Article
Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant.
Dalton transactions (Cambridge, England : 2003) - 28 Oct 2011
Whitehouse Christopher J C, Yang Wen, Yorke Jake A, Tufton Henry G, Ogilvie Lydia C I, Bell Stephen G, Zhou Weihong, Bartlam Mark, Rao Zihe, Wong Luet-Lok
Abstract excerpt
The substrate-free crystal structure of a five-mutation directed evolution variant of CYP102A1 (P450(BM3)) with generic activity-enhancing properties ("KT2") has been determined to 1.9-Å resolution. There is a close resemblance to substrate-bound structures of the wild-type enzyme (WT). The disruption of two salt bridges that link the G- and I-helices in WT causes conformational changes that break several...
Topics
- Bacterial Proteins
- Benzene Derivatives
- Catalysis
- Crystallography, X-Ray
- Cytochrome P-450 Enzyme System
- Electron Transport
- Electrons
- Hydrogen Bonding
- Kinetics
- Mutation
- NADPH-Ferrihemoprotein Reductase
- Oxidation-Reduction