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.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 我们的研究重点是了解催化不同反应的同源酶组中趋异进化的结构基础。 我们对烯醇化酶超家族感兴趣，这是一组机制多样的酶，它们共享羧酸根阴离子底物的烯醇化，以及乳清苷 5-单磷酸 (OMPDC) 超家族，一组功能不同的酶，没有明显的机制属性，以及 D-核酮糖1,5-二磷酸羧化酶/加氧酶超家族。 所有三个同源酶组都具有 (b/a)8 折叠，这是结构特征酶中最常见的折叠。 目前，我们正在使用 Chimera 来可视化和叠加所有三个同源组成员的结构。 我们还使用 SFLD 来协助我们的生物信息学分析。