Cytidine monophosphate kinase (CMP kinase)

Cytidine monophosphate kinase is an enzyme that catalyzes the transfer of a phosphoryl group from ATP to cytidine monophosphate (CMP) (and can also act on deoxy-CMP and uridine monophosphate), producing cytidine diphosphate (CDP) and ADP[5][6]. In bacteria, the enzyme is essential for nucleic acid precursor synthesis and involved in cellular viability and pathogenicity[1][4][6]. The enzyme is structurally a member of the nucleoside monophosphate (NMP) kinase family, containing specific active site residues critical for catalysis[1][4]. Bacterial CMP kinase (e.g., from Yersinia pseudotuberculosis) is implicated as a potential antibiotic target because its inhibition attenuates virulence and growth, while its human counterpart (encoded by the CMPK1 gene) participates in normal nucleotide biosynthesis[3][5]. Essentiality can vary by species—lethal in some bacteria, but not all[4]. CMP kinase is also known as cytidylate kinase and is involved in the central metabolism of nucleotides[5][6]. No approved drugs specifically target human CMP kinase, but the bacterial enzyme is under investigation as a novel antimicrobial target[1][3][6].

Other names

Cytidylate kinaseUMP-CMP kinaseCMKCMPK1 (human gene)

Inhibitors block the phosphorylation of cytidine monophosphate (CMP) to cytidine diphosphate (CDP), disrupting nucleotide biosynthesis and nucleic acid synthesis in pathogens[1][4][6].