1887

Abstract

Summary: The effect of the glucose analogue 5-thio-D-glucose (5TG) on the yeast was studied. Derepression of mitochondrial respiratory chain cytochromes, alcohol dehydrogenase (isoenzyme II), NADH dehydrogenase and maltase was inhibited by 0.5-2 mM-5TG. Growth rate was only slightly affected. Ethanol was efficiently produced with 2 mM-5TG in medium initially containing 0.25% glucose. Mutants resistant to the growth inhibitory effects of 5TG on glycerol medium showed resistance to the catabolite repressing effects of glucose. Other mutants, known to be catabolite repression resistant, showed resistance to 5TG. The analogue seems to inhibit derepression of glucose repressible enzymes with greater potency than glucose itself.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-132-12-3309
1986-12-01
2024-04-20
Loading full text...

Full text loading...

/deliver/fulltext/micro/132/12/mic-132-12-3309.html?itemId=/content/journal/micro/10.1099/00221287-132-12-3309&mimeType=html&fmt=ahah

References

  1. Adams B. D. 1972; Induction of galactokinase in Saccharomyces cerevisiae: kinetics of induction and glucose effects. Journal of Bacteriology 111:308–315
    [Google Scholar]
  2. Barnett J. A. 1976; The utilization of sugar by yeasts. Advances in Carbohydrate Chemistry and Biochemistry 32:125–234
    [Google Scholar]
  3. Bradford M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  4. Ciriacy M. 1975; Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae . I. Isolation and genetic analysis of adh mutants Mutation Research 29:315–326
    [Google Scholar]
  5. Egilsson V., Evans I. H., Wilkie D. 1979; Toxic and mutagenic effects of carcinogens on the mitochondria of Saccharomyces cerevisiae . Molecular and General Genetics 174:39–46
    [Google Scholar]
  6. Entian K.-D. 1980; Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Molecular and General Genetics 178:633–637
    [Google Scholar]
  7. Entian K.-D., Frölich K.-U. 1984; Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catabolite and regulatory domains for triggering carbon catabolite repression. Journal of Bacteriology 158:29–35
    [Google Scholar]
  8. Furst A., Michels C. A. 1977; An evaluation of d-glucosamine as a gratuitous catabolite repressor of Saccharomyces carlsbergensis . Molecular and General Genetics 155:309–314
    [Google Scholar]
  9. Gascon S., Neuman N. P., Lampen J. O. 1968; Comparative study of the properties of the purified internal and external invertases from yeast. Journal of Biological Chemistry 243:1573–1577
    [Google Scholar]
  10. Gudnason V., Ingvarsson S., Jonasdottir A., Andresdottir V., Egilsson V. 1984; Isoenzyme patterns and subcellular localization of hexokinases in human breast cancer and non-pathological breast tissue. International Journal of Cancer 34:63–66
    [Google Scholar]
  11. Hackel R. A., Khan N. A. 1978; Genetic control of invertase formation in Saccharomyces cerevisiae . II. Isolation and characterization of mutants conferring invertase hyperproduction in strain EK-6B carrying the sue3 gene. Molecular and General Genetics 164:295–302
    [Google Scholar]
  12. Hughes A. R., Wilkie D. 1970; Preferential inhibition of respiration in Saccharomyces cerevisiae: correlation with chlorpromazine. Biochemical Pharmacology 19:2555–2560
    [Google Scholar]
  13. Khan N. A., Greener A. 1977; Effects of petite mutation on maltose and alfa-methyl-glucoside fermentation. Molecular and General Genetics 150:107–108
    [Google Scholar]
  14. Matern H., Holzer H. 1977; Catabolite inactivetion of the galactose uptake mechanism in yeast. Journal of Biological Chemistry 252:6399–6402
    [Google Scholar]
  15. Skaftason J., Johannesson Th. 1975; Akvardanir a alcoholi (ethanoli) i blodi Timarit logfraedingafelagsins (Reykjavik). 25:5–17
    [Google Scholar]
  16. Trinder P. 1969; Determination of blood glucose using an oxidase-peroxidase system with a non-carcinogenic chromogen. Clinical Pathology 22:158–161
    [Google Scholar]
  17. UNO I., Matsumoto K., Adachi K., Ishikawa T. 1984; Characterization of cyclic AMP requiring yeast mutants: alterations in the catalytic subunit of protein kinase. Journal of Biological Chemistry 259:12508–12513
    [Google Scholar]
  18. Van Wijk R. J., Ovwehand H., van den Bos T., Koningsberger V. V. 1969; Induction and catabolite repression of alpha-methyl-glucosidase synthesis in protoplasts of Saccharomyces cerevisiae . Biochimica et biophysica acta 186:178–191
    [Google Scholar]
  19. Witt I., Kronau R., Holzer H. 1966; Repression von Alkoholdehydrogenase, Malatdehydrogenase, Isocitratlyase und Malatsynthase in Hefe durch Glucose. Biochimica et biophysica acta 118:522–537
    [Google Scholar]
  20. Zimmermann F. K., Eaton N. R. 1974; Genetics of induction and catabolite repression of maltase synthesis in Saccharomyces cerevisiae . Molecular and General Genetics 134:261–272
    [Google Scholar]
  21. Zimmermann F. K., Scheel I. 1977; Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. Molecular and General Genetics 154:75–82
    [Google Scholar]
  22. Zimmermann F. K., Kaufmann I., Rasenberger H., Haussmann P. 1977; Genetics of carbon catabolite repression in Saccharomyces cerevisiae . Genes involved in the derepression process. Molecular and General Genetics 151:95–103
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-132-12-3309
Loading
/content/journal/micro/10.1099/00221287-132-12-3309
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error