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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Biochemical and biophysical research communications

Phosphorylation of dGMP analogs by vaccinia virus TMP kinase and human GMP kinase

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemical and biophysical research communications - 23 Jul 2009

Auvynet C, Topalis D, Caillat C, Munier-Lehmann H, Seclaman E, Balzarini J, Agrofoglio LA, Kaminski PA, Meyer P, Deville-Bonne D, El Amri C

Link to Pubmed [PMID] – 19631609

Biochem. Biophys. Res. Commun. 2009 Oct;388(1):6-11

Vaccinia virus thymidylate kinase, although similar in sequence to human TMP kinase, has broader substrate specificity and phosphorylates (E)-5-(2-bromovinyl)-dUMP and dGMP. Modified guanines such as glyoxal-dG, 8-oxo-dG, O(6)-methyl-dG, N(2)-ethyl-dG and N(7)-methyl-dG were found present in cancer cell DNA. Alkylated and oxidized dGMP analogs were examined as potential substrates for vaccinia TMP kinase and also for human TMP and GMP kinases. Molecular models obtained from structure-based docking rationalized the enzymatic data. All tested nucleotides are found surprisingly substrates of vaccinia TMP kinase and also of human GMP kinase. Interestingly, O(6)-methyl-dGMP is the only analog specific for the vaccinia enzyme. Thus, O(6)-Me-dGMP could be useful for designing new compounds of medical interest either in antipoxvirus therapy or in experimental combined gene/chemotherapy of cancer. These results also provide new insights regarding dGMP analog reaction with human GMP kinase and their slow recycling by salvage pathway nucleotide kinases.

http://www.ncbi.nlm.nih.gov/pubmed/19631609