HELICOBATER PYLORI FBP ALDOLASE

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。 醛缩酶是从原核生物到哺乳动物的所有生物体中普遍存在的酶。它们有能力裂解碳-碳键。它们在糖酵解中的作用最为人所知，在糖酵解中，1，6-二磷酸果糖(FBP)醛缩酶将FBP分解为二羟丙酮-磷酸(DHAP)和甘油脱氢-3-磷酸。由于缺乏真正的反应中间体晶体结构，对残基的催化作用一直受到阻碍。 本项目的目的是研究幽门螺杆菌醛缩酶的催化机理，该酶是一种II类果糖-1，6-二磷酸缩醛酶。我们计划用天然和突变的醛缩酶晶体进行底物和药物浸泡实验，以深入了解与催化有关的活性部位的残基。 由于在哺乳动物中没有发现第二类抗生素，这些研究可能会导致一种新的抗生素类别的开发。

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. Aldolase are ubiquitous enzymes found in all organisms, from prokaryotes to mammals. They have the ability to cleave carbon-carbon bonds. Their role is best known in glycolysis where fructose-1,6-bisphosphate (FBP) aldolase cleaves FBP to dihydroxyacetone-phosphate (DHAP) and glyceraldehy-3-phosphate. The catalytic role assigment to residues has beeen hampered by the lack of genuine reaction intermediate crystallographic structures. The aim of this project is to study the catalytic mechanism of Helicobacter pylori aldolase, which is a class II fructose-1,6-bisphosphate aldolase. We are planning to use subtrate and drugs soaking experiments with native and mutant aldolase crystals to get insight about residues of the active site implicated in the catalysis. As Class II are not found in mammals, these study could lead to the developpement of a new class ot antibiotics.