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Information on EC 3.1.3.26 - 4-phytase and Organism(s) Escherichia coli and UniProt Accession P07102
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EC Tree
3.1.3.26 4-phytaseSpecify your search results
Word Map
- 3.1.3.26
- phosphorus
-
broiler
- meal
- aspergillus
-
phytic
- wheat
-
bird
- ash
- soybean
- phosphatases
- corn
- tibia
-
poultry
-
corn-soybean
-
starter
-
digesta
- xylanase
- bran
- cereal
-
allotted
-
monogastric
-
meal-based
-
quadratic
- flour
-
barrows
-
manure
- ileum
-
feedstuffs
-
p-deficient
- hexaphosphate
-
antinutritional
- gizzard
-
metabolizable
-
indigestible
-
grower
- synthesis
-
excreta
- agriculture
-
housed
- uteroferrin
- biotechnology
-
chromic
-
coli-derived
-
wheat-based
-
non-starch
-
equivalency
- food industry
-
cereal-based
-
insps
-
antinutrient
-
corn-based
-
sourdough
- apase
-
carbohydrase
- nutrition
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phytase, purple acid phosphatase, 6-phytase, histidine acid phosphatase, ronozyme, phytase b, phya2, multiple inositol polyphosphate phosphatase, phya1, minpp, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phytase
AppA2 phytase
phytase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
6-phytase
-
-
-
-
AppA2 phytase
-
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 4-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-89-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
additional information
?
-
-
highest activity under anaerobic conditions, during the exponential growth no activity observed
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
strong affinity for sodium phytate as substrate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
-
-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
constitutive enzyme
-
?
additional information
?
-
-
highest activity under anaerobic conditions, during the exponential growth no activity observed
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na+
a high concentration of sodium chloride shifts the pH optimum to 2.0 from 5.5
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 (smal intestinal digesta) phytate phosphorus hydrolysis is greatly inhibited
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01945
myo-inositol hexakisphosphate
pH 5.0, 37°C, recombinant wild-type enzyme, substrate is sodium phytate
0.35
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
0.36
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73S, pH 4.5, 37°C
0.53
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73D, pH 4.5, 37°C
0.61
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73E, pH 4.5, 37°C
0.67
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73T, pH 4.5, 37°C
0.016
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 4.5, at 37°C
0.3
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.7
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
0.8
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Pichia pastoris (pGAPZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.2
myo-inositol hexakisphosphate
-
37°C, pH 3.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.5
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Schizosaccharomyces pombe. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
1.8
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Pichia pastoris (pGAPZalphaA) or Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
2.1
myo-inositol hexakisphosphate
-
37°C, pH 5.5, enzyme expressed in Saccharomyces cerevisiae. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6931
myo-inositol hexakisphosphate
-
in 0.1 M sodium acetate buffer, pH 4.5, at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
661
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73T, pH 4.5, 37°C
1199
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73E, pH 4.5, 37°C
1554
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73D, pH 4.5, 37°C
6017
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant enzyme mutant G73S, pH 4.5, 37°C
6776
myo-inositol-1,2,3,4,5,6-hexakisphosphate
recombinant wild-type enzyme, pH 4.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
a high concentration of sodium chloride shifts the pH optimum to 2.0 from 5.5
5.5
3.5
4.5
3.5
-
recombinant enzyme. 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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 5.5
-
pH 2.0: about 70% of maximal activity, pH 5.5: 40-50% of maximal activity enzyme, recombinant enzyme from different expression systems. 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
3 - 5.7
-
pH 3.0: about 30% of maximal activity, pH 5.7: about 70% of maximal activity, hydrolysis of myo-inositol hexakisphosphate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
55
-
recombinant enzyme. 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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
activity range of wild-type and mutant enzyme, profile overview
37 - 65
-
37°C: about 35% of maximal activity, 65°C: 60-80% of maximal activity, recombinant enzyme from different expression systems. 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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
transgenic expression in Brassica napus. 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 59% when compared to wild-type. When phytate is used as the sole phosphate source, phosphate accumulation in seeds increases by 47. 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
additional information
catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
additional information
-
catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
molecular modeling using the crystal structure, overview
additional information
-
molecular modeling using the crystal structure, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G73D
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73E
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73L
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73S
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73T
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G73Y
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
S392F
site-directed mutagenesis, three-dimensional structure analysis, modeling, and comparison to wild-type structure. The mutant phytase shows 12.8%, 9.6% and 10.3% higher phytase activity at pH 6, 7 and 8, respectively, compared to wild-type enzyme, and the mutant enzymes shows thermostability improvement of 74% and 78.4% at 80°C and 90°C, respectively, compared to wild-type
D144N/V227A
38% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D
mutant releases 25% more inorganic phosphorus from soy phytate than the wild-type enzyme, mutant shows higher thermostability compared to wild-type, Km (myo-inositol hexakisphosphate) lower compared to wild-type, kcat similar to wild-type
D144N/V227A/G344D/D112N
7% higher specific activity than wild-type, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/D112N/K46E/G103S/S209G
23% higher specific activity than wild-type, lower efficiency for soy phytate hydrolysis compared to wild-type enzyme
D144N/V227A/G344D/K46E
similar efficiency for soy phytate hydrolysis as compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
D144N/V227A/G344D/K65E
lower efficiency for soy phytate hydrolysis compared to wild-type enzyme, mutant shows higher thermostability compared to wild-type
Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
-
highly active phytase with no loss of activity after heating at 62°C for 1 h and 27% of its initial activity after 10 min at 85°C, which is a significant improvement over the appA parental phytase. The mutant enzyme also shows a 3.5fold enhancement in gastric stability
additional information
additional information
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
additional information
-
no further improvement in thermostability is observed by adding other mutations to D144N/V227A/G344D, which might result from unfavorable electrostatic interactions or structural perturbation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
10 min, stable, recombinant enzyme from different expression systems. 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
60
62
-
1 h, no loss of activity, mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
65
-
10 min, 55-70% loss of activity, recombinant enzyme from different expression systems. 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
75
-
10 min, 10-20% loss of activity, recombinant enzyme from different expression systems. 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
75.7
-
Tm-value for mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
85
-
10 min, 27% loss of activity,mutant enzyme Q84W/Y277D/W68E/K97C/R181Y/N226C/A95P/S168E
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme expressed in Pichia pastoris is not inactivated by pelleting above 80°C, enzyme expressed in Saccharomyces cerevisiae and Pseudomonas fluorescens are inactivated by pelleting above 80°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 by gel filtration to homogeneity
purified by ultrafiltration and Macro-Prep high S-cation exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene APPA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115
gene appA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
expression of the enzyme in three inducible yeast systems: Saccharomyces cerevisiae (pYES2), Schizosaccharomyces pombe (pDS472a), and Pichia pastoris (pPICZalphaA), and one constitutive system: Pichia pastoris (pGAPTalphaA). During 8-day batch fermentation in shaking flasks, the inducible Pichia system produces the highest activity whereas the Schizosaccharomyces pombe system produces the lowest 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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Greiner, R.; Konietzny, U.; Jany, K.D.
Purification and characterization of two phytases from Escherichia coli
Arch. Biochem. Biophys.
303
107-113
1993
Escherichia coli
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
Garrett, J.B.; Kretz, K.A.; O'Donoghue, E.; Kerovuo, J.; Kim, W.; Barton, N.R.; Hazlewood, G.P.; Short, J.M.; Robertson, D.E.; Gray, K.A.
Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement
Appl. Environ. Microbiol.
70
3041-3046
2004
Escherichia coli
Lee, S.; Kim, T.; Stahl, C.H.; Lei, X.G.
Expression of Escherichia coli AppA2 phytase in four yeast systems
Biotechnol. Lett.
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2005
Escherichia coli
Pang, Y.; Applegate, T.J.
Effects of copper source and concentration on in vitro phytate phosphorus hydrolysis by phytase
J. Agric. Food Chem.
54
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2006
Escherichia coli, Peniophora lycii
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
Escherichia coli
Cowieson, A.J.; Ravindran, V.
Effect of phytic acid and microbial phytase on the flow and amino acid composition of endogenous protein at the terminal ileum of growing broiler chickens
Br. J. Nutr.
98
745-752
2007
Escherichia coli
Elkhalil, E.A.; Maenner, K.; Borriss, R.; Simon, O.
In vitro and in vivo characteristics of bacterial phytases and their efficacy in broiler chickens
Br. Poult. Sci.
48
64-70
2007
Escherichia coli
Augspurger, N.R.; Webel, D.M.; Baker, D.H.
An Escherichia coli phytase expressed in yeast effectively replaces inorganic phosphorus for finishing pigs and laying hens
J. Anim. Sci.
85
1192-1198
2007
Escherichia coli
Martinez-Amezcua, C.; Parsons, C.M.; Baker, D.H.
Effect of microbial phytase and citric acid on phosphorus bioavailability, apparent metabolizable energy, and amino acid digestibility in distillers dried grains with solubles in chicks
Poult. Sci.
85
470-475
2006
Escherichia coli
Cowieson, A.J.; Acamovic, T.; Bedford, M.R.
Phytic acid and phytase: implications for protein utilization by poultry
Poult. Sci.
85
878-885
2006
Escherichia coli
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
Escherichia coli, Peniophora lycii
Greiner, R.; Farouk, A.E.; Carlsson, N.G.; Konietzny, U.
myo-inositol phosphate isomers generated by the action of a phytase from a Malaysian waste-water bacterium
Protein J.
26
577-584
2007
Escherichia coli, Secale cereale
Kim, M.S.; Weaver, J.D.; Lei, X.G.
Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase
Appl. Microbiol. Biotechnol.
79
751-758
2008
Escherichia coli (Q6RK08), Escherichia coli
Ullah, A.H.; Sethumadhavan, K.; Mullaney, E.J.
Salt effect on the pH profile and kinetic parameters of microbial phytases
J. Agric. Food Chem.
56
3398-3402
2008
Aspergillus niger, Escherichia coli (P07102), Escherichia coli
Fu, D.; Li, Z.; Huang, H.; Yuan, T.; Shi, P.; Luo, H.; Meng, K.; Yang, P.; Yao, B.
Catalytic efficiency of HAP phytases is determined by a key residue in close proximity to the active site
Appl. Microbiol. Biotechnol.
90
1295-1302
2011
Escherichia coli (P07102), Escherichia coli
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
Escherichia coli (P07102)
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