A Highly Active Single-Mutation Variant of P450BM3 (CYP102A1) (pages 1654–1656)
Christopher J. C. Whitehouse, Stephen G. Bell, Wen Yang, Jake A. Yorke, Christopher F. Blanford, Anthony J. F. Strong, Edward J. Morse, Mark Bartlam, Zihe Rao and Luet-Lok Wong
Article first published online: 2 JUN 2009 | DOI: 10.1002/cbic.200900279
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.