STRUCTURE AND MECHANISM OF PLP DEPENDENT ENZYMES

PLP依赖性酶的结构和机制

• 批准号: 2627556
• 负责人: ROBERT STEPHEN PHILLIPS
• 金额: $ 2.44万
• 依托单位: UNIVERSITY OF GEORGIA
• 依托单位国家: 美国
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-09-01 至 2001-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2627556
• 关键词: X ray crystallography; aminoacid metabolism; carbon carbon lyase; chemical kinetics; enzyme mechanism; enzyme structure; enzyme substrate; hydrolase; kynurenine; mutant; nonradiation isotope effect; phenols; pyridoxal phosphate; site directed mutagenesis; stop flow technique; tryptophanase; tyrosine

DESCRIPTION This is a competitive renewal application to provide continued support for collaborative studies on the enzymatic mechanisms of tyrosine phenol-lyase. This enzyme uses 5'-periodical phosphate (PLP) as a cofactor, and it is involved in several amino acid modification reactions including transaminations, decarboxylations and beta and gamma eliminations. Several biologically active metabolites involved in a variety of important biological processes, including neurotransmission, depend on similar enzymes. In the present studies the collaborators will continue on their previous course and will generate three dimensional structures of wild-type tyrosine phenol-lyase with substrates and substrate analogs. The structural results of these studies will guide additional experiments for the generation of variant forms of the enzyme. In addition, kinetic studies using multiple isotope effects will be done to identify the rate limiting step in tyrosine phenol-lyase mediated catalysis.

描述 这是一个竞争性更新申请，可为 关于酪氨酸酚酶酶促机制的协作研究。 该酶使用5'-诊断磷酸盐（PLP）作为辅因子，它是 参与了几种氨基酸修饰反应，包括 转移，脱羧，β和伽马消除。 一些 生物活性代谢产物参与了各种重要的 包括神经传递在内的生物过程取决于类似 酶。 在目前的研究中，合作者将继续他们的 上一门课程，将生成野生型的三维结构 带有底物和底物类似物的酪氨酸苯酚 - 洛酶。 结构 这些研究的结果将指导其他实验 酶变体形式的产生。 此外，动力学研究 将使用多种同位素效应来确定限制速率 酪氨酸 - 洛碱介导的催化。