1. A mutant of Escherichia coli, devoid of phosphopyruvate synthetase, glucosephosphate isomerase and 6-phosphogluconate dehydrogenase activities, grew readily on gluconate and inducibly formed an uptake system for gluconate, gluconate kinase and 6-phosphogluconate dehydratase while doing so. 2. This mutant also grew on glucose 6-phosphate and inducibly formed 6-phosphogluconate dehydratase; however, the formation of the gluconate uptake system and gluconate kinase was not induced under these conditions. 3. The use of the Entner–Doudoroff pathway for the dissimilation of 6-phosphogluconate, derived from either gluconate or glucose 6-phosphate, by this mutant was also demonstrated by the accumulation of 2-keto-3-deoxy-6-phosphogluconate (3-deoxy-6-phospho-l-glycero-2-hexulosonate) from both these substrates in a similar mutant that also lacked phospho-2-keto-3-deoxygluconate aldolase activity. 4. Glucose 6-phosphate inhibits the continued utilization of fructose by cultures of the mutants growing on fructose, as it does in wild-type E. coli. 5. The mutants do not use glucose for growth. This is shown to be due to insufficiency of phosphopyruvate, which is required for glucose uptake.
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Research Article|
June 01 1973
Utilization of gluconate by Escherichia coli. Induction of gluconate kinase and 6-phosphogluconate dehydratase activities Available to Purchase
H. L. Kornberg;
H. L. Kornberg
1Department of Biochemistry, School of Biological Sciences, University of Leicester, Leicester LE1 7RH, U.K.
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Anne K. Soutar
Anne K. Soutar
1Department of Biochemistry, School of Biological Sciences, University of Leicester, Leicester LE1 7RH, U.K.
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Publisher: Portland Press Ltd
© 1973 London: The Biochemical Society
1973
Biochem J (1973) 134 (2): 489–498.
Citation
H. L. Kornberg, Anne K. Soutar; Utilization of gluconate by Escherichia coli. Induction of gluconate kinase and 6-phosphogluconate dehydratase activities. Biochem J 1 June 1973; 134 (2): 489–498. doi: https://doi.org/10.1042/bj1340489
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