6-PHOSPHOGLUCONATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Abstract
A 6-phosphogluconate dehydrogenase from L. mesenteroides was purified partially and characterized. The rate of diphospho-pyridine nucleotide (DPN) reduction is 25 times greater than that of triphosphpyridine nucleotide (TPN). Stimulation of enzymatic activity by Mg++ was demonstrable after dialysis against 0.04 [image] glycylglycine at pH 7.5. Dissociation constants were 7.78 x 10-5 [image] 6-phosphoglyconate, and 3.5 x 10-5 [image] DPN. The role of the enzyme is discussed in relation to the hexosemonophosphate pathways described for yeast and Escherichia coli.