Abstract
Entering the fold: A common structural motif in hydrolytic enzymes is the alpha,beta-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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Catalysis
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Epoxide Hydrolases / chemistry*
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Epoxide Hydrolases / genetics
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Esterases / chemistry*
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Esterases / genetics
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Evolution, Molecular
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Hydrolysis
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Molecular Sequence Data
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Mutation
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Protein Conformation
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Protein Folding
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Styrenes / chemistry
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Substrate Specificity
Substances
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Styrenes
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Esterases
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Epoxide Hydrolases