Grishin M N, Kodentsova V M, Abdraimova U A, Nikolaeva O P, Petushkova E V
Biokhimiia. 1985 Sep;50(9):1517-22.
It was demonstrated that the dialdehyde derivative of ATP is a good substrate for Ca-ATPase of heavy meromyosin (Km = (1.2-1.4) X 10(-4) M; V = VATP). At the same time, this compound can induce irreversible inhibition of the enzyme. Since oxo-ATP is rapidly hydrolyzed by myosin to form oxo-ADP, this inhibition is the result of the enzyme interaction with oxo-ADP. It was found that the kinetics of heavy meromyosin inhibition by oxo-ADP are typical of affinity modification; in this case ATP fully protects heavy meromyosin from the activity loss. Similar results on the irreversible inhibition of the ATPase activity under the action of oxo-ADP were obtained in the presence of myosin, heavy meromyosin, subfragment I and natural actomyosin and in the absence of bivalent cations, thus suggesting the modification of the active center of myosin ATPase.
已证明，ATP的二醛衍生物是重酶解肌球蛋白的Ca - ATP酶的良好底物（Km = (1.2 - 1.4)×10⁻⁴ M；V = VATP）。同时，该化合物可诱导该酶的不可逆抑制。由于氧代ATP被肌球蛋白迅速水解形成氧代ADP，这种抑制是酶与氧代ADP相互作用的结果。发现氧代ADP对重酶解肌球蛋白的抑制动力学是典型的亲和修饰；在这种情况下，ATP可完全保护重酶解肌球蛋白不失活。在有肌球蛋白、重酶解肌球蛋白、亚片段I和天然肌动球蛋白存在以及无二价阳离子的情况下，在氧代ADP作用下对ATP酶活性的不可逆抑制也得到了类似结果，从而表明肌球蛋白ATP酶活性中心发生了修饰。
