Diversity in the Oxidation of Substrates by Cytochrome P450 2D6: Lack of an Obligatory Role of Aspartate 301−Substrate Electrostatic Bonding

Cytochrome P450 (P450) 2D6 was first identified as the polymorphic human debrisoquine hydroxylase and subsequently shown to catalyze the oxidation of a variety of drugs containing a basic nitrogen. Residue Asp301 has been characterized as being involved in electrostatic interactions with substrates...

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Veröffentlicht in:	Biochemistry (Easton) 2002-09, Vol.41 (36), p.11025-11034
Hauptverfasser:	Guengerich, F. Peter, Miller, Grover P, Hanna, Imad H, Martin, Martha V, Léger, Serge, Black, Cameron, Chauret, Nathalie, Silva, José M, Trimble, Laird A, Yergey, James A, Nicoll-Griffith, Deborah A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amines - chemistry Amino Acid Substitution - genetics Aspartic Acid - chemistry Aspartic Acid - genetics Baculoviridae - genetics Benzenesulfonamides Binding Sites Catalysis Cytochrome P-450 CYP2D6 - chemistry Cytochrome P-450 CYP2D6 - genetics Cytochrome P-450 CYP2D6 - isolation & purification Humans Hydrogen Bonding Ligands Microsomes, Liver - enzymology Oxidation-Reduction Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Spiro Compounds - chemistry Static Electricity Substrate Specificity Sulfonamides - chemistry
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