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

71 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

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