The substrate binding site of human liver cytochrome P450 2C9: an NMR study.

Poli-Scaife, S; Attias, R; Dansette, P M; Mansuy, D

Poli-Scaife, S; Attias, R; Dansette, P M; Mansuy, D.

Affiliation

Poli-Scaife S; Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, URA 400 CNRS, Université Paris V, 45 Rue des Saints-Pères, 75270 Paris Cedex 06, France.

Biochemistry ; 36(42): 12672-82, 1997 Oct 21.

Article in En | MEDLINE | ID: mdl-9335524

Subject(s)

Aryl Hydrocarbon Hydroxylases; Cytochrome P-450 Enzyme System/chemistry; Cytochrome P-450 Enzyme System/metabolism; Microsomes, Liver/enzymology; NADPH-Ferrihemoprotein Reductase/metabolism; Protein Conformation; Steroid 16-alpha-Hydroxylase; Steroid Hydroxylases/chemistry; Steroid Hydroxylases/metabolism; Animals; Binding Sites; Cytochrome P-450 Enzyme System/isolation & purification; Diclofenac/metabolism; Humans; Isomerism; Kinetics; Lauric Acids/metabolism; Models, Chemical; Models, Molecular; NADPH-Ferrihemoprotein Reductase/isolation & purification; Nuclear Magnetic Resonance, Biomolecular; Rats; Spectrophotometry; Steroid Hydroxylases/isolation & purification; Sulfaphenazole/chemistry; Sulfaphenazole/metabolism; Ticrynafen/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Protein Conformation / Steroid Hydroxylases / Microsomes, Liver / Aryl Hydrocarbon Hydroxylases / NADPH-Ferrihemoprotein Reductase / Cytochrome P-450 Enzyme System / Steroid 16-alpha-Hydroxylase Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Biochemistry Year: 1997 Document type: Article Affiliation country: France

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