Studies on a gram-positive hydrogen bacterium, Nocardia opaca strain 1b - II. Enzyme formation and regulation under the influence of hydrogen or fructose as growth substrates.
In Nocardia opaca strain 1b the key enzymes of the Entner-Doudoroff pathway, 6-phosphogluconate dehydrase and 2-keto-3-deoxy-6-phosphogluconate aldolase, are inducible, while glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase are constitutively formed. In autotrophically grown cells the fructose diphosphate aldolase has six-fold specific activity compared to fructose- or gluconate-grown cells. Molecular hydrogen represses the adaptation to fructose, glucose, or gluconate and inhibits the utilization of glucose or fructose. Glucose-6-phosphate dehydrogenase has been purified 22fold. It utilizes either NADP of NAD as coenzyme; it requires magnesium ions for maximal activity. The dehydrogenation reaction is competitively inhibited by rather high concentrations (2-6 mM) of ATP, and in a similar fashion by phosphoenolpyruvate. Homotropic or heterotropic interactions between substrate molecules were not detected. The effect of ATP is relieved by equimolar concentrations of magnesium.