Combinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450BM3 for Selective Hydroxylation of Large Substrates

Jared C. Lewis, Simone M. Mantovani, Yu Fu, Christopher D. Snow, Russell S. Komor, Chi-Huey Wong, Frances H. Arnold

Research output: Contribution to journalArticlepeer-review

91 Scopus citations

Abstract

Made for each other: Combinatorial alanine substitution of active site residues in a thermostable cytochrome P450BM3 variant was used to generate an enzyme that is active with large substrates. Selective hydroxylation of methoxymethylated monosaccharides, alkaloids, and steroids was thus made possible (see Scheme). This approach could be useful for improving the activity of enzymes that show only limited activity with larger substrates. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish (US)
Pages (from-to)2502-2505
Number of pages4
JournalChemBioChem
Volume11
Issue number18
DOIs
StatePublished - Nov 24 2010
Externally publishedYes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): KUS-F1-028-03
Acknowledgements: J.C.L. is supported by a U.S. National Institutes of Health Pathways to Independence Award (1K99M087551-01A1). S.M.M. is supported by the Fundacao Coordenadoria de Aperfeicoamento de Pessoal de Nivel Superior (CAPES; 1756-09-5). This work was supported by the U.S. National Institutes of Health (2R01 M068664-05A1), the U.S. Department of Energy, Office of Basic Science, grant DE-FG02-06ER15762, and King Abdullah University of Science and Technology (KAUST), Award No. KUS-F1-028-03.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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