Summary
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1.
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.
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2.
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.
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3.
No significant variations were observed in the values of glucose-6-phosphate dehydrogenase from the two groups of yeasts.
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4.
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.
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Abbreviations
- FDPase:
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Fructose-1,6-diphosphatase
- PFK:
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Phosphofructokinase
- G6PDH:
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Glucose-6-phosphate dehydrogenase
References
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).
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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
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DOI: https://doi.org/10.1007/BF00411787