Fernández A, Costas M J, Sillero M A, Sillero A
Biochem Biophys Res Commun. 1984 May 31;121(1):155-61. doi: 10.1016/0006-291x(84)90700-9.
Diadenosine tetraphosphate, Ap4A, doubled the activity of AMP deaminase from rat muscle, with an activation constant of 0.005 mM, in the presence of 0.05 mM AMP. The presence of Ap4A appeared to induce Michaelian kinetic behavior. The activation by Ap4A was not dependent on the presence of either MgCl2 or KCl in the reaction mixture. Diguanosine tetraphosphate was inhibitor of the enzyme. Diadenosine and diguanosine triphosphates, adenylosuccinate and xanthosine monophosphate were neither inhibitors nor activators of the reaction.
四磷酸二腺苷(Ap4A)在存在0.05 mM AMP的情况下,使大鼠肌肉中的AMP脱氨酶活性提高了一倍,激活常数为0.005 mM。Ap4A的存在似乎诱导了米氏动力学行为。Ap4A的激活不依赖于反应混合物中MgCl2或KCl的存在。四磷酸二鸟苷是该酶的抑制剂。二磷酸二腺苷和二磷酸二鸟苷、腺苷酸琥珀酸和单磷酸黄嘌呤既不是该反应的抑制剂也不是激活剂。