Studies on the Mechanism and Control of Enzyme Action

研究建议涉及核磁共振 光谱学将允许我们测量 配体结合，这也将提供对 基质之间存在的空间关系， 当它们与酶结合时。 酸性和 与催化作用有关的酶上的碱性基团， 底物结合将使用pH方案进行研究 动力学 CyS344的修饰导致酶 失活 这种影响是否是由于CyS344在 活动站点，或者修改是否只是阻止AMPS 合成酶从呈现其天然构象，将是 使用位点特异性诱变的方案进行研究。 腺苷酸琥珀酸（AMPS）合成酶，如果第一个承诺 AMP生物合成的一步，因此起着重要作用。 在新陈代谢中起关键作用。 这种酶如何作为一种 催化剂及其在分子水平上的调节方式是 关键是要了解它的基本作用， 新陈代谢.

Studies are proposed involving nuclear magnetic resonance spectroscopy that will permit us to measure the kinetics of ligand binding and that will also provide an understanding of the spatial relationships that exist among substrates and effectors when they are bound to the enzyme. Acidic and basic groups on the enzyme associated with catalysis and substrate binding will be studied using the protocol of pH kinetics. Modification of CyS344 leads to enzyme inactivation. Whether this effect is due to CyS344 being at the active site, or whether modification simply prevents AMPS synthetase from assuming its native conformation, will be investigated using the protocol of site-specific mutagenesis. Adenylosuccinate (AMPS) synthetase if the first committed step in AMP biosynthesis from IMP and therefore plays a pivotal role in metabolism. How this enzyme acts as a catalyst and how it is regulated at the molecular level is crucial to an understanding of its fundamental role in metabolism.