Ainsworth S, Macfarlane N
Biochem J. 1975 Jan;145(1):63-71. doi: 10.1042/bj1450063.
The paper reports a comparative study of the effects of Mn2+, Ni2+ and Co2+ on the reaction of ADP with phosphoenolypyruvate when catalysed by K+-activated rabbit muscle pyruvate kinase. The activation and subsequent inhibition that occurs as the bivalent ion concentration is increased is taken as evidence that the substrates of the enzyme are phosphoenolypyruvate, uncomplexed ADP and free bivalent cation. Kinetic constants for the binding of the bivalent cation to the enzyme are reported.
该论文报道了一项关于Mn2+、Ni2+和Co2+对K+激活的兔肌丙酮酸激酶催化ADP与磷酸烯醇丙酮酸反应的影响的比较研究。随着二价离子浓度增加而出现的激活及随后的抑制作用被视为该酶的底物是磷酸烯醇丙酮酸、未络合的ADP和游离二价阳离子的证据。文中报道了二价阳离子与该酶结合的动力学常数。