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Published December 2011 | Accepted Version
Journal Article Open

Cytochrome P450: taming a wild type enzyme

Abstract

Protein engineering of cytochrome P450 monooxygenases (P450s) has been very successful in generating valuable non-natural activities and properties, allowing these powerful catalysts to be used for the synthesis of drug metabolites and in biosynthetic pathways for the production of precursors of artemisinin and paclitaxel. Collected experience indicates that the P450s are highly 'evolvable' – they are particularly robust to mutation in their active sites and readily accept new substrates and exhibit new selectivities. Their ability to adapt to new challenges upon mutation may reflect the nonpolar nature of their active sites as well as their high degree of conformational variability.

Additional Information

© 2011 Elsevier Ltd. Available online 14th March 2011. The authors acknowledge the support of the U.S. Department of Energy, BES grant DE-FG02-06ER15762, National Institutes of Health ARRA grant 2R01GM068664-05A1, and National Institutes of Health grant 1R01-DA028299. RL acknowledges the support of NIH fellowship 1F32GM095061-01. The content is solely the responsibility of the authors and does not necessarily represent the official views of any of the funding agencies. We thank Eric Brustad, Philip Romero, Kersten Rabe, Mike Chen, and Indira Wu for helpful comments on various drafts of this review.

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August 19, 2023
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