Abstract
The catalytic activity of 6-phosphogluconate dehydrogenase, isolated from sheep liver, has been found to be markedly inhibited by fructose-1,6-diphosphate (F-1,6-PP). Activity measurements carried out in the presence and absence of F-1,6-PP indicate that the inhibition is competitive with respect to 6-phosphogluconate (6-PG), and non-competitive with respect to TPN. A Ki value of 7.08 ± 3.10 × 10−5 M for F-1,6-PP may be calculated from the kinetic measurements. As the Km for 6-PG (1.5 × 10−5 M), the K1 for F-1,6-PP, and the concentrations of 6-PG and F-1,6-PP in liver, are all comparable, it appears that the inhibition of 6-phosphogluconate dehydrogenase by F-1,6-PP may be of significance in the regulation of carbohydrate metabolism in the liver.
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