Advertisement

Biochemistry (Moscow)

, Volume 67, Issue 10, pp 1089–1098 | Cite as

Pyridoxal 5"-Phosphate as a Catalytic and Conformational Cofactor of Muscle Glycogen Phosphorylase b

  • N. B. Livanova
  • N. A. Chebotareva
  • T. B. Eronina
  • B. I. Kurganov
Article

Abstract

This review summarizes data on structure of muscle glycogen phosphorylase b and the role of the cofactor pyridoxal 5"-phosphate in catalysis and stabilizing the native conformation of the enzyme. Specific attention is paid to the stabilizing role of pyridoxal 5"-phosphate upon denaturation of phosphorylase b. Stability of holoenzyme, apoenzyme, and enzyme reduced by sodium borohydride is compared.

glycogen phosphorylase b mechanism of reaction pyridoxal 5"-phosphate regulation thermal inactivation quaternary structure 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

REFERENCES

  1. 1.
    Parnas, J. K., and Baranowski, T. (1935) Compt. Rend. Soc. Biol., 120, 307–311.Google Scholar
  2. 2.
    Cori, C. F., and Cori, G. T. (1936) Proc. Soc. Exp. Biol. Med., 34, 202–205.Google Scholar
  3. 3.
    Cori, G. T., Colowick, S. P., and Cori, C. F. (1938) J. Biol. Chem., 123, 381–389.Google Scholar
  4. 4.
    Cori, G. T., and Cori, C. F. (1945) J. Biol. Chem., 158, 324–332.Google Scholar
  5. 5.
    Madsen, N. B., and Cori, C. F. (1956) J. Biol. Chem., 223, 1055–1066.Google Scholar
  6. 6.
    Wang, J. H., Shonka, M. L., and Graves, D. J. (1965) Biochemistry, 4, 2296–2301.Google Scholar
  7. 7.
    Krebs, E. G., and Fischer, E. H. (1956) Biochim. Biophys. Acta, 20, 150–156.Google Scholar
  8. 8.
    Graves, D. J., and Wang, J. H. (1972) in The Enzymes (Boyer, P. D., ed.) Vol. 7, Academic Press, New York, pp. 435–482.Google Scholar
  9. 9.
    Dombradi, V. (1981) Int. J. Biochem., 13, 125–139.Google Scholar
  10. 10.
    Oikonomakos, N. G., Acharya, K. R., and Johnson, L. N. (1992) in Post–translational Modifications of Proteins (Harding, J. J., and Grabbe, M. J. C., eds.) CRC Press, Boca Raton, pp. 81–150.Google Scholar
  11. 11.
    Kurganov, B. I. (1995) in Proteins and Peptides (Ivanov, V. T., and Lipkin, V. M., eds.) Nauka, Moscow, pp. 109–117.Google Scholar
  12. 12.
    Livanova, N. B., and Kornilaev, B. A. (1996) Biochemistry (Moscow), 61, 1432–1442.Google Scholar
  13. 13.
    Morgan, H. E., and Parmeggiani, A. (1964) J. Biol. Chem., 239, 2440–2445.Google Scholar
  14. 14.
    Okazaki, T., Nakazawa, A., and Hayashi, O. (1968) J. Biol. Chem., 243, 5266–5271.Google Scholar
  15. 15.
    Silonova, G. V., and Lisovskaya, N. P. (1967) Doklady AN SSSR, 174, 718–721.Google Scholar
  16. 16.
    Klinov, S. V., Chebotareva, N. A., Kurganov, B. I., Litvak, Zh. I., Zhilina, T. A., Glebova, G. D., Pekel, N. D., and Beresovskii, V. M. (1984) Bioorg. Khim., 10, 1161–1170.Google Scholar
  17. 17.
    Cori, G. T., Colowick, S. P., and Cori, C. F. (1939) J. Biol. Chem., 127, 771–782.Google Scholar
  18. 18.
    Kasvinsky, P. J., Madsen, N. B., and Fletterick, R. J. (1978) J. Biol. Chem., 253, 1290–1296.Google Scholar
  19. 19.
    Cohen, P., Duewer, T., and Fischer, E. H. (1971) Biochemistry, 10, 2683–2694.Google Scholar
  20. 20.
    Silonova, G. V., and Kurganov, B. I. (1970) Mol. Biol. (Moscow), 4, 445–459.Google Scholar
  21. 21.
    Feldmann, K., Zeisel, H., and Helmreich, E. (1972) Proc. Natl. Acad. Sci. USA, 69, 2278–2282.Google Scholar
  22. 22.
    Titani, K., Koide, A., Hermann, J., Ericsson, L. H., Kumar, S., Wade, R. D., Walsh, K. A., Neurath, H., and Fischer, E. H. (1977) Proc. Natl. Acad. Sci. USA, 74, 4762–4766.Google Scholar
  23. 23.
    Nakano, K., Hwang, P. K., and Fletteric, R. J. (1986) FEBS Lett., 204, 283–287.Google Scholar
  24. 24.
    Barford, D., and Johnson, L. N. (1992) Protein Sci., 1, 472–493.Google Scholar
  25. 25.
    Johnson, G. F., Tu, J. I., Bartlett, M. L., and Graves, D. J. (1970) J. Biol. Chem., 245, 5560–5568.Google Scholar
  26. 26.
    Johnson, L. N., and Barford, D. (1990) J. Biol. Chem., 265, 2409–2412.Google Scholar
  27. 27.
    Barford, D., and Johnson, L. N. (1989) Nature, 340, 609–616.Google Scholar
  28. 28.
    Kasvinsky, P. J., Shechosky, S., and Fletterick, R. J. (1978) J. Biol. Chem., 253, 9102–9106.Google Scholar
  29. 29.
    Sprang, S., Fletterick, R., Stern, M., Yang, D., Madsen, N. B., and Sturtevant, J. (1982) Biochemistry, 21, 2036–2048.Google Scholar
  30. 30.
    Meyer, F., Heilmeyer, L. M. G., Jr., Haschke, R. H., and Fischer, E. H. (1970) J. Biol. Chem., 245, 6642–6648.Google Scholar
  31. 31.
    Helmreich, E., Michaelides, M. C., and Cori, C. F. (1967) Biochemistry, 6, 3695–3710.Google Scholar
  32. 32.
    Baranowski, T., Illingworth, B., Brown, D. H., and Cori, C. F. (1957) Biochim. Biophys. Acta, 25, 16–21.Google Scholar
  33. 33.
    Helmreich, E. J. M. (1992) BioFactors, 3, 159–172.Google Scholar
  34. 34.
    Braunstein, A. E., and Shemyakin, M. M. (1952) Doklady AN SSSR, 85, 1115–1118.Google Scholar
  35. 35.
    Braunstein, A. E., and Shemyakin, M. M. (1953) Biokhimiya, 18, 393–411.Google Scholar
  36. 36.
    Braunstein, A. E. (1973) The Enzymes (Boyer, P. D., ed.) Vol. 9, Academic Press, N. Y., pp. 379–481.Google Scholar
  37. 37.
    Snell, E. E. (1958) Vitamins and Hormones, 16, 77–125.Google Scholar
  38. 38.
    Fisher, E. H., Kent, A., Snyder, E., and Krebs, E. G. (1958) J. Am. Chem. Soc., 80, 2906.Google Scholar
  39. 39.
    Hedrick, J. L., Shaltiel, S., and Fischer, E. H. (1966) Biochemistry, 5, 2117–2125.Google Scholar
  40. 40.
    Feldman, K., Zeisel, H., and Helmreich, E. J. M. (1976) Eur. J. Biochem., 65, 285–291.Google Scholar
  41. 41.
    Shaltiel, S., Hedrick, J. L., Pocker, A., and Fischer, E. H. (1969) Biochemistry, 8, 5189–5196.Google Scholar
  42. 42.
    Graves, D. J., Parrish, R. F., Uhing, R. J., and Korytnyk, W. (1976) in Regulatory Mechanism of Carbohydrate Metabolism (Essmann, V., ed.) Pergamon Press, Oxford, pp. 195–204.Google Scholar
  43. 43.
    Parrish, R. F., Uhing, R. J., and Graves, D. J. (1977) Biochemistry, 16, 4824–4831.Google Scholar
  44. 44.
    Chang, Y. C., McCalmont, T., and Graves, D. J. (1983) Biochemistry, 22, 4987–4993.Google Scholar
  45. 45.
    Johnson, L. N., Hajdu, J., Acharya, K. R., Stuart, D. I., McLaughlin, P. I., and Barford, D. (1989) in Allosteric Enzymes (Herve, G., ed.) CRC Press, Boca Raton, pp. 81–127.Google Scholar
  46. 46.
    Helmreich, E., and Cori, C. F. (1964) Proc. Natl. Acad. Sci. USA, 51, 131–138.Google Scholar
  47. 47.
    Kastenschmidt, L. L., Kastenschmidt, J., and Helmreich, E. (1968) Biochemistry, 7, 4543–4556.Google Scholar
  48. 48.
    Feldmann, K., and Hull, W. E. (1977) Proc. Natl. Acad. Sci. USA, 74, 836–860.Google Scholar
  49. 49.
    Feldmann, K., Hörl, M., Klein, H. W., and Helmreich, E. J. M. (1978) Proc. FEBS, 42, 205–218.Google Scholar
  50. 50.
    Helmreich, E. J. M., and Klein, H. W. (1980) Angew. Chem. Int. Ed. Engl., 19, 441–455.Google Scholar
  51. 51.
    Palm, D., Klein, H. W., Schinzel, R., Buehner, M., and Helmreich, E. J. M. (1990) Biochemistry, 29, 1099–1106.Google Scholar
  52. 52.
    Lisovskaya, N. P., and Silonova, G. V. (1970) Biokhimiya, 35, 448–457.Google Scholar
  53. 53.
    Kurganov, B. I., Klinov, S. V., and Chebotareva, N. A. (1994) Uspekhi Biol. Khim., 34, 83–110.Google Scholar
  54. 54.
    Chebotareva, N. A., Klinov, S. V., and Kurganov, B. I. (2001) Biotech. Genet. Eng. Rev., 18, 265–297.Google Scholar
  55. 55.
    Cori, C. F., and Illingworth, B. (1957) Proc. Natl. Acad. Sci. USA, 43, 547–552.Google Scholar
  56. 56.
    Shaltiel, Sh., Hedrick, J. L., and Fischer, E. H. (1966) Biochemistry, 5, 2108–2116.Google Scholar
  57. 57.
    Chebotareva, N. A., Sugrobova, N. P., Bulanova, L. N., Poznanskaya, A. A., Kurganov, B. I., and Gunar, V. I. (1995) Biochemistry (Moscow), 60, 1551–1558.Google Scholar
  58. 58.
    Gunar, V. I., Sugrobova, N. P., Chebotareva, N. A., Stepanova, S. V., Poznanskaya, A. A., and Kurganov, B. I. (1990) in Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors (Fukui, T., Kagamiyama, H., Soda, K., and Wada, H., eds.) Pergamon Press, Oxford, pp. 417–419.Google Scholar
  59. 59.
    Chebotareva, N. A., Sugrobova, N. P., Poznanskaya, A. A., Bulanova, L. N., Lyubarev, A. E., and Gunar, V. I. (1994) Doklady AN SSSR, 335, 255–257.Google Scholar
  60. 60.
    Weisshaar, H. D., and Palm, D. (1972) Biochemistry, 11, 2146–2154.Google Scholar
  61. 61.
    Avramovic–Zikic, O., Smillie, L. B., and Madsen, N. B. (1970) J. Biol. Chem., 245, 1558–1565.Google Scholar
  62. 62.
    Chebotareva, N. A., Kurganov, B. I., Lyubarev, A. E., Davidov, D. R., and Pekel, N. D. (1991) Biochimie, 73, 1329–1343.Google Scholar
  63. 63.
    Kurganov, B. I., Kornilaev, B. A., Chebotareva, N. A., Malikov, V. P., Orlov, V. N., Lyubarev, A. E., and Livanova, N. B. (2000) Biochemistry, 39, 13144–13152.Google Scholar
  64. 64.
    Kornilaev, B. A., Kurganov, B. I., Eronina, T. B., and Livanova, N. B. (1996) Biochemistry (Moscow), 61, 628–634.Google Scholar
  65. 65.
    Kornilaev, B. A., Kurganov, B. I., Eronina, T. B., Chebotareva, N. A., Livanova, N. B., Orlov, V. N., and Chernyak, V. Ya. (1997) Mol. Biol. (Moscow), 31, 98–107.Google Scholar
  66. 66.
    Kornilaev, B. A., Kurganov, B. I., Livanova, N. B., Eronina, T. B., Orlov, V. N., Chernyak, V. Ya., and Poglazov, B. F. (1997) Doklady RAN, 352, 256–258.Google Scholar
  67. 67.
    DeVincenzi, D. L., and Hedrick, J. L. (1970) Biochemistry, 9, 2048–2058.Google Scholar
  68. 68.
    Eronina, T. B., Chebotareva, N. A., Livanova, N. B., and Kurganov, B. I. (2001) Biochemistry (Moscow), 66, 449–455.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2002

Authors and Affiliations

  • N. B. Livanova
    • 1
  • N. A. Chebotareva
    • 1
  • T. B. Eronina
    • 1
  • B. I. Kurganov
    • 1
  1. 1.Bach Institute of BiochemistryRussian Academy of SciencesMoscowRussia

Personalised recommendations