InterPro domain: IPR035105

Deoxycytidylate deaminase ( 3.5.4.12 ) (dCMP deaminase) hydrolyzes deoxycytidylate mono phosphate (dCMP) into deoxyuridine mono phosphate (dUMP), thus providing the nucleotide substrate for thymidylate synthase. The enzyme requires zinc for catalytic activity which is regulated by the ratio of dCTP to dTTP, both the end products of the pyrimidine salvage pathway [ 1 , 2 , 3 ]. It contains a cytidine and deoxycytidylate deaminase domain.

This entry represents a domain found in a group of deoxycytidylate deaminases.

This domain can also be found in cytidine and dCMP deaminase domain-containing protein 1 (CDADC1), which may play an important role in testicular development and spermatogenesis [ 4 ].

1. Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli. J. Biol. Chem. 268, 12983-9
2. T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit. J. Biol. Chem. 268, 2288-91
3. Crystal structures of Streptococcus mutans 2'-deoxycytidylate deaminase and its complex with substrate analog and allosteric regulator dCTP x Mg2+. J. Mol. Biol. 377, 220-31
4. NYD-SP15: a novel gene potentially involved in regulating testicular development and spermatogenesis. Biochem. Genet. 44, 409-23