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Information on EC 3.5.4.13 - dCTP deaminase and Organism(s) Escherichia coli and UniProt Accession P28248

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.13 dCTP deaminase
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This record set is specific for:
Escherichia coli
UNIPROT: P28248 not found.
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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
dctp deaminase, dcd:dut, deoxycytidine triphosphate deaminase, dctp deaminase:dutpase, 5-methyl-dctp deaminase, dctp deaminase:deoxyuridine triphosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-methyl-dCTP deaminase
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-
-
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dCTP deaminase
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-
-
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deoxycytidine triphosphate deaminase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dCTP + H2O = dUTP + NH3
show the reaction diagram
reaction involves S111, A124, E138 and two water molecules
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
dCTP aminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37289-18-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dCTP + H2O
dUTP + NH3
show the reaction diagram
dCTP + H2O
dUTP + NH3
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dCTP + H2O
dUTP + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.24
dCTP
pH 6.8, 37°C, recombinant wild-type enzyme
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant E138A bound to dTTP and mutant H121A bound to dCTP, hanging drop vapour diffusion method, 3.7 mg/ml E138A or 5.1 mg/ml H121A in 20 mM magnesium chloride, 50 mM HEPES, pH 6.8, and 5 mM nucleotide, mixing of 0.002 ml of protein solution with an equal volume of reservoir solution containing 34% PEG 400, 0.2 mM MgCl2, and 0.1 m HEPES, pH 7.5, equilibration against 1 ml of mother liquor, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.6-2.7 A resolution
recombinant mutant E138D in complex with dUTP, hanging drop vapour diffusion method, 0.002 ml of 2 mg/ml protein in solution with 5 mM dUTP and 20 mM MgSO4 is mixed with 0.002 ml reservoir solution containing 27.5% PEG 400, 50 mM MgSO4 and 0.1 M HEPES, pH 7.5, equilibration against 0.5 ml of reservoir solution, room temeprature, crystal X-ray diffraction structure determination and analysis at 2.1 A resolution
wild-type and mutant E138A, in complex with Mg2+ and dUTP, and dCTP
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E138A
E138D
site-directed mutagenesis, the mutant enzyme shows a 140fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme
E138Q
no enzymic activity, no change in overall structure compared to wild-type
H121A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
R115A
no enzymic activity, no change in overall structure compared to wild-type
R115Q
site-directed mutagenesis, inactive mutant
S111C
site-directed mutagenesis, inactive mutant
S111T
site-directed mutagenesis, the mutant enzyme shows a 30fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme, modeling of the active site of the S111T enzyme, overview
V122G
site-directed mutagenesis, inactive mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, L.; Weiss, B.
Dcd (dCTP deaminase) gene of Escherichia coli: Mapping, cloning, sequencing, and identification as a locus of suppressors of lethal dut (dUTPase) mutations
J. Bacteriol.
174
5647-5653
1992
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Speed, R.R.; Winkler, H.H.
Deamination of deoxycytidine nucleotides by the obligate intracytopplasmic bacterium Rickettsia prowazekii
J. Bacteriol.
173
4902-4903
1991
Escherichia coli, Rickettsia prowazekii, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Weiss, B.; Wang, L.
De novo synthesis of thymidylate via deoxycytidine in dcd (dCTP deaminase) mutants of Escherichia coli
J. Bacteriol.
176
2194-2199
1994
Escherichia coli
Manually annotated by BRENDA team
Estevenon, A.M.; Kooistra, J.; Sicard, N.
An Escherichia coli strain deficient for both exonuclease V and deoxycytidine triphosphate deaminase shows enhanced sensitivity to ionizing radiation
Mol. Gen. Genet.
246
514-518
1995
Escherichia coli
Manually annotated by BRENDA team
Johansson, E.; Fan?, M.; Bynck, J.H.; Neuhard, J.; Larsen, S.; Sigurskjold, B.W.; Christensen, U.; Willemoes, M.
Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
J. Biol. Chem.
280
3051-3059
2005
Escherichia coli (P28248), Escherichia coli
Manually annotated by BRENDA team
Thymark, M.; Johansson, E.; Larsen, S.; Willemoes, M.
Mutational analysis of the nucleotide binding site of Escherichia coli dCTP deaminase
Arch. Biochem. Biophys.
470
20-26
2008
Escherichia coli (P28248), Escherichia coli
Manually annotated by BRENDA team
Johansson, E.; Thymark, M.; Bynck, J.H.; Fanoe, M.; Larsen, S.; Willemoes, M.
Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme
FEBS J.
274
4188-4198
2007
Escherichia coli (P28248), Escherichia coli
Manually annotated by BRENDA team