1887

Abstract

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.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-109-1-89
1978-11-01
2020-01-29
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-109-1-89
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error