Thermally driven asymmetric reaction using a chiral space of a thermostable esterase

2014 Fiscal Year Final Research Report

• Project/Area Number: 24655160
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Chemistry related to living body
• Research Institution: Keio University
• Principal Investigator: MIYAMOTO KENJI 慶應義塾大学, 理工学部, 准教授 (60360111)
• Co-Investigator(Kenkyū-buntansha): YOSHIDA Shosuke 京都大学, 工学(系)研究科, 研究員 (80610766)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 熱駆動型反応 / 好熱性エステラーゼ / 脱炭酸反応 / 変異酵素 / ドミノ型反応

Outline of Final Research Achievements

In this study, the active site of the hyperthermophilic enzyme is used as "a heat resistant chiral space". We designed a compound which was not originally a substrate of the enzyme, but was binded to the active site. We aimed to achieve a variety of thermally driven asymmetric reactions using a heat resistant chiral space.
Arylmethylmalonic acid monoester was selected as a substrate, and the mutant esterase to which the hydrolyzing activity disappeared was used. Under high temperature conditions, the aimed ester was obtained, and the optical purity was also high. In addition, it was confirmed that the asymmetric decarboxylation occurred when this mutant was act on prochiral arylmechylmalonic acid. We have been succeeded in developing thermally driven asymmetric reactions.

Free Research Field

酵素工学