Biochemistry (Moscow)

, Volume 66, Issue 10, pp 1067–1076 | Cite as

Study of the Properties of Phosphorylating D-Glyceraldehyde-3-phosphate Dehydrogenase

  • N. K. Nagradova
Article

Abstract

The properties of the active center of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are considered with emphasis on the structure of anion-binding sites and their role in catalysis. The results of studies on the molecular mechanism of the effect of NAD+ on the enzyme conformation are discussed. Experimental evidence is presented supporting the idea that negative cooperativity of NAD+ binding and half-of-the-sites reactivity exhibited by GAPDH are generated by different mechanisms. Data obtained with rabbit muscle and Escherichia coli GAPDH point to preexisting asymmetry in these tetramers. Structural determinants that can control the transition of the tetramer from the symmetric to the asymmetric state were found.

D-glyceraldehyde-3-phosphate dehydrogenase catalytic mechanism active center domains half-of-the-sites reactivity preexisting asymmetry 

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REFERENCES

  1. 1.
    Skarzynski, T., Moody, P. C., and Wonacott, A. J. (1987) J. Mol. Biol., 193, 171–187.Google Scholar
  2. 2.
    Skarzynski, T., and Wonacott, A. J. (1988) J. Mol. Biol., 203, 1097–1118.Google Scholar
  3. 3.
    Duee, E., Olivier-Deyris, L., Fanchon, E., Corbier, C., Branlant, G., and Dideberg, O. (1996) J. Mol. Biol., 257, 814–838.Google Scholar
  4. 4.
    Bernhard, S. A., and MacQuarrie, R. A. (1973) J. Mol. Biol., 74, 73–78.Google Scholar
  5. 5.
    Koshland, D. E., Jr., Nemethy, G., and Filmer, D. (1966) Biochemistry, 5, 365–385.Google Scholar
  6. 6.
    Seydoux, F., Malhotra, O. P., and Bernhard, S. A. (1974) in CRC Critical Reviews in Biochemistry ( Fasman, G. D., ed.) Vol. 2, CRC Press, Cleveland, Ohio, pp. 227–257.Google Scholar
  7. 7.
    Stallcup, W. B., and Koshland, D. E., Jr. (1973) J. Mol. Biol., 80, 41–62.Google Scholar
  8. 8.
    Convay, A., and Koshland, D. E., Jr. (1968) Biochemistry, 7, 4011–4023.Google Scholar
  9. 9.
    Malhotra, O. P., and Bernhard, S. A. (1973) Proc. Natl. Acad. Sci. USA, 70, 2077–2081.Google Scholar
  10. 10.
    Cardon, J. W., and Boyer, P. D. (1982) J. Biol. Chem., 257, 7615–7622.Google Scholar
  11. 11.
    Kellershohn, N., and Seydoux, F. J. (1979) Biochemistry, 18, 2465–2470.Google Scholar
  12. 12.
    Stallcup, W. B., and Koshland, D. E., Jr. (1972) Biochem. Biophys. Res. Commun., 49, 1108–1114.Google Scholar
  13. 13.
    Byers, L. D., and Koshland, D. E., Jr. (1975) Biochemistry, 14, 3661–3669.Google Scholar
  14. 14.
    Malhotra, O. P., Bernhard, S. A., and Seydoux, F. (1981) Biochimie, 63, 131–141.Google Scholar
  15. 15.
    Levitzki, A., and Koshland, D. E., Jr. (1978) Curr. Topics Cell Regul., 10, 1–40.Google Scholar
  16. 16.
    Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossmann, M. G. (1974) J. Mol. Biol., 90, 25–49.Google Scholar
  17. 17.
    Segal, H. L., and Boyer, P. D. (1953) J. Biol. Chem., 204, 265–281.Google Scholar
  18. 18.
    Garavito, R. M., Rossmann, M. G., Argos, P., and Eventoff, W. (1977) Biochemistry, 16, 5065–5071.Google Scholar
  19. 19.
    Branden, C.-I., and Eklund, H. (1980) in Dehydrogenases Requiring Nicotinamide Coenzymes ( Jeffery, J., ed.) Birkhauser Verlag, Basel, pp. 41–84.Google Scholar
  20. 20.
    Nagradova, N. K., and Asryants, R. A. (1975) Biochim. Biophys. Acta, 386, 365–368.Google Scholar
  21. 21.
    Nagradova, N. K., Asryants, R. A., Benkevich, N. V., and Safronova, M. I. (1976) FEBS Lett., 69, 246–248.Google Scholar
  22. 22.
    Nagradova, N. K., Asryants, R. A., and Benkevich, N. V. (1978) Biochim. Biophys. Acta, 527, 319–326.Google Scholar
  23. 23.
    Asryants, R. A., Benkevich, N. V., and Nagradova, N. K. (1983) Biokhimiya, 48, 193–200.Google Scholar
  24. 24.
    Asryants, R. A., Rychkova, O. Yu., and Nagradova, N. K. (1983) Biokhimiya, 48, 531–538.Google Scholar
  25. 25.
    Douzhenkova, I. V., Asryants, R. A., Muronetz, V. I., and Nagradova, N. K. (1986) Biokhimiya, 51, 1899–1907.Google Scholar
  26. 26.
    Douzhenkova, I. V., Asryants, R. A., and Nagradova, N. K. (1988) Biochim. Biophys. Acta, 957, 60–70.Google Scholar
  27. 27.
    Asryants, R. A., Ashmarina, L. I., Muronetz, V. I., and Nagradova, N. K. (1980) FEBS Lett., 118, 141–144.Google Scholar
  28. 28.
    Kuzminskaya, E. V., Asryants, R. A., and Nagradova, N. K. (1991) Biochim. Biophys. Acta, 1075, 123–130.Google Scholar
  29. 29.
    Banas, T., Krotkiewska, B., Marcinkowska, A., and Wolny, M. (1983) Acta Biochem. Pol., 30, 324–334.Google Scholar
  30. 30.
    Corbier, C., Michels, S., Wonacott, A. J., and Branlant, G. (1994) Biochemistry, 33, 3260–3265.Google Scholar
  31. 31.
    Yun, M., Park, C.-G., Kim, J.-Y., and Park, H.-W. (2000) Biochemistry, 39, 10702–10710.Google Scholar
  32. 32.
    Nagradova, N. K., and Schmalhausen, E. V. (1998) Biochemistry (Moscow), 63, 504–515.Google Scholar
  33. 33.
    Asryants, R. A., Kuzminskaya, E. V., Tishkov, V. I., Douzhenkova, I. V., and Nagradova, N. K. (1989) Biochim. Biophys. Acta, 997, 159–166.Google Scholar
  34. 34.
    Levitzki, A. (1973) Biochem. Biophys. Res. Commun., 54, 889–893.Google Scholar
  35. 35.
    Schlessinger, J., and Levitzki, A. (1974) J. Mol. Biol., 82, 547–561.Google Scholar
  36. 36.
    Levitzki, A. (1974) J. Mol. Biol., 90, 451–458.Google Scholar
  37. 37.
    Ivanov, M. V., Klichko, V. I., Nikulin, I. R., Asryants, R. A., and Nagradova, N. K. (1982) Eur. J. Biochem., 125, 291–297.Google Scholar
  38. 38.
    Klichko, V. I., Ivanov, M. V., and Nagradova, N. K. (1986) Biokhimiya, 51, 465–475.Google Scholar
  39. 39.
    Ivanov, M. V., Asryants, R. A., and Nagradova, N. K. (1976) Int. J. Biochem., 7, 473–478.Google Scholar
  40. 40.
    Ivanov, M. V., and Nagradova, N. K. (1977) Biokhimiya, 42, 211–222.Google Scholar
  41. 41.
    Henis, Y. I., and Levitzki, A. (1980) Eur. J. Biochem., 112, 59–73.Google Scholar
  42. 42.
    Gloggler, K. G., Balasubramanian, K., Beth, A., Park, J. H., and Trommer, W. E. (1982) Biochim. Biophys. Acta, 706, 197–202.Google Scholar
  43. 43.
    Biesecker, G., Harris, J. I., Tierry, J. C., Walker, J. E., and Wonacott, A. J. (1977) Nature, 266, 328–333.Google Scholar
  44. 44.
    Levashov, P. A., Orlov, V. N., Boschi-Muller, S., Talfournier, F., Asryants, R. A., Bulatnikov, I. G., Muronetz, V. I., Branlant, G., and Nagradova, N. K. (1999) Biochim. Biophys. Acta, 1433, 294–306.Google Scholar
  45. 45.
    Ho, Y.-S., and Tsou, C.-L. (1979) Nature (London), 277, 245–246.Google Scholar
  46. 46.
    Kuzminskaya, E. V., Asryants, R. A., and Nagradova, N. K. (1992) Biochem. Biophys. Res. Commun., 187, 577–583.Google Scholar
  47. 47.
    Nagradova, N. K., Kuzminskaya, E. V., and Asryants, R. A. (1993) Biotechnol. Àppl. Biochem., 18, 157–163.Google Scholar
  48. 48.
    Nagradova, N. K., Asryants, R. A., Kuzminskaya, E. V., Ashmarina, L. I., and Muronetz, V. I. (1996) in Chemical Modification of Enzymes ( Kurganov, B. I., Nagradova, N. K., and Lavrik, O. I., eds.) Nova Science Publishers, Inc., New York, pp. 59–125.Google Scholar
  49. 49.
    Levashov, P. A., Schmalhausen, E. V., Muronetz, V. I., and Nagradova, N. K. (1995) Biochem. Mol. Biol. Int., 37, 991–1000.Google Scholar
  50. 50.
    Nagradova, N. K., Schmalhausen, E. V., Levashov, P. A., Asryants, R. A., and Muronetz, V. I. (1996) Biotechnol. Appl. Biochem., 61, 47–56.Google Scholar
  51. 51.
    Nagradova, N. K. (2000) FEBS Lett., 487, 327–332.Google Scholar
  52. 52.
    Viratelle, O. M., and Seydoux, F. (1975) J. Mol. Biol., 92, 193–205.Google Scholar
  53. 53.
    Martin, W., and Cerff, R. (1986) Eur. J. Biochem., 159, 323–331.Google Scholar
  54. 54.
    Ho, Y.-S., Liang, S. J., and Tsou, C. L. (1980) Biochim. Biophys. Acta, 613, 249–255.Google Scholar
  55. 55.
    Aletta, J. M., Cimato, T. R., and Ettinger, M. J. (1998) Trends Biochem. Sci., 23, 89–91.Google Scholar
  56. 56.
    Tang, J., Kao, P., and Herschman, H. R. (2000) J. Biol. Chem., 275, 19866–19876.Google Scholar
  57. 57.
    Zhang, X., Zhou, L., and Cheng, X. (2000) EMBO J., 19, 3509–3519.Google Scholar
  58. 58.
    Dryjanski, M., Lehmann, T., Abriola, D., and Pietruszko, R. (1999) J. Prot. Chem., 18, 627–636.Google Scholar
  59. 59.
    Zhou, J., and Weiner, H. (2000) Biochemistry, 39, 12019–12024.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2001

Authors and Affiliations

  • N. K. Nagradova
    • 1
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

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