Published December 10, 2010 | Version Accepted Version + Supplemental Material
Journal Article Open

Combinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450_(BM3) for Selective Hydroxylation of Large Substrates

  • 1. ROR icon University of Chicago
  • 2. ROR icon State University of Campinas
  • 3. ROR icon Scripps Research Institute
  • 4. ROR icon California Institute of Technology
  • 5. ROR icon Genomics Research Center, Academia Sinica

Abstract

Made for each other: Combinatorial alanine substitution of active site residues in a thermostable cytochrome P450_(BM3) 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.

Additional Information

© 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Received: September 21, 2010. Published online on November 24, 2010. 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.

Attached Files

Accepted Version - nihms356634.pdf

Supplemental Material - cbic_201000565_sm_miscellaneous_information.pdf

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cbic_201000565_sm_miscellaneous_information.pdf

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Additional details

Identifiers

PMCID
PMC4447097
Eprint ID
21785
Resolver ID
CaltechAUTHORS:20110118-104553247

Funding

NIH
1K99M087551-01A1
NIH
2R01 M068664-05A1
Fundacao Coordenadoria de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
1756-09-5
Department of Energy (DOE)
DE-FG02-06ER15762
King Abdullah University of Science and Technology (KAUST)
KUS-F1-028-03

Dates

Created
2011-01-31
Created from EPrint's datestamp field
Updated
2021-11-09
Created from EPrint's last_modified field