HELICOBATER PYLORI FBP ALDOLASE

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 醛缩酶是从原核生物到哺乳动物的所有生物中普遍存在的酶。 它们具有裂解碳-碳键的能力。 它们的作用在糖酵解中最为人所知，其中果糖-1，6-二磷酸（FBP）醛缩酶将FBP切割成二羟丙酮-磷酸（DHAP）和甘油醛-3-磷酸。 由于缺乏真正的反应中间体晶体结构，残基的催化作用受到阻碍。 本课题的目的是研究幽门螺杆菌醛缩酶的催化机制。 我们正计划使用底物和药物浸泡实验与天然和突变的醛缩酶晶体，以了解有关的催化活性位点的残基。 由于在哺乳动物中没有发现II类抗生素，这些研究可能会导致一类新抗生素的开发。

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.