Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids

Chem Commun (Camb). 2019 Nov 28;55(96):14462-14465. doi: 10.1039/c9cc06447h.

Abstract

Structure-based engineering of a NAD+-dependent secondary alcohol dehydrogenase from Micrococcus luteus led to a 1800-fold increase in catalytic efficiency for NADP+. Furthermore, the engineered enzymes (e.g., D37S/A38R/V39S/T15I) were successfully coupled to a NADPH-dependent Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440 for redox-neutral biotransformations of C18 fatty acids into C9 chemicals.

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / metabolism*
  • Binding Sites
  • Biotransformation
  • Fatty Acids / metabolism
  • Genetic Engineering
  • Kinetics
  • Micrococcus luteus / enzymology*
  • Mixed Function Oxygenases / metabolism
  • Molecular Dynamics Simulation
  • Oxidation-Reduction
  • Pseudomonas / enzymology

Substances

  • Fatty Acids
  • Mixed Function Oxygenases
  • Alcohol Oxidoreductases
  • isopropanol dehydrogenase (NADP)