title: A new dehydrogenase from Clostridium acetobutylicum for asymmetric synthesis: dynamic reductive kinetic resolution entry into the Taxotère side chain.
abstract: An NADP-dependent alcohol dehydrogenase from Clostridium acetobutylicum (CaADH) has been expressed and characterized. CaADH enantioselectively reduces aromatic α-, β- and γ-keto esters to the corresponding D-hydroxy esters and provides a building block for the Taxotère side chain (95% yield, 95% de, 99% ee) by dynamic reductive kinetic resolution (DYRKR).
authors.affiliation: Department of Chemistry & Nebraska Center for Energy Sciences Research, University of Nebraska, Lincoln, NE, USA.
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Applegate
authors.forename: Ross W
authors.initials: RW
authors.lastname: Cheloha
authors.forename: David L
authors.initials: DL
authors.lastname: Nelson
authors.forename: David B
authors.initials: DB
authors.lastname: Berkowitz
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000447:Aldehydes / Q000737:chemistry; D055162:Biocatalysis; D046969:Clostridium acetobutylicum / Q000201:enzymology*; D004952:Esters; D007659:Ketones / Q000737:chemistry; D007700:Kinetics; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
chemical_list: D000447:Aldehydes; D004952:Esters; D007659:Ketones; D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; C084155:alcohol dehydrogenase (NAD(P)+)