Evolution of structure and substrate specificity ind-alanine:d-Alanine ligases and related enzymes |
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Authors: | Stefan Evers Barbara Casadewall Murielle Charles Sylvie Dutka-Malen Marc Galimand Patrice Courvalin |
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Institution: | 1. Unité des Agents Antibactériens, CNRS EP J0058, Institut Pasteur, 28 Rue du Docteur Roux, 75724, Paris, Cedex 15, France
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Abstract: | Thed-alanine:d-alanine-ligase-related enzymes can have three preferential substrate specificities. Usually, these enzymes synthesized-alanyl-d-alanine. In vancomycin-resistant Gram-positive bacteria, structurally related enzymes synthesized-alanyl-d-lactate or Dalanyl-d-serine. The sequence of internal fragments of eight structurald-alanine:d-alanine ligase genes from enterococci has been determined. Alignment of the deduced amino acid sequences with those of other
related enzymes from Gram-negative and Gram-positive bacteria revealed the presence of four distinct sequence patterns in
the putative substrate-binding sites, each correlating with specificity to a particular substrate (d-alanine:d-lactate ligases exhibited two patterns). Phylogenetic analysis showed different clusters. The enterococcal subtree was largely
superimposable on that derived from 16S rRNA sequences. In lactic acid bacteria, structural divergence due to differences
in substrate specificity was observed. Glycopeptide resistance proteins VanA and VanB, the VanC-type ligases, and Dd1A and
DdlB from enteric bacteria andHaemophilus influenzae constituted separate clusters.
Correspondence to: P. Courvalin |
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Keywords: | Cell-wall synthesis Peptidoglycan Enterococcus Glycopeptides Antibiotic resistance |
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