STRUCTURE-FUNCTION RELATIONSHIPS IN FE- AND CO-CONTAINING NITRILE HYDRATASES

含铁和共基腈水合酶的结构-功能关系

• 批准号: 7954544
• 负责人: ROBERT A SCOTT
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954544
• 关键词: Aldehydes; Amides; Amidines; Amines; Bioremediations; Carboxylic Acids; Chemicals; Comamonas testosteroni; Computer Retrieval of Information on Scientific Projects Database; Enzymes; Esters; Funding; Goals; Grant; Heterocyclic Compounds; Institution; Ketones; Nitriles; Organic Chemicals; Pesticides; Pharmacologic Substance; Polymers; Process; Production; Reaction; Research; Research Personnel; Resources; Solvents; Source; Spectrum Analysis; Structure-Activity Relationship; United States National Institutes of Health; Work; absorption; chemical reaction; insight; medical specialties; nitrile hydratase; structural biology; synchrotron radiation; tool

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. The overall goal of this research is to use x-ray absorption spectroscopy to analyze the reaction mechanism of nitrile hydratases (NHases). The importance of this project is underscored by the extensive industrial use of nitriles to produce a broad number of specialty chemicals containing amines, amides, amidines, carboxylic acids, esters, aldehydes, ketones, and heterocyclic compounds. These compounds are used in a wide array of chemical reactions as feedstock for the production of solvents, extractants, pharmaceuticals, pesticides, and polymers. The proposed research aims to define the reaction mechanisms for both the Co-type nitrile hydratase from Pseudonocardia thermophila JCM 3095 (PtNHase) and the Fe-type NHase from Comamonas testosteroni (CtNHase). The successful completion of the proposed work will not only provide insight into the catalytic mechanism of NHase enzymes, but will also provide new insight into the use of NHase enzymes in organic chemical processing, industrial syntheses, and bioremediation tools.

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。 本研究的总体目标是利用X射线吸收光谱分析腈水合酶（NHases）的反应机制。该项目的重要性突显了腈在工业上的广泛用途，以生产多种含有胺、酰胺、脒、羧酸、酯、醛、酮和杂环化合物的特种化学品。这些化合物广泛用于化学反应，作为生产溶剂、萃取剂、药物、农药和聚合物的原料。本研究旨在明确来自嗜热假诺卡氏菌 JCM 3095 的 Co 型腈水合酶 (PtNHase) 和来自睾酮丛毛单胞菌的 Fe 型 NHase (CtNHase) 的反应机制。该工作的成功完成不仅将为NHase酶的催化机制提供深入的见解，而且还将为NHase酶在有机化学加工、工业合成和生物修复工具中的使用提供新的见解。