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Information on EC 3.1.3.8 - 3-phytase and Organism(s) Bacillus subtilis and UniProt Accession P42094
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3.1.3.8 3-phytaseSpecify your search results
Word Map
- 3.1.3.8
- phosphorus
- meal
-
broiler
- ash
- phytases
-
corn-soybean
- agriculture
- synthesis
-
phytic
-
barrows
- tibia
-
allotted
-
housed
-
meal-based
-
digesta
-
quadratic
-
nonphytate
-
phytase-supplemented
-
equivalency
-
growing-finishing
- nutrition
-
monogastric
-
excreta
-
indigestible
- ficuum
-
dicalcium
-
chromic
-
manure
-
p-deficient
-
corn-based
-
gain:feed
-
phytate-p
-
grower
-
crates
-
maize-soybean
-
low-phosphorus
-
t-cannulas
- 6-phytase
-
phosphorus-deficient
-
monocalcium
-
phytate-degrading
- food industry
-
as-fed
- biotechnology
-
feedstuffs
-
cornstarch
-
wheat-based
- analysis
-
metabolisable
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
microbial phytase, natuphos, alkaline phytase, 3-phytase, phytase a, beta-propeller phytase, atpap15, cell-bound phytase, acid phytase, appa2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-phytase
-
-
-
-
MYO-inositol-hexaphosphate 3-phosphohydrolase
-
-
-
-
pH 2.5 optimum acid phosphatase
-
-
-
-
PhyC
phytase
phytase C
phytate 1-phosphatase
-
-
-
-
Phytate 3-phosphatase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
phytase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 3-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
37288-11-2
-
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 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
ADP + H2O
? + phosphate
80% of the activity with myo-inositol hexakisphosphate
-
-
?
AMP + H2O
adenosine + phosphate
10% of the activity with myo-inositol hexakisphosphate
-
-
?
ATP + H2O
? + phosphate
97% 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
-
-
-
-
?
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
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
after 10 min D-myo-inositol 1,2,4,5,6-pentakisphosphate is the major degradation product, accompanied by small amounts of D-myo-inositol 1,2,3,4,6-pentakisphosphate, D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate. After 30 min, the quantity of D-myo-inositol 1,2,4,5,6-pentakisphosphate decreases and the levels of D-myo-inositol 2,4,5,6-tetrakisphosphate and D-myo-inositol 1,2,35-tetrakisphosphate increases. After 90 min the major products are Ins(1,3,5) P3 and Ins(2,4,6)P3
?
myo-inositol hexakisphosphate + H2O
myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
highest activity at 2.05 mM substrate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
phytate
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
? + phosphate
-
substrate Na-phytate
-
-
?
additional information
?
-
-
the native enzyme is also active on ADP, ATP, alpha- and beta-glycerophosphate, 2-naphthyl phosphate, and 4-nitrophenyl phosphate. No activity with sodium tripolyphosphate, fructose-6-phosphate, diphosphate, AMP
-
-
?
additional information
?
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
additional information
?
-
-
enzyme activity assay using color reagent containing 1.5% w/v ammonium molybdate, 5.5% v/v sulfuric acid solution, and 2.7% w/v ferrous sulfate
-
-
?
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 1,2,4,5,6-pentakisphosphate + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-inositol hexakisphosphate + H2O
? + phosphate
-
inducible enzyme
-
?
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Ca2+
-
the crystal structure of the enzyme in complex with inorganic phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site
Ca2+
required, assay in presence of 1.5 mM. The removal of Ca2+ causes a change in the CD-spectrum. The addition of Ca2+ to the apoenzyme results in an increase in the mean residue ellipticity, indicating a recovery of beta-sheet elements
additional information
-
the enzyme is inhibited by metal ions Mn2+, Zn2+, Ca2+, Cu2+, Fe2+, Mg2+, and Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by myo-inositol hexasulfate up to 2 mM, no inhibition by F- up to 10 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
0.49
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
0.54
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
0.78
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
1.4
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
1.5
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
1.77
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
2.19
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
typical Michaelis-Menten kinetics
-
additional information
additional information
-
typical Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1837.8
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
2450.5
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
2510.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
2527.8
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
4965.7
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
7367.6
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
7860
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
8430.1
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2267.5
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant wild-type enzyme
2368.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant wild-type enzyme
4695.6
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G
4767.2
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K265N
5080.3
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K265N
5231.8
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G/K70R/K111E/N121S
5258.8
myo-inositol hexakisphosphate
pH 7.0, 37°C, recombinant mutant D24G
6235.5
myo-inositol hexakisphosphate
pH 4.5, 37°C, recombinant mutant D24G/K70R/K111E/N121S
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13.82
purified recombinant His-tagged wild-type enzyme, pH 7.0, 60°C
17.24
purified recombinant His-tagged mutant S51A/K265E, pH 7.0, 60°C
18.14
purified recombinant His-tagged mutant D24G/S51A, pH 7.0, 60°C
18.17
purified recombinant His-tagged mutant D24G/N121S, pH 7.0, 60°C
18.88
purified recombinant His-tagged mutant D24G/K111E, pH 7.0, 60°C
19.27
purified recombinant His-tagged mutant D24G/K265E, pH 7.0, 60°C
19.33
purified recombinant His-tagged mutant D24G/S51A/K265E, pH 7.0, 60°C
19.67
purified recombinant His-tagged mutant D24G/K70R, pH 7.0, 60°C
19.7
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Escherichia coli, pH 7.0, 60°C
19.72
purified recombinant His-tagged mutant D24G/K265N, pH 7.0, 60°C
19.73
purified recombinant His-tagged mutant D24G/K70R/K111E/N121S, pH 7.0, 60°C
22.7
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Pichia pastoris, pH 7.0, 60°C
30.4
purified recombinant enzyme mutant D24G/K70R/K111E/N121S, expressed in Bacillus subtilis, pH 7.0, 60°C
8.9
recombinant enzyme secreted from heterologously expressing Pichia pastoris, pH 5.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
-
pH 5.5: about 35% of maximal activity, pH 7.5: about 95% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
37
55
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 65
-
37°C: about 40% of maximal activity, 65°C: about 40% of maximal activity
additional information
additional information
the highest activities of wild-type and D24G expressed in Pichia pastoris are achieved at 50°C and 55°C, decreased by 10°C and 5°C compared to those expressed in Escherichia coli, respectively. Temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis, overview
additional information
-
the highest activities of wild-type and D24G expressed in Pichia pastoris are achieved at 50°C and 55°C, decreased by 10°C and 5°C compared to those expressed in Escherichia coli, respectively. Temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
molecular docking of wild-type and mutant enzymes, homology modelling using the enzyme structure of the phytase from Bacillus amyloliquefaciens (PDB ID 2POO) as the template, overview. Residues D24, S51 and K70 have a relatively large influence on the catalytic activity probably because they are adjacent to the active site cleft. The enzyme is composed of six beta-sheets and possesses six calcium binding sites. The 25 amino acid residues except V60, involved in calcium binding, are highly conserved
additional information
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
-
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
additional information
-
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 45000, Pichia pastoris-expressed Phy168 after deglycosylation, SDS-PAGE
?
x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
two potential N-glycosylated sites within the Asn-Xaa-Ser/Thr sequence are found in the phy168 phytase. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115
proteolytic modification
the mature peptide sequence lacked RHGXRXP, a conserved motif at the catalytic site of acidic phytases. The enzyme contains a signal peptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the enzyme in complex with phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D24G
D24G/K111E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K265N
D24G/K70R
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R/K111E/N121S
D24G/N121S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A
site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type at pH 7.0, 60°C
D24G/S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
K265E
S51A
S51A/K265E
additional information
D24G
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G shows 62.7, 68.3, and 17.9% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. The specific activity of the Escherichia coli-expressed D24G at pH 7.0 and 37°C is improved by 40.3 % as compared with that of the wild-type, while the improvement is 91.9% in Bacillus subtilis and 82.2% in Pichia pastoris, respectively. Overall, the mutant's activity is increased compared to the wild-type
D24G
site-directed mutagenesis, the mutant shows 29.7% activity compared to the wild-type at pH 7.0, 60°C, and 76.6% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows 42.7% activity compared to the wild-type at pH 7.0, 60°C, and 84.2% at pH 4.5, 37°C
D24G/K265N
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
D24G/K70R/K111E/N121S
site-directed mutagenesis, the Bacillus subtilis-expressed variant D24G/K70R/K111E/N121S shows 54.1, 42.6, and 10.8% higher specific activity than those expressed in Escherichia coli at pH 7.0, 60°C, pH 7.0, 37°C, and pH 4.5, 37°C, respectively. Overall, the mutant's activity is significantly increased compared to the wild-type
D24G/K70R/K111E/N121S
site-directed mutagenesis, the mutant shows 42.8% activity compared to the wild-type at pH 7.0, 60°C, and 121.1% at pH 4.5, 37°C
K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
K265E
site-directed mutagenesis, the mutant shows similar activity compared to wild-type
S51A
site-directed mutagenesis, the mutant shows 13.5% activity compared to the wild-type at pH 7.0, 60°C, and 79.5% at pH 4.5, 37°C
S51A
site-directed mutagenesis. Overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, overall, the mutant's activity is increased compared to the wild-type
S51A/K265E
site-directed mutagenesis, the mutant shows increased activity compared to wild-type at pH 7.0, 60°C
additional information
directed evolution and library screening, pH and tempearture profiles of the mutant enzymes compared to the wild-type enzyme, detailed overview
additional information
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
additional information
-
the specific activities of the Bacillus subtilis-expressed phy168 proteins are mostly higher than those of the corresponding phy168 enzymes expressed in Escherichia coli. The activties of wild-type and mutant enzymes vary dependent on conditions and expression system, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
purified native enzyme, the activity remains fairly stable over pH range of pH 4.0 to pH 8.0, 83% of maxcimal activity remain after 6 h, pH profile, overview
715310
6 - 7
-
partially purified enzyme, 30 min, completely stable at, 85% activity remains after 24 h
750883
8 - 10
-
partially purified enzyme, 30 min, 1.16fold activation, completely stable for 24 h
750883
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
pH 7.0, 37°C, 70% activity remains for the purified recombinant enzyme mutant expressed from Bacillus subtilis, 25% activity remains for the purified recombinant enzyme mutant expressed from Pichia pastoris, and 50% activity remains for the purified recombinant enzyme mutant expressed from Escherichia coli
60
75
80
95
-
about 55% loss of activity after 15 min, about 75% loss of activity after 30 min, with 5 mM Ca2+
additional information
60
recombinant and native enzymes, 5 mM CaCl2, pH 5.5 or pH 7.5, stable
60
-
partially purified enzyme, retains 83% and 60% of its initial activity after 90 and 120 min, respectively
80
deglycosylated native enzyme, 5 mM CaCl2, 10 min, 68% of initial activity remaining at pH 7.5, 36% at pH 5.5
80
deglycosylated recombinant enzyme, 5 mM CaCl2, 10 min, 85% of initial activity remaining at pH 7.5, 11% at pH 5.5
80
-
purified native enzyme, 40% of original activity remaining after 30 min
additional information
temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis
additional information
-
temperature profiles of the mutants expressed in Pichia pastoris and Bacillus subtilis
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography
native enzyme 24fold by ethanol precipitation, anion exchange chromatography, and gel filtration
-
recombinant thioredoxin-His-tagged enzyme and His-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene phy, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
gene phy168, recombinant expression of wild-type and mutant enzymes in Bacillus subtilis strain WB800N, Escherichia coli TOP10 cells or strain BL21, and Pichia pastoris strain GS115, subcloning in Escherichia coli, evaluation of the best expression systems, overview. High glycosylation degree of the proteins when expressed in Pichia pastoris strain GS115, when the expression host is changed from Escherichia coli to Pichia pastoris, deglycosylation is conducted. The enzyme expressed in Pichia pastoris is secreted. Wild-type enzyme and the mutants D24G, D24G/K70R/K111E/N121S secreted by Pichia pastoris show decreased thermostability compared with those expressed in Escherichia coli, correspondingly. This reduction in residual activity might be ascribed to the N-glycosylation of phy168 in Pichia pastoris
gene phyC, overexpression in Pichia pastoris strain KM71
expression in Pichia pastoris strain GS115, methanol induction, the recombinant enzyme is secreted
gene phyC, DNA and amino acid determination and analysis, functional recombinant expression of thioredoxin-His-tagged enzyme from vector pET32a-PhyC and His-tagged enzyme from vector pET21a-PhyC in Escherichia coli cytoplasm. The concentration of the alkaline phytase expressed by pET32a is approximately 59% greater than that expressed by pET21, but its phytase activity is approximately 77% lower
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
metal-depleted apoenzyme can be restored by Ca2+, Sr2+,Co2+, Ba2+, Cu2+, La3+, Ni+, Tb2+, and Mn2+ to 44.1%, 29.8%, 36.7%, 26.9%, 1.9%, 30.0%, 34.2%, 8.3%, and 34.9% of its reference activity, respectively
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
-
the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme
synthesis
-
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
additional information
-
the enzyme is useful as animal feed additive, in dephytinization of food ingredients, and bioremediation of phosphorous pollution in the environment
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
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.
-
Kerovuo, J.; Lauraeus, M.; Nurminen, P.; Kalkkinen, N.; Apajalahti, J.
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Bacillus subtilis, Bacillus subtilis VTT E-68013
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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
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Bacillus subtilis, Bacillus licheniformis (Q8KTX7)
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Bacillus subtilis, Bacillus subtilis VTT E-68013
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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
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Structure
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Bacillus subtilis
Farhat, A.; Chouayekh, H.; Ben Farhat, M.; Bouchaala, K.; Bejar, S.
Gene cloning and characterization of a thermostable phytase from Bacillus subtilis US417 and assessment of its potential as a feed additive in comparison with a commercial enzyme
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Bacillus subtilis (Q84B22), Bacillus subtilis US417 (Q84B22)
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Expression of a Bacillus phytase C gene in Pichia pastoris and properties of the recombinant enzyme
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Bacillus subtilis (O31097), Bacillus subtilis, Bacillus subtilis VTT E-68013 (O31097)
Viader-Salvado, J.M.; Gallegos-Lopez, J.A.; Carreon-Trevino, J.G.; Castillo-Galvan, M.; Rojo-Dominguez, A.; Guerrero-Olazaran, M.
Design of thermostable beta-propeller phytases with activity over a broad range of pHs and their overproduction by Pichia pastoris
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Bacillus subtilis (O31097), Bacillus subtilis (P42094), Bacillus subtilis (Q70E78), Bacillus subtilis (Q84B22), Bacillus subtilis (Q93GB6), Bacillus subtilis (Q9F657), Bacillus subtilis
Hong, S.; Chu, I.; Chung, K.
Purification and biochemical characterization of thermostable phytase from newly isolated Bacillus subtilis CF92
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Bacillus subtilis, Bacillus subtilis CF92
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Yao, M.; Lu, W.; Chen, T.; Wang, W.; Fu, Y.; Yang, B.; Liang, A.
Effect of metals ions on thermostable alkaline phytase from Bacillus subtilis YCJS isolated from soybean rhizosphere soil
Ann. Microbiol.
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Bacillus subtilis (H9C9P0)
Chen, W.; Yu, H.; Ye, L.
Comparative study on different expression hosts for alkaline phytase engineered in Escherichia coli
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179
997-1010
2016
Bacillus subtilis (P42094), Bacillus subtilis, Bacillus subtilis 168 (P42094)
Chen, W.; Ye, L.; Guo, F.; Lv, Y.; Yu, H.
Enhanced activity of an alkaline phytase from Bacillus subtilis 168 in acidic and neutral environments by directed evolution
Biochem. Eng. J.
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2015
Bacillus subtilis (P42094), Bacillus subtilis 168 (P42094)
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Rocky-Salimi, K.; Hashemi, M.; Safari, M.; Mousivand, M.
A novel phytase characterized by thermostability and high pH tolerance from rice phyllosphere isolated Bacillus subtilis B.S.46
J. Adv. Res.
7
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2016
Bacillus subtilis, Bacillus subtilis B.S.46
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