SYNTHESIS OF GALACTOSE ANALOGS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 酶如何利用与底物分子的非反应部分的结合作用来催化底物分子反应部分的化学转化是我研究的主要重点之一。这些相互作用为酶向活性构象的结构转变提供能量。通常提出的用酶的活性构象来解释酶催化的陈述包括那些假定酶稳定过渡态或破坏酶-底物复合体中基态稳定的陈述，或两者兼而有之。这些都是非常笼统的陈述，没有明确地解释特定酶的作用。对于少数几种酶，需要从结构和动力学两个方面对催化进行具体的描述。丝氨酸蛋白酶、异构酶和半乳糖代谢酶是我在这一领域的研究课题。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The question of how enzymes utilize binding interactions directed to nonreacting parts of substrate molecules to catalyze the chemical transformations of the reacting parts of substrates is one principalfocus of my research. These interactions provide the energy for thestructural transition of enzymes into active conformations. Statementsthat are commonly advanced to explain enzymatic catalysis by theactive conformation of an enzyme include those in which the enzyme ispostulated to stabilize transition states or to destabilize groundstates in enzyme-substrate complexes, or both. These are very generalstatements that do not explicitly account for the actions ofparticular enzymes. A specific description of catalysis, in bothstructural and dynamic terms, is needed for a few enzymes. Serineproteases, isomerases, and the enzymes of galactose metabolism aresubjects of my research in this field.