Ben-Bassat A, Goldberg I
Biochim Biophys Acta. 1980 Jan 11;611(1):1-10. doi: 10.1016/0005-2744(80)90036-4.
Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADPH+ 1-oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP+ 2-oxidoreductase, EC 1.1.1943) have been purified from methanol-grown Pseudomonas C. Glucose-6-phosphate dehydrogenase exhibits activity with either NADP+ or NAD+ as coenzymes, V NADP+ = 0.96 V NAD+.Km values of 22, 290, and 250 microns are obtained for NADP+, NAD+ and glucose 6-phosphate (NADP+ as the coenzyme), respectively. ATP inhibits Glc-6P dehydrogenase activity with NAD+ as coenzyme and to a less extent the activity with DANP+. In the presence of MgCl2, ATP inhibition of Blc-6P dehydrogeanse activity is abolished. 6-Phosphogluconate dehydrogenase has a dual specificity for both NADP+ or NAD+ as coenzymes, V NADP+ = 1.66 V NAD+.Km values of 20, 500 and 100 microns are obtained for NADP+, NAD+ and 6-phosphogluconate (NADP+ as the coenzyme), respectively. With NAD+ as the coenzyme ATP inhibits 6-phosphogluconate dehydrogeanse activity, while with NADP+ as the coenzyme, activity was less affected. The possible role of these enzymes in the metabolism of one-carbon (C1)-compounds in Pseudomonas C is discussed and compared with other methylotrophic microorganisms.
已从甲醇培养的假单胞菌C中纯化出葡萄糖-6-磷酸脱氢酶（D-葡萄糖-6-磷酸：NADPH + 1-氧化还原酶，EC 1.1.1.49）和6-磷酸葡萄糖酸脱氢酶（6-磷酸-D-葡萄糖酸：NADP + 2-氧化还原酶，EC 1.1.1.943）。葡萄糖-6-磷酸脱氢酶以NADP +或NAD +作为辅酶均表现出活性，V NADP + = 0.96 V NAD +。以NADP +、NAD +和葡萄糖6-磷酸（以NADP +作为辅酶）为底物时，Km值分别为22、290和250微摩尔。ATP抑制以NAD +作为辅酶时的Glc-6P脱氢酶活性，对以DANP +作为辅酶时的活性抑制作用较小。在MgCl2存在下，ATP对Blc-6P脱氢酶活性的抑制作用被消除。6-磷酸葡萄糖酸脱氢酶对NADP +或NAD +作为辅酶具有双重特异性，V NADP + = 1.66 V NAD +。以NADP +、NAD +和6-磷酸葡萄糖酸（以NADP +作为辅酶）为底物时，Km值分别为20、500和100微摩尔。以NAD +作为辅酶时，ATP抑制6-磷酸葡萄糖酸脱氢酶活性，而以NADP +作为辅酶时，活性受影响较小。讨论了这些酶在假单胞菌C中一碳（C1）化合物代谢中的可能作用，并与其他甲基营养微生物进行了比较。
