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Converting an Esterase into an Epoxide Hydrolase

Authors


  • We thank Prof. Dick Janssen for providing the gene of Agrobacterium radiobacter epoxide hydrolase and Dr. Santosh Padhi for preparation of several site-directed mutants. U.T.B. thanks the German Research Foundation (DFG, grant Bo1862/4-1), and R.J.K. the US National Science Foundation (CHE-0616560) for financial support.

Abstract

Entering the fold: A common structural motif in hydrolytic enzymes is the α,β-hydrolase fold. The interconversion of one enzyme into another by introduction of mechanistically important residues is not enough; only substitution of a loop allows epoxide hydrolase activity in the esterase scaffold to be formed (see picture; structure comparison of epoxide hydrolases (green) with the esterase (orange)). The result is an enantioselective chimeric enzyme.

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