CRYSTAL STRUCTURE OF MEND

MEND 的晶体结构

• 批准号: 7721255
• 负责人: DAVID A SANDERS
• 金额: $ 0.7万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-05-15 至 2009-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721255
• 关键词: Carbon; Computer Retrieval of Information on Scientific Projects Database; Enzymes; Funding; Grant; Institution; Pathway interactions; Research; Research Personnel; Resources; Source; Structure; United States National Institutes of Health; Vitamin K 2; adduct; carboxylate; enzyme structure

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. (1R,6R)-2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase, also called MenD, participates in the menaquinone (Vitamin K2) biosynthetic pathway. The enzyme is a part of the superfamily of ThDP-dependent enzymes, however it is the only enzyme known to catalyze a Stetter-like 1,4-addition of a ThDP adduct to the alpha-carbon of an unsaturated carboxylate. The crystal structure of this enzyme will be important for clarifying the mechanism of this important enzyme.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 (1R,6R)-2-琥珀酰-6-羟基-2,4-环己二烯-1-羧酸酯 (SCHHC) 合酶，也称为 MenD，参与甲基萘醌（维生素 K2）生物合成途径。 该酶是 ThDP 依赖性酶超家族的一部分，但它是已知唯一能够催化 ThDP 加合物与不饱和羧酸酯的 α-碳发生类似 Stetter 1,4-加成反应的酶。 这种酶的晶体结构对于阐明这种重要酶的机制非常重要。