Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.

doi:10.1016/S1074-5521(99)89009-7

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Article

Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.

Chemistry & biology - 1 Mar 1999

Lessard I A, Walsh C T

Abstract excerpt

BACKGROUND: Vancomycin-resistant enterococci are pathogenic bacteria that attenuate antibiotic sensitivity by producing peptidoglycan precursors that terminate in D-Ala-D-lactate rather than D-Ala-D-Ala. A key enzyme in effecting antibiotic resistance is the metallodipeptidase VanX, which reduces the cellular pool of the D-Ala-D-Ala dipeptide. RESULTS: We constructed eleven mutants, using the recently determined...

Topics

Anti-Bacterial Agents
Bacterial Proteins
Carboxypeptidases
DNA Mutational Analysis
DNA, Recombinant
Dipeptidases
Drug Resistance, Microbial
Electrophoresis, Polyacrylamide Gel
Enterococcus
Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Mutagenesis, Site-Directed

Mutation

Peptide Synthases

Protein Structure, Tertiary

Serine-Type D-Ala-D-Ala Carboxypeptidase

Vancomycin

Source

Open in PubMed

Identifiers

PMID: 10074467
DOI: 10.1016/S1074-5521(99)89009-7

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