Highly Active Single-Mutation Variant of P450BM₃ (CYP102A1)

The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450BM₃ (CYP102A1) has the unexpected and d...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2009-07, Vol.10 (10), p.1654-1656
Main Authors: Whitehouse, Christopher J.C, Bell, Stephen G, Yang, Wen, Yorke, Jake A, Blanford, Christopher F, Strong, Anthony J.F, Morse, Edward J, Bartlam, Mark, Rao, Zihe, Wong, Luet-Lok
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
catalysis
Catalytic Domain
Crystallography, X-Ray
Cytochrome P-450 Enzyme System - chemistry
Cytochrome P-450 Enzyme System - genetics
Cytochrome P-450 Enzyme System - metabolism
cytochromes P450
CH bond activation
enzyme evolution
Fatty Acids - metabolism
Kinetics
Mutation
NADPH-Ferrihemoprotein Reductase - chemistry
NADPH-Ferrihemoprotein Reductase - genetics
NADPH-Ferrihemoprotein Reductase - metabolism
oxidation
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
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Summary:The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450BM₃ (CYP102A1) has the unexpected and desirable effect of enhancing the activity of this fatty acid hydroxylase with a broad range of non-natural substrates, as illustrated by the figure.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200900279