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Chembiochem. 2009 Jul 6;10(10):1654-6. doi: 10.1002/cbic.200900279.

A highly active single-mutation variant of P450BM3 (CYP102A1).

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1
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, UK.

Abstract

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 P450(BM3) (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.

PMID:
19492389
DOI:
10.1002/cbic.200900279
[Indexed for MEDLINE]
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