PROBES OF STRUCTURE AND MECHANISM IN COPPER AMINE

铜胺结构与机理的探讨

• 批准号: 3296148
• 负责人: JUDITH P KLINMAN
• 金额: $ 14.7万
• 依托单位: UNIVERSITY OF CALIFORNIA BERKELEY
• 依托单位国家: 美国
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-02-01 至 1992-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3296148
• 关键词: amine oxidase (flavin); chemical binding; chemical structure function; cofactor; copper; covalent bond; cow; dialysis; electron spin resonance spectroscopy; enzyme mechanism; enzyme structure; eukaryote; high performance liquid chromatography; mass spectrometry; nuclear magnetic resonance spectroscopy; oxidation reduction reaction; prokaryote; proteolysis; pyrroles; quinoline; stereochemistry; ultraviolet spectrometry

Copper containing amine oxidases represent a major experimental challenge with regard to the identity of a covalently bound cofactor, the role of active site copper and chemical mechanism. Recent evidence suggests that bovine plasma amine oxidase (BPAO) may contain pyrroloquinoline quinone, a new redox cofactor hitherto seen exclusively in prokaryotes. The goals of this proposal to obtain characterization a detailed of structure and mechanism in BPAO with the expectation that such studies will expand our knowledge of the general class of copper amine oxidases. Our work will focus on four areas: (I) Structure of the organic cofactor; (II) Substrate-cofactor interactions; (III) Active site copper; and (IV) Relationship among pro-and eukaryotic enzymes containing pyrroloquinoline quinone

含铜胺氧化酶代表了一个主要的实验 关于共价结合的身份的挑战 辅助因子、活性位点铜的作用和化学机制。 最近的证据表明牛血浆胺氧化酶 (BPAO) 可能含有吡咯喹啉醌，一种新的氧化还原剂 迄今为止，辅因子仅存在于原核生物中。 的目标 该建议旨在获得结构的详细表征 和 BPAO 的机制，期望此类研究 将扩展我们对铜胺一般类别的了解 氧化酶。 我们的工作将集中在四个领域： (I) 有机辅因子的结构； (II) 底物-辅因子相互作用； (III) 活性位点铜；和 （四）原核酶与真核酶之间的关系 吡咯并喹啉醌