SUMMARY: Certain enzymes of glucose catabolism in were studied and their activities in steady-state chemostat cultures were measured under various nutrient limitations. 2-Keto-3-deoxy-6-phosphogluconate aldolase was separated from 6-phosphogluconate dehydratase by affinity chromatography and the previously observed inhibition of the Entner-Doudoroff enzymes by tricarboxylic acids and ATP was attributed to chelation of Mn and Mg which activate the dehydratase. Glucose-6-phosphate dehydrogenase was unaffected by phosphopyruvate while fructose-1,6-bisphosphate aldolase was activated by Co, K or NH ions. Transketolase, transaldolase and triosephosphate isomerase were present but previous reports of 6-phosphogluconate dehydrogenase activity were shown to be artefacts. The findings confirm the major role of the Entner-Doudoroff pathway in glucose catabolism in . Pyruvate dehydrogenase, a key enzyme for carbon entry to the tricarboxylic acid cycle and to poly-β-hydroxybutyrate synthesis, was inhibited by acetyl-coenzyme A and NADH.


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