Deoxycytidylate deaminase (dCMP deaminase)

Deoxycytidylate deaminase is a zinc-dependent enzyme involved in pyrimidine metabolism, specifically catalyzing the hydrolytic deamination of deoxycytidine-5'-monophosphate (dCMP) to deoxyuridine-5'-monophosphate (dUMP), which is an essential precursor for thymidylate synthase and DNA synthesis. It is a homohexamer allosterically regulated by dCTP (activator) and dTTP (inhibitor), modulating its activity to maintain balanced nucleotide pools for DNA replication and repair. The enzyme is predominantly found in rapidly dividing cells and has structural similarities with cytidine deaminase, possessing a conserved zinc-binding motif essential for its catalytic function. Its significance in cell proliferation and DNA synthesis makes it relevant as a potential therapeutic target, particularly in cancer chemotherapy where enzymes of nucleotide metabolism are frequently inhibited.

Other names

dCMP deaminaseDCMP deaminaseCytidine-5'-monophosphate deaminaseDeoxycytidine 5'-monophosphate deaminase

Drugs may inhibit or modulate dCMP deaminase to affect DNA synthesis or induce cytotoxicity in rapidly dividing cells (anticancer mechanism) Anti-metabolite drugs block pyrimidine synthesis via deamination modulation