Uridine monophosphate kinase (UMP kinase)

Uridine monophosphate kinase (UMPK, also called uridylate kinase) is an enzyme that catalyzes the reversible phosphorylation of uridine monophosphate (UMP) to uridine diphosphate (UDP) using ATP as the phosphate donor[2][4]. This reaction is a key step in the *de novo* and salvage pathways of pyrimidine nucleotide biosynthesis, essential for DNA and RNA synthesis in all organisms[2][3][4]. In bacteria, UMP kinase is encoded by the pyrH gene and is structurally and kinetically distinct from eukaryotic NMP kinases[3][5][1]. The enzyme's function is vital for bacterial viability: mutations in pyrH result in conditional lethality, making bacterial UMP kinase a promising target for novel antimicrobials[3][5]. The human homolog (CMPK1) has broader specificity but is closely related. No clinical drugs currently target UMP kinase directly, but its essential role in nucleotide metabolism, particularly in rapidly dividing or infected cells, makes it of pharmacological interest primarily in anti-infective research[2][5].

Other names

UMP kinaseUridylate kinaseUMPKpyrH (bacterial gene name)EC 2.7.4.4

Inhibition leads to depletion of UTP (and CTP), impairing RNA and DNA synthesis in cells where the enzyme is essential[3] Potential allosteric or active site inhibition (as per bacterial enzyme research)[5][1]