PMID:4869212

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Fraenkel, DG (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase.J. Bacteriol. 95:1267-71

Abstract Glucose is metabolized in Escherichia coli chiefly via the phosphoglucose isomerase reaction; mutants lacking that enzyme grow slowly on glucose by using the hexose monophosphate shunt. When such a strain is further mutated so as to yield strains unable to grow at all on glucose or on glucose-6-phosphate, the secondary strains are found to lack also activity of glucose-6-phosphate dehydrogenase. The double mutants can be transduced back to glucose positivity; one class of transductants has normal phosphoglucose isomerase activity but no glucose-6-phosphate dehydrogenase. An analogous scheme has been used to select mutants lacking gluconate-6-phosphate dehydrogenase. Here the primary mutant lacks gluconate-6-phosphate dehydrase (an enzyme of the Enter-Doudoroff pathway) and grows slowly on gluconate; gluconate-negative mutants are selected from it. These mutants, lacking the nicotinamide dinucleotide phosphate-linked glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase, grow on glucose at rates similar to the wild type. Thus, these enzymes are not essential for glucose metabolism in E. coli.
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Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status

Glucose-6-Phosphate Dehydrogenase

GO:0004345

glucose-6-phosphate dehydrogenase activity

IMP: Inferred from Mutant Phenotype

F

See Table 1.

complete

Gluconate-6-Phosphate Dehydrogenase

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

IMP: Inferred from Mutant Phenotype

F

See Table 2.

complete

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