Information on EC 3.5.4.12 - dCMP deaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.5.4.12
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RECOMMENDED NAME
GeneOntology No.
dCMP deaminase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of amidines
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-
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PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
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pyrimidine deoxyribonucleotides biosynthesis from CTP
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Pyrimidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
dCMP aminohydrolase
Also acts on some 5-substituted dCMPs.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-deoxycytidylate deaminase
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2-deoxycytidylate deaminase
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5-mdCMP deaminase
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5-methyldeoxycytidine monophosphate deaminase
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dCMP deaminase
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dCMP deaminase
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dCMP deaminase
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dCMP-aminohydrolase
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dCMP-dCTP deaminase
O41078
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dCMPase
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dCMPD
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deaminase, deoxycytidylate
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deoxy-CMP-deaminase
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deoxycytidine deaminase
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deoxycytidine monophosphate deaminase
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deoxycytidine monophosphate deaminase
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deoxycytidine nucleotide deaminase
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deoxycytidine-5'-monophosphate aminohydrolase
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deoxycytidine-5'-phosphate deaminase
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deoxycytidine-5?-monophosphate deaminase
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deoxycytidylate aminohydrolase
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deoxycytidylate deaminase
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deoxycytidylate deaminase
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deoxycytidylate deaminase
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deoxycytidylate deaminase
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T2-dCMP deaminase
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T2-phage infected
T2-deoxycytidylate deaminase
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T2-phage infected
T2-phage deoxycytidylate deaminase
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T2-phage infected
T4-dCMP deaminase
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T4-phage infected
T4-deaminase
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T4-phage infected
T4-phage deoxycytidylate deaminase
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T4-phage infected
CAS REGISTRY NUMBER
COMMENTARY
9026-92-0
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ED40
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Manually annotated by BRENDA team
Bacillus subtilis ED40
strain ED40
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Manually annotated by BRENDA team
host Bacillus subtilis
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Manually annotated by BRENDA team
bacteriophage SP8
host Bacillus subtilis
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Manually annotated by BRENDA team
BHK-21/C13 cells, baby-hamster
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Manually annotated by BRENDA team
BHK-21/C13 cells, baby-hamster, enzyme from non-infected cells and cells infected by Herpes simplex
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Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli
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Manually annotated by BRENDA team
T2-phage infected Escherichia coli
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Manually annotated by BRENDA team
T2-phage infected Escherichia coli; T2r+-infected Escherichia coli B; T2-, T4-, and T6-phage induced enzyme in Escherichia coli
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Manually annotated by BRENDA team
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
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Manually annotated by BRENDA team
T2r+-infected Escherichia coli B
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Manually annotated by BRENDA team
; T2-, T4-, and T6-phage induced enzyme in Escherichia coli; T4-phage infected Escherichia coli; wild-type and R115E and R115Q, mutant enzymes that no longer requires dCTP for activation, and mutant F112A
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Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli; T4-phage infected Escherichia coli
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Manually annotated by BRENDA team
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
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Manually annotated by BRENDA team
T4-phage infected Escherichia coli; wild-type and mutant F112A
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Manually annotated by BRENDA team
T2-, T4-, and T6-phage induced enzyme in Escherichia coli
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Manually annotated by BRENDA team
donkey; three conformational isomers of dCMPase, the conformation of the enzyme with no ligands, the activated form, R form: dCTP-Mg complex and the inhibited form, T form: dTTP-Mg complex
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Manually annotated by BRENDA team
Herpes simplex virus
host baby-hamster, BHK-21/C13 cells; induced by
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Manually annotated by BRENDA team
Herpes simplex virus
induced by
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Manually annotated by BRENDA team
human; patients with acute nonlymphocytic leukemia
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Manually annotated by BRENDA team
Ehrlich's ascites tumor cells and various gastrointestinal tumors
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Manually annotated by BRENDA team
subsp. mycoides
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Manually annotated by BRENDA team
no activity in Escherichia coli
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Manually annotated by BRENDA team
no activity in Escherichia coli
enzyme not detectable in Escherichia coli until after infection with T-even bacteriophage
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Manually annotated by BRENDA team
no activity in Escherichia coli
enzyme not detectable in Escherichia coli until after infection with T-even bacteriophage; wild type Escherichia coli contains no dCMP deaminase
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Manually annotated by BRENDA team
no activity in Escherichia coli
wild type Escherichia coli contains no dCMP deaminase
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Manually annotated by BRENDA team
no activity in Salmonella typhimurium
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Manually annotated by BRENDA team
no activity in Salmonella typhimurium
do not contain dCMP deaminase
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Manually annotated by BRENDA team
i.e. PBCV-1 , a chlorovirus from host Chlorella sp. strain NC64A
SwissProt
Manually annotated by BRENDA team
induced by
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Manually annotated by BRENDA team
Sea urchin
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Manually annotated by BRENDA team
induced by
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Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
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no coenzyme required
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TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after treatment with guanidine hydrochloride, 6 M, complete reactivation with 50 mM 2-mercaptoethanol, original hexameric structure restored
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after denaturation with EDTA, mutants R115E and R115Q restored 54% and 60% of original activities, wild-type enzyme only marginally restored; after treatment with guanidine-HCl, 6 M, complete reactivation on removal of denaturant by dilution or dialysis
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