Greatly reduced amino acid alphabets in directed evolution: making the right choice for saturation mutagenesis at homologous enzyme positions.
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.
Reetz
Manfred T
MT
Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470, Mülheim/Ruhr, Germany. reetz@mpi-muelheim.mpg.de
Wu
Sheng
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D055162:Biocatalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019020:Directed Molecular Evolution; D007659:Ketones / Q000737:chemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016296:Mutagenesis; D010082:Oxepins / Q000138:chemical synthesis / Q000737:chemistry; D010084:Oxidation-Reduction; D016415:Sequence Alignment; D013237:Stereoisomerism
D000596:Amino Acids; D007659:Ketones; D010082:Oxepins; D003577:Cytochrome P-450 Enzyme System; C045704:acetone monooxygenase