Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids

Chem Commun (Camb). 2012 May 25;48(42):5115-7. doi: 10.1039/c2cc18103g. Epub 2012 Apr 19.

Abstract

CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Fatty Acids / biosynthesis*
  • Fatty Acids / chemistry
  • Hydroxylation
  • Marinobacter / enzymology
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Mutation
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Fatty Acids
  • Mixed Function Oxygenases