Combinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450BM3 for Selective Hydroxylation of Large Substrates
AuthorsLewis, Jared C.
Mantovani, Simone M.
Snow, Christopher D.
Komor, Russell S.
Wong , Chi-Huey
Arnold, Frances H.
KAUST Grant NumberKUS-F1-028-03
Online Publication Date2010-11-24
Print Publication Date2010-12-10
Permanent link to this recordhttp://hdl.handle.net/10754/597800
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AbstractMade 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.
CitationLewis JC, Mantovani SM, Fu Y, Snow CD, Komor RS, et al. (2010) Combinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450BM3 for Selective Hydroxylation of Large Substrates. ChemBioChem 11: 2502–2505. Available: http://dx.doi.org/10.1002/cbic.201000565.
SponsorsJ.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.
PubMed Central IDPMC4447097
CollectionsPublications Acknowledging KAUST Support
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