Characterisation of a catabolic epoxide hydrolase from a Corynebacterium sp.

Elisa Misawa, Chan K N Chan Kwo Chion, Ian V. Archer, Marc P. Woodland, Ning Yi Zhou, Semra F. Carter, David A. Widdowson, David J. Leak

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48 Citations (SciVal)


The epoxide hydrolase (EH) from Cornyebacterium sp. C12, which grows on cyclohexene oxide as sole carbon source, has been purified to homogeneity in two steps, involving anion exchange followed by hydrophobic-interaction chromatography. The purified enzyme is multimeric (probably tetrameric) with a subunit size of 32,140 Da. The gene encoding Corynebacterium EH was located on a 3.5-kb BamHI fragment of C12 chromosomal DNA using a DNA probe generated by PCR using degenerate primers based on the N-terminal and an internal amino acid sequence. Sequencing and database comparison of the predicted amino acid sequence of Cornybacterium EH shows that it is similar to mammalian and plant soluble EH, and the recently published sequence of epichlorohydrin EH from Agrobacterium radiobacter AD1 [Rink, R., Fennema, M., Smids, M., Dehmel, U. and Janssen, D. B. (1997) J. Biol. Chem. 272, 14650-14657], particularly around the catalytic site. All of these proteins belong to the α/β-hydrolase-fold family of enzymes. Similarity to the mammalian microsomal EH is weaker.

Original languageEnglish
Pages (from-to)173-183
Number of pages11
JournalEuropean Journal of Biochemistry
Issue number1
Publication statusPublished - 1 Apr 1998


  • Corynebacterium C12
  • Cyclohexene oxide
  • Epoxide hydrolase
  • α/β hydrolase fold

ASJC Scopus subject areas

  • Biochemistry


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