Evolved CYP102A1 (P450BM3) variants oxidise a range of non-natural substrates and offer new selectivity options

Chem Commun (Camb). 2008 Feb 28:(8):966-8. doi: 10.1039/b718124h. Epub 2008 Jan 11.

Abstract

The evolution of CYP102A1 variants with enhanced activity and altered specificity characteristics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus megaterium / enzymology
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Benzene Derivatives / chemistry
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / isolation & purification
  • Directed Molecular Evolution*
  • Enzyme Activation
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / isolation & purification
  • Molecular Structure
  • Mutagenesis
  • NADPH-Ferrihemoprotein Reductase
  • Naphthalenes / chemistry
  • Oxidation-Reduction
  • Substrate Specificity
  • Time Factors

Substances

  • Bacterial Proteins
  • Benzene Derivatives
  • Naphthalenes
  • n-propylbenzene
  • naphthalene
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases