Hsu C L, Joshi J G
Chem Biol Interact. 1977 Apr;17(1):61-7. doi: 10.1016/0009-2797(77)90072-2.
Inhibition by aurinetricarboxylic acid (ATA) of glucose-6-phosphate (G6P) dehydrogenase was "competitive" with respect to G6P and "mixed type" with respect to NADP+. Inhibited enzyme bound two molecules of ATA. Kinetic constants, Km, Ki at varying pH suggested possible binding of the inhibitor by the sulfhydryl of the enzyme; of the several enzymes tested only milk xanthine oxidase and G6P dehydrogenase from bovine adrenal was inhibited by ATA.
金精三羧酸(ATA)对葡萄糖-6-磷酸(G6P)脱氢酶的抑制作用,就G6P而言是“竞争性”的,而就NADP⁺而言是“混合型”的。被抑制的酶结合了两分子的ATA。在不同pH值下的动力学常数Km、Ki表明抑制剂可能与酶的巯基结合;在所测试的几种酶中,只有牛奶黄嘌呤氧化酶和牛肾上腺的G6P脱氢酶被ATA抑制。