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β-Lactam antibiotics react with penicillin binding proteins (PBPs) to form relatively stable acyl-enzyme complexes. We describe structures derived from the reaction of piperacillin with PBP3 (Pseudomonas aeruginosa) including not only the anticipated acyl-enzyme complex but also an unprecedented complex with (5S)-penicilloic acid, which was formed by C-5 epimerization of the nascent (5R)-penicilloic acid product. Formation of the complex was confirmed by solution studies, including NMR. Together, these results will be useful in the design of new PBP inhibitors and raise the possibility that noncovalent PBP inhibition by penicilloic acids may be of clinical relevance.

Original publication

DOI

10.1021/cb400200h

Type

Journal article

Journal

ACS Chem Biol

Publication Date

18/10/2013

Volume

8

Pages

2112 - 2116

Keywords

Coordination Complexes, Inhibitory Concentration 50, Magnetic Resonance Spectroscopy, Models, Molecular, Penicillanic Acid, Penicillin-Binding Proteins, Pseudomonas