Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1

Appl Environ Microbiol. 1992 Oct;58(10):3407-9. doi: 10.1128/aem.58.10.3407-3409.1992.

Abstract

Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)-indanol (83% R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96% R), 1-indanone, and trans-1,3-indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)-indanol.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cloning, Molecular
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics*
  • Hydroxylation
  • Indans / chemistry
  • Indans / metabolism*
  • Oxygenases / genetics
  • Oxygenases / metabolism*
  • Pseudomonas putida / genetics*
  • Stereoisomerism

Substances

  • Indans
  • Oxygenases
  • toluene dioxygenase