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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3532-3535 |
| Number of pages | 4 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 48 |
| Issue number | 19 |
| DOIs | |
| State | Published - Apr 27 2009 |
Keywords
- Directed evolution
- Enantioselectivity
- Enzyme catalysis
- Epoxide hydrolases
- Esterases
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