Most lipases cannot hydrolyze amides although their active sites are similar to those of serine-proteases that catalyze hydrolysis of amides. Recently, we proposed molecular basis for the enhanced lipasecatalyzed N-acylation of 1-phenylethanamine with methoxyacetate. We suggested that the hydrogen atom connected to the nitrogen atom of the amine substrate may interrupt formation of the key hydrogen bond between the catalytic histidine and the nitrogen atom of the substrate. The disruption could be avoided by using methoxyacetate as an acyl donor. The methoxy group of the acyl donor can hydrogen bond with the nitrogen atom and thus the proton does not interrupt the key hydrogen bond. We introduced a residue to serve a similar role of the methoxy group into a lipase. We prepared a mutant of Candida antarctica lipase B (CAL-B) to construct a hydrogen bond between the residue introduced and the nitrogen atom. The mutant enzyme clearly showed improved hydrolysis activity toward p-nitroacetanilide.
저자
Seongsoon Park [ Department of Chemistry, Sungshin Women’s University ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
1. 생물공학 분야의 발전을 위한 연구 협력
2. 생물공학의 실용화를 촉진시키기 위한 산학 협동
3. 학술연구 발표회, 강연회, 연수회 등 학술활동의 개최
4. 국,영문 학술지,소식지,학술회의 Proceedings 및 학술도서의 발간
5. 생물공학 발전을 위한 정책 건의
6. 기타 국제 교류 등 본 학회의 목적 달성을 위한 제반 활동