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

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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Letters in Drug Design & Discovery

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

Volume: 3 Issue: 8

Author(s): Ellen Z. Baum

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

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.

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Baum Z. Ellen, Discovery of a Non-β-Lactam Inhibitor of Escherichia Coli L, Dcarboxypeptidase A Using a Coupled Fluorescent Assay, Letters in Drug Design & Discovery 2006; 3 (8) . https://dx.doi.org/10.2174/157018006778194691