Information on EC 3.1.3.62 - multiple inositol-polyphosphate phosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.62
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RECOMMENDED NAME
GeneOntology No.
multiple inositol-polyphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate
show the reaction diagram
formerly D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-myo-inositol (1,3,4)-trisphosphate biosynthesis
-
-
phytate degradation I
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phytate degradation II
-
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Inositol phosphate metabolism
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SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-hexakisphosphate 5-phosphohydrolase
This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3.
CAS REGISTRY NUMBER
COMMENTARY hide
116958-30-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
avian
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
male Japanese white rabbits, 4 weeks old
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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A0FHB0, A0FHB1, A0FHB2, A0FHB3
SwissProt
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
2,3-bisphosphoglycerate + H2O
2-phosphoglycerate + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
?
D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
show the reaction diagram
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
show the reaction diagram
inositol 1,3,4,6-tetrakisphosphate + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
inositol 3,4,5,6-tetrakisphosphate + H2O
?
show the reaction diagram
-
about 10% of activity with inositol 1,3,4,5-tetrakisphosphate
-
-
?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
scyllo-inositol hexakisphosphate + H2O
scyllo-inositol pentakisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
show the reaction diagram
-
enzyme may be regulated by the intracellular concentrations of inositol tris- and tetrakisphosphates
-
?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
show the reaction diagram
-
inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
-
?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
show the reaction diagram
-
inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
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?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ammonium phosphate buffer
ATP
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weak
CTP
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more effective inhibitor than GTP
Endogenous heat-stable inhibitor
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GTP
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marked inhibition
Inositol 1,3,4,5,6-pentakisphosphate
inositol 1,3,4-trisphosphate
Inositol 1,4,5-trisphosphate
inositol 3,4,5,6-tetrakisphosphate
Inositol hexakisphosphate
UTP
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more effective inhibitor than GTP
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ammonium phosphate buffer
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1 to 10 mM activates, higher concentrations are inhibitory
hemoglobin
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from turkey, activates by removing the inhibitors inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
2,3-bisphosphoglycerate
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recombinant enzyme, at 37C
0.00013 - 0.008
D-myo-Inositol 1,3,4,5-tetrakisphosphate
0.00004
Inositol 1,3,4,5,6-pentakisphosphate
-
pH 7.4, 37C
0.0000003 - 0.334
Inositol hexakisphosphate
0.06 - 0.14
myo-inositol hexakisphosphate
1.74
scyllo-inositol hexakisphosphate
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-
additional information
additional information
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kinetic data of the cytosolic enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000025 - 0.00006
Inositol 1,3,4,5,6-pentakisphosphate
0.00175
inositol 1,3,4-trisphosphate
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pH 7.4, 37C
0.002
Inositol 1,4,5-trisphosphate
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pH 7.4, 37C
0.0005
inositol 3,4,5,6-tetrakisphosphate
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pH 7.4, 37C
0.0000005 - 0.000003
Inositol hexakisphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.009
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using 2,3-bisphosphoglycerate as substrate, at 37C
0.7
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specific activity of recombinant avian MINPP
4.29
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pH 7.4, liver enzyme
4.66
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pH 7.4, 37C, membrane-bound enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
assay at
5 - 9
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plateau within the range, inositol 1,3,4,5,6-pentakisphosphate or inositol hexakisphosphate as substrate, in absence of Mg2+
6.1
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inositol 1,3,4,5-tetrakisphosphate as substrate, in absence of Mg2+
8
assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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assay at
additional information
-
assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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chondrocyte progenitor cell line, developmentally specific changes in MINPP expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
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lymphoma cell line
Manually annotated by BRENDA team
mRNA expression; mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
mRNA expression; mRNA expression
Manually annotated by BRENDA team
2.5 kb mRNA expression
Manually annotated by BRENDA team
mRNA expression; mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
mRNA expression; mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
1 * 47000, liver enzyme, doublet, SDS-PAGE
51000
x * 51000, recombinant MIPP expressed in Escherichia coli M15, SDS-PAGE and Western blot analysis
53400
x * 53400, recombinant MIPP expressed in Escherichia coli M15, amino acid sequence analysis
53800
SDS-PAGE; SDS-PAGE
54500
x * 54500, inclusive the putative signal sequence, amino acid sequence analysis
55100
x * 55100, inclusive the putative signal sequence, amino acid sequence analysis
64000
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SDS-PAGE
66000
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particulate enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.4
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 37
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20% v/v glycerol, 1 mg/ml bovine serum albumin, up to 12 months, stable
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-80C, at least 3 months
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-80C, several months, stable
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0C, 10 mM Tris-HCl, pH 7.4, 100 mM KCl, 1 mM dithiothreitol, up to 1 month, stable
4C, within weeks, loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
22400fold from liver
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Ni-Sepharose column chromatography
partial
particulate enzyme: 38374fold, soluble enzyme: partial
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purification is carried out on a Ni-sepharose column
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recombinant (MMU)Minpp1 fusion protein expressed in Escherichia coli JM109
recombinant MIPP expressed in Escherichia coli M15
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding residues 19-445 of avian MINPP or residues 31-483 of human MINPP lacking the N-terminal ER targeting sequences and the C-terminal ER retention signals are amplified by PCR and cloned into pGEM Tvector and transformed into Escherichia coli
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cloned in Escherichia coli; expressed in Escherichia coli
expressed in Escherichia coli
A0FHB0, A0FHB1, A0FHB2, A0FHB3
expressed in Pichia pastoris
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full-length Minpp cDNA is cloned and stably overexpressed in murine ATDC-5 cells at 2fold higher levels than in wild-type ATDC-5 cells, cellular effects of overexpression
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His-tag fusion, expression in Pichia pastoris
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located on chromosome 10q23, genomic organization
MINPP gene encoding multiple inositol polyphosphate phosphatase
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MIPP cDNA from Jurkat T-cells is cloned and expressed in Escherichia coli M15 without the ER-targeting domain, full-length sequence
MIPP cDNA from liver and kidney is cloned and expressed in Escherichia coli M15, full-length sequence
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N-terminal truncated cytosolic MIPP is expressed in the beta-cell line HIT M2.2.2, expression increases the basal Ca2+-concentration to a more normal level
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sequenced and expressed in Escherichia coli JM109, located on chromosome 19, genomic organization
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q78A
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Km: 0.06 (myo-inositol hexakisphosphate). Q78A mutant shows differences in its specificity profile compared to wild-type enzyme: relative to inositol hexakisphosphate, the activity towards other organic phosphates are as follows: p-nitrophenyl phosphate: 7%, ATP: 12%, ribose 1-phosphate: 3%
T27G
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Km: 0.092 (myo-inositol hexakisphosphate)
H370A
mutant with less than 5% of activity of wild-type enzyme
H89A
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catalytically compromised mutant of MIPP1 that shows only 1% of the 2,3-diphosphoglycerate phosphatase activity of the wild type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-affinity chromatography
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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recombinant avian MINPP (0.7 micromol/mg protein/min) is the most active phytase found to date in any animal cell