Continuous assay for VanX, the D-alanyl-D-alanine dipeptidase required for high-level vancomycin resistance

Anal Biochem. 1999 Jul 15;272(1):94-9. doi: 10.1006/abio.1999.4166.

Abstract

The reaction of L-alanine-p-nitroanilide with VanX was studied in an effort to develop a continuous assay for VanX activity for future kinetic and inhibition studies. VanX, containing Zn(II), Co(II), Fe(II), or Ni(II), catalyzes the hydrolysis of L-alanine-p-nitroanilide producing L-alanine and p-nitroaniline as products; the formation of the latter product (epsilon(404nm) = 10, 700 M(-1) cm(-1)) can be continuously monitored using UV-VIS spectrophotometry. Zn(II)-, Co(II)-, Fe(II)-, and Ni(II)-containing VanX exhibit saturation kinetics when L-alanine-p-nitroanilide is used as the substrate with K(m) and k(cat) values ranging from 300 to 700 microM and 0.028 to 0.080 s(-1), respectively. Inhibition studies using O-[(1S)-aminoethylhydroxyphosphinyl]-D-lactic acid as the inhibitor and L-alanine-p-nitroanilide as the substrate yielded a K(i) of 400 +/- 8 microM at pH 7.0. These studies reveal a continuous assay of VanX activity which could be used to further study the kinetic mechanism of VanX and to allow for the development of high-throughput screening for inhibitors of VanX.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aniline Compounds
  • Bacterial Proteins / analysis*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Dipeptidases / analysis*
  • Dipeptidases / genetics
  • Dipeptidases / metabolism
  • Dipeptides / metabolism
  • Drug Resistance, Microbial / genetics
  • Enterococcus faecium / drug effects
  • Enterococcus faecium / enzymology
  • Enterococcus faecium / genetics
  • Enzyme Inhibitors / pharmacology
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Kinetics
  • Metals / metabolism
  • Recombinant Proteins / analysis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Serine-Type D-Ala-D-Ala Carboxypeptidase*
  • Spectrophotometry
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity
  • Vancomycin / pharmacology

Substances

  • Aniline Compounds
  • Bacterial Proteins
  • Dipeptides
  • Enzyme Inhibitors
  • Metals
  • Recombinant Proteins
  • alanine-4-nitroanilide
  • alanylalanine
  • Vancomycin
  • Dipeptidases
  • Serine-Type D-Ala-D-Ala Carboxypeptidase
  • VanX dipeptidase