Hydrolase-catalyzed asymmetric carbon-carbon bond formation in organic synthesis

被引:70
|
作者
Guan, Zhi [1 ]
Li, Ling-Yu [1 ]
He, Yan-Hong [1 ]
机构
[1] Southwest Univ, Key Lab Appl Chem Chongqing Municipal, Sch Chem & Chem Engn, Chongqing 400715, PR, Peoples R China
来源
RSC ADVANCES | 2015年 / 5卷 / 22期
基金
中国国家自然科学基金;
关键词
BAYLIS-HILLMAN REACTION; MICHAEL-TYPE ADDITIONS; C-C; ALDOL REACTION; ENZYME PROMISCUITY; BIOCATALYTIC PROMISCUITY; CHIRAL AUXILIARIES; P1; NUCLEASE; LIPASE; ACETALDEHYDE;
D O I
10.1039/c4ra11462k
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Enzyme catalytic promiscuity, in which the active site of an enzyme has the ability to catalyze more than one chemical transformation, has received widespread attention as more catalytic promiscuities of existing enzymes have been discovered. In this field, hydrolases have been mainly studied due to their commercial availability, high stability, broad substrate scope and high catalytic efficiency in media containing organic solvents. In this study, we review the hydrolase-catalyzed asymmetric carbon-carbon bond-forming reactions for the preparation of enantiomerically enriched compounds in organic synthesis. To date, these hydrolase-catalyzed asymmetric reactions include the direct asymmetric aldol, Michael, Mannich and Morita-Baylis-Hillman reactions. The hydrolase-catalyzed non-enantioselective examples were not included.
引用
收藏
页码:16801 / 16814
页数:14
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