Liao C L, Atkinson D E
J Bacteriol. 1971 Apr;106(1):37-44. doi: 10.1128/jb.106.1.37-44.1971.
Pyruvate kinase (EC 2.7.1.40) from Azotobacter vinelandii responds sharply to the adenylate energy charge, with a decrease in activity at high values of charge, as expected for an enzyme of an adenosine triphosphate-regenerating sequence. Glycolytic intermediates, especially glucose 6-phosphate, fructose 6-phosphate, and fructose-1,6-diphosphate, strongly stimulate the reaction and overcome the inhibition caused by high values of energy charge. Thus, the properties of this enzyme depend on interaction between energy charge and the concentrations of hexose phosphates. The properties of pyruvate kinase, together with those of phosphoenolpyruvate carboxylase, aspartokinase, and citrate synthase, seem adapted to provide appropriate partitioning of phosphoenolpyruvate between competing pathways in response to metabolic need.
来自棕色固氮菌的丙酮酸激酶(EC 2.7.1.40)对腺苷酸能荷有敏锐的反应,在高能荷值时活性降低,这对于三磷酸腺苷再生序列中的一种酶来说是预期的。糖酵解中间产物,尤其是6-磷酸葡萄糖、6-磷酸果糖和1,6-二磷酸果糖,能强烈刺激该反应并克服高能荷值引起的抑制作用。因此,这种酶的特性取决于能荷与己糖磷酸浓度之间的相互作用。丙酮酸激酶的特性,连同磷酸烯醇式丙酮酸羧化酶、天冬氨酸激酶和柠檬酸合酶的特性,似乎适合于根据代谢需求在竞争途径之间对磷酸烯醇式丙酮酸进行适当的分配。