Abstract
Biocatalytic direct monohydroxylation of anilides has been achieved on preparative scale using mutant cytochrome P450BM3 enzymes. Representative mono- and disubstituted N-trifluoromethanesulfonyl anilides are shown to be converted in most cases to the corresponding 4-hydroxy derivatives, with substituent hydroxylation also occurring in two cases. By mutation variation, it is possible to achieve selective hydroxylation of either ring- or side-chain sites.
MeSH terms
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Anilides / chemistry
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Anilides / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Cytochrome P-450 Enzyme System / chemistry
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Cytochrome P-450 Enzyme System / metabolism*
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Hydroxylation
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Molecular Structure
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NADPH-Ferrihemoprotein Reductase / chemistry
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NADPH-Ferrihemoprotein Reductase / metabolism*
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Protein Engineering*
Substances
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Anilides
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Bacterial Proteins
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Cytochrome P-450 Enzyme System
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NADPH-Ferrihemoprotein Reductase
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flavocytochrome P450 BM3 monoxygenases