Structural and mechanistic studies of Ser/Lys dyad proteases

Ser/Lys 二元蛋白酶的结构和机制研究

• 批准号: 250131-2007
• 负责人: Paetzel, Mark
• 金额: $ 2.7万
• 依托单位: Simon Fraser University
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2009
• 资助国家: 加拿大
• 起止时间: 2009-01-01 至 2010-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=426248
• 关键词: Structural; mechanistic; studies; Ser; Lys

The objectives of the proposed research program is to investigate the structural and mechanistic details of two unrelated families of proteolytic enzymes (one bacterial and one viral) that have evolved the same unusual catalytic mechanism. These proteases; bacterial signal peptidase and viral VP4 protease both utilize an essential lysine and serine in their hydrolytic reactions. The deprotonated lysine is thought to serve as the general-base by abstracting the proton from the serine hydroxyl thereby activating it for nucleophilic attack on the scissile carbonyl of the substrate.

拟议的研究计划的目标是调查两个不相关的蛋白水解酶家族（一个细菌和一个病毒）的结构和机制细节，它们已经进化出相同的不寻常的催化机制。这些蛋白酶;细菌的信号肽酶和病毒的VP4蛋白酶在水解反应中都使用必需的赖氨酸和丝氨酸。去质子赖氨酸被认为是通过从丝氨酸羟基上提取质子，从而激活它对底物的可剪切羰基进行亲核攻击的通用碱。