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Volume 113, Issue 2

Characterization of Two Fructose Bisphosphatase Isoenzymes from the Hydrogen Bacterium 1b Free

Abstract

Summary: Two distinct forms of fructose 1,6-bisphosphatase, designated form A and form B, have been partially purified from autotrophically grown cells of the hydrogen bacterium 1b. Form A was present when the organism was grown under autotrophic conditions but was not synthesized during heterotrophic growth. Form B was detected in both autotrophically and heterotrophically grown organisms, suggesting that it is a constitutive enzyme. The molecular weights were estimated to be 140000 for form A and 190000 for form B. Both purified enzymes showed fructose bisphosphatase as well as sedoheptulose bisphosphatase activity, with pH optima of 8·2 and 8·8 to 9·0 for forms A and B, respectively. The ratio of fructose bisphosphatase to sedoheptulose bisphosphatase activity was 0·6 for form A and about 4·5 for form B. The enzymes required Mg for activity; Mn could only partially replace Mg. Form A was inhibited by ATP and ribulose bisphosphate. AMP exerted a strong allosteric inhibition on form B which was also inhibited by NAD and NADH. Phospho /pyruvate activated form B. On the basis of these results, different physiological roles for the two forms of fructose bisphosphatase are suggested.

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© Society for General Microbiology, 1979
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1979-08-01
2025-11-10

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References

  1. Abdelal A. T., Schlegel H. G. 1974; Purification and regulatory properties of fructose 1,6- diphosphatase from Hydrogenomonas eutropha. Journal of Bacteriology 120:304–310
     [Google Scholar]
  2. Aggag M., Schlegel H. G. 1973; Studies on a Gram-positive hydrogen bacterium, Nocardia opaca strain 1b. I. Description and physiological characterization. Archiv für Mikrobiologie 88:299–318
     [Google Scholar]
  3. Ames B. N. 1966; Assay of inorganic phosphate. Methods in Enzymology 8:115–116
     [Google Scholar]
  4. Bassham J. A. 1971; The control of photosynthetic carbon metabolism. Science 172:526–534
     [Google Scholar]
  5. Bonsignore A., Mangiarotti G., Mangiarotti M. A., De Flora A., Pontremoli S. 1963; Cleavage of sedoheptulose 1,7-diphosphate by a purified rat liver diphosphatase. Journal of Biological Chemistry 238:3151–3154
     [Google Scholar]
  6. Buchanan B. B., Schürmann P., Kalberer P. P. 1971; Ferredoxin-activated fructose diphosphatase of spinach chloroplasts: resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation. Journal of Biological Chemistry 246:5952–5959
     [Google Scholar]
  7. Buchanan B. B., Schürmann P., Wolosiuk R. A. 1976; Appearance of sedoheptulose-1,7-diphosphatase activity on conversion of chloro-plast fructose-1,6-diphosphatase from dimer to monomer form. Biochemical and Biophysical Research Communications 69:970–978
     [Google Scholar]
  8. Ecker C. 1977 Nachweis der plasmidgebundenen, autotrophes Wachstum ermöglichenden Enzyme bei Nocardia Ph.D. thesis University of Göttingen, F.R.G:
     [Google Scholar]
  9. Enser M., Shapiro S., Horecker B. L. 1969; Immunological studies of liver, kidney, and muscle fructose 1,6-diphosphatases. Archives of Biochemistry and Biophysics 129:377–383
     [Google Scholar]
  10. Fraenkel D. G., Pontremoli S., Horecker B. L. 1966; The specific fructose diphosphatase of Escherichia coli: properties and partial purification. Archives of Biochemistry and Biophysics 114:4–12
     [Google Scholar]
  11. Horecker B. L., Melloni E., Pontremoli S. 1975; Fructose 1,6-bisphosphatase: properties of the neutral enzyme and its modification by proteolytic enzymes. Advances in Enzymology and Related Areas of Molecular Biology 42:193–226
     [Google Scholar]
  12. Joint I. R., Morris I., Fuller R. C. 1972; Purification of a complex of alkaline fructose 1,6-bisphosphatase and phosphoribulokinase from Rhodospirillum rubrum. Journal of Biological Chemistry 247:4833–4838
     [Google Scholar]
  13. Mukkada A. J., Bell E. J. 1971; Partial purification and properties of the fructose 1,6-diphosphatase from Acinetobacter lwoffi. Archives of Biochemistry and Biophysics 142:22–31
     [Google Scholar]
  14. Nimmo H. G., Tipton K. F. 1975; The purification of fructose 1,6-diphosphatase from ox liver and its activation by ethylenediaminetetra- acetate. Biochemical Journal 145:323–334
     [Google Scholar]
  15. Opheim D. J., Bernlohr R. W. 1975; Purification and regulation of fructose-1,6-bisphos- phatase from Bacillus licheniformis. Journal of Biological Chemistry 250:3024–3033
     [Google Scholar]
  16. Probst I., Schlegel H. G. 1973; Studies on a Gram-positive hydrogen bacterium, Nocardia opaca strain 1b. II. Enzyme formation and regulation under the influence of hydrogen or fructose as growth substrates. Archiv für Mikrobiologie 88:319–330
     [Google Scholar]
  17. Racker E., Schroeder E. A. R. 1958; The reductive pentose phosphate cycle. II. Specific C-1 phosphatases for fructose 1,6-diphosphate and sedoheptulose 1,7-diphosphate. Archives o, Biochemistry and Biophysics 74:326–344
     [Google Scholar]
  18. Reh M., Schlegel H. G. 1975; Chemolitho-autotrophie als eine übertragbare autonome Eigenschaft von Nocardia opaca 1b. Nachrichten der Akademie der Wissenschaften in Göttingen. II. Mathematisch-Physikalische Klasse 12:207–216
     [Google Scholar]
  19. Reiland J. L. 1971; Gel filtration. Methods in Enzymology 22:287–321
     [Google Scholar]
  20. Rosen O. M. 1966; Purification and properties of fructose 1,6-diphosphatase from Polysphondylium pallidum. Archives of Biochemistry and Biophysics 114:31–37
     [Google Scholar]
  21. Rosen O. M., Rosen S. M., Horecker B. L. 1965; Purification and properties of a specific fructose 1,6-diphosphatase from Candida utilis. Archives of Biochemistry and Biophysics 112:411–420
     [Google Scholar]
  22. Schlegel H. G., Kaltwasser H., Gottschalk G. 1961; Ein Submersverfahren zur Kultur wasserstoffoxydierender Bakterien: wachstums-physiologische Untersuchungen. Archiv für Mikrobiologie 38:209–222
     [Google Scholar]
  23. Schürmann P., Wolosiuk R. A. 1978; Studies on the regulatory properties of chloroplast fructose-1,6-bisphosphatase. Biochimica et biophysica acta 522:130–138
     [Google Scholar]
  24. Springate C. F., Stachow C. S. 1972a; Fructose 1,6-diphosphatase from Rhodopseudomonas palustris. I. Purification and properties. Archives of Biochemistry and Biophysics 152:1–12
     [Google Scholar]
  25. Springate C. F., Stachow C. S. 1972b; Fructose 1,6-diphosphatase from Rhodopseudomonas palustris. II. Regulatory properties. Archives of Biochemistry and Biophysics 152:13–20
     [Google Scholar]
  26. Taketa K., Pogell B. M. 1965; Allosteric inhibition of rat liver fructose 1,6-diphosphatase by adenosine 5′-monophosphate. Journal of Biological Chemistry 240:651–662
     [Google Scholar]
  27. Tejwani G. A., Pedrosa F. O., Pontremoli S., Horecker B. L. 1976; The purification and properties of rat liver fructose 1,6-bisphosphatase. Archives of Biochemistry and Biophysics 177:253–264
     [Google Scholar]
  28. Van Tol A., Black W. J., Horecker B. L. 1972; Activation of rabbit muscle fructose diphosphatase by EDTA and the effect of divalent cations. Archives of Biochemistry and Biophysics 151:591–596
     [Google Scholar]
  29. Yoshida M., Oshima T. 1971; The thermostable allosteric nature of fructose 1,6-diphosphatase from an extreme thermophile. Biochemical and Biophysical Research Communications 45:495–500
     [Google Scholar]
  30. Zimmermann G., Kelly G. J., Latzko E. 1976; Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase. European Journal of Biochemistry 70:361–367
     [Google Scholar]
  31. Zimmermann G., Kelly G. J., Latzko E. 1978; Purification and properties of spinach leaf cytoplasmic fructose-1,6-bisphosphatase. Journal of Biological Chemistry 253:5952–5956
     [Google Scholar]
/content/journal/micro/10.1099/00221287-113-2-347
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Characterization of Two Fructose Bisphosphatase Isoenzymes from the Hydrogen Bacterium Nocardia opaca 1b
Microbiology 113, 347 (1979); https://doi.org/10.1099/00221287-113-2-347
/content/journal/micro/10.1099/00221287-113-2-347
/content/journal/micro/10.1099/00221287-113-2-347
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