海螺（Concholepas concholepas）中锰离子激活的和果糖-1,6-二磷酸修饰的镁离子激活的丙酮酸激酶的比较动力学研究。

Comparative kinetic studies of Mn2+-activated and fructose-1,6-P-modified Mg2+-activated pyruvate kinase from Concholepas concholepas.

作者信息

Carvajal N, González R, Morán A, Oyarce A M

出版信息

Comp Biochem Physiol B. 1985;82(1):63-5. doi: 10.1016/0305-0491(85)90128-2.

Abstract

Initial velocity and product inhibition studies of Mn2+-activated and FDP-modified Mg2+-activated pyruvate kinase from Concholepas concholepas, were performed. Evidence is presented to show that the Mn2+-enzyme catalyzes an ordered sequential mechanism, with ADP being the first substrate and pyruvate the last product. The results presented are consistent with a random combination of reactants with the FDP-modified Mg2+-activated enzyme and the formation of the dead-end complexes enzyme ADP-ATP and enzyme-PEP-ATP.

摘要

对来自海螺（Concholepas concholepas）的锰离子激活和FDP修饰的镁离子激活的丙酮酸激酶进行了初始速度和产物抑制研究。有证据表明，锰离子酶催化一种有序的顺序机制，其中ADP是第一个底物，丙酮酸是最后一个产物。给出的结果与反应物与FDP修饰的镁离子激活酶的随机组合以及死端复合物酶-ADP-ATP和酶-PEP-ATP的形成一致。