15542-96-8Relevant articles and documents
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Stoffelsma et al.
, p. 1000,1003 (1968)
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Asymmetric bioreduction of activated carbon-carbon double bonds using Shewanella yellow enzyme (SYE-4) as novel enoate reductase
Iqbal, Naseem,Rudroff, Florian,Brigé, Ann,Van Beeumen, Jozef,Mihovilovic, Marko D.
experimental part, p. 7619 - 7623 (2012/09/07)
Shewanella yellow enzyme (SYE-4), a novel recombinant enoate reductase, was screened against a variety of different substrates bearing an activated double bond, such as unsaturated cyclic ketones, diesters, and substituted imides. Dimethyl- and ethyl esters of 2-methylmaleic acid were selectively reduced to (R)-configured succinic acid derivatives and various N-substituted maleimides furnished the desired (R)-products in up to >99% enantiomeric excess. Naturally occurring (+)-carvone was selectively reduced to (-)-cis- dihydrocarvone and (-)-carvone was converted to the diastereomeric product, respectively. Overall SYE-4 proved to be a useful biocatalyst for the selective reduction of activated CC double bonds and complements the pool of synthetic valuable enoate reductases.
Free and supported phosphorus ylides as strong neutral bronsted bases
Goumri-Magnet,Guerret,Gornitzka,Cazaux,Bigg,Palacios,Bertrand
, p. 3741 - 3744 (2007/10/03)
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