InterPro domain: IPR016473

General Information

  • Identifier IPR016473
  • Description Deoxycytidylate deaminase

Abstract

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.


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

Species distribution

Gene table

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