Hydrolase-catalyzed Michael addition of 1,3-dicarbonyl compounds to α,β-unsaturated compounds in organic solvent

作者：Xu, Jian-Ming; Zhang, Fu; Wu, Qi; Zhang, Qing-Yi; Lin, Xian-Fu^*

来源：Journal of Molecular Catalysis B: Enzymatic , 2007, 49(1-4): 50-54.

DOI：10.1016/j.molcatb.2007.08.004

• enzymes
• Michael additions
• 1,3-dicarbonyl compounds
• D-aminoacylase
• catalysis

A novel strategy to perform Michael additions between 1,3-dicarbonyl compounds and alpha,beta-unsaturated compounds was developed by the catalysis of hydrolase. We found that 11 hydrolase could catalyze the enzymatic Michael addition reaction to form the carbon-carbon bond. In 2-methyl-2-butanol D-aminoacylase showed high Michael addition activity. The influence of substrate and Michael acceptor structure on Michael addition was evaluated systematically. Some control experiments demonstrated that the active site Of D-aminoacylase was responsible for the enzymatic Michael addition reaction. This novel Michael addition activity of hydrolase is of practical significance in expanding the application of enzymes and in the evolution of new biocatalysts.

• 出版日期2007-11-16
• 单位浙江大学