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Enzyme Nomenclature
Information on EC 3.6.1.65 - (d)CTP diphosphatase
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3.6.1.65 (d)CTP diphosphataseIUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP. It also acts on 5-methyl-dCTP, 5-hydroxy-dCTP and 8-hydroxy-dGTP.
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Word Map
- 3.6.1.65
- 5-methyl-dctp
- dctp
- 8-hydroxy-dgtp
- hydrolases
-
mutt-type
-
h2o2-induced
-
mutt
-
nudix
- nucleoside
-
sanitization
-
deoxynucleotides
-
transversion
- pyrimidine
-
2-oh-datp
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(d)CTP diphosphohydrolase
-
-
-
-
(d)CTP pyrophosphohydrolase
-
-
-
-
nudG
nudG
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + H2O = CMP + diphosphate
(1)
-
-
-
dCTP + H2O = dCMP + diphosphate
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(deoxy)cytidine 5'-triphosphate diphosphohydrolase
The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP. It also acts on 5-methyl-dCTP, 5-hydroxy-dCTP and 8-hydroxy-dGTP.
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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
5-hydroxy-dCTP + H2O
5-hydroxy-dCMP + diphosphate
-
4.3% of the activity with 5-hydroxy-CTP
-
?
arabinosyl-CTP + H2O
arabinosyl-CMP + diphosphate
3% of the activity with 5-methyl-dCTP
-
-
?
CDP + H2O
cytidine + diphosphate
2% of the activity with 5-methyl-dCTP
-
-
?
CTP + H2O
CMP + diphosphate
48% of the activity with 5-methyl-dCTP
-
-
?
dCTP + H2O
dCMP + diphosphate
23% of the activity with 5-methyl-dCTP
-
-
?
dTTP + H2O
dTMP + diphosphate
2% of the activity with 5-methyl-dCTP
-
-
?
dUTP + H2O
dUMP + diphosphate
1% of the activity with 5-methyl-dCTP
-
-
?
additional information
?
-
enzyme is highly specific for pyrimidine (deoxy)nucleoside triphosphates. Like other Nudix hydrolases, the enzyme cleaves its substrates to produce a nucleoside monophosphate and diphosphate
-
-
?
additional information
?
-
-
enzyme is highly specific for pyrimidine (deoxy)nucleoside triphosphates. Like other Nudix hydrolases, the enzyme cleaves its substrates to produce a nucleoside monophosphate and diphosphate
-
-
?
additional information
?
-
no substrates: CMP, dCMP, dATP, ATP, dGTP, GTP, dUTP, CDP-ethanolamine, CDP-choline, CDP-glucose, CDP-glycerol
-
-
?
additional information
?
-
-
no substrates: CMP, dCMP, dATP, ATP, dGTP, GTP, dUTP, CDP-ethanolamine, CDP-choline, CDP-glucose, CDP-glycerol
-
-
?
additional information
?
-
-
the enzyme shows no binding or hydrolysis activity against (p)ppGpp and 8-oxo-dGTP
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
absolute requirement for a divalnt cation. No activity in presence of Zn2+, Co2+, Ca2+
additional information
-
absolute requirement for a divalnt cation. No activity in presence of Zn2+, Co2+, Ca2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0055
2-hydroxy-dATP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
4.86
2-hydroxy-dATP
-
pH and temperature not specified in the publication
0.31
2-hydroxy-dATP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
0.027
2-hydroxy-dATP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.067
2-hydroxy-dATP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
0.19
2-hydroxy-dATP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
0.0057
5-Methyl-dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
0.24
5-Methyl-dCTP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
0.22
5-Methyl-dCTP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
0.0069
5-Methyl-dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
0.015
5-Methyl-dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
0.028
5-Methyl-dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.77
dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
0.99
dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.93
dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
0.65
dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.89
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.45
2-hydroxy-dATP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
1.4
2-hydroxy-dATP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
1.42
2-hydroxy-dATP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
1.93
2-hydroxy-dATP
-
pH and temperature not specified in the publication
2.7
2-hydroxy-dATP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
0.17
2-hydroxy-dATP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
6.5
5-Methyl-dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
35
5-Methyl-dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
11
5-Methyl-dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
9.1
5-Methyl-dCTP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
7.7
5-Methyl-dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
2.8
5-Methyl-dCTP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
8.8
dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
2.7
dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
2.1
dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
6.3
dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
82
2-hydroxy-dATP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
4.6
2-hydroxy-dATP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
21
2-hydroxy-dATP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
6.4
2-hydroxy-dATP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
14
2-hydroxy-dATP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
1400
5-Methyl-dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
38
5-Methyl-dCTP
-
mutant D118A, pH not specified in the publication, temperature not specified in the publication
13
5-Methyl-dCTP
-
mutant E33A, pH not specified in the publication, temperature not specified in the publication
780
5-Methyl-dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
944
5-Methyl-dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
1300
5-Methyl-dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
14
dCTP
-
mutant R72A, pH not specified in the publication, temperature not specified in the publication
6.4
dCTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
3.5
dCTP
-
mutant D118N, pH not specified in the publication, temperature not specified in the publication
2.3
dCTP
-
mutant D118E, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (613 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K38R
-
substrate 5-methyl-dCTP, about 40% of wild-type activity, substrate dCTP, 5% of wild-type activity
K38A
-
substrate 5-methyl-dCTP, about 30% of wild-type activity, substrate dCTP, 10% of wild-type activity
E55Q
-
substrate 5-methyl-dCTP, about 110% of wild-type activity, substrate dCTP, 10% of wild-type activity
E55D
-
substrate 5-methyl-dCTP, about 40% of wild-type activity, substrate dCTP, 2% of wild-type activity
E55A
-
substrate 5-methyl-dCTP, about 20% of wild-type activity, substrate dCTP, 1%of wild-type activity
E43A
-
substrate 5-methyl-dCTP, about 20% of wild-type activity, substrate dCTP, 1%of wild-type activity
L53A
-
substrate 5-methyl-dCTP, about 30% of wild-type activity, substrate dCTP, 30% of wild-type activity
R51A
-
substrate 5-methyl-dCTP, about 5% of wild-type activity, substrate dCTP, 1% of wild-type activity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kamiya, H.; Iida, E.; Harashima, H.
Important amino acids in the phosphohydrolase module of Escherichia coli Orf135
Biochem. Biophys. Res. Commun.
323
1063-1068
2004
Escherichia coli
brenda
Iida, E.; Satou, K.; Mishima, M.; Kojima, C.; Harashima, H.; Kamiya, H.
Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 protein
Biochemistry
44
5683-5689
2005
Escherichia coli, Escherichia coli JD22899
brenda
Fujikawa, K.; Kasai, H.
The oxidized pyrimidine ribonucleotide, 5-hydroxy-CTP, is hydrolyzed efficiently by the Escherichia coli recombinant Orf135 protein
DNA Repair
1
571-576
2002
Escherichia coli (P77788), Escherichia coli
brenda
OHandley, S.; Dunn, C.; Bessman, M.
Orf135 from Escherichia coli is a nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP
J. Biol. Chem.
276
5421-5426
2001
Escherichia coli (P77788), Escherichia coli
brenda
Rihtman, B.; Bowman-Grahl, S.; Millard, A.; Corrigan, R.M.; Clokie, M.R.J.; Scanlan, D.J.
Cyanophage MazG is a pyrophosphohydrolase but unable to hydrolyse magic spot nucleotides
Environ. Microbiol. Rep.
11
448-455
2019
Synechococcus phage S-PM2
brenda
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