Levels of phosphofructokinase, glucose-6-phosphate dehydrogenase and fructose-1,6-diphosphatase activities have been compared in different yeasts belonging to glucose fermenting and non-fermenting groups grown in different conditions.
Phosphofructokinase was present in all the fermentative species tested. On the contrary its level was not measurable in any of the aerobic yeasts tested with the exception of Pichia species.
No significant variations were observed in the values of glucose-6-phosphate dehydrogenase from the two groups of yeasts.
The synthesis of fructose-1,6-diphosphatase was repressed in both groups, by growth in sugar carbon sources. However, a remarkable difference in the sensitivity of the fructose-1,6-diphosphatase from both groups towards inhibition by AMP was observed. The enzyme from all fermentative yeasts tested showed a strong inhibition by AMP (1 mM producing about 80% inhibition) while the enzyme from aerobic yeasts showed different responses, inhibition ranging from 10% in Rhodotorula and Sporobolomyces, to 90% in Pichia.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
This is the net price. Taxes to be calculated in checkout.
Amerine, M. A., Kunkee, R. E.: Microbiology of wine making. Ann. Rev. Microbiol. 22, 323–358 (1968).
Avigad, G.: Inhibition of glucose-6-phosphate dehydrogenase by ATP. Proc. nat. Acad. Sci. (Wash.) 56, 1543–1547 (1966).
Brady, R. J., Chambliss, G. H.: The lack of phosphofructokinase activity in several species of Rhodotorula. Biochem. biophys. Res. Commun. 29, 898–903 (1967).
Eagon, R. G.: Rate limiting effects of pyridine nucleotides on carbohydrate catabolic pathways of microorganisms. Biochem. biophys. Res. Commun. 12, 274–279 (1963).
Gancedo, C., Gancedo, J. M., Sols, A.: Metabolite repression of fructose-1,6-diphosphatase in yeast. Biochem. biophys. Res. Commun. 26, 528–531 (1967a).
———: Regulation of the concentration or activity of pyruvate kinase in yeasts and its relationship to gluconeogenesis. Biochem. J. 102, 23c-25c (1967b).
—, Salas, M. L., Giner, A.: Reciporcal effects of carbon sources on the levels of an AMP sensitive fructose-1,6-diphosphatase and phosphofructokinase in yeast. Biochem. biophys. Res. Commun. 20, 15–20 (1965).
Heick, H. M. C., Barrette, M.: Alcohol dehydrogenase activity in the yeast Lipomyces starkeyi. Biochim. biophys. Acta (Amst.) 212, 8–12 (1970).
Höfer, M., Becker, J. U., Brand, K., Deckner, K., Betz, A.: A study of the enzyme equipment of the yeast Rhodotorula gracilis. FEBS Letters 3, 322–324 (1969).
Litchfield, J. M., Ordal, Z. J.: The oxidative metabolism of Rhodotorula gracilis. Canad. J. Microbiol. 4, 205–213 (1958).
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).
Salas, M., Viñuela, E., Sols, A.: Spontaneous and enzymatically catalyzed anomerization of glucose-6-phosphate and anomeric specificity of related enzymes. J. biol. Chem. 240, 561–568 (1965).
About this article
Cite this article
Gancedo, J.M., Gancedo, C. Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non fermenting yeasts. Archiv. Mikrobiol. 76, 132–138 (1971). https://doi.org/10.1007/BF00411787
- Carbon Source
- Significant Variation