Abstract
Enantioselective mutants of the thermally robust phenyl acetone monooxygenase (PAMO) as catalysts in Baeyer-Villiger reactions have been evolved by utilizing saturation mutagenesis in which drastically reduced amino acid alphabets are employed at homologous enzyme positions.
MeSH terms
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Amino Acid Sequence
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Amino Acids / chemistry*
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Biocatalysis
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Cytochrome P-450 Enzyme System / chemistry*
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Cytochrome P-450 Enzyme System / genetics
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Cytochrome P-450 Enzyme System / metabolism*
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Directed Molecular Evolution*
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Ketones / chemistry
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Kinetics
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Molecular Sequence Data
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Molecular Structure
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Mutagenesis*
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Oxepins / chemical synthesis
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Oxepins / chemistry
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Oxidation-Reduction
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Sequence Alignment
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Stereoisomerism
Substances
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Amino Acids
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Ketones
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Oxepins
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Cytochrome P-450 Enzyme System
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acetone monooxygenase