1238894-49-9Relevant academic research and scientific papers
Expanding the Substrate Specificity of Thermoanaerobacter pseudoethanolicus Secondary Alcohol Dehydrogenase by a Dual Site Mutation
Musa, Musa M.,Bsharat, Odey,Karume, Ibrahim,Vieille, Claire,Takahashi, Masateru,Hamdan, Samir M.
, p. 798 - 805 (2018)
Here, we report the asymmetric reduction of selected phenyl-ring-containing ketones by various single- and dual-site mutants of Thermoanaerobacter pseudoethanolicus secondary alcohol dehydrogenase (TeSADH). The further expansion of the size of the substrate binding pocket in the mutant W110A/I86A not only allowed the accommodation of substrates of the single mutants W110A and I86A within the expanded active site but also expanded the substrate range of the enzyme to ketones bearing two sterically demanding groups (bulky–bulky ketones), which are not substrates for the TeSADH single mutants. We also report the regio- and enantioselective reduction of diketones with W110A/I86A TeSADH and single TeSADH mutants. The double mutant exhibited dual stereopreference to generate the Prelog products most of the time and the anti-Prelog products in a few cases.
Straightforward synthesis of enantiopure 2,3-dihydrobenzofurans by a sequential stereoselective biotransformation and chemical intramolecular cyclization
Mangas-Sanchez, Juan,Busto, Eduardo,Gotor-Fernandez, Vicente,Gotor, Vicente
supporting information; experimental part, p. 3498 - 3501 (2010/10/20)
(Equation Presented). A new family of optically active 2,3- dihydrobenzofurans has been prepared by a simple chemoenzymatic asymmetric strategy. This synthetic approach is based on the combination of a lipase-mediated kinetic resolution of 1-aryl-2-propanols or bioreduction of the corresponding ketones followed by an intramolecular cyclization reaction. These novel compounds have been prepared in enantiopure form and in good overall yield through a straightforward route.
