69617-84-1Relevant articles and documents
Enzymatic production of both enantiomers of rhododendrol
Musa, Musa M.
, p. 6719 - 6721 (2014)
An asymmetric synthetic approach to produce (R)- and (S)-rhododendrol is described. W110A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase (W110A Te SADH), an (S)-specific mutant of TeSADH, is used in this approach. The enantioselective redu
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 (2018/02/21)
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.
Deracemization of Secondary Alcohols by using a Single Alcohol Dehydrogenase
Karume, Ibrahim,Takahashi, Masateru,Hamdan, Samir M.,Musa, Musa M.
, p. 1459 - 1463 (2016/05/02)
We developed a single-enzyme-mediated two-step approach for deracemization of secondary alcohols. A single mutant of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase enables the nonstereoselective oxidation of racemic alcohols to ketones, followed by a stereoselective reduction process. Varying the amounts of acetone and 2-propanol cosubstrates controls the stereoselectivities of the consecutive oxidation and reduction reactions, respectively. We used one enzyme to accomplish the deracemization of secondary alcohols with up to >99 % ee and >99.5 % recovery in one pot and without the need to isolate the prochiral ketone intermediate.