Alteration of substrate specificity of fructosyl-amino acid oxidase from Ulocladium sp. JS-103

J Biosci Bioeng. 2006 Sep;102(3):241-3. doi: 10.1263/jbb.102.241.

Abstract

We showed by random mutagenesis that one-amino-acid substitution at Arg94 in fructosyl-amino acid oxidase from Ulocladium sp. JS-103 enhanced substrate specificity toward fructosyl valine (FV), a model compound of hemoglobin A(1c). Kinetic analysis showed that the specificity of the R94W mutant enzyme toward FV was 14-fold that of the wild-type enzyme. The mutant enzyme obtained will be useful in developing an enzymatic measurement method for hemoglobin A(1c).

MeSH terms

  • Amino Acid Oxidoreductases / chemistry
  • Amino Acid Oxidoreductases / genetics*
  • Amino Acid Oxidoreductases / metabolism
  • Amino Acid Substitution*
  • Ascomycota / chemistry
  • Ascomycota / enzymology
  • Ascomycota / genetics*
  • Biological Assay / methods
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Glycated Hemoglobin / analysis
  • Humans
  • Mutagenesis / genetics*
  • Mutation, Missense*
  • Substrate Specificity / genetics
  • Valine / analogs & derivatives
  • Valine / chemistry
  • Valine / metabolism

Substances

  • Fungal Proteins
  • Glycated Hemoglobin A
  • fructosylvaline
  • Amino Acid Oxidoreductases
  • amadoriase
  • Valine