NDLI: Transpeptidase-mediated incorporation of D-Amino Acids into bacterial peptidoglycan

Content Provider	PubMed Central
Author	Lupoli, Tania J. Tsukamoto, Hirokazu Doud, Emma H. Wang, Tsung-shing Andrew Walker, Suzanne Kahne, Daniel
Abstract	The beta-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 crosslinking 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 non-canonical D-amino acids can be introduced into the bacterial cell wall.
Related Links	http://dx.doi.org/10.1021/ja2040656
Ending Page	10751
Page Count	4
Starting Page	10748
File Format	PDF
ISSN	00027863
e-ISSN	15205126
Journal	Journal of the American Chemical Society
Issue Number	28
Volume Number	133
Language	English
Publisher Date	2011-07-20
Access Restriction	Open
Subject Keyword	Colloid and Surface Chemistry Biochemistry Chemistry(all) Catalysis Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Colloid and Surface Chemistry Biochemistry Catalysis

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