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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism*
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Binding Sites
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Cytochrome P-450 Enzyme System / chemistry*
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Cytochrome P-450 Enzyme System / metabolism*
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Electron Transport / physiology*
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Mixed Function Oxygenases / chemistry*
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Mixed Function Oxygenases / metabolism*
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Models, Molecular
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Multigene Family
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NADPH-Ferrihemoprotein Reductase
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Oxidation-Reduction
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Protein Conformation
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Protein Structure, Tertiary
Substances
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Bacterial Proteins
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Cytochrome P-450 Enzyme System
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Mixed Function Oxygenases
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NADPH-Ferrihemoprotein Reductase
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flavocytochrome P450 BM3 monoxygenases