Article
The catalytic site of cytochrome P4504A11 (CYP4A11) and its L131F mutant.
The Journal of biological chemistry - 4 Sept 1998
Dierks E A, Zhang Z, Johnson E F, de Montellano P R
Abstract excerpt
CYP4A11, the principal known human fatty acid omega-hydroxylase, has been expressed as a polyhistidine-tagged protein and purified to homogeneity. Based on an alignment with P450BM-3, the CYP4A11 L131F mutant has been constructed and similarly expressed. The two proteins are spectroscopically ind...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Binding Sites
- Cytochrome P-450 CYP4A
- Cytochrome P-450 Enzyme Inhibitors
- Cytochrome P-450 Enzyme System
- Fatty Acids, Omega-3
- Humans
- Imidazoles
- Imines
- Mixed Function Oxygenases
- Models, Molecular
- Molecular Sequence Data
- Mutation
- NADPH-Ferrihemoprotein Reductase
- Recombinant Proteins
- Sequence Homology, Amino Acid
- Stereoisomerism
