XRAY ABSORPTION SPECTROSCOPY OF NUCLEOPHILIC ZN ENZYMES

亲核锌酶的 X 射线吸收光谱

• 批准号: 6586681
• 负责人: James E. Penner-Hahn
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586681
• 关键词: biomaterials; biomedical resource; proteins; spectrometry; structural biology; biomaterials; biomedical resource; proteins; spectrometry; structural biology

Recent work has revealed the existence of a novel class of Zn enzymes, in which the Zn appears to function to activate a coordinated thiolate toward nucleophilic attack. Experiments are proposed on three such enzymes that are involved in various aspects of methyl transfer: cobalamin-dependent and cobalamin-independent methionine synthase and cobamide: coenzyme M methyl transferase. EXAFS measurements on the native enzyme, on site directed mutants, and on enzyme samples with a variety of substrates and substrate analogs are proposed, with the goal of elucidating the three dimensional geometry of the Zn active sites.

最近的工作揭示了一类新型Zn的存在 酶，其中Zn似乎起作用以激活协调 硫酸盐朝着亲核攻击。 提出了实验 甲基各个方面涉及的三种酶 转移：与钴胺素依赖和钴胺素无关的蛋氨酸 合酶和共酰胺：辅酶M甲基转移酶。 exafs 对天然酶的测量，位于现场的突变体和 具有多种底物和底物类似物的酶样品是 提出的目的是阐明三维几何形状 Zn活跃位点。