Letters in Drug Design & Discovery

G. Perry
University of Texas
San Antonio, TX
USA
Email: lddd@benthamscience.org

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Discovery of a Non-β-Lactam Inhibitor of Escherichia Coli L, Dcarboxypeptidase A Using a Coupled Fluorescent Assay

Author(s): Ellen Z. Baum.

Abstract:

During peptidoglycan recycling in Escherichia coli, L, D-carboxypeptidase A cleaves the tetrapeptide L-Ala-γ-D-Glu-meso-diaminopimelic acid-D-Ala, producing tripeptide and D-Ala. Previous studies utilized substrate purified from bacteria, with HPLC detection of tripeptide. Herein, synthetic peptide substrate containing L-Lys in place of diaminopimelic acid, and a fluorescent assay for D-Ala, were used to identify a benzoxazine as a non-β-lactam inhibitor of the enzyme.

Keywords: Carboxypeptidase, Bacterial cell wall, Peptidoglycan recycling, Murein

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Article Details

VOLUME: 3
ISSUE: 8
Year: 2006
Page: [561 - 566]
Pages: 6
DOI: 10.2174/157018006778194691
Price: $58