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.
Similar content being viewed by others
REFERENCES
Skarzynski, T., Moody, P. C., and Wonacott, A. J. (1987) J. Mol. Biol., 193, 171–187.
Skarzynski, T., and Wonacott, A. J. (1988) J. Mol. Biol., 203, 1097–1118.
Duee, E., Olivier-Deyris, L., Fanchon, E., Corbier, C., Branlant, G., and Dideberg, O. (1996) J. Mol. Biol., 257, 814–838.
Bernhard, S. A., and MacQuarrie, R. A. (1973) J. Mol. Biol., 74, 73–78.
Koshland, D. E., Jr., Nemethy, G., and Filmer, D. (1966) Biochemistry, 5, 365–385.
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.
Stallcup, W. B., and Koshland, D. E., Jr. (1973) J. Mol. Biol., 80, 41–62.
Convay, A., and Koshland, D. E., Jr. (1968) Biochemistry, 7, 4011–4023.
Malhotra, O. P., and Bernhard, S. A. (1973) Proc. Natl. Acad. Sci. USA, 70, 2077–2081.
Cardon, J. W., and Boyer, P. D. (1982) J. Biol. Chem., 257, 7615–7622.
Kellershohn, N., and Seydoux, F. J. (1979) Biochemistry, 18, 2465–2470.
Stallcup, W. B., and Koshland, D. E., Jr. (1972) Biochem. Biophys. Res. Commun., 49, 1108–1114.
Byers, L. D., and Koshland, D. E., Jr. (1975) Biochemistry, 14, 3661–3669.
Malhotra, O. P., Bernhard, S. A., and Seydoux, F. (1981) Biochimie, 63, 131–141.
Levitzki, A., and Koshland, D. E., Jr. (1978) Curr. Topics Cell Regul., 10, 1–40.
Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossmann, M. G. (1974) J. Mol. Biol., 90, 25–49.
Segal, H. L., and Boyer, P. D. (1953) J. Biol. Chem., 204, 265–281.
Garavito, R. M., Rossmann, M. G., Argos, P., and Eventoff, W. (1977) Biochemistry, 16, 5065–5071.
Branden, C.-I., and Eklund, H. (1980) in Dehydrogenases Requiring Nicotinamide Coenzymes ( Jeffery, J., ed.) Birkhauser Verlag, Basel, pp. 41–84.
Nagradova, N. K., and Asryants, R. A. (1975) Biochim. Biophys. Acta, 386, 365–368.
Nagradova, N. K., Asryants, R. A., Benkevich, N. V., and Safronova, M. I. (1976) FEBS Lett., 69, 246–248.
Nagradova, N. K., Asryants, R. A., and Benkevich, N. V. (1978) Biochim. Biophys. Acta, 527, 319–326.
Asryants, R. A., Benkevich, N. V., and Nagradova, N. K. (1983) Biokhimiya, 48, 193–200.
Asryants, R. A., Rychkova, O. Yu., and Nagradova, N. K. (1983) Biokhimiya, 48, 531–538.
Douzhenkova, I. V., Asryants, R. A., Muronetz, V. I., and Nagradova, N. K. (1986) Biokhimiya, 51, 1899–1907.
Douzhenkova, I. V., Asryants, R. A., and Nagradova, N. K. (1988) Biochim. Biophys. Acta, 957, 60–70.
Asryants, R. A., Ashmarina, L. I., Muronetz, V. I., and Nagradova, N. K. (1980) FEBS Lett., 118, 141–144.
Kuzminskaya, E. V., Asryants, R. A., and Nagradova, N. K. (1991) Biochim. Biophys. Acta, 1075, 123–130.
Banas, T., Krotkiewska, B., Marcinkowska, A., and Wolny, M. (1983) Acta Biochem. Pol., 30, 324–334.
Corbier, C., Michels, S., Wonacott, A. J., and Branlant, G. (1994) Biochemistry, 33, 3260–3265.
Yun, M., Park, C.-G., Kim, J.-Y., and Park, H.-W. (2000) Biochemistry, 39, 10702–10710.
Nagradova, N. K., and Schmalhausen, E. V. (1998) Biochemistry (Moscow), 63, 504–515.
Asryants, R. A., Kuzminskaya, E. V., Tishkov, V. I., Douzhenkova, I. V., and Nagradova, N. K. (1989) Biochim. Biophys. Acta, 997, 159–166.
Levitzki, A. (1973) Biochem. Biophys. Res. Commun., 54, 889–893.
Schlessinger, J., and Levitzki, A. (1974) J. Mol. Biol., 82, 547–561.
Levitzki, A. (1974) J. Mol. Biol., 90, 451–458.
Ivanov, M. V., Klichko, V. I., Nikulin, I. R., Asryants, R. A., and Nagradova, N. K. (1982) Eur. J. Biochem., 125, 291–297.
Klichko, V. I., Ivanov, M. V., and Nagradova, N. K. (1986) Biokhimiya, 51, 465–475.
Ivanov, M. V., Asryants, R. A., and Nagradova, N. K. (1976) Int. J. Biochem., 7, 473–478.
Ivanov, M. V., and Nagradova, N. K. (1977) Biokhimiya, 42, 211–222.
Henis, Y. I., and Levitzki, A. (1980) Eur. J. Biochem., 112, 59–73.
Gloggler, K. G., Balasubramanian, K., Beth, A., Park, J. H., and Trommer, W. E. (1982) Biochim. Biophys. Acta, 706, 197–202.
Biesecker, G., Harris, J. I., Tierry, J. C., Walker, J. E., and Wonacott, A. J. (1977) Nature, 266, 328–333.
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.
Ho, Y.-S., and Tsou, C.-L. (1979) Nature (London), 277, 245–246.
Kuzminskaya, E. V., Asryants, R. A., and Nagradova, N. K. (1992) Biochem. Biophys. Res. Commun., 187, 577–583.
Nagradova, N. K., Kuzminskaya, E. V., and Asryants, R. A. (1993) Biotechnol. Àppl. Biochem., 18, 157–163.
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.
Levashov, P. A., Schmalhausen, E. V., Muronetz, V. I., and Nagradova, N. K. (1995) Biochem. Mol. Biol. Int., 37, 991–1000.
Nagradova, N. K., Schmalhausen, E. V., Levashov, P. A., Asryants, R. A., and Muronetz, V. I. (1996) Biotechnol. Appl. Biochem., 61, 47–56.
Nagradova, N. K. (2000) FEBS Lett., 487, 327–332.
Viratelle, O. M., and Seydoux, F. (1975) J. Mol. Biol., 92, 193–205.
Martin, W., and Cerff, R. (1986) Eur. J. Biochem., 159, 323–331.
Ho, Y.-S., Liang, S. J., and Tsou, C. L. (1980) Biochim. Biophys. Acta, 613, 249–255.
Aletta, J. M., Cimato, T. R., and Ettinger, M. J. (1998) Trends Biochem. Sci., 23, 89–91.
Tang, J., Kao, P., and Herschman, H. R. (2000) J. Biol. Chem., 275, 19866–19876.
Zhang, X., Zhou, L., and Cheng, X. (2000) EMBO J., 19, 3509–3519.
Dryjanski, M., Lehmann, T., Abriola, D., and Pietruszko, R. (1999) J. Prot. Chem., 18, 627–636.
Zhou, J., and Weiner, H. (2000) Biochemistry, 39, 12019–12024.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Nagradova, N.K. Study of the Properties of Phosphorylating D-Glyceraldehyde-3-phosphate Dehydrogenase. Biochemistry (Moscow) 66, 1067–1076 (2001). https://doi.org/10.1023/A:1012472627801
Issue Date:
DOI: https://doi.org/10.1023/A:1012472627801