Chen Y, Xu G
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Biochim Biophys Acta. 1997 Mar 7;1338(1):31-6. doi: 10.1016/s0167-4838(96)00185-9.
Spinach chloroplast fructose 1,6-bisphosphatase, like its counterparts from animal sources, can be activated by monovalent cations such as potassium and ammonium ions. The extents of activation are closely related to the pH values and the concentrations of magnesium ions. The activation effect is most prominent when the concentrations of magnesium ions are high enough to exert inhibitory side effect on the enzyme. Similar to the cases of enzymes from mammalian tissues, activation of the chloroplast enzyme by monovalent cations is, at least partially, due to overcoming of the inhibitory effect by the excess of magnesium ions. The enzyme can also be activated by low concentrations of guanidine hydrochloride, which probably involves a similar mechanism compared with that by monovalent cations.
菠菜叶绿体果糖1,6 -二磷酸酶与其动物来源的对应物一样,可被单价阳离子如钾离子和铵离子激活。激活程度与pH值和镁离子浓度密切相关。当镁离子浓度高到足以对该酶产生抑制副作用时,激活效果最为显著。与哺乳动物组织中的酶情况类似,单价阳离子对叶绿体酶的激活至少部分是由于克服了过量镁离子的抑制作用。该酶也可被低浓度的盐酸胍激活,这可能涉及与单价阳离子激活类似的机制。