| Enantioselective alpha-hydroxylation of 2-arylacetic acid derivatives and buspirone catalyzed by engineered cytochrome P450 BM-3. | |
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MedLine Citation:
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PMID: 16669674 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Here we report that an engineered microbial cytochrome P450 BM-3 (CYP102A subfamily) efficiently catalyzes the alpha-hydroxylation of phenylacetic acid esters. This P450 BM-3 variant also produces the authentic human metabolite of buspirone, R-6-hydroxybuspirone, with 99.5% ee. |
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Authors:
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Marco Landwehr; Lisa Hochrein; Christopher R Otey; Alex Kasrayan; Jan-E Bäckvall; Frances H Arnold |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 128 ISSN: 0002-7863 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2006 May |
Date Detail:
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Created Date: 2006-05-03 Completed Date: 2007-08-28 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
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Languages: eng Pagination: 6058-9 Citation Subset: IM |
Affiliation:
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Division of Chemistry and Chemical Engineering 210-41, California Institute of Technology, Pasadena, California 91125-4100, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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chemistry*,
genetics Buspirone / chemistry* Catalysis Cytochrome P-450 Enzyme System / chemistry*, genetics Hydroxylation Mixed Function Oxygenases / chemistry*, genetics Mutagenesis, Site-Directed NADPH-Ferrihemoprotein Reductase Phenylacetates / chemistry* Stereoisomerism |
| Grant Support | |
ID/Acronym/Agency:
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R01 GM068664-01/GM/NIGMS NIH HHS; R01 GM068664-01/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Phenylacetates; 36505-84-7/Buspirone; 9035-51-2/Cytochrome P-450 Enzyme System; EC 1.-/Mixed Function Oxygenases; EC 1.6.2.4/NADPH-Ferrihemoprotein Reductase; EC 1.6.2.4/flavocytochrome P450 BM3 monoxygenases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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