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Formation of pyrophosphate during ATP: Glutamine synthetase-adenylyltransferase-reaction in E. coli

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Summary

The ATP:glutamine synthetase adenylyltransferase reaction was studied with γ-32P-labelled ATP.ATP, phosphate, and pyrophosphate were separated by electrophoresis and the radioactivity of these substances was determined quantitatively. For each mole of AMP covalently attached to glutamine synthetase, one mole of pyrophosphate is formed. The equation for the reaction is therefore:

$$\begin{gathered} 12 ATP + glutamine synthetase \xrightarrow{{Mg + + , glutamine}} \hfill \\ glutamine synthetase( - AMP)_{12} + 12 pyrophosphate. \hfill \\ \end{gathered}$$

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References

  • Ebner, E., Gancedo, C., Holzer, H.: ATP: Glutamine Synthetase Adenylyltransferase (Escherichia coli B). In: Methods in Enzymology (S. P. Colowick, and N. O. Kaplan, eds.), vol. 17; Metabolism of Amino Acids and Amines (H. Tabor, and C. W. Tabor, eds.) New York: Academic Press 1970 (in press).

    Google Scholar 

  • Ebner, E., Wolf, D.: unpublished results.

  • Kingdon, H. S., Shapiro, B. M., Stadtman, E. R.: Regulation of glutamine synthetase, VIII. ATP:glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase. Proc. nat. Acad. Sci. (Wash.) 58, 1703–1710 (1967).

    Google Scholar 

  • Lamprecht, W., Trautschold, I.: Bestimmung mit Hexokinase und Zwischenferment. In: Bergmeyer, H. U.: Methoden der enzymatischen Analyse, S. 543–551. Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Mans, R. J., Novelli, G. D.: Measurement of the incorporation of radioactive amino acids into protein by a filterpaper disk method. Arch. Biochem. Biophys. 94, 48–53 (1961).

    Google Scholar 

  • Mantel, M., Holzer, H.: Reversibility of the ATP:glutamine synthetase adenylyltransferase reaction. Proc. nat. Acad. Sci. (Wash.) (in press) (1970).

  • Mecke, D., Holzer, H.: Repression und Inaktivierung von Glutaminsynthetase in Escherichia coli durch NH4 +. Biochim. biophys. Acta (Amst.) 122, 341–351 (1966).

    Google Scholar 

  • Mecke, D., Wulff, K., Liess, K., Holzer, H.: Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli. Biochem. biophys. Res. Commun. 24, 452–458 (1966).

    Google Scholar 

  • Shapiro, B. M., Ginsburg, A.: Effects of specific divalent cations on some physical and chemical properties of glutamine synthetase from Escherichia coli. Taut and relaxed enzyme forms. Biochemistry 7, 2153–2167 (1968).

    Google Scholar 

  • —, Kingdon, H. S., Stadtman, E. R.: Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proc. nat. Acad. Sci. (Wash.) 58, 642–649 (1967).

    Google Scholar 

  • Wulff, K.: Mechanismus der Regulation von Glutaminsynthetase in Escherichia coli durch enzymatisch katalysierte Inaktivierung. Dissertation, Naturwissenschaftlich-Mathematische Fakultät der Universität Freiburg i. Br. 1967.

  • —, Mecke, D., Holzer, H.: Mechanism of the enzymatic inactivation of glutamine synthetase from E. coli. Biochem. biophys. Res. Commun. 28, 740–745 (1967).

    Google Scholar 

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Heinrich, C.P., Battig, F.A., Mantel, M. et al. Formation of pyrophosphate during ATP: Glutamine synthetase-adenylyltransferase-reaction in E. coli . Archiv. Mikrobiol. 73, 104–110 (1970). https://doi.org/10.1007/BF00410313

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