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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 我们的研究集中在理解的结构基础上，不同的进化组的同源酶，催化不同的反应。 我们感兴趣的烯醇化酶超家族，一组机械多样的酶，共享烯醇化的羧酸阴离子底物，乳清酸核苷5-单磷酸（OMPDC）超家族，一组功能不同的酶，共享没有可辨别的机械属性，和D-核酮糖1，5-二磷酸羧化酶/加氧酶超家族。 所有三个同源酶组共享（B/a）8倍，这是结构特征酶中最常见的折叠。 目前，我们正在使用嵌合体来可视化和分析所有三个同源组的成员的结构。 我们还使用SFLD来协助我们的生物信息学分析。