Stereoselectivities of microbial epoxide hydrolases

Curr Opin Chem Biol. 1999 Feb;3(1):16-21. doi: 10.1016/s1367-5931(99)80004-0.


Epoxide hydrolases from bacterial and fungal sources are highly versatile biocatalysts for the asymmetric hydrolysis of epoxides on a preparative scale. Besides kinetic resolution, which yields the corresponding enantiomerically enriched vicinal diol and the remaining nonconverted epoxide, enantioconvergent processes are also possible, which lead to the formation of a single enantiomeric diol from a racemic oxirane. The data available to date indicate that the enantioselectivities of enzymes from certain microbial sources can be correlated to the substitutional pattern of various types of substrates: red yeasts (e.g. Rhodotorula or Rhodosporidium sp.) give best enantioselectivities with monosubstituted oxiranes; fungal cells (e.g. from Aspergillus and Beauveria sp.) are best suited for styrene oxide-type substrates; bacterial enzymes, on the other hand (in particular from Actinomycetes such as Rhodococcus and Nocardia sp.) are the biocatalysts of choice for more highly substituted 2,2- and 2,3-disubstituted epoxides.

Publication types

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

MeSH terms

  • Bacteria / enzymology*
  • Epoxide Hydrolases / metabolism*
  • Epoxy Compounds / chemical synthesis
  • Epoxy Compounds / chemistry
  • Stereoisomerism
  • Yeasts / enzymology*


  • Epoxy Compounds
  • Epoxide Hydrolases