GENOMIC ENZYMOLOGY: THE ENOLASE SUPERFAMILY AND OMPDC SUPRAFAMILY

基因组酶学：烯醇化酶超家族和 OMPDC 超家族

• 批准号: 8363583
• 负责人: JOHN A GERLT
• 金额: $ 1.68万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363583
• 关键词: Anions; Bioinformatics; Chimera organism; Enzymatic Biochemistry; Enzymes; Evolution; Funding; Genomics; Grant; Imagery; Informatics; National Center for Research Resources; Oxygenases; Principal Investigator; Reaction; Research; Research Infrastructure; Resources; Source; Structure; United States National Institutes of Health; base; biocomputing; carboxylate; cost; enolase; interest; member; orotidylic acid; ribulose

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Our studies focus on understanding the structural bases for divergent evolution in groups of homologous enzymes that catalyze different reactions. We are interested in the enolase superfamily, a group of mechanistically diverse enzymes that share enolization of a carboxylate anion substrate, and the orotidine 5-monophosphate (OMPDC) suprafamily, a group of functionally distinct enzymes that share no discernible mechanistic attributes, and D-ribulose 1,5-bisphosphate carboxylase/oxygenase superfamily. All three homologous groups of enzymes share the (b/a)8-fold, the most commonly observed fold in structurally characterized enzymes. At present we are using Chimera to visualize and superimpose structures of members of all three homologous groups. We also use the SFLD to assist with our bioinformatic analyses.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 我们的研究着重于理解在催化不同反应的同源酶中发散进化的结构碱基。 We are interested in the enolase superfamily, a group of mechanistically diverse enzymes that share enolization of a carboxylate anion substrate, and the orotidine 5-monophosphate (OMPDC) suprafamily, a group of functionally distinct enzymes that share no discernible mechanistic attributes, and D-ribulose 1,5-bisphosphate carboxylase/oxygenase superfamily. 所有三个同源酶都共享（B/A）8倍，是结构表征酶中最常见的折叠。 目前，我们正在使用嵌合体可视化和叠加所有三个同源群体的成员的结构。 我们还使用SFLD来协助我们的生物信息学分析。