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

✍ Scribed by 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.

Book ID
124069930
Publisher
American Chemical Society
Year
2002
Tongue
English
Weight
159 KB
Volume
41
Category
Article
ISSN
0006-2960

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📜 SIMILAR VOLUMES

Roles of phenylalanine at position 120 a
Roles of phenylalanine at position 120 and glutamic acid at position 222 in the oxidation of chiral substrates by cytochrome P450 2D6
✍ Kazufumi Masuda; Keietsu Tamagake; Takashi Katsu; Fumihiro Torigoe; Keita Saito; 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 350 KB

## Abstract The roles of Phe‐120 and Glu‐222 in the oxidation of chiral substrates bunitrolol (BTL) and bufuralol (BF) by CYP2D6 are discussed. Wild‐type CYP2D6 (CYP2D6‐WT) oxidized BTL to 4‐hydroxybunitrolol (4‐OH‐BTL) with substrate enantioselectivity of (__R__)‐(+)‐BTL > (__S__)‐(−)‐BTL. The sam