title: Kinetic resolution of aliphatic acyclic beta-hydroxyketones by recombinant whole-cell Baeyer-Villiger monooxygenases--formation of enantiocomplementary regioisomeric esters.
abstract: A set of various linear aliphatic beta-hydroxyketones was investigated as substrates in the enzymatic kinetic and regioselective Baeyer-Villiger oxidation catalyzed by 12 Baeyer-Villiger monooxygenases from different bacterial origin. Excellent enantioselectivities (E >100) could be observed with 4-hydroxy-2-ketones. After acyl migration, the ester undergoes hydrolysis followed by the formation of optically active 1,2-diols. Furthermore, resolution of 5-hydroxy-3-ketones gave access to the 'abnormal' esters, which broadens applicability of these enzymes in organic chemistry. Additionally, it was noticed, that several substrates were converted by different enzymes in an enantiocomplementary way and with high optical purities.
authors.affiliation: University of Greifswald, Institute of Biochemistry, Department of Biotechnology and Enzyme Catalysis, Greifswald, Germany.
authors.forename: Jessica
authors.initials: J
authors.lastname: Rehdorf
authors.forename: Alenka
authors.initials: A
authors.lastname: Lengar
authors.forename: Uwe T
authors.initials: UT
authors.lastname: Bornscheuer
authors.forename: Marko D
authors.initials: MD
authors.lastname: Mihovilovic
mesh_terms: D055162:Biocatalysis; D001711:Biotransformation; D004926:Escherichia coli / Q000201:enzymology; D004952:Esters; D007659:Ketones / Q000737:chemistry*; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004952:Esters; D007659:Ketones; D011994:Recombinant Proteins; D006899:Mixed Function Oxygenases