a favorable nitrogen source for submerged fermentations. NaH2PO4 favors 34% higher enzyme yield than the control, which is followed by 19% higher activity in KH2PO4 in solid-state fermentation at 0.015% w/v. The addition of Tween-20 in submerged fermentations shows a maximum yield of 12.6 U/ml while, SDS suppresses the growth of the fungus. None of the surfactants favors the enzyme yield in solid-state fermentation. CaCl2 is extensively efficient in stimulating more than 55% higher phytase production in submerged fermentation at 0.01% v/v. In solid-state fermentation, none of the metal salts stimulates phytase production
-
DEAE cation exchange chromatography and Sephadex100 gel filtration
-
native enzyme 10.1fold by cationic exchange chromatography, anionic exchange chromatography, and chromatofocusing
-
nickel-nitrilotriacetic acid metal affinity chromatography, DEAE cation-exchange chromatography, and Sephadex-100 gel filtration
-
recombinant mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography
recombinant N-terminally His6-tagged wild-type and mutant enzymes by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Kluyveromyces lactis strain GG799 culture supernatant by lyophilization, anion exchange chromatography, and hydrophobic interaction chromatography
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris (constitutive or inducible) and Saccharomyces cerevisiae (inducible)
gene phyA, expression in Pichia pastoris strain X33, subcloning in Escherichia coli strain JM109 and DH5alpha
concerted action of endogenous phytase, EC 3.1.3.26, and heterologous phytase from Aspergillus niger, EC 3.1.3.8, on phytic acid degradation in seed of transgenic Triticum aestivum L.
-
expressed in Pichia pastoris strain GS115
expressed in Pichia pastoris strain X33
-
expression in Arabidopsis thliana. The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
-
expression in Glycine max, inserted into soybean transformation plasmid under control of constitutive and seed-specific promoters
-
expression in Medicago truncatula
-
expression in Nicotiana tabacum
-
expression in Pichia pastoris
expression in Zea mays
-
gene phyA, the mutants are constructed and expressed in Kluyveromyces lactis strain GG799, the enzymes are secreted
gene phyI1s, DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged wild-type and mutant enzymes
-
recombinant expression of wild-type and mutant enzymes in Kluyveromyces lactis strain GG799, the enzymes are secreted
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
agriculture
analysis
biotechnology
nutrition
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Dvorakova, J.; Volfova, O.; Kopecky, J.
Characterization of phytase produced by Aspergillus niger
Folia Microbiol. (Praha)
42
349-352
1997
Aspergillus niger
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Casey, A.; Walsh, G.
Purification and characterization of extracellular phytase from Aspergillus niger ATCC 9142
Bioresour. Technol.
86
183-188
2003
Aspergillus niger
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team