MECHANISMS FOR ENZYME CATALYSIS OF HETEROLYTIC REACTION

酶催化杂解反应的机理

• 批准号: 2184726
• 负责人: John P Richard
• 金额: $ 17.79万
• 依托单位: STATE UNIVERSITY OF NEW YORK AT BUFFALO
• 依托单位国家: 美国
• 财政年份: 1992
• 资助国家: 美国
• 起止时间: 1992-05-01 至 1997-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2184726
• 关键词: MECHANISMS; ENZYME; CATALYSIS; HETEROLYTIC; REACTION

项目成果

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Brønsted acid-base catalysis of beta-D-galactopyranosyl group transfer.

β-半乳糖苷酶（大肠杆菌，lac Z）的结构-反应性关系。

• 发表时间: 1996-09-24
• 影响因子: 2.9
• 作者: Richard, J P;Huber, R E;Lin, S;Heo, C;Amyes, T L
• 通讯作者: Amyes, T L

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 2. Reactions of the galactosyl-enzyme intermediate with alcohols and azide ion.

β-半乳糖苷酶（大肠杆菌，lac Z）的结构-反应性关系。

• 发表时间: 1995-09-19
• 影响因子: 2.9
• 作者: Richard, J P;Westerfeld, J G;Lin, S;Beard, J
• 通讯作者: Beard, J

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 1. Brønsted parameters for cleavage of alkyl beta-D-galactopyranosides.

β-半乳糖苷酶（大肠杆菌，lac Z）的结构-反应性关系。

• 发表时间: 1995-09-19
• 影响因子: 2.9
• 作者: Richard, J P;Westerfeld, J G;Lin, S
• 通讯作者: Lin, S

Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q beta-galactosidases.

β-半乳糖苷酶（大肠杆菌，lac Z）的结构-反应性关系。

• 发表时间: 1996-09-24
• 影响因子: 2.9
• 作者: Richard, J P;Huber, R E;Heo, C;Amyes, T L;Lin, S
• 通讯作者: Lin, S