多胺对酵母AMP脱氨酶激活作用的定量构效关系研究
Quantitative structure activity relationship studies on the activation of yeast AMP deaminase by polyamines.
作者信息
Yoshino M, Murakami K
出版信息
Int J Biochem. 1987;19(2):209-11. doi: 10.1016/0020-711x(87)90335-1.
Quantitative structure activity relationship studies on the activation of AMP deaminase by polyamines were carried out. Polyamine enhanced the maximal velocity of AMP deaminase without changing the affinity for the substrate AMP. Activation by polyamines of AMP deaminase can be accounted for by the simple Michaelis-Menten mechanism in the presence of ATP. A close correlation between the structure and activation constants for polyamines suggests that the binding of polyamine to AMP deaminase involves primarily polar interactions.
开展了关于多胺对AMP脱氨酶激活作用的定量构效关系研究。多胺提高了AMP脱氨酶的最大反应速度，而不改变对底物AMP的亲和力。在ATP存在的情况下，多胺对AMP脱氨酶的激活作用可通过简单的米氏机制来解释。多胺的结构与激活常数之间密切相关，这表明多胺与AMP脱氨酶的结合主要涉及极性相互作用。
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