86527-08-4Relevant articles and documents
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.
Selective acylation of aliphatic alcohols in the presence of phenolic hydroxyl groups
Sabitha, Gowravaram,Subba Reddy, Basi V.,Kiran Kumar Reddy, Garudammagari S.,Yadav, Jhillu S.
, p. 63 - 64 (2007/10/03)
A new and efficient method for the selective acylation of aliphatic hydroxyl groups in the presence of phenolic groups using a mixture of trimethyl orthoacetate and trimethylsilyl chloride at room temperature is reported. The reactions are selective, high yielding and complete within 3-6 h.
