Magnetic Resonance Investigations of Ternary Complexes of Enzyme–Metal–Substrate
Magnetic Resonance Investigations of Ternary Complexes of Enzyme–Metal–Substrate
复制标题
酶-金属-底物三元复合物的磁共振研究
作者：
M. Cohn;J. Leigh
金属离子在那些需要容易解离的金属离子活化剂的酶促反应中的作用的分配导致了许多实验研究和更多的推测。这类酶反应的一些已被足够详细地检查，以指定哪些反应物种与金属离子相互作用。Malmstrom等人的工作 * Wold和Ballou对酵母烯醇化酶催化反应的平衡和动力学的研究表明，金属与酶而不是与底物的结合对于反应的催化至关重要。另一方面，在肌酸激酶 ** 和3-磷酸甘油酸激酶”催化的反应中，金属与腺嘌呤核苷酸的结合被认为是必要的过程。
HE assignment of the role of metal ions in those enzymatic reactions requiring metal ion activators which are readily dissociable has led to many experimental investigations and even more speculation". A few enzyme reactions of this class have been examined in sufficient detail to specify which reacting species interacts with the metal ion. The work of Malmstrom et al.* and of Wold and Ballouº on the equilibrium and kinetics of the reaction catalysed by yeast enolase yielded evidence that the metal binding to the enzyme rather than to the substrate is essential for the catalysis of the reaction. On the other hand, in the reactions catalysed by creatine kinase** and 3-phosphoglycerate kinase", binding of the metal to the adenine nucleotides has been implicated as the essential process.