Since its discovery in the 1980s, the fatty acid hydroxylase flavocytochrome P450 (cytochrome P450) BM3 (CYP102A1) from Bacillus megaterium has been adopted as a paradigm for the understanding of structure and mechanism in the P450 superfamily of enzymes. P450 BM3 was the first P450 discovered as a fusion to its redox partner – a eukaryotic-like diflavin reductase. This fact fuelled the interest in soluble P450 BM3 as a model for the mammalian hepatic P450 enzymes, which operate a similar electron transport chain using separate, membrane-embedded P450 and reductase enzymes. Structures of each of the component domains of P450 BM3 have now been resolved and detailed protein engineering and molecular enzymology studies have established roles for several amino acids in, e.g. substrate binding, coenzyme selectivity and catalysis. The potential of P450 BM3 for biotechnological applications has also been recognized, with variants capable of industrially important transformations generated using rational mutagenesis and forced evolution techniques. This paper focuses on recent developments in our understanding of structure and mechanism of this important enzyme and highlights important problems still to be resolved.
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August 2005
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Conference Article|
August 01 2005
Flavocytochrome P450 BM3: an update on structure and mechanism of a biotechnologically important enzyme
A.J. Warman;
A.J. Warman
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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O. Roitel;
O. Roitel
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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R. Neeli;
R. Neeli
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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H.M. Girvan;
H.M. Girvan
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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H.E. Seward;
H.E. Seward
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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S.A. Murray;
S.A. Murray
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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K.J. McLean;
K.J. McLean
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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M.G. Joyce;
M.G. Joyce
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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H. Toogood;
H. Toogood
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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R.A. Holt;
R.A. Holt
†Avecia Biotechnology, Belasis Avenue, Billingam, Cleveland TS23 1YN, U.K.
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D. Leys;
D. Leys
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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N.S. Scrutton;
N.S. Scrutton
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
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A.W. Munro
A.W. Munro
1
*Department of Biochemistry, University of Leicester, The Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.
1To whom correspondence should be addressed (email awm9@le.ac.uk).
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Publisher: Portland Press Ltd
Received:
April 13 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (4): 747–753.
Article history
Received:
April 13 2005
Citation
A.J. Warman, O. Roitel, R. Neeli, H.M. Girvan, H.E. Seward, S.A. Murray, K.J. McLean, M.G. Joyce, H. Toogood, R.A. Holt, D. Leys, N.S. Scrutton, A.W. Munro; Flavocytochrome P450 BM3: an update on structure and mechanism of a biotechnologically important enzyme. Biochem Soc Trans 1 August 2005; 33 (4): 747–753. doi: https://doi.org/10.1042/BST0330747
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