Article
Active-site topologies of human CYP2D6 and its aspartate-301 --> glutamate, asparagine, and glycine mutants.
Archives of biochemistry and biophysics - 1 Jul 1996
Mackman R, Tschirret-Guth R A, Smith G, Hayhurst G P, Ellis S W, Lennard M S, Tucker G T, Wolf C R, Ortiz de Montellano P R
Abstract excerpt
Cytochrome P450 2D6 (CYP2D6) catalyzes the oxidation of substrates with a positively charged nitrogen atom 5-7 angstroms from the site of the oxidation. The active-site topology of CYP2D6 is examined here with phenyl-, 2-naphthyl-, and p-biphenyldiazene, which react with P450 enzymes to form sigm...
Topics
- Asparagine
- Aspartic Acid
- Binding Sites
- Cytochrome P-450 CYP2D6
- Cytochrome P-450 Enzyme System
- Electrochemistry
- Glutamic Acid
- Glycine
- Humans
- Hydrazines
- Imines
- Mixed Function Oxygenases
- Models, Molecular
- Molecular Structure
- Mutation