Mechanism of Nickel Incorporation into Urease

镍掺入脲酶的机制

• 批准号: 8916011
• 负责人: Robert Hausinger
• 金额: $ 11.4万
• 依托单位: Michigan State University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1990
• 资助国家: 美国
• 起止时间: 1990-01-15 至 1992-06-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8916011&HistoricalAwards=false
• 关键词: Mechanism; Nickel; Incorporation; into; Urease

The biosynthesis of enzyme metallocenters is very poorly understand. This proposal is aimed at understanding the general mechanism for incorporation of the metal into the protein matrix using urease as a model. Urease, synthesized as an apo-enzyme, requires an accessory factor for the formation of its novel, bi- nickel active site. The nature of the accessory factor is unknown; however, two newly identified genes appear to play a role in this process. Mutants of these genes will be generated and the effects of the mutations on the apo-protein will be determined. The accessory protein (s) will be isolated and characterized for cellular location, Ni binding and interaction with apo-urease. The research will increase our understanding of how metalloproteins are formed, and our understanding of the biochemistry of nickel in living systems.

酶代谢中心的生物合成很差 明白 这一建议旨在了解一般 金属结合到蛋白质基质中的机制 以尿素酶为模型。 尿素酶，作为一种脱辅基酶合成， 需要一个辅助因素，以形成其新颖的，双- 镍活性中心 附随因素的性质是 未知;然而，两个新发现的基因似乎发挥了作用。 在这个过程中的作用。 这些基因的突变体将产生 突变对脱辅基蛋白的影响 测定 将分离辅助蛋白， 表征细胞定位、Ni结合和相互作用 脱尿素酶 这项研究将增加我们对 金属蛋白质的形成，以及我们对金属蛋白质的理解 镍在生命系统中的生物化学。