Niehaus W G, Dilts R P
Arch Biochem Biophys. 1984 Jan;228(1):113-9. doi: 10.1016/0003-9861(84)90052-3.
Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) was purified from mycelium of Aspergillus parasiticus (1-11-105 Whl). The enzyme had a molecular weight of 1.8 X 10(5) and was composed of four subunits of apparently equal size. The substrate was very strict, only glucose 6-phosphate and glucose being oxidized by NADP or thio-NADP. Zinc ion was a powerful inhibitor of the enzyme, inhibition being competitive with respect to glucose 6-phosphate, with Ki about 2.5 microM. Other divalent metal ions which also serve as inhibitors are nickel, cadmium, and cobalt. It is proposed that the stimulation of polyketide synthesis by zinc ion may be mediated in part by inhibition. of glucose-6-phosphate dehydrogenase.
从寄生曲霉（1-11-105 Whl）的菌丝体中纯化出葡萄糖-6-磷酸脱氢酶（EC 1.1.1.49）。该酶的分子量为1.8×10⁵，由四个大小明显相等的亚基组成。其底物特异性很强，只有6-磷酸葡萄糖和葡萄糖能被NADP或硫代NADP氧化。锌离子是该酶的强效抑制剂，对6-磷酸葡萄糖表现为竞争性抑制，抑制常数Ki约为2.5微摩尔。其他同样作为抑制剂的二价金属离子有镍、镉和钴。有人提出，锌离子对聚酮化合物合成的刺激作用可能部分是通过抑制6-磷酸葡萄糖脱氢酶来介导的。
