73777-49-8Relevant academic research and scientific papers
Enzymed in organic synthesis: oxidoreductions
Fang, Jim-Min,Lin, Chun-Hung,Bradshaw, Curt W.,Wong, Chi-Huey
, p. 967 - 978 (1995)
This article reviews the use of several oxidoreduction enzymes, including monooxygenases, chloroperoxidase, arene dioxygenase, lipoxygenase, galactose oxidase and alcohol dehydrogenases, in the preparation of optically pure or enriched epoxides, halohydrins, sulfoxides, hydroxyperoxides, alcohols, cyclohexadienediols, lactones and α-hydroxy aldehydes.The mechanisms of some of these enzyme-catalysed transformations, and their scopes and limitations in synthetic chemistry are also discussed.Representative syntheses of a key intermmediate of 5-lipoxygenase inhibitor, a seven-carbon C-glycoside and an active component of the antibiotic bialaphos have been experimentally illustrated using Lactobacillus alcohol dehydrogenase, chloroperoxidase and glutamate dehydrogenase, respectively.
Enantioselective Synthesis of Both Enantiomers of Phosphinothricin via Asymmetric Hydrogenation of α-Acylamido Acrylates
Zeiss, Hans-Joachim
, p. 1783 - 1788 (2007/10/02)
Both enantiomers of phoshinothricin (1), a naturally occuring amino acid that contains the unique methylphosphinate moiety, were prepared by asymmetric hydrogenation of α-acylamido acrylate precursors 7.L-1 and peptides containing L-1 are inhibitors of the enzyme glutamine synthetase (GS).Inhibition of GS is responsible for the antibiotical and herbicidal properties of these compounds.Synthesis of substrates 7 and parameters influencing the enantioselectivity are discussed.Substrate concentration and solvent polarity appear to have the most marked effects on enantiomeric excesses for a given catalyst system.Enantiomeric excesses reach 91percent for hydrogenations with (R,R)-NORPHOS- and (S,S)-CHIRAPHOS-derived catalysts.
