Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone

Biosci Biotechnol Biochem. 2002 Dec;66(12):2651-7. doi: 10.1271/bbb.66.2651.

Abstract

Microorganisms were screened for ones that reduced 3,5,5-trimethyl-2-cyclohexene-1,4-dione (ketoisophorone; KIP), and several strains were found to produce (6R)-2,2,6-trimethylcyclohexane-1,4-dione (levodione). The enzyme catalyzing the reduction of the C=C bond of KIP to yield (6R)-levodione was isolated from Candida macedoniensis AKU4588. The results of primary structural analysis and its enzymatic properties suggested that the enzyme might be an Old Yellow Enzyme family protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Candida / enzymology*
  • Cyclohexanones / chemistry*
  • Cyclohexanones / metabolism*
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Molecular Weight
  • NADPH Dehydrogenase / chemistry
  • NADPH Dehydrogenase / isolation & purification
  • NADPH Dehydrogenase / metabolism*
  • Oxidation-Reduction
  • Protein Subunits
  • Sequence Alignment
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Stereoisomerism
  • Substrate Specificity
  • Temperature

Substances

  • Cyclohexanones
  • Protein Subunits
  • ketoisophorone
  • isophorone
  • NADPH Dehydrogenase