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

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.

最近的工作揭示了存在一类新的锌 酶，其中锌似乎起到激活协调的 硫醇化以进行亲核攻击。 实验建议在 这三种酶涉及甲基化的各个方面， 转移：钴胺素依赖性和钴胺素非依赖性蛋氨酸 合成酶和钴酰胺：辅酶M甲基转移酶。 EXAFS 对天然酶、定点突变体和 具有多种底物和底物类似物的酶样品被 提出，目的是阐明三维几何 锌的活性部位。