Molecular modelling of CYP1 family enzymes CYP1A1, CYP1A2, CYP1A6 and CYP1B1 based on sequence homology with CYP102

被引：53

作者：

Lewis, DFV ^{[1
]}

Lake, BG

George, SG

Dickins, M

Eddershaw, PJ

Tarbit, MH

Beresford, AP

Goldfarb, PS

Guengerich, FP

机构：

[1] Univ Surrey, Sch Biol Sci, Mol Toxicol Grp, Guildford GU2 5XH, Surrey, England

[2] BIBRA Int, Carshalton SM5 4DS, Surrey, England

[3] Univ Stirling, NERC, Unit Aquat Biochem, Stirling FK9 4LA, Scotland

[4] Glaxo Grp Res Ltd, Ware SG12 0DP, Herts, England

[5] Vanderbilt Univ, Med Ctr, Dept Biochem, Nashville, TN 37232 USA

[6] Vanderbilt Univ, Med Ctr, Ctr Mol Toxicol, Nashville, TN 37232 USA

来源：

TOXICOLOGY | 1999年 / 139卷 / 1-2期

关键词：

rat; amino acid; human;

D O I：

10.1016/S0300-483X(99)00098-0

中图分类号：

R9 [药学];

学科分类号：

1007 [药学];

摘要：

Molecular modelling of a number of CYP1 family enzymes from rat, plaice and human is described based on amino acid sequence homology with the haemoprotein domain of CYP102, a unique bacterial P450 of known structure. The interaction of various substrates and inhibitors within the putative active sites of rat CYP1A1, human CYP1A2, a fish CYP1 enzyme CYP1A6 (from plaice) and human CYP1B1, is shown to be consistent with P450-mediated oxidation in each example or, in the case of inhibitors, mechanism of inhibition. It is reported that relatively small changes between the enzymes' active site regions assist in the rationalization of CYP1 enzyme preferences for particular substrate types, and a template of superimposed CYP1A2 substrates is shown to fit the putative active site of the human CYP1A2 enzyme. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：53 / 79

页数：27

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