HELICOBATER PYLORI FBP ALDOLASE

幽门螺杆菌FBP醛缩酶

• 批准号: 8170591
• 负责人: JURGEN SYGUSCH
• 金额: $ 0.22万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-07-01 至 2011-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170591
• 关键词: Active Sites; Aldehyde-Lyases; Antibiotics; Carbon; Cleaved cell; Computer Retrieval of Information on Scientific Projects Database; Dihydroxyacetone Phosphate; Enzymes; Fructose; Funding; Glycolysis; Grant; Helicobacter pylori; Institution; Lead; Mammals; Organism; Pharmaceutical Preparations; Prokaryotic Cells; Reaction; Research; Research Personnel; Resources; Role; Source; United States National Institutes of Health; inorganic phosphate; insight; mutant; research study

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 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 1,6-二磷酸果糖 (FBP) 醛缩酶将 FBP 裂解为磷酸二羟丙酮 (DHAP) 和 3-磷酸甘油醛。 由于缺乏真正的反应中间体晶体结构，对残基的催化作用分配受到阻碍。该项目的目的是研究幽门螺杆菌醛缩酶的催化机制，它是一种 II 类果糖-1,6-二磷酸醛缩酶。 我们计划对天然和突变醛缩酶晶体进行底物和药物浸泡实验，以深入了解催化中涉及的活性位点残基。由于在哺乳动物中未发现 II 类醛缩酶，这些研究可能会导致新一类醛缩酶的开发ot 抗生素。