Spencer P, Paine L J, Scawen M D, Atkinson T, Gore M G
Department of Biochemistry, School of Biochemical and Physiological Sciences, University of Southampton, England.
FEBS Lett. 1990 Jan 1;259(2):297-300. doi: 10.1016/0014-5793(90)80031-d.
Evidence is presented to demonstrate that the Zn2+ -depleted, inactive form of the glycerol dehydrogenase from Bacillus stearothermophilus exists in one of two possible conformations in equilibrium, the position of which is temperature sensitive. The conformation of the metal-depleted enzyme favoured by higher temperatures (20-40 degrees C) is able to bind Zn2+ and regain catalytic activity, whereas that favoured at lower temperatures (0-10 degrees C) is unable to bind metal ions and is thus inactive. This equilibrium is also pH dependent with a pK of 6.6. At pH 6.0, the equilibrium lies in favour of the form of the enzyme able to bind metal ions and exhibit activity.
有证据表明，嗜热脂肪芽孢杆菌甘油脱氢酶的锌离子缺失的无活性形式以两种可能的构象之一存在于平衡状态，其位置对温度敏感。较高温度（20 - 40摄氏度）有利于的金属缺失酶的构象能够结合锌离子并恢复催化活性，而较低温度（0 - 10摄氏度）有利于的构象则无法结合金属离子，因此无活性。这种平衡也依赖于pH值，其pK为6.6。在pH 6.0时，平衡有利于能够结合金属离子并表现出活性的酶形式。
