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

Handle URI:
http://hdl.handle.net/10754/597800
Title:
Combinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450BM3 for Selective Hydroxylation of Large Substrates
Authors:
Lewis, Jared C.; Mantovani, Simone M.; Fu, Yu; Snow, Christopher D.; Komor, Russell S.; Wong , Chi-Huey; Arnold, Frances H.
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.
Citation:
Lewis 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.
Publisher:
Wiley-Blackwell
Journal:
ChemBioChem
KAUST Grant Number:
KUS-F1-028-03
Issue Date:
24-Nov-2010
DOI:
10.1002/cbic.201000565
PubMed ID:
21108271
PubMed Central ID:
PMC4447097
Type:
Article
ISSN:
1439-4227
Sponsors:
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.
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorLewis, Jared C.en
dc.contributor.authorMantovani, Simone M.en
dc.contributor.authorFu, Yuen
dc.contributor.authorSnow, Christopher D.en
dc.contributor.authorKomor, Russell S.en
dc.contributor.authorWong , Chi-Hueyen
dc.contributor.authorArnold, Frances H.en
dc.date.accessioned2016-02-25T12:56:56Zen
dc.date.available2016-02-25T12:56:56Zen
dc.date.issued2010-11-24en
dc.identifier.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.en
dc.identifier.issn1439-4227en
dc.identifier.pmid21108271en
dc.identifier.doi10.1002/cbic.201000565en
dc.identifier.urihttp://hdl.handle.net/10754/597800en
dc.description.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.en
dc.description.sponsorshipJ.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.en
dc.publisherWiley-Blackwellen
dc.subjectAlkaloidsen
dc.subjectBiocatalysisen
dc.subjectCytochromesen
dc.subjectMonosaccharidesen
dc.subjectSteroidsen
dc.titleCombinatorial Alanine Substitution Enables Rapid Optimization of Cytochrome P450BM3 for Selective Hydroxylation of Large Substratesen
dc.typeArticleen
dc.identifier.journalChemBioChemen
dc.identifier.pmcidPMC4447097en
dc.contributor.institutionDepartment of Chemistry, University of Chicago, Chicago, IL 60637, USA.en
kaust.grant.numberKUS-F1-028-03en

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.