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Comparative Study
. 1991 Feb 26;30(8):2017-21.
doi: 10.1021/bi00222a002.

Identification of vancomycin resistance protein VanA as a D-alanine:D-alanine ligase of altered substrate specificity

T D Bugg  1 , S Dutka-Malen, M Arthur, P Courvalin, C T Walsh
Affiliations
Comparative Study

Identification of vancomycin resistance protein VanA as a D-alanine:D-alanine ligase of altered substrate specificity

T D Bugg et al. Biochemistry. .

Abstract

High-level glycopeptide resistance in Enterococcus faecium BM4147 is mediated by a 38-kDa protein VanA, whose amino acid sequence is related to Gram-negative D-alanine:D-alanine (D-Ala-D-Ala) ligases [Dutka-Malen, S., Molinas, C., Arthur, M., & Courvalin, P. (1990) Mol. Gen. Genet. 224, 364-372]. We report purification of VanA and demonstrate that it has D-Ala-D-Ala ligase activity but has substantially modified substrate specificity, compared with Gram-negative D-Ala-D-Ala ligases. VanA preferentially condenses D-Ala with D-Met or D-Phe, raising the possibility that its cellular role is to synthesize a modified cell-wall component, which is subsequently not recognized by vancomycin.

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