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STRUCTURAL STUDIES ON ENZYMES INVOLVED IN SIALIC ACID TRANSFERASE, SULFUR ASSIMI

唾液酸转移酶硫阿西米的结构研究

基本信息

批准号：
8170091
负责人：
ANDREW J FISHER
金额：
$ 0.27万
依托单位：
STANFORD UNIVERSITY
依托单位国家：
美国
项目类别：
财政年份：
2010
资助国家：
美国
起止时间：
2010-05-01 至 2011-02-28
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/8170091
关键词：
Architecture Assimilations Bacterial Infections Bilin Biliverdine Biological Process Carbohydrates Cell physiology Computer Retrieval of Information on Scientific Projects Database Data Electron Spin Resonance Spectroscopy Electrons Enzymes Ferredoxin Funding Glycoconjugates Goals Grant Hour Inorganic Sulfates Institution Life Light Malignant Neoplasms Molecular Molecular Structure Oligosaccharides Organism Oxidoreductase Pathway interactions Photoreceptors Phycobiliproteins Phytochrome Plants Play Polysaccharides Process Regulation Research Research Personnel Resources Role Sialic Acids Sialyltransferases Source Sulfur System Therapeutic Time Transferase United States National Institutes of Health Unspecified or Sulfate Ion Sulfates chromophore enzyme mechanism enzyme structure inhibitor/antagonist mutant photosynthetic bacteria phycobilin response

项目摘要

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. 1) One system is involved in sialyltransferases, or enzymes that add sialic acid onto acceptor carbohydrates. Sialyltransferases are key enzymes that catalyze the synthesis of sialic acid-containing oligosaccharides, polysaccharides, and glycoconjugates that play pivotal roles in many physiologically and pathologically critical processes in both prokaryotic and eukaryotic organisms. Despite their important biological functions, little is known about the molecular architecture and catalytic mechanism of these enzymes. Our long-term goals of this project are to elucidate the molecular structure and catalytic mechanism of STs and to develop ST inhibitors as potent therapeutics that can be used to treat cancers and pathogenic bacterial infections. 2) Another cellular pathway the lab is investigating is in sulfur assimilation and the sulfate activation pathway. The lab has determined a number of enzyme structures in this pathway from diverse organisms using data collected at SSRL. This proposal will focus on better understanding the structural requirements for regulation of the first two enzymes in the pathway as well as subsequent enzymes involved in the synthesis of sulfur containing biomolecules. 3) Finally, a new project the lab has initiated recently is investigating the structural features on plant and photosynthetic bacteria enzymes involved in chromophore synthesis. In particular, synthesis of phytochromes that regulate many cellular processes in response to light. PcyA, a representative ferredoxin-dependent bilin reductase is responsible for the formation of phycocyanobilin (PCB), the precursor of the chromophores of the photoreceptor phytochrome and a number of phycobiliproteins. This PcyA enzyme reduces biliverdin by four electrons, and proceeds through two radical intermediates, which have been confirmed by EPR spectroscopy. We have generated mutants that extend the life time of these radicals to many hours. Radical enzyme has been formed in the crystal and confirmed by EPR.

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