ATP：谷氨酰胺合成酶腺苷酰转移酶反应的可逆性。
Reversibility of the ATP:glutamine synthetase adenylyltransferase reaction.
作者信息
Mantel M, Holzer H
出版信息
Proc Natl Acad Sci U S A. 1970 Mar;65(3):660-7. doi: 10.1073/pnas.65.3.660.
Abstract
The reversibility of adenylylation of glutamine synthetase from E. coli by adenylyltransferase was demonstrated. Several positive effectors (Gln, 2-hydroxyethyl-S-cysteine, Trp and Met) stimulate the back reaction in the same manner as the forward reaction. The apparent Michaelis constant for PP(i) is 2.2 mM at pH 7.35. The pH optimum of the back reaction is 6.5-7 while the pH optimum of the forward reaction is 7.6. The apparent equilibrium constant in the presence of 10 mM Mg(2+) at pH 7.36 is 8.5 in favor of adenylylated glutamine synthetase and PP(i). The equilibrium constant is strongly dependent from pH and from Mg(2+) concentration. There is a difference of about 0.5 to 1 kcal/mole free energy between the adenylyl-O-tyrosine bond and the pyrophosphate bond of adenosine triphosphate (ATP). It follows from these considerations that the adenylyl-O-tyrosine bond is an "energy-rich phosphate bond."
摘要
已证明大肠杆菌谷氨酰胺合成酶的腺苷酸化可被腺苷酸转移酶逆转。几种正效应物（谷氨酰胺、2-羟乙基-S-半胱氨酸、色氨酸和甲硫氨酸）刺激逆反应的方式与正反应相同。在pH 7.35时，PP(i)的表观米氏常数为2.2 mM。逆反应的最适pH为6.5 - 7，而正反应的最适pH为7.6。在pH 7.36、存在10 mM Mg(2+)的情况下，表观平衡常数为8.5，有利于腺苷酸化谷氨酰胺合成酶和PP(i)。平衡常数强烈依赖于pH和Mg(2+)浓度。腺苷酰-O-酪氨酸键与三磷酸腺苷（ATP）的焦磷酸键之间的自由能差约为0.5至1千卡/摩尔。从这些考虑可以得出，腺苷酰-O-酪氨酸键是一种“高能磷酸键”。
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