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J Am Chem Soc. 2011 Jul 20;133(28):10748-51. doi: 10.1021/ja2040656. Epub 2011 Jun 27.

Transpeptidase-mediated incorporation of D-amino acids into bacterial peptidoglycan.

Author information

1
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Abstract

The β-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse D-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical D-amino acids can be introduced into the bacterial cell wall.

PMID:
21682301
PMCID:
PMC3172152
DOI:
10.1021/ja2040656
[Indexed for MEDLINE]
Free PMC Article

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