Skip to main content
SpringerLink
Log in

Synthese von Phosphoenolpyruvat aus Pyruvat durch Extrakte aus Hydrogenomonas eutropha Stamm H 16

Biosynthesis of phosphoenolpyruvate from pyruvate by extracts from Hydrogenomonas eutropha strain H 16

  • Published:
Archiv für Mikrobiologie Aims and scope Submit manuscript

Summary

Crude extracts from Hydrogenomonas eutropha strain H 16 catalyze the biosynthesis of phosphoenolpyruvate from pyruvate and adenosine triphosphate. Under identical conditions extracts from Escherichia coli synthesized phosphoenol-pyruvate from pyruvate also.

The reaction product phosphoenolpyruvate has been identified by paper chromatography, by employing radioactive pyruvate and by a coupled enzyme assay, using a purified preparation of 3-deoxy-d-arabino-heptulonic acid-7-phosphate synthase. AMP has been found as the second product of the PEP-synthase reaction. From these results it is concluded that strain H 16 contains an enzyme phosphorylating pyruvate directly.

Zusammenfassung

Zellfreie Extrakte aus Hydrogenomonas eutropha Stamm H 16 katalysieren die Biosynthese von Phosphoenolpyruvat aus Pyruvat und Adenosintriphosphat. Unter identischen Bedingungen erfolgte diese Synthese auch durch Extrakte aus Escherichia coli.

Das Reaktionsprodukt Phosphoenolpyruvat wurde durch Papierchromatographie, durch Anwendung von radioaktivem Pyruvat und durch einen gekoppelten enzymatischen Test unter Einsatz eines gereinigten Präparates von 3-Desoxy-d-arabino-heptulosonsäure-7-phosphat Synthase, AMP wurde als zweites Produkt der PEP-Synthasereaktion nachgewiesen. Die Versuchsergebnisse lassen darauf schließen, daß der Stamm H 16 über ein Enzym verfügt, welches Pyruvat direkt phosphoryliert.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

DAHP:

3-Desoxy-d-arabino-heptulosonsäure-7-phosphat

DTT:

Dithiothreitol

PEP:

Phosphoenolpyruvat

P:

ortho-Phosphat

PP:

Pyrophosphat

Literatur

  • Adam, H.: Adenosin-5′-diphosphat. In: H.-U. Bergmeyer, Methoden enzymatischer Analyse, pp. 573–577. Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Benziman, M.: Implication of the direct phosphorylation of pyruvate in cellulose synthesis by Acetobacter xylinum. Biochem. biophys. Res. Commun. 24, 391–394 (1966).

    PubMed  Google Scholar 

  • Buchanan, B. B., Evans, M. C. W.: The synthesis of phosphoenolpyruvate from pyruvate and ATP by extracts of photosynthetic bacteria. Biochem. biophys. Res. Commun. 22, 484–488 (1966).

    PubMed  Google Scholar 

  • Cooper, R. A., Kornberg, H. I.: Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli. Biochim. biophys. Acta (Amst.) 104, 618–620 (1965).

    Google Scholar 

  • ——: The direct synthesis of phosphoenolpyruvate from pyruvate by Escherichia coli. Proc. roy. Soc. B 168, 263–280 (1967).

    Google Scholar 

  • Doy, C. H.: The nature of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase in extracts of wild-type Neurospora crassa: A ping-pong reaction controlled by two activating substrates and three allosteric negative modifiers. Biochim. biophys. Acta (Amst.) 159, 352–366 (1968).

    Google Scholar 

  • —, Brown, K. D.: Control of aromatic biosynthesis: The multiplicity of 7-phospho-2-oxo-3-deoxy-d-arabino heptonate d-erythrose-4-phosphate lyase (pyruvate phosphorylating) in Escherichia coli W. Biochim. biophys. Acta (Amst.) 104, 377–389 (1965).

    Google Scholar 

  • Evans, H. J., Wood, H. G.: P-enolpyruvate synthesis from pyruvate. Fed. Proc. 27, 588 (1968).

    Google Scholar 

  • Friedrich, C. G.: Isolierung Antimetabolit-resistenter, Metabolite ausscheidender Mutanten von Hydrogenomonas H16 und Untersuchung der DAHP-Synthase. Diplomarbeit Göttingen 1970.

  • Frings, W., Schlegel, H. G.: Zur Synthese von C4-Dicarbonsäuren aus Pyruvat durch Hydrogenomonas eutropha. Stamm H 16 Arch. Mikrobiol. 79 204–219 (1971).

    PubMed  Google Scholar 

  • Gollub, E., Zalkin, H., Sprinson, D. B.: Correlation of genes and enzymes, and studies on regulation of the aromatic pathway in Salmonella. J. biol. Chem. 242, 5323–5328 (1967).

    PubMed  Google Scholar 

  • Hanes, C. S., Isherwood, F. A.: Separation of the phosphate esters on the filter paper chromatogram. Nature (Lond.) 164, 1107–1112 (1949).

    Google Scholar 

  • Hatch, M. D., Slack, C. R.: The participation of phosphoenolpyruvate synthetase in photosynthetic CO2-fixation of tropical grasses. Arch. Biochem. 120, 224–225 (1967).

    PubMed  Google Scholar 

  • Herman, N. J., Bell, E. J.: Metabolic control in Acinetobacter sp. I. Effect of C4 versus C2 and C3 substrates on isocitrate lyase synthesis. Canad. J. Microbiol. 16, 769–774 (1970).

    Google Scholar 

  • Hirsch, P.: CO2-Fixierung durch Knallgasbakterien. II. Chromatographischer Nachweis der frühzeitigen Fixierungsprodukte. Arch. Mikrobiol. 46, 53–78 (1963).

    PubMed  Google Scholar 

  • Kimberg, D. V., Yielding, K. L.: Pyruvate kinase. Structural and functional changes induced by diethylstilbestrol and certain steroid hormones. J. biol. Chem. 237, 3233–3239 (1962).

    PubMed  Google Scholar 

  • Maruyama, H., Easterday, R. L., Chang, H. C., Lane, M. D.: The enzymatic carboxylation of phosphoenolpyruvate. I. Purification and properties of phosphoenolpyruvate carboxylase. J. biol. Chem. 241, 2405–2412 (1966).

    PubMed  Google Scholar 

  • Metzner, H.: Papierchromatographische Trennung der Photosynthese-Intermediärprodukte. Naturwissenschaften 49, 183 (1962).

    Google Scholar 

  • O'Brien, R. W., Stern, J. R.: Role of sodium in determining alternate pathways of aerobic citrate catabolism in Aerobacter aerogenes. J. Bact. 99, 389–394 (1969).

    PubMed  Google Scholar 

  • Reeves, R. E.: A new enzyme with the glycolytic function of pyruvate kinase. J. biol. Chem. 243, 3202–3204 (1968).

    PubMed  Google Scholar 

  • —, Menzies, R. A., Hsu, D. S.: The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium. J. biol. Chem. 243, 5486–5491 (1968).

    PubMed  Google Scholar 

  • Slack, C. R.: The photoactivation of a phosphopyruvate synthase in leaves of Amaranthus palmeri. Biochem. biophys. Res. Commun. 30, 483–486 (1968).

    Google Scholar 

  • Smith, T. E.: Escherichia coli phosphoenolpyruvate carboxylase. Characterization and sedimentation behavior. Arch. Biochem. 128, 611–622 (1968).

    PubMed  Google Scholar 

  • Sprinson, D. B., Srinivasan, P. R., Katagiri, M.: 3-deoxy-d-arabinoheptulosonic acid 7-phosphate synthetase from Escherichia coli. In: S. P. Colowick, N. O. Kaplan, Methods in enzymology, Vol. 5, pp. 394–402. New York: Academic Press 1962.

    Google Scholar 

  • Srinivasan, P. R., Katagiri, M., Sprinson, D. B.: The conversion of phosphoenolpyruvic acid and d-erythrose 4-phosphate to 5-dehydroquinic acid. J. biol. Chem. 234, 713–715 (1959).

    PubMed  Google Scholar 

  • —, Sprinson, D. B.: 2-keto-3-deoxy-d-arabo-heptonic acid 7-phosphate synthetase. J. biol. Chem. 234, 716–722 (1959).

    PubMed  Google Scholar 

  • Taylor, C. B., Bailey, E.: Activation of liver pyruvate kinase by fructose 1,6-diphosphate. Biochem. J. 102, 32C (1967).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut für Mikrobiologie der Gesellschaft für Strahlen, Göttingen, Deutschland

    W. Frings & H. G. Schlegel

  2. Umweltforschung mbH München in Göttingen, Göttingen, Deutschland

    W. Frings & H. G. Schlegel

Authors
  1. W. Frings
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. H. G. Schlegel
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Frings, W., Schlegel, H.G. Synthese von Phosphoenolpyruvat aus Pyruvat durch Extrakte aus Hydrogenomonas eutropha Stamm H 16 . Archiv. Mikrobiol. 79, 220–230 (1971). https://doi.org/10.1007/BF00408785

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00408785

Search

Navigation