STRUCTURAL STUDIES ON SOLUBLE AND MEMBRANE BOUND PROTEINS INVOLVED IN OXIDATIVE

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。子项目及 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。 甘油代谢途径是一种基本的生化途径，对必需细胞组分的生物合成和能量产生至关重要。在功能上，甘油的摄取依赖于细胞质甘油激酶（GlpK），其为甘油的非ATP依赖性摄取提供化学驱动力。甘油摄取的增强是通过由甘油促进剂（GlpF）形成的膜通道介导的。另一种膜蛋白，甘油-3-磷酸（G3 P）脱氢酶（GlpD），将甘油-3-磷酸氧化为二羟丙酮磷酸，其可用于通过糖酵解途径产生能量，并提供线粒体呼吸链的酶III的还原当量。此外，GlpD可以合成G3 P，用于掺入细胞膜的甘油磷脂的生物合成。GlpD的可溶性同系物是甘油磷酸氧化酶（GlpO），其催化将G3 P氧化为DHAP的相同反应，并且还通过G3 P穿梭体在呼吸中起作用，所述G3 P穿梭体将还原当量物转化为线粒体电子传递链。因此，所有这些酶在生物合成途径和能量生产中发挥着非常重要的作用。 建议进行全面的结构研究。

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. The glycerol metabolic pathway is a fundamental biochemical pathway, crucial to the biosynthesis of essential cellular components and for energy production. Functionally, the uptake of glycerol relies on the cytoplasmic glycerol kinase (GlpK), which provides the chemical driving force for the non-ATP dependent uptake of glycerol. Enhanced glycerol uptake is mediated through the membrane-channel formed by the glycerol facilitator (GlpF). Another membrane protein, the glycerol-3-phosphate (G3P) dehydrogenase (GlpD), oxidizes glycerol-3-phosphate to dihydroxyacetone phosphate, which can be utilized in energy production via the glycolytic pathway and provides reducing equivalents to Enzyme III of the mitochondrial respiratory chain. Additionally, the GlpD can synthesize G3P for the biosynthesis of the glycerophospholipids that are incorporated into cellular membranes. A soluble homolog of the GlpD is the glycerophosphate oxidase (GlpO), which catalyzes the same reaction of oxidizing G3P to DHAP and also plays a role in respiration through the G3P shuttle that recycles reducing equivalents to the mitochondrial electron transport chain. Consequently, all of these enzymes play highly important roles in biosynthetic pathways and in energy production. Comprehensive structural studies are proposed.