BIOTIN CARBOXY TERMINAL DOMAIN FOLDING CALORIMETRY E COLI ACETYL COA CARBOXYLASE

生物素羧基末端折叠量热法 大肠杆菌乙酰辅酶A羧化酶

• 批准号: 6122028
• 负责人: DOROTHY BECKETT
• 金额: --
• 依托单位: JOHNS HOPKINS UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-08-05 至 1998-08-04
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6122028
• 关键词: biological products; biomaterials; biomedical resource; education; enzymes; human tissue; model design /development; nucleic acids; technology /technique development

In biotin-dependent carboxylases, the biotin moiety is covalently bonded to the Biotin Carboxyl Carrier (BCC) functionality of the enzyme via an amide linkage to the epsilon amino group of a single lysine residue. In E. coli acetyl-CoA carboxylase, the BCC functionality resides in a separate 17 kD subunit. An 87 residue C-terminal domain fragment (BCCP87) of this subunit has been shown to behave identically to the intact protein in the enzyme-catalyzed biotination reaction. High resolution structures of both the apo- and holo-forms of the domain are available. The folding properties of the apo- and holo-forms of BCCP87 will be studied by differential scanning calorimetry to determine the contribution, if any, of a post-translational modification to the thermodynamic stability of the protein. Results of the thermodynamic studies will be combined with the available structural data to determine the structural basis of any measured differences in the energetics of folding.

在生物素依赖性羧化酶中，生物素部分是共价键 与生物素羧基载体 (BCC) 功能键合 酶通过酰胺键连接到单个的ε氨基上 赖氨酸残基。 在大肠杆菌乙酰辅酶A羧化酶中，BCC 功能位于一个单独的 17 kD 亚基中。 87残基 该亚基的 C 端结构域片段 (BCCP87) 已被证明 与酶催化的完整蛋白质的行为相同 生物素化反应。 apo- 和 apo- 的高分辨率结构 该域的全息形式是可用的。 折叠特性 BCCP87 的脱辅基和全息形式将通过差示扫描进行研究 量热法以确定的贡献（如果有的话） 翻译后修饰对热力学稳定性的影响 蛋白质。 热力学研究的结果将与 可用的结构数据来确定任何结构的基础 测量了折叠能量的差异。