Mutation in a "tesB-like" hydroxyacyl-coenzyme A-specific thioesterase gene causes hyperproduction of extracellular polyhydroxyalkanoates by Alcanivorax borkumensis SK2

J Bacteriol. 2006 Dec;188(24):8452-9. doi: 10.1128/JB.01321-06. Epub 2006 Sep 22.

Abstract

A novel mutant of the marine oil-degrading bacterium Alcanivorax borkumensis SK2, containing a mini-Tn5 transposon disrupting a "tesB-like" acyl-coenzyme A (CoA) thioesterase gene, was found to hyperproduce polyhydroxyalkanoates (PHA), resulting in the extracellular deposition of this biotechnologically important polymer when grown on alkanes. The tesB-like gene encodes a distinct novel enzyme activity, which acts exclusively on hydroxylated acyl-CoAs and thus represents a hydroxyacyl-CoA-specific thioesterase. Inactivation of this enzyme results in the rechanneling of CoA-activated hydroxylated fatty acids, the cellular intermediates of alkane degradation, towards PHA production. These findings may open up new avenues for the development of simplified biotechnological processes for the production of PHA as a raw material for the production of bioplastics.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Alkanes / metabolism
  • Biotechnology / methods*
  • Culture Media
  • DNA Transposable Elements
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Gammaproteobacteria / enzymology*
  • Gammaproteobacteria / genetics
  • Gammaproteobacteria / growth & development
  • Microscopy, Electron, Scanning
  • Mutation*
  • Polyesters / metabolism*
  • Substrate Specificity
  • Thiolester Hydrolases / genetics*
  • Thiolester Hydrolases / metabolism
  • Up-Regulation

Substances

  • Acyl Coenzyme A
  • Alkanes
  • Culture Media
  • DNA Transposable Elements
  • Polyesters
  • Thiolester Hydrolases
  • octadecane