Biotinylation, catalyzed by biotin protein ligase (BPL), is a posttranslational process found in both prokaryotic and eukaryotic organisms that links the cofactor biotin to biotin-dependent enzymes. Biotinylation proceeds in two steps: the formation of a biotin-5'-AMP intermediate from ATP and biotin, followed by a transfer of biotin (acylation) to a lysine residue of targeted proteins, including enzymes which are essential in the production of proteins and fatty acids. Biotin protein ligases are important in biological processes and are therefore of interest for the development of novel antibiotics. We are interested in the synthesis and biological evaluation of the nonhydrolyzable analogs of the intermediate biotin-5'-AMP. This presentation will discuss the synthetic approaches pursued for the nonhydrolyzable derivatives and preliminary data on antibacterial activity as well as the inhibitory activity toward human BPL.

Synthesis and biological activity investigation of biotin-5'-AMP analogs

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.