TRITRICHOMONAS FOETUS PURINE SALVAGE ENZYMES

胎儿毛滴虫嘌呤挽救酶

• 批准号: 6586519
• 负责人: FRANK G WHITBY
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586519
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; infection; parasitism; proteins; radiography; structural biology

We propose to collect native and derivative data from crystals of two enzymes that form part of the purine salvage pathway of the parasitic protozoan Tritrichomomas foetus. One of these enzymes, Inosine Monophosphate Dehydrogenase (IMPDH) catalyzes the NAD-dependent oxidation of inosine monophosphate (IMP) to xanthine monophosphate (XMP). The structure of this enzyme will be the first IMPDH structure determined and it will serve as a model in determining the structures of both of the human IMPDH isoforms. Under a variety of circumstances, IMPDH represents an attractive target for the design of specific inhibitors which are likely to be very effective in the treatment of cancer, in preventing tissue rejection, as an antiviral agent, and in the control of parasitic infections of humans and livestock.

我们建议从晶体中收集原始数据和衍生数据 两种酶，构成了嘌呤挽救途径的一部分 寄生原生动物三孔虫胎儿。其中一种酶， 肌苷单磷酸脱氢酶(IMPDH)催化 依赖NAD的肌苷一磷酸(IMP)氧化生成黄嘌呤 单磷酸盐(XMP)。这种酶的结构将是第一个 确定了IMPDH的结构，并将作为确定 这两种人类IMPDH亚型的结构。在一个变种之下 在各种情况下，IMPDH是设计的一个有吸引力的目标 一系列特定的抑制剂，这些抑制剂可能在 癌症治疗，在防止组织排斥中，作为一种抗病毒药物 在控制人类寄生虫感染和 家畜。