Article
Roles of Residues F206 and V367 in Human CYP2B6: Effects of Mutations on Androgen Hydroxylation, Mechanism-Based Inactivation, and Reversible Inhibition.
Drug metabolism and disposition: the biological fate of chemicals - 1 Nov 2016
Lin Hsia-Lien, Zhang Haoming, Kenaan Cesar, Hollenberg Paul F
Abstract excerpt
The crystal structures of human CYP2B6 indicate that Phe206 and Val367 are in close proximity to the substrate binding site and suggest that both residues may play important roles in substrate metabolism and inhibitor binding. To test this hypothesis, we investigated the effects of mutating these residues to Ala on the regiospecificity of CYP2B6 for the metabolism of testosterone and androstenedione. For...
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