Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for N(epsilon)-acylated substrates.

ABSTRACT: Penicillin-binding proteins (PBPs) are bacterial enzymes involved in the final stages of cell wall biosynthesis and are the lethal targets of beta-lactam antibiotics. Despite their importance, their roles in cell wall biosynthesis remain enigmatic. A series of eight substrates, based on variation of the pentapeptide Boc-l-Ala-gamma-d-Glu-l-Lys-d-Ala-d-Ala, were synthesized to test specificity for three features of PBP substrates: (1) the presence or absence of an N(epsilon)-acyl group, (2) the presence of d-IsoGln in place of gamma-d-Glu, and (3) the presence or absence of the N-terminal l-Ala residue. The capacity of these peptides to serve as substrates for Neisseria gonorrhoeae (NG) PBP3 was assessed. NG PBP3 demonstrated good catalytic efficiency (2.5 x 10(5) M(-1) s(-1)) with the best

SUBMITTER: Peddi S 

PROVIDER: S-EPMC2756183 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature