Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics

Chem Commun (Camb). 2001 Sep 21:(18):1752-3. doi: 10.1039/b103548g.

Abstract

ORF22 from the chloroeremomycin gene cluster has been cloned, expressed and characterised as a hydroxymandelate oxidase (HmO) that is involved in the formation of both (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / isolation & purification
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acids / biosynthesis*
  • Bacterial Proteins*
  • Chromatography, Gas
  • Gene Expression Regulation, Bacterial
  • Glycine / analogs & derivatives*
  • Glycine / biosynthesis*
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism
  • Molecular Structure
  • Oxidoreductases / genetics
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Resorcinols
  • Spectrophotometry
  • Vancomycin / analogs & derivatives*
  • Vancomycin / chemistry*

Substances

  • Amino Acids
  • Bacterial Proteins
  • Membrane Proteins
  • ORF22 protein, Corynebacterium glutamicum
  • Resorcinols
  • chloroeremomycin
  • 3,5-dihydroxyphenylglycine
  • Vancomycin
  • 4-hydroxyphenylglycine
  • Oxidoreductases
  • Alcohol Oxidoreductases
  • L-mandelate dehydrogenase
  • Glycine