STRUCTURE-ACTIVITY RELATIONSHIPS IN FORMALDEHYDE DEHYDROGENASE

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。 这是与霍华德·罗宾逊合作的一个正在进行的项目。我们早期的工作表明，活性中心锌在催化循环中发生了独特的移动。我们现在正在探索甲醛脱氢酶(FDH)活性部位的构效关系。利用高通量筛选，我们已经确定了抑制FDH的新化合物。这些结构研究的目的是确定已识别的化合物在FDH位点上的相互作用，并利用这些信息设计更好的FDH抑制剂，以用于研究FDH在细胞代谢中的作用

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. This is a ongoing project in collaboration with Howard Robinson. Our earlier work has shown a unique movement of active site zinc during the catalytic cycle. We are now exploring the structure-activity relationships in the formaldehyde dehydrogenase (FDH) active site. Using high throughput screening, we have identified novel compounds that inhibit FDH. The goal of the structural studies is to identify the interactions of the identified compounds in FDH site and use the information in designing better inhibitors of FDH that can be used for exporing the role of FDH in cellular metabolism