| Literature DB >> 12076537 |
Andrew W Munro1, David G Leys, Kirsty J McLean, Ker R Marshall, Tobias W B Ost, Simon Daff, Caroline S Miles, Stephen K Chapman, Dominikus A Lysek, Christopher C Moser, Christopher C Page, P Leslie Dutton.
Abstract
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.Entities:
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Year: 2002 PMID: 12076537 DOI: 10.1016/s0968-0004(02)02086-8
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807