84194-70-7Relevant 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 (2018/02/21)
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.
Kinetic resolution of diarylmethanols using a mutated variant of lipase CALB
Engstr?m, Karin,Vallin, Michaela,Hult, Karl,B?ckvall, Jan-E.
experimental part, p. 7613 - 7618 (2012/09/07)
An enzymatic kinetic resolution of diarylmethanols via acylation has been developed. This was achieved by the use of a mutated variant of CALB that accepts larger substrates compared to the wild type. By the use of diarylmethanols with two differently sized aryl groups, enantioselective transformations were achieved. A larger size-difference led to a higher enantioselectivity. In addition, substrates with electronically different aryl groups, such as phenyl and pyridyl, also gave an enantioselective reaction. The highest E value was observed with a substrate where steric and electronic effects were combined.
Highly enantioselective dynamic kinetic resolution of 1,2-diarylethanols by a lipase-ruthenium couple
Kim, Mahn-Joo,Choi, Yoon Kyung,Kim, Sol,Kim, Daeho,Han, Kiwon,Ko, Soo-Byung,Park, Jaiwook
supporting information; experimental part, p. 1295 - 1298 (2009/04/11)
A practical procedure has been developed for the dynamic kinetic resolution of 1,2-diarylethanols. This procedure employs a highly enantioselective lipase from Pseudomonas stutzeri (trade name, lipase TL) as the resolution catalyst and a ruthenium complex as the racemization catalyst. Sixteen 1,2-diarylethanols have been efficiently resolved to provide their acetyl derivatives with good yields (95-97%) and high enantiomeric excesses (96-99%).
Highly enantioselective lipase-catalyzed reactions at high temperatures up to 120°C in organic solvent
Ema, Tadashi,Kageyama, Masafumi,Korenaga, Toshinobu,Sakai, Takashi
, p. 3943 - 3947 (2007/10/03)
Lipase-catalyzed kinetic resolutions of 1,1-diphenyl-2-propanol were performed at high temperatures up to 120°C. Burkholderia cepacia lipase immobilized on porous ceramic particles, lipase PS-C II (Amano Enzyme Inc.), gave an enantiopure product at 40-120
