EC number:3.5.4.12

Enzyme

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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
ID:3.5.4.12
Description:dCMP deaminase.
Alternative Name: Deoxycytidylate deaminase.
Prosite: PDOC00702;
PDB:
PDBScop
Cath: 3.40.140.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.4.12
BRENDA Enzyme Link: BRENDA 3.5.4.12
KEGG Enzyme Link: KEGG3.5.4.12
BioCyc Enzyme Link: BioCyc 3.5.4.12
ExPASy Enzyme Link: ExPASy3.5.4.12
EC2PDB Enzyme Link: EC2PDB 3.5.4.12
ExplorEnz Enzyme Link: ExplorEnz 3.5.4.12
PRIAM enzyme-specific profiles Link: PRIAM 3.5.4.12
IntEnz Enzyme Link: IntEnz 3.5.4.12
MEDLINE Enzyme Link: MEDLINE 3.5.4.12

EC number:3.5.4.12

MSA:

3.5.4.12;
Phylogenetic Tree:

3.5.4.12;
Uniprot:
M-CSA:
RHEA:22924 dCMP + H(+) + H2O = dUMP + NH4(+)
RULE(radius=1) [*:1]:[n;H0;+0:2]:[c;H0;+0:3](:[*:4])-[NH2;+0:5].[H+;H0:6].[OH2;+0:7]>>[*:1]:[nH;+0:2]:[c;H0;+0:3](:[*:4])=[O;H0;+0:7].[NH3;+0:5]
Reaction
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References

TitleAuthorsDatePubMed ID
Properties of an affinity-column-purified human deoxycytidylate deaminase.Maley GF, Lobo AP, Maley F1993 Mar 58448179
Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli.Weiner KX, Weiner RS, Maley F, Maley GF1993 Jun 157685356
Three-dimensional structure of the R115E mutant of T4-bacteriophage 2'-deoxycytidylate deaminase.Almog R, Maley F, Maley GF, Maccoll R, Van Roey P2004 Nov 215504034