Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Buspirone / chemistry*
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Catalysis
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Cytochrome P-450 Enzyme System / chemistry*
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Cytochrome P-450 Enzyme System / genetics
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Hydroxylation
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Mixed Function Oxygenases / chemistry*
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Mixed Function Oxygenases / genetics
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Mutagenesis, Site-Directed
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NADPH-Ferrihemoprotein Reductase
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Phenylacetates / chemistry*
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Stereoisomerism
Substances
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Bacterial Proteins
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Phenylacetates
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Cytochrome P-450 Enzyme System
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Mixed Function Oxygenases
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NADPH-Ferrihemoprotein Reductase
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flavocytochrome P450 BM3 monoxygenases
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Buspirone