Abstract
When E. coli was grown in the presence of 2:4-dinitrophenol there was a two- to sixfold increase in the activity of glucose 6-phosphate dehydrogenase in the cell-free extracts, but no change in the phosphogluconate-dehydro-genase activity of these extracts. When E. coli was grown in the presence of Na azide, the changes in the extractable activities of either enzyme were of questionable significance. Extracts of E. coli were capable of degrading 6-phosphogluconate slowly in the absence of pyridine nucleotides. This activity was greater in cells grown with gluconate in the medium than with glucose, and was increased by the presence of dinitrophenol.