HIGH RESOLUTION DATA ON HUMAN CATALASE

人类过氧化氢酶的高分辨率数据

• 批准号: 6437587
• 负责人: CHRISTOPHER D PUTNAM
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437587
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; human tissue; proteins; radiography; structural biology

Catalase is one of the critical antioxident enzymes that constitutes a major defense system against superoxide and hydrogen peroxide by converting H2O2 to H2O and O2. The bovine catalase structure complexed with NADPH was solved to 2.5 E a decade ago. Since that time, the role of the bound NADPH is poorly understood and the structure of the human enzyme, despite its critical role in regulation of the cellular redox potential in apoptosis, response to pathogens, DNA damage and aging, has been ignored. Given the central role of catalase in humans, we wish to examine the structural basis of mRNA binding by human catalase through crystallography.

过氧化氢酶是一种重要的抗氧化酶， 构成了一个主要的防御系统， 过氧化物通过将H2O2转化为H2O和O2。 牛过氧化氢酶 10年前，与NADPH复合的结构被解析为2.5E。 从那时起，对结合的NADPH的作用了解甚少， 人体酶的结构，尽管它在 细胞凋亡中细胞氧化还原电位的调节， 病原体，DNA损伤和衰老，一直被忽视。 鉴于中央 过氧化氢酶在人类中的作用，我们希望研究的结构基础， 通过晶体学研究人过氧化氢酶与mRNA的结合。