Hydroxylation of fatty acids by microsomal and reconstituted cytochrome P450 2B1

FEBS Letters

Alterman, Michail A.¹  Hanzlik, Robert P.² 

[1] Biochemical Research Service Laboratory, University of Kansas, 1251 Wescoe Hall Drive, Lawrence, KS 66045-7582, USA;Department of Medicinal Chemistry, 1251 Wescoe Hall Drive, Lawrence, KS 66045-7582, USA

关键词: Cytochrome P450 2B1;    Fatty acid;    ω-Hydroxylation;    Microsome;    CYP;    cytochrome(s) P450;    PB;    phenobarbital;   

DOI  :  10.1016/S0014-5793(02)02260-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Understanding the mechanisms by which cytochrome(s) P450 (CYP) discriminate good from poor substrates, and orient them for highly regio- and stereoselective oxidation, has considerable intrinsic and practical importance. Here we present results of a study of fatty acid hydroxylation by CYP2B1 in a reconstituted system and in microsomes from phenobarbital-pretreated rats. The results indicate that 2B1 prefers decanoic acid as the optimum fatty acid substrate (among C₈–C₁₆) and that it hydroxylates positions five or more methylene groups distant from the carboxylate carbon. That hydroxylation does not occur at carbon atoms closer to the carboxyl group than the C₆ position suggests that these carbons may not reach the ferryl oxygen because the carboxyl group is anchored to a specific site at a fixed distance from the heme iron.

【 授权许可】

Unknown