Woodruff W W, Wolfenden R
J Biol Chem. 1979 Jul 10;254(13):5866-7.
Hoping to exploit the special affinity of enzymes for unstable intermediates in substrate transformation, we have determined the effectiveness of possible analogs of ene-diolate intermediates as inhibitors of spinach ribose-5-phosphate isomerase. 4-Phosphoerythronic acid was found to be a very strong competitive inhibitor, with a Ki value almost 3 orders of magnitude lower than the Km value of ribose 5-phosphate, and very much lower than the Ki value of any other inhibitor that was examined.
为了利用酶对底物转化中不稳定中间体的特殊亲和力，我们测定了烯二醇酸中间体的可能类似物作为菠菜核糖-5-磷酸异构酶抑制剂的有效性。发现4-磷酸赤藓糖酸是一种非常强的竞争性抑制剂，其Ki值比核糖5-磷酸的Km值低近3个数量级，并且远低于所检测的任何其他抑制剂的Ki值。
