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Literature summary for 3.4.13.22 extracted from

  • Van Der Aart, L.; Lemmens, N.; Van Wamel, W.; Van Wezel, G.
    Substrate inhibition of VanA by D-alanine reduces vancomycin resistance in a VanX-dependent manner (2016), Antimicrob. Agents Chemother., 60, 4930-4939 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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Streptomyces coelicolor ATCC BAA-471
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General Information

General Information Comment Organism
physiological function exogenous D-Ala competes with D-Lac as a substrate for ligase VanA and reduces vancomycin resistance. The effect is augmented by several orders of magnitude in the absence of the D-Ala-D-Ala peptidase VanX. High concentrations of D-Ala lead to the production of a significant amount of wild-type cell wall precursors, while vanX-null mutants produce primarily wild-type precursors. This enhances the efficacy of vancomycin in the vancomycin-resistant model organism Streptomyces coelicolor, and the susceptibility of vancomycin-resistant clinical isolates of Enterococcus faecium increases by up to 100fold. The enhanced vancomycin sensitivity of Streptomyces coelicolor cells correlates directly to increased binding of the antibiotic to the cell wall Streptomyces coelicolor