Article
Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.
Archives of biochemistry and biophysics - 1 Mar 2011
Girvan Hazel M, Dunford Adrian J, Neeli Rajasekhar, Ekanem Idorenyin S, Waltham Timothy N, Joyce M Gordon, Leys David, Curtis Robin A, Williams Paul, Fisher Karl, Voice Michael W, Munro Andrew W
Abstract excerpt
Bacillus megaterium P450 BM3 (BM3) is a P450/P450 reductase fusion enzyme, where the dimer is considered the active form in NADPH-dependent fatty acid hydroxylation. The BM3 W1046A mutant was generated, removing an aromatic "shield" from its FAD isoalloxazine ring. W1046A BM3 is a catalytically active NADH-dependent lauric acid hydroxylase, with product formation slightly superior to the NADPH-driven enzyme. The...
Topics
- Bacillus megaterium
- Bacterial Proteins
- Cytochrome P-450 Enzyme System
- Electron Transport
- Fatty Acids
- Flavin Mononucleotide
- Heme
- Hydroxylation
- Mutation