Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in Streptomyces toyocaensis, Escherichia coli and Synechocystis: attributes of catalytic efficiency, stereoselectivity and regulation with implications for function.

@article{Lessard1998HomologsOT,
  title={Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in Streptomyces toyocaensis, Escherichia coli and Synechocystis: attributes of catalytic efficiency, stereoselectivity and regulation with implications for function.},
  author={I A Lessard and Steven D Pratt and Dewey Granville McCafferty and Dirksen E Bussiere and Charles Hutchins and Barry L. Wanner and Leonard Katz and Christopher T Walsh},
  journal={Chemistry & biology},
  year={1998},
  volume={5 9},
  pages={489-504}
}
BACKGROUND Vancomycin-resistant enterococci are pathogenic bacteria that have altered cell-wall peptidoglycan termini (D-alanyl-D-lactate [D-Ala-D-lactate] instead of D-alanyl-D-alanine [D-Ala-D-Ala]), which results in a 1000-fold decreased affinity for binding vancomycin. The metallodipeptidase VanX (EntVanX) is key enzyme in antibiotic resistance as it reduces the cellular pool of the D-Ala-D-Ala dipeptide. RESULTS A bacterial genome search revealed vanX homologs in Streptomyces toyocaensis… CONTINUE READING

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