VISUALIZATION OF MANDELATE RACEMASE

扁桃酸消旋酶的可视化

• 批准号: 6280218
• 负责人: CAROLYN KOO
• 金额: $ 0.01万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-07-01 至 1999-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6280218
• 关键词: biomedical resource

Mandelate racemase interconverts the enantiomers of mandelate through an enzymatic base extraction of the alpha-hydrogen as a proton. One method of stdying the mechanism of this reaction is visualizing the enzyme's active site through x-ray crystallographic data. In collaboration with Professor Greg Petsko and coworkers, crystals of the native enzyme, enzyme-substrate complex and mutant enzymes were produced and the data were refined beyond 2.5 Angstroms resolution. The UCSF Computer Graphics Laboratory is invaluable in visualizing these crystallographic data sets. From this study, further site directed mutagenesis and future work will be proposed to test the importance of active site residues in catalysis. The UCSF CGL provides an indispensable service necessary for this research.

扁桃酸消旋酶使扁桃酸的对映体相互转化 通过酶促碱提取α-氢作为 质子 研究该反应机理的一种方法是 通过X射线晶体学观察酶的活性部位 数据 在与格雷格·佩茨科教授和同事的合作中， 天然酶、酶-底物复合物和突变体的晶体 酶的产生和数据被精炼超过2.5埃 分辨率 UCSF计算机图形实验室是无价的， 可视化这些晶体学数据集。 从这项研究中， 进一步的定点诱变和未来的工作将被提出， 测试活性位点残基在催化作用中的重要性。 大学旧金山 CGL为这项研究提供了不可或缺的服务。