XRAY ABSORPTION STUDIES OF RESTRICTION ENZYME FROM BACILLUS SPECIES (BSLI)

芽孢杆菌属限制性酶 (BSLI) 的 X 射线吸收研究

• 批准号: 6205766
• 负责人: EVA S VANAMEE
• 金额: --
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-09-01 至 2000-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6205766
• 关键词: bacteria; biological products; biomedical resource; enzymes; proteins; spectrometry

XAFS data of native TBADH has been collected on zinc and cobalt K-edges. Analysis of EXAFS and edge data of native enzyme and its metal derivatives will provide the ground base for the assignment of coordination environment and accurate metal-ligand distances at the active site. Inhibition Studies: XAFS measurements on inhibited TBADH were conducted using TBADH-DMSO (dimethyl sulfoxide) complex. DMSO is known to inhibit ALDH in a transition state manner. X-ray crystallography studies of ALDH-DMSO complexes show that the DMSO ligand is directly bound to the catalytic zinc ion. XAFS and edge data will be collected on native TBADH and Cd/Co substituted TBADH complexed with DMSO. Assigning the coordination environment and metal-ligand distances of the active site in TBADH-DMSO complex will provide the structure of the transition state analogue of TBADH and a relevant structural intermediate in the catalytic pathway. SCIENTICIC SUBPROJECT 60

已收集锌和钴的天然 TBADH 的 XAFS 数据 K 边。 天然酶及其相关的 EXAFS 和边缘数据分析 金属衍生品将为分配提供基础 配位环境和准确的金属配体距离 活跃站点。 抑制研究：XAFS 测量抑制 TBADH 使用 TBADH-DMSO（二甲基亚砜）复合物进行。 已知 DMSO 以过渡态方式抑制 ALDH。 X射线 ALDH-DMSO 复合物的晶体学研究表明 DMSO 配体直接与催化锌离子结合。 XAFS 和边缘 将收集天然 TBADH 和 Cd/Co 取代 TBADH 的数据 与DMSO复合。 分配协调环境和 TBADH-DMSO 复合物中活性位点的金属-配体距离 提供 TBADH 的过渡态类似物的结构和 催化途径中的相关结构中间体。 科学 子项目 60