2555-14-8Relevant articles and documents
Preparation of γ-siloxyallyltributylstannanes and their use in the synthesis of (±)-1-deoxy-6,8a-di-epi-castanospermine
Chevallier, Floris,Le Grognec, Erwan,Beaudet, Isabelle,Fliegel, Florian,Evain, Michel,Quintard, Jean-Paul
, p. 3128 - 3133 (2004)
γ-Siloxyallyltributylstannanes were selectively obtained as E or Z isomers from β-tributylstannylacrolein upon reaction with lithium or magnesium alkylcyanocuprates. The ability of the reagents to give a high syn selectivity when added to iminium salts ha
Simple and efficient synthesis of N-alkyl and N-aryl succinimides in hot water
Bozdo?an, Burcu,Er?at?r, Mehmet,Demirkol, Onur,Akba?lar, Dilek,Giray, E. Sultan
, p. 217 - 223 (2017/01/22)
A new, simple synthesis of succinimides is described. The reactions were carried out under the ultimate green conditions excluding both catalyst and organic solvent by applying simple stirring at 100 °C. A wide variety of N-susbstituted succinimides have been prepared in high yields by using succinic acid and primary amines in hot water. Yield of N-alkyl substituted succinimides were found to be higher than those of N-aryl substituted succinimides.
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.
