P450BM3: the very model of a modern flavocytochrome

被引：344

作者：

Munro, AW

Leys, DG

McLean, KJ

Marshall, KR

Ost, TWB

Daff, S

Miles, CS

Chapman, SK

Lysek, DA

Moser, CC

Page, CC

Dutton, PL

机构：

[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England

[2] Univ Edinburgh, Dept Chem, Edinburgh EH9 3JJ, Midlothian, Scotland

[3] ETH Honggerberg, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

[4] Univ Penn, Dept Biochem & Biophys, Johnson Res Fdn, Philadelphia, PA 19104 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2002年 / 27卷 / 05期

关键词：

D O I：

10.1016/S0968-0004(02)02086-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

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页码：250 / 257

页数：8

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