Advertisement

Excited-State vs Ground-State Structure of the Pyridoxal 5’-Phosphate Site in Glycogen Phosphorylase b

  • S. Veinberg
  • I. Z. Steinberg
  • S. Shaltiel
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Pyridoxal 5’-phosphate (PLP) is an essential constituent of glycogen phosphorylase (Baranowski et al., 1957). Removal of this cofactor from the enzyme, even under very mild, fully reversible conditions, results in an apoenzyme devoid of catalytic activity (Shaltiel et al., 1966; Hedrick et al., 1966). Furthermore, several properties of the PLP site suggest that the cofactor plays a key role in the enzyme by either participating directly in catalysis or by being involved in the transfer of a regulatory signal to or from the enzyme (cf. Shaltiel et al., 1972) .

Keywords

Circular Polarization Optical Activity Glycogen Phosphorylase Anisotropy Factor Circular Dichroism Measurement 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Arrio-Dupont, M.: Biochem. Biophys. Res. Commun. 44, 653 (1971)PubMedCrossRefGoogle Scholar
  2. Baranowski, T., Illingworth, B., Brown, D.H., Cori, C.F.: Biochim. Biophys. Acta 25, 16 (1957)PubMedCrossRefGoogle Scholar
  3. Carl Jones, D., Cowgill, R.W.: Biochemistry 10, 4276 (1971)CrossRefGoogle Scholar
  4. Cortijo, M., Shaltiel, S.: Europ. J. Biochem. 29, 134 (1972)Google Scholar
  5. Cortijo, M., Steinberg, I.Z., Shaltiel, S.: J.Biol. Chem. 246, 933 (1971)Google Scholar
  6. Cortijo, M., Llor, J., Gimenez, J.S., Garcia-Blanco, F.: Europ. J. Biochem., 65, 521 (1976)Google Scholar
  7. Feldman, K., Helmreich, E.J.M., unpubl. results Fischer, E.H., Krebs, E.G., Kent, A.B.: Biochem. Prep. 6, 68 (1958)Google Scholar
  8. Forrey, A.W., Sevilla, C.L., Saari, J.C., -Fischer, E.H.: Biochemistry 10, 3132 (1971)Google Scholar
  9. Gafni, A., Hardt, H., Schlessinger, J., Steinberg, I.Z.: Biochim. Biophys. Acta 387, 256 (1975)Google Scholar
  10. Gafni, A., Steinberg, I.Z.: Photochem. Photobiol. 15, 93 (1972)Google Scholar
  11. Hedrick, J.L., Shaltiel, S., Fischer, E.H.: Biochemistry 5, 2117 (1966)Google Scholar
  12. Honikel, K.O., Madsen, N.B.: J. Biol. Chem. 247, 1057 (1972)Google Scholar
  13. Johnson, G.F., Tu, J.I., Bartlett, M.L.S., Graves, D.J.: J. Biol. Chem. 245, 5560 (1970)Google Scholar
  14. Kent, A.B., Krebs, E.G., Fischer, E.H.: J. Biol. Chem. 232, 549 (1958)Google Scholar
  15. Krebs, E.G., Love, D.S., Bratvold, G.E., Trayser, K.A. ,~yer, W.L., Fischer, E.H.: Biochemistry 2, 1022 (1964)Google Scholar
  16. Pfeuffer, T., Ehrlich, J., Helmreich, E.J.M.: Biochemistry 11, 2136 (1972)Google Scholar
  17. Schlessinger, J., Steinberg, I.Z.: Proc. Nat. Acad. Sci. U.~ 69, 769 (1972)Google Scholar
  18. Schlessinger, J., Gafni, A., Steinberg, I.Z.: J. Am. Chem. Soc~96, 7396 (1974)Google Scholar
  19. Shaltiel, S., Cortijo, M.: Biochem. Biophys. Res. Commun. 41, 59~(1970)Google Scholar
  20. Shaltiel, S., Fischer, E.H.: Israel J. Chem., 127, p. 1 (1967)Google Scholar
  21. Shaltiel, S., Cortijo, M., Zaidenzaig, Y.: In: Metabolic Interconversion of Enzymes. Wieland, 0., Holzer, H., Helmreich, E.J.M. (eds.). Berlin: Springer, 1972, p. 73Google Scholar
  22. Shaltiel, S., Hedrick, J.L., Fischer, E.H.: Biochemistry 5, 2108 (1966)PubMedCrossRefGoogle Scholar
  23. Steinberg, I.Z.: In: Concepts of Biochemical Fluorescence. Chen, R., Edelhoch, H. (eds.). New York: Marcel Dekker, 1975Google Scholar
  24. Steinberg, I.Z., Gafni, A.: Rev. Sci. Instrum. 43, 409 (1972)CrossRefGoogle Scholar
  25. Veinberg, S., Shaltiel, S., Steinberg, I.Z.: Israel J. Chem., 421 (1974)Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1976

Authors and Affiliations

  • S. Veinberg
  • I. Z. Steinberg
  • S. Shaltiel

There are no affiliations available

Personalised recommendations