Hydroxylation of anilides by engineered cytochrome P450BM3

Org Biomol Chem. 2017 Oct 25;15(41):8780-8787. doi: 10.1039/c7ob02236k.

Abstract

Biocatalytic direct monohydroxylation of anilides has been achieved on preparative scale using mutant cytochrome P450BM3 enzymes. Representative mono- and disubstituted N-trifluoromethanesulfonyl anilides are shown to be converted in most cases to the corresponding 4-hydroxy derivatives, with substituent hydroxylation also occurring in two cases. By mutation variation, it is possible to achieve selective hydroxylation of either ring- or side-chain sites.

MeSH terms

  • Anilides / chemistry
  • Anilides / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / metabolism*
  • Hydroxylation
  • Molecular Structure
  • NADPH-Ferrihemoprotein Reductase / chemistry
  • NADPH-Ferrihemoprotein Reductase / metabolism*
  • Protein Engineering*

Substances

  • Anilides
  • Bacterial Proteins
  • Cytochrome P-450 Enzyme System
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases