Information on EC 3.6.1.64 - inosine diphosphate phosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.64
-
RECOMMENDED NAME
GeneOntology No.
inosine diphosphate phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dIDP + H2O = dIMP + phosphate
show the reaction diagram
IDP + H2O = IMP + phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
inosine diphosphate phosphatase
The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional U8 snoRNA-decapping enzyme and IDP phosphatase
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
knockdown in HeLa MR cells causes cell cycle arrest in S-phase, reduces cell proliferation, and leads to increased accumulation of single-strand breaks in nuclear DNA as well as increased levels of inosine in RNA
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
AMP + phosphate
show the reaction diagram
-
-
-
?
dGDP + H2O
dGMP + phosphate
show the reaction diagram
-
-
-
?
dIDP + H2O
dIMP + phosphate
show the reaction diagram
-
-
-
?
dITP + H2O
dIMP + diphosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
ITP + H2O
IDP + phosphate
show the reaction diagram
-
-
-
?
XDP + H2O
XMP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
rate of the catalytic cycle is primarily regulated by the product-release step
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
maximum activity at 1 mM
Zn2+
may partly substitue for Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IMP
product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.285
ADP
pH 7.5, 37°C
0.32
dGDP
pH 7.5, 37°C
0.088
dIDP
pH 7.5, 37°C
24.1
dITP
pH 7.5, 37°C
0.33
GDP
pH 7.5, 37°C
0.062
IDP
pH 7.5, 37°C
0.0082 - 22.1
ITP
0.0062 - 15.7
XDP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.096
ADP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.008
dGDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.016
dIDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.053
dITP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.009
GDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.016
IDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
0.013 - 0.051
ITP
0.006 - 0.043
XDP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
ADP
Homo sapiens
Q96DE0
pH 7.5, 37°C
13
0.0257
dGDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
1140
0.183
dIDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
7184
0.0022
dITP
Homo sapiens
Q96DE0
pH 7.5, 37°C
2839
0.0261
GDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
53
0.251
IDP
Homo sapiens
Q96DE0
pH 7.5, 37°C
444
0.0023 - 1.55
ITP
229
0.0027 - 0.99
XDP
4060
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0098 - 0.0213
IMP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024 - 3.174
IMP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
temperature-dependent increase in IDP hydrolyzing activity up to 60°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
and lung, highest expression
Manually annotated by BRENDA team
and kidney, highest expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant A22V,structure forms an alpha/beta/alpha sandwich which is constituted by two beta-sheets, one being composed of two parallel beta-strands lined by two anti-parallel beta-strands and the second one by three anti-parallel beta-strands. The protein is decorated with five additional motifs being part of the hydrophobic core or serving roles to stabilize the dimer
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A22V
crystallization data