Overview:

Uridylate kinase, also known as UMP kinase, in E. coli catalyze the phosphorylation of UMP and ATP to yield UDP and ADP with Mg2+ as the cofactor (1). Bacterial UMP kinases are hexamers and are allosterically activated by GTP and allosterically inhibited by UTP (1,2). They are the most studied nucleoside monophosphate (NMP) kinase in their family and have sequence similarity to aspartokinases, glutamate kinases, and Pseudomonas aeruginosa carbamate kinase (2). UMP kinase is a regulatory enzyme in the de novo biosynthetic pathway of pyrimidine molecules (3).

Gene Aliases:

pyrH, smbA, UMPK, UMP kinase

Genbank Number:

X78809

References:

1. Briozzo, P. et al. Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophospohate kinases and sheds new light on enzyme regulation. J. Biol. Chem. 2005, 280:25533-25540. 2. Serina, L. et al. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleosides and UTP. Biochemistry. 1995, 34(15): 5066-5074. 3. Bucurenci, N. et al. Mutational analysis of UMP Kinase from Escherichia coli. J Bacteriol. 1998, 180(3): 473-477.