VISUALIZATION OF MANDELATE RACEMASE

苦杏仁酸消旋酶对扁桃酸对映体的相互转化 通过酶碱萃取α-氢作为一种 质子。研究该反应机理的一种方法是 用X射线结晶学方法显示酶的活性部位 数据。在格雷格·佩茨科教授和同事的合作下， 天然酶、酶-底物复合体和突变体的晶体 酶被生产出来，数据被提炼到2.5埃以上 决议。加州大学旧金山分校的计算机图形实验室在 可视化这些晶体数据集。从这项研究来看， 进一步的定点突变和未来的工作将被提出 测试活性中心残基在催化中的重要性。加州大学旧金山分校 CGL为这项研究提供了不可或缺的服务。

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.