Information on EC 3.1.3.72 - 5-phytase

for references in articles please use BRENDA:EC3.1.3.72
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.3.72
-
RECOMMENDED NAME
GeneOntology No.
5-phytase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
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-
-
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SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 5-phosphohydrolase
The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P3.
CAS REGISTRY NUMBER
COMMENTARY hide
37341-58-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
vars. Pinto, Navy, Red Kidney, Chili No. 494071, Netherlands No. 477020 and 486345, Black Beauty Turtle, Black Turtle G-0681 and T-39
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
var. Early Alaska
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + H2O
?
show the reaction diagram
-
103% relative activity
-
-
?
AMP + H2O
?
show the reaction diagram
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5% relative activity
-
-
?
ATP + H2O
?
show the reaction diagram
-
41% relative activity
-
-
?
Ca-phytate + H2O
?
show the reaction diagram
-
133% relative activity
-
-
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myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
show the reaction diagram
Na-phytate + H2O
?
show the reaction diagram
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100% relative activity
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
phenyl phosphate + H2O
?
show the reaction diagram
-
32% relative activity
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
myo-inositol-1,2,3,4,6-pentakisphosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
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0.166 M, enhances activity
K2SO4
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0.166 M, enhances activity
KCl
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0.5 M, activates
Na2SO4
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0.166 M, enhances activity
NaCl
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0.5 M, activates
NH4Cl
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0.5 M, enhances activity
Sr2+
-
activates
additional information
-
not activated by Mg2+, Mn2+, Cu2+ and Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuSO4
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moderately inhibits phytase activity
MgCl2
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0.166 M
MgSO4
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0.5 M
phosphate
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inhibition by the phosphate released from enzyme
vanadate
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0.25-3 mM, 78-83% inhibition
ZnSO4
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moderately inhibits phytase activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+ H2PO4-
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can stimulate high-phytase production
additional information
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sucrose poorly supports phytase production. Maximal phytase yield is obtained with 2% (v/v) inoculum, phytase activity decreases at lower and higher inoculum concentrations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0072 - 0.081
myo-inositol-1,2,3,4,5,6-hexakisphosphate
0.372
p-nitrophenyl phosphate
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37C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.006
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in crude extracts
0.017
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crude extract
0.019
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in DEAE-purified preparations
12.69
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partially purified phytase
56
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3300fold purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8.5
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is catalytically active under alkaline pH range 8-10, showing 90% of the optimal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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partially purified phytase
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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pollen grain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
integral component of the storage body membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
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1 * 41000, SDS-PAGE, 1 * 46000, SDS-PAGE
46000
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1 * 41000, SDS-PAGE, 1 * 46000, SDS-PAGE
88000
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gel filtration
118000
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by Ferguson plot analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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1 * 41000, SDS-PAGE, 1 * 46000, SDS-PAGE
homodimer
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in the range of 52000-55000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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10 min, stable
60
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ca. 80% activity at pH 8.0 for up to 3 h in the presence/absence of 5 mM CaCl2. In the presence/absence of 5 mM CaCl2, phytase is also stable at 80C and shows ca. 100% of residual activity for 30 min at pH 8.0 and then declines sharply thereafter
additional information
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heat stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable, large loss of activity during the purification procedures
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, stable for 4 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in absence of Triton X-100, very little enzyme activity is extracted from seeds
partial purification, extraction with 0.1% Triton X-100 increases recovery by nearly 4fold
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partially purified, 6.5fold, by gel filtration
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recovery is most complete when detergent or phospholipase C is included in extracting medium
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selective precipitation by heat and ammonium sulfate followed by anion exchange and chromatofocusing chromatography and gel filtration, purified 3300fold, to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
synthesis
transgenic expression in Pichia pastoris. Increasing isoform Alp2 copy number is detrimental to heterologous expression, clones with one copy of wild-type Alp2 produce the highest activity, clones with two, four and seven or more copies produce 70%, 25% and 10% respectively, of enzyme activity. Use of a sequence-optimized Alp2 gene increases the yield of the active enzyme by 25-50% in one/two copy clones. Reducing the temperature during heterologous expression leads to increases of 1.2-20fold suggesting that protein folding and post-translational processes may be the dominant factors limiting ALP2 expression