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. 1969 Jun;98(3):1151–1158. doi: 10.1128/jb.98.3.1151-1158.1969

Glucose-6-Phosphate Dehydrogenase and Its Deficiency in Mutants of Corynebacterium glutamicum

Ernel D Ihnen 1, Arnold L Demain 1
PMCID: PMC315308  PMID: 5788701

Abstract

Corynebacterium glutamicum is a member of a group of taxonomically related glutamate-excreting bacteria which utilize glucose both by the Embden-Meyerhof and the pentose phosphate pathways, the latter sequence accounting for 10 to 38% of the glucose metabolized. Some of the properties of glucose-6-phosphate dehydrogenase in crude extracts of C. glutamicum were studied. The enzyme was rapidly inactivated by dilution in tris (hydroxymethyl)aminomethane-hydrochloride buffer. This inactivation was prevented by the presence of 0.45 m NaCl. Mg++ was required for enzyme activity, but Mn++, Ca++, Sr++, and Ba++ were equally effective. Growth of the organism under differing conditions did not markedly affect the specific activity of the enzyme. A generally applicable method for detecting colonies deficient in glucose-6-phosphate dehydrogenase was developed. Mutants so obtained were found to be auxotrophic for tryptophan. Upon reversion of the tryptophan requirement, the revertants still retained the property of glucose-6-phosphate dehydrogenase deficiency. Neither the mutants nor the revertants could grow as rapidly as the parent culture in glucose, in gluconate, or in a complex medium.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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