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Information on EC 3.6.1.64 - inosine diphosphate phosphatase and Organism(s) Homo sapiens and UniProt Accession Q96DE0

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     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.64 inosine diphosphate phosphatase
IUBMB Comments
The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
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This record set is specific for:
Homo sapiens
UNIPROT: Q96DE0
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
(deoxy)inosine diphosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
U8 snoRNA-decapping enzyme
-
(deoxy)inosine diphosphatase
-
-
Nudt16
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
IDP + H2O = IMP + phosphate
show the reaction diagram
(1)
dIDP + H2O = dIMP + phosphate
show the reaction diagram
(2)
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
inosine diphosphate phosphatase
The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
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
-
hydrolysis of ITP generates IMP but not phosphate
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
maximum activity at 1 mM
Zn2+
may partly substitue for Mn2+
additional information
INHIBITOR
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
pH 7.5, 37°C
0.008
dGDP
pH 7.5, 37°C
0.016
dIDP
pH 7.5, 37°C
0.053
dITP
pH 7.5, 37°C
0.009
GDP
pH 7.5, 37°C
0.016
IDP
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
pH 7.5, 37°C
0.0257
dGDP
pH 7.5, 37°C
0.183
dIDP
pH 7.5, 37°C
0.0022
dITP
pH 7.5, 37°C
0.0261
GDP
pH 7.5, 37°C
0.251
IDP
pH 7.5, 37°C
0.0023 - 1.55
ITP
0.0027 - 0.99
XDP
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NUD16_HUMAN
195
0
21273
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A22V
crystallization data
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iyama, T.; Abolhassani, N.; Tsuchimoto, D.; Nonaka, M.; Nakabeppu, Y.
NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest
Nucleic Acids Res.
38
4834-4843
2010
Homo sapiens, Homo sapiens (Q96DE0), Mus musculus (Q6P3D0)
Manually annotated by BRENDA team
Tresaugues, L.; Lundbaeck, T.; Welin, M.; Flodin, S.; Nyman, T.; Silvander, C.; Graeslund, S.; Nordlund, P.
Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate
PLoS ONE
10
e0131507
2015
Homo sapiens (Q96DE0)
Manually annotated by BRENDA team