ChemCatChem · 2009 · 76 citations · 35 references
Life SciencesBiochemistryMicrobiologyBiochemical GeneticsEnzymologyMicrobial GeneticsMicrobial Metabolic EngineeringThermostable EnzymesActive Site AnalysisAlcohol Dehydrogenase CatalysisCatalytic Residue ConservationKetonesPoint Mutation AnalysisPoint Mutation Effects
The asymmetric reduction of benzylic and heteroaryl ketones to the corresponding (R)-alcohols using I86A Thermoanaerobacter ethanolicus alcohol dehydrogenase (I86A TeSADH) is described. This single amino acid mutation not only makes the active site of I86A TeSADH able to accommodate more sterically demanding substituents than those accommodated by wild-type TeSADH, but it also reverses the substrate stereospecificity of TeSADH.
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Recent developments in asymmetric reduction of ketones with biocatalysts
Kaoru Nakamura, Rio Yamanaka, Tomoko Matsuda et al. · Tetrahedron Asymmetry · 2003 · 510 citations