78510-02-8Relevant articles and documents
Equilibration of 1-Octanol with Alcohol Dehydrogenase. Evidence for Horse Liver Alcohol Dehydrogenase Responsibility for Exchange of the 1-pro-S Hydrogen Atom
Shapiro, Stuart,Arunachalam, Thangavel,Caspi, Eliahu
, p. 1642 - 1646 (1983)
Equilibration of hydrogen atoms of 1-octanol with water, mediated by the system horse liver alcohol dehydrogenase-NAD/NADH-diaphorase, involves a rapid exchange of 1-pro-R hydrogen atoms and a slow exchange of 1-pro-S hydrogen atoms.Yeast alcohol dehydrogenase has an apparent absolute stereospecificity for the 1-pro-R hydrogen atom of 1-octanol; replacement of horse liver dehydrogenase by yeast alcohol dehydrogenase in the above system results in exchange of only the 1-pro-R hydrogen atom of 1-octanol.In the absence of horse liver or yeast alcohol dehydrogenase, no exchange of C-1 hydrogen atoms of 1-octanol occurs.Thus, horse liver alcohol dehydrogenase is directly responsible for promoting exchange of the 1-pro-S hydrogen atom of 1-octanol with water hydrogen atoms.
Method used for reduction of tertiary amide into alcohols and/or amines
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Paragraph 0167-0170, (2019/08/07)
The invention discloses a method used for reduction of tertiary amide into alcohols and/or amines. The method comprises following steps: tertiary amide, an alkali metal reagent, and a proton donor agent are added into an organic solvent for a following reaction selectively: when the proton donor agent is a raw material alcohol and/or inorganic salt aqueous solution, the reaction product is an alcohol compound and/or tertiary amine compound. The method is capable of realizing selective reduction of tertiary amide into alcohols and tertiary amine compounds, the yield is high, the suitable rangeis wide, operation is safe and simple, the adopted raw materials are cheap and easily available; no precious metal catalyst, toxic silanes, and flammable and combustible metal hydrides are adopted; notoxic by product is generated; reaction is more friendly to the environment; problems in the prior art that amide compound reducing method operation is complex, conditions are strict, and control ofproducts is difficult are solved.
Topological study of mechanistic diversity in conjugated fatty acid biosynthesis
Bhar, Palash,Reed, Darwin W.,Covello, Patrick S.,Buist, Peter H.
supporting information; experimental part, p. 6686 - 6690 (2012/08/27)
Variations on an oxidative theme: The precision with which FAD2-type desaturases carry out C-H activation reactions on flexible lipidic substrates is astonishing. The conformational space available within the active site of these enzymes has been explored using deuterium-labeled substrates, and evidence for a novel quasi-eclipsed conformer has been uncovered. The scheme shows some prototypical substrate conformations. Copyright