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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : European journal of biochemistry / FEBS

Reaction of human UMP-CMP kinase with natural and analog substrates

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in European journal of biochemistry / FEBS - 01 Apr 2003

Pasti C, Gallois-Montbrun S, Munier-Lehmann H, Veron M, Gilles AM, Deville-Bonne D

Link to Pubmed [PMID] – 12694191

Eur. J. Biochem. 2003 Apr;270(8):1784-90

UMP-CMP kinase catalyses an important step in the phosphorylation of UTP, CTP and dCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies. The reactivity of human UMP-CMP kinase towards natural substrates and nucleotide analogs was reexamined. The expression of the recombinant enzyme and conditions for stability of the enzyme were improved. Substrate inhibition was observed for UMP and CMP at concentrations higher than 0.2 mm, but not for dCMP. The antiviral analog l-3TCMP was found to be an efficient substrate phosphorylated into l-3TCDP by human UMP-CMP kinase. However, in the reverse reaction, the enzyme did not catalyse the addition of the third phosphate to l-3TCDP, which was rather an inhibitor. By molecular modelling, l-3TCMP was built in the active site of the enzyme from Dictyostelium. Human UMP-CMP kinase has a relaxed enantiospecificity for the nucleoside monophosphate acceptor site, but it is restricted to d-nucleotides at the donor site.

http://www.ncbi.nlm.nih.gov/pubmed/12694191