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Information on EC 3.6.1.65 - (d)CTP diphosphatase and Organism(s) Escherichia coli and UniProt Accession P77788

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.65 (d)CTP diphosphatase
IUBMB 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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This record set is specific for:
Escherichia coli
UNIPROT: P77788
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
orf135, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(d)CTP diphosphohydrolase
-
-
-
-
(d)CTP pyrophosphohydrolase
-
-
-
-
nudG
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxy-CTP + H2O
5-hydroxy-CMP + diphosphate
show the reaction diagram
-
-
-
?
5-hydroxy-dCTP + H2O
5-hydroxy-dCMP + diphosphate
show the reaction diagram
-
4.3% of the activity with 5-hydroxy-CTP
-
?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
show the reaction diagram
-
-
-
?
arabinosyl-CTP + H2O
arabinosyl-CMP + diphosphate
show the reaction diagram
3% of the activity with 5-methyl-dCTP
-
-
?
CDP + H2O
cytidine + diphosphate
show the reaction diagram
2% of the activity with 5-methyl-dCTP
-
-
?
CTP + H2O
CMP + diphosphate
show the reaction diagram
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
2% of the activity with 5-methyl-dCTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
1% of the activity with 5-methyl-dCTP
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
show the reaction diagram
-
-
-
-
?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
8-hydroxy-dGTP + H2O
8-hydroxy-dGMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP + H2O
CMP + diphosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
about 10% of the activity with Mg2+
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0557
5-hydroxy-CTP
pH 8.5, 30°C
0.172
5-Methyl-dCTP
pH 9.0, 37°C
0.428 - 0.551
CTP
0.767 - 1.72
dCTP
0.0055 - 0.31
2-hydroxy-dATP
0.0057 - 0.24
5-Methyl-dCTP
0.41
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.65 - 0.99
dCTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35.1
5-hydroxy-CTP
pH 8.5, 30°C
51.7
5-Methyl-dCTP
pH 9.0, 37°C
9.28 - 25.8
CTP
14.3 - 17.4
dCTP
0.17 - 2.7
2-hydroxy-dATP
2.8 - 35
5-Methyl-dCTP
0.89
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2.1 - 8.8
dCTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
630
5-hydroxy-CTP
pH 8.5, 30°C
301
5-Methyl-dCTP
pH 9.0, 37°C
21.7 - 47
CTP
10.1 - 18
dCTP
4.6 - 82
2-hydroxy-dATP
13 - 1400
5-Methyl-dCTP
2.2
8-hydroxy-dGTP
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2.3 - 14
dCTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
193
substrate 5-methyl-dCTP, pH 9.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D118A
-
impaired hydrolysis of substrate 2-hydroxy-dATP
D118E
-
increase in hydrolysis of substrate 2-hydroxy-dATP
D118N
-
impaired hydrolysis of substrate 2-hydroxy-dATP
E33A
-
increase in hydrolysis of substrate 2-hydroxy-dATP
E33Q
-
increase in hydrolysis of substrate 2-hydroxy-dATP
E43A
-
substrate 5-methyl-dCTP, about 20% of wild-type activity, substrate dCTP, 1%of wild-type activity
E52A
-
complete loss of activity
E52D
-
complete loss of activity
E52Q
-
complete loss of activity
E55A
-
substrate 5-methyl-dCTP, about 20% of wild-type activity, substrate dCTP, 1%of wild-type activity
E55D
-
substrate 5-methyl-dCTP, about 40% of wild-type activity, substrate dCTP, 2% of wild-type activity
E55Q
-
substrate 5-methyl-dCTP, about 110% of wild-type activity, substrate dCTP, 10% of wild-type activity
E56A
-
complete loss of activity
E56D
-
complete loss of activity
E56Q
-
complete loss of activity
G36A
-
complete loss of activity
G37A
-
complete loss of activity
K38A
-
substrate 5-methyl-dCTP, about 30% of wild-type activity, substrate dCTP, 10% of wild-type activity
K38R
-
substrate 5-methyl-dCTP, about 40% of wild-type activity, substrate dCTP, 5% 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
R72A
-
impaired hydrolysis of substrate 2-hydroxy-dATP
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as glutathione S-transferase fusion protein
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team