Structure and Mechanism Studies of Dienelactone Hyd ,

双烯内酯水解酶（DLH）的结构已得到解决， 目前正在以高分辨率进行改进。 奥利斯医生计划 使用组合来确定DLH的酶促机制 溶液研究和底物结合研究， 晶体蛋白质 他还将从结构和化学上 表征DLH的催化三元组使用两个衍射 方法和NMR。 此外，两种蛋白质的晶体， 与DNA、单链结合蛋白和DNA相互作用 连接酶，已经获得，现在将进行研究。 对生物如何进化以利用新营养源的研究 既迷人又对人类的生存至关重要 生命系统。 酶DLH是一个理想的模型系统， 在分子水平上理解这种进化。 DLH是一个 在细菌中起作用的酮己二酸途径的组分 和真菌，它拥有许多不同的分支， 在每一种中，儿茶酚或儿茶酚衍生物 分解代谢

The structure of dienelactone hydrolase (DLH) has been solved and is currently being refined at high resolution. Dr. Ollis plans to determine the enzymatic mechanism of DLH using a combination of solution studies and substrate binding studies with the crystalline protein. He will also structurally and chemically characterize the catalytic triad of DLH using both diffraction methods and NMR. In addition, crystals of two proteins that interact with DNA, a single stranded binding protein and a DNA ligase, have been obtained and will now be studied. The study of how organisms evolve to utilize new nutrient sources is both fascinating and of critical importance for the survival of living systems. The enzyme DLH is an ideal model system to understand this evolution at a molecular level. DLH is a component of the ketoadipate pathway which operates in bacteria and fungi and which possesses of a number of different branches, in each of which catechol or a catechol derivative is catabolized.