Bornmann L, Hess B, Zimmermann-Telschow H
Proc Natl Acad Sci U S A. 1974 Apr;71(4):1525-9. doi: 10.1073/pnas.71.4.1525.
Pyruvate kinase (EC 2.7.1.40) of S. carlsbergensis is a tetrameric enzyme, composed of four identical subunits each of which contains 1 mole of L-valine noncovalently bound. The enzyme readily dissociates into monomeric units. L-Valine and magnesium or manganese ions are specific primers of the renaturation process of the enzyme. The amino acid induces renaturation with a K(0.5) of 17 muM and a pseudo first-order rate constant of 0.019 min(-1) at 25 degrees with respect to the monomeric species, indicating that L-valine influences the folding of the monomeric form from a disordered state to its native conformation being followed by a spontaneous reassociation with formation of the tetrameric enzyme. Independently, magnesium and manganese ions induce the renaturation with a first-order rate constant of the same magnitude.
卡尔斯伯酵母的丙酮酸激酶（EC 2.7.1.40）是一种四聚体酶，由四个相同的亚基组成，每个亚基含有1摩尔非共价结合的L-缬氨酸。该酶很容易解离成单体单元。L-缬氨酸和镁离子或锰离子是该酶复性过程的特异性引发剂。该氨基酸诱导复性，相对于单体形式，在25℃时K(0.5)为17μM，假一级速率常数为0.019 min⁻¹，这表明L-缬氨酸影响单体形式从无序状态折叠成其天然构象，随后自发重新缔合形成四聚体酶。独立地，镁离子和锰离子以相同大小的一级速率常数诱导复性。
