TRITRICHOMONAS FOETUS PURINE SALVAGE ENZYMES

我们建议收集天然和衍生数据的晶体 两种酶形成嘌呤补救途径的一部分， 寄生原生动物胎儿三毛滴虫。 其中一种酶， 肌苷一磷酸脱氢酶（IMPDH）催化 NAD依赖的肌苷一磷酸（IMP）氧化为黄嘌呤 单磷酸（XMP）。 这种酶的结构将是第一个 IMPDH结构确定，并将作为确定 人IMPDH同种型的结构。 以各种 在各种情况下，IMPDH是设计的一个有吸引力的目标， 可能对治疗癌症非常有效的特定抑制剂， 治疗癌症，防止组织排斥，作为抗病毒药物 制剂，并在控制人类的寄生虫感染， 牲畜

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.