Deville-Bonne D, Else A J
Laboratoire d'Enzymologie, CNRS, Gif-sur-Yvette, France.
Eur J Biochem. 1991 Sep 15;200(3):747-50. doi: 10.1111/j.1432-1033.1991.tb16240.x.
Tetrameric Escherichia coli phosphofructokinase dissociates reversibly on incubation under hydrostatic pressures of 80 MPa and above, yielding inactive dimers and monomers. The transition is dependent upon enzyme concentration and presence of ligands. The substrate, D-fructose 6-phosphate, which bridges the intersubunit interface at the active site, produces a massive stabilization to pressure, whereas ATP, which binds to only one subunit, induces only a mild stabilization. Both the positive allosteric regulator, GDP, and the negative allosteric regulator, phosphoenolpyruvate, whose binding sites lie at the other subunit interface, produce an intermediate effect. Of these ligands, only ATP increases the rate of reactivation after depressurization.
四聚体大肠杆菌磷酸果糖激酶在80兆帕及以上的静水压力下孵育时会可逆地解离，产生无活性的二聚体和单体。这种转变取决于酶浓度和配体的存在。底物D-果糖6-磷酸在活性位点桥接亚基间界面，对压力有巨大的稳定作用，而仅与一个亚基结合的ATP仅诱导轻微的稳定作用。正构变构调节剂GDP和负构变构调节剂磷酸烯醇丙酮酸，其结合位点位于另一个亚基界面，产生中间效应。在这些配体中，只有ATP能提高减压后的再激活速率。
