PURIFICATION AND PROPERTIES OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM BEET LEAVES

We have purified to homogeneity 6-Phosphogluconate dehydrogenase from leaves of silver beet (Beta vulgaris L.) by means of cation-exchange and affinity chromatography. The enzyme is a homodimer of 52 kDa subunits; it catalyzes NADP dependent oxidation of 6-P-gluconate with Michaelian substrate saturation. The activity is affected by some intermediates of carbohydrate metabolism, particularly erythrose-4-P. Subcellular fractionation studies indicate the cytosolic location of the enzyme.