The oxidative pathway of carbohydrate metabolism in Escherichia coli. 3. Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in cells grown under different conditions

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Abstract
E. coli was grown in synthetic medium with glucose or gluconate under aerobic and anaerobic conditions, and with arabinose and Na lactate under aerobic conditions. Glucose 6-phosphate dehydrogenase in extracts from cells grown under all conditions tested reduced triphosphopyridine nucleotide (TPN) at a mean rate of 0.26 [mu]mole/minute/mg of protein. Phospho-gluconate dehydrogenase in the same extracts reduced TPN at a mean rate of 0.14 [mu]mole/minute/mg of protein. Activity of these enzymes in terms of molecules of substrate oxidized/minute/cell were calculated, and compared with the uptake of glucose from the medium as experimentally determined. Infection with T-6r + or T-2r+ bacteriophage did not change the extractable activity of glucose 6-phosphate dehydrogenase or phosphogluconate dehydrogenase in E. coli.