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