Deoxycytidylate kinase (dCMP kinase)

Deoxycytidylate kinase (dCMP kinase) is an enzyme that catalyzes the ATP-dependent phosphorylation of deoxycytidylate (dCMP) to deoxycytidine diphosphate (dCDP), and also phosphorylates cytidylate (CMP) and uridine monophosphate (UMP) with similar efficiency in eukaryotes[5]. It plays a central role in the nucleotide salvage pathway by allowing cells to recycle nucleosides and is essential for the synthesis and maintenance of DNA precursors[1][2][7]. The enzyme enables activation (phosphorylation) of many nucleoside analog drugs (including anticancer and some antiviral drugs), thereby making deoxycytidylate kinase a critical pharmacological target and a determinant of chemotherapy response. It is a bifunctional kinase in eukaryotes and is structurally distinct from some related kinases in prokaryotes[5]. Dysfunction or altered expression may contribute to drug resistance in cancer therapy[7].

Other names

cytidylate kinasedeoxycytidine monophosphokinaseCTP:CMP phosphotransferasedCMP kinaseUMP-CMP kinaseATP:UMP-CMP phosphotransferasepyrimidine nucleoside monophosphate kinaseuridine monophosphate-cytidine monophosphate phosphotransferase

Drugs (e.g., nucleoside analogs) are phosphorylated by this enzyme to their monophosphate forms, which is an essential activation step required for their cytotoxic or antiviral activity[1][7][9]