Abstract
Some enzymatic activities of the glycolytic and hexose monophosphate pathways of Candida parapsilosis, a yeast lacking alcohol dehydrogenase but able to grow on high glucose concentrations, were compared to those of Saccharomyces cerevisiae. Cells were grown either on 8% glucose or on 2% glycerol and activities measured under optimal conditions. Results were as follows: glycolytic enzymes of C. parapsilosis, except glyceraldehyde 3-phosphate dehydrogenase, exhibited an activity weaker than that of S. cerevisiae, especially when yeasts were grown on glycerol. Fructose-1,6 bisphosphatase, an enzyme implicated in gluconeogenesis and in the hexose monophosphate pathway, and known to be very sensitive to catabolite repression in S. cerevisiae, was always active in C. parapsilosis even when cells were grown on 8% glucose. However, the allosteric properties towards AMP and fructose-2,6-bisphosphate were the same in both strains. Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, two other enzymes of the hexose monophosphate pathway, exhibited a higher activity in C. parapsilosis than in S. cerevisiae. Regulation of two important control points of the glycolytic flux, phosphofructokinase and pyruvate kinase, was investigated. In C. parapsilosis phosphofructokinase was poorly sensitive to ATP but fructose-2,60bisphosphate completely relieved the light ATP inhibition. Pyruvate kinase did not require fructose-1,6-bisphosphate for its activity, and by this way, did not regulate the glycolytic flux. The high glyceraldehyde-3-P-dehydrogenase activity, together with the relative insensitivity of fructose-1,6-bisphosphatase to catabolite repression and the high glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities suggested that in C. parapsilosis, as in other Candida species and opposite to S. cerevisiae, the glucose degradation mainly occurred through the hexose monophosphate pathway, under both growth conditions used.
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Abbreviations
- C. parapsilosis :
-
Candida parapsilosis
- S. cerevisiae :
-
Saccharomyces cerevisiae
- C. utilis :
-
Candida utilis
References
Aust A, Yun S, Suelter CH (1975) Pyruvate kinase from yeast (Saccharomyces cerevisiae). In: Wood WA (ed) Methods in enzymol, vol XLII. Academic Press New York London, pp 176–182
Barnard EA (1975) Hexokinases from yeast. In: Wood WA (ed) Methods in enzymol, vol XLII. Academic Press, New York London, pp 6–20
Bartrons R, Van Schaftingen F, Vissers S, Hers HG (1982) The stimulation of yeast phosphofructokinase by fructose 2,6-bis-phosphate. FEBS Lett 143:137–140
Barwell CJ, Hess B (1971) Regulation of pyruvate kinase during glyconeogenesis in Saccharomyces cerevisiae. FEBS Lett 19:1–4
Boiteux A, Hess B (1981) Design of glycolysis. Philosophic Transaction Research Society London Bulletin 293:5–22
Bruinenberg PM, Waslander GW, Van Dijken JP, Schoffers WA (1986) A comparative radiospirometric study of glucose metabolism in yeast. Yeast 2:117–121
Byers LD (1982) Glyceraldehyde 3-P-dehydrogenase from yeast. In: Wood WA (ed) Methods in enzymol, vol 89. Academic Press, New York London, pp 326–335
Camougrand N, Caubet R, Velours G, Guérin M (1983) Evidence for an alternative and non-phosphorylating pathway for NADH reoxidation in a yeast resistant to glucose repression. Eur J Biochem 135:367–371
Camougrand N, Velours G, Guérin M (1986) The resistance of C. parapsilosis to drugs. Biol Cell 56:71–78
Camougrand N, Velours G, Guerin M (1987) The energetic growth yields of the yeast Candida parapsilosis. Biol Cell 61 (in press)
Colowick SP (1973) The hexokinases. In: Boyer PO (ed) The enzymes, 3rd edn, vol IX. Academic Press, New York, pp 1–48
De la Pena P, Barros F, Gascon S, Ramos S, Laro PS (1982) The electrochemical proton gradient of Saccharomyces. Eur J Biochem 123:447–453
Funayama S, Gancedo JM, Gancedo C (1980) Turnover of yeast fructose-bisphosphatase in different metabolic conditions. Eur J Biochem 109:61–66
Gancedo C, Salas ML, Giner A, Sols A (1965) Biochemical reciprocal effects of carbon source on the levels of an AMP-sensitive fructose-1,6-diphosphatase, phosphofructokinase in yeast. Biochem Biophys Res Commun 20:15–20
Gancedo JM, Gancedo C (1971) Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeasts. Arch Microbiol 76:132–138
Gancedo JM, Lagunas R (1973) Contribution of the pentosephosphate pathway to glucose metabolism in S. cerevisiae: a critical analysis on the use of labelled glucose. Plant Sci Letters 1:193–198
Guérin M, Camougrand N, Velours G, Guérin B (1982) New mutants resistant to glucose repression affected in the regulation of the NADH reoxidation. Eur J Biochem 124:457–463
Guérin M, Camougrand N (1986) The alternate oxidase of Candida parapsilosis. Eur J Biochem 159:519–524
Haeckel R, Hess B, Lauterborn N, Wuster KH (1968) Purification and allosteric properties of yeast pyruvate kinase. Hoppe-Seyler's Z Physiol Chem 349:699–714
Hirai M, Tanaka A, Fukui S (1975) Difference in pyruvate kinase regulation among three groups of yeasts. Biochim Biophys Acta 391:282–291
Kuby SA, Noltmann EA (1966) Glucose 6-phosphate dehydrogenase (crystalline) from brewer's yeast. In: Wood WA (ed) Methods in enzymol, vol IX. Academic Press, New York London, pp 116–125
Lederer B, Vissers S, Van Schaftingen F, Hers HG (1981) Fructose-2,6-biphosphate in yeast. Biochem Biophys Res Commun 103:1281–1287
Lodder J (1970) The yeasts, a taxonomic study, 2nd edn. Elsevier North-Holland, Amsterdam
Maitra PK (1970) A glucokinase from Saccharomyces cerevisiae. J Biol Chem 245:2423–2431
Pontremoli S, Traniello S (1975) Fructose-1,6-diphosphate and sedoheptulose-1,7-diphosphatase from Candida utilis. In: Wood WA (ed) Methods in enzymol, vol XLII. Academic Press, New York London, pp 347–353
Racker E (1962) d-Fructose-1,6-diphosphatbestimmung mit Fructose-1,6-diphosphatase. In: Bergmeyer MU (ed) Methoden der enzymatischen Analyse, pp 160–163
Rippa M, Signorini M (1975) 6-Phosphogluconate dehydrogenase from C. utilis. In: Wood WA (ed) Methods in enzymol, vol XLI. Academic Press, New York London, pp 237–240
Rutter WJ, Hunsley JR, Groves WF, Calder J, Rajkumar TV, Woodfin BM (1966) Fructose diphosphate aldolase. In: Wood WA (ed) Methods in enzymol, vol XI Academic Press, New York London, pp 479–498
Scopes RK (1975) 3-Phosphoglycerate kinase of Baker's yeast. In: Wood WA (ed) Methods in enzymol, vol XLII Academic Press, New York London, pp 134–138
Stellwagen E, Wilgus H (1975) Phosphofructokinase of yeast. In: Wood WA (ed) Methods in enzymol, vol XLII. Academic Press, New York London, pp 78–85
Suomalainen H, Oura E (1971) Yeast nutrition and solute uptake. In: Rose AH, Harrison JS (eds) The yeasts, vol 2. Academic Press, New York London, pp 2–74
Van Schaftingen E, Hers HG (1981) Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-biphosphate. Proc Natl Acad Sci USA 78:2861–2863
Westhead EW (1966) Enolase from yeast and rabbit muscle. In: Wood WA (ed) Methods in enzymol, vol IX. Academic Press, New York London, pp 670–679
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Caubet, R., Guerin, B. & Guerin, M. Comparative studies on the glycolytic and hexose monophosphate pathways in Candida parapsilosis and Saccharomyces cerevisiae . Arch Microbiol 149, 324–329 (1988). https://doi.org/10.1007/BF00411650
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DOI: https://doi.org/10.1007/BF00411650