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.

在依赖生物素的羧酸酶中，生物素部分是共价的 粘合到生物素羧基载体（BCC）的功能 通过酰胺连接到单个单一的Epsilon氨基的酶 赖氨酸残留物。 在大肠杆菌乙酰辅酶A羧化酶中，BCC 功能位于单独的17 kD亚基中。 87个残留物 该亚基的C末端结构域片段（BCCP87）已显示为 与酶催化的完整蛋白质的行为相同 生物因子反应。 apo-和apo-的高分辨率结构 可以使用该域的全面形式。 折叠特性 BCCP87的apo-和holo形式将通过差分扫描来研究 量热法以确定A的贡献（如果有） 翻译后修改对热力学稳定性的修饰 蛋白质。 热力学研究的结果将与 可用的结构数据，以确定任何的结构基础 测量的折叠能量差异。