Advertisement

Biochemistry (Moscow)

, 76:1061 | Cite as

Interaction of transketolase from human tissues with substrates

  • L. E. MeshalkinaEmail author
  • O. N. Solovjeva
  • G. A. Kochetov
Article
  • 82 Downloads

Abstract

The Michaelis constant values for substrates of transketolase from human tissues were determined over a wide range of substrate concentrations. It is shown that K m values determined by other authors are significantly overestimated and explained why this is so.

Key words

human tissues transketolase thiamine diphosphate Km for substrates of human tissues transketolase 

Abbreviations

DOETDP

α,β-dioxyethylthiamine diphosphate

DTT

dithiothreitol

F-6-P

fructose-6-phosphate

GAPD

glyceraldehyde-3-phosphate dehydrogenase

hTK

human transketolase

R-5-P

ribose-5-phosphate

sTK

Saccharomyces cerevisiae transketolase

TDP

thiamine diphosphate

TK

transketolase

X-5-P

xylulose-5-phosphate

References

  1. 1.
    Datta, A. G., and Racker, E. (1961) J. Biol. Chem., 236, 617–628.PubMedGoogle Scholar
  2. 2.
    Kochetov, G. A. (1982) Methods Enzymol., 90, 209–223.PubMedCrossRefGoogle Scholar
  3. 3.
    Kochetov, G. A. (1986) Biokhimiya, 51, 2010–2029.Google Scholar
  4. 4.
    Schenk, G., Duggleby, R., and Nixon, P. (1998) Int. J. Biochem. Cell Biol., 30, 1297–1318.PubMedCrossRefGoogle Scholar
  5. 5.
    Lindqvist, Y., Schneider, G., Ermler, V., and Sundstrom, M. (1992) EMBO J., 11, 2373–2379.PubMedGoogle Scholar
  6. 6.
    Nikkola, M., Lindqvist, Y., and Schneider, G. (1994) J. Mol. Biol., 238, 387–404.PubMedCrossRefGoogle Scholar
  7. 7.
    Sundstrom, M., Lindqvist, Y., and Schneider, G. (1992) FEBS Lett., 313, 229–231.PubMedCrossRefGoogle Scholar
  8. 8.
    Nilsson, U., Lindqvist, Y., Kluger, R., and Schneider, G. (1993) FEBS Lett., 326, 145–148.PubMedCrossRefGoogle Scholar
  9. 9.
    Konig, S., Schellenberger, A., Neef, H., and Schneider, G. (1994) J. Biol. Chem., 269, 10879–10882.PubMedGoogle Scholar
  10. 10.
    Nilsson, U., Meshalkina, L., Lindqvist, Y., and Schneider, G. (1997) J. Biol. Chem., 272, 1864–1869.PubMedCrossRefGoogle Scholar
  11. 11.
    Schenk, G., Duggleby, R. G., and Nixon, P. F. (1998) Jnt. J. Biochem. Cell. Biol., 30, 369–378.CrossRefGoogle Scholar
  12. 12.
    Obiol-Pardo, C., and Rubio-Martinez, J. (2009) J. Mol. Graph. Model., 27, 723–734.PubMedCrossRefGoogle Scholar
  13. 13.
    McCool, B. A., Plonk, S. G., Martin, P. R., and Singleton, C. K. (1993) J. Biol. Chem., 268, 1397–1404.PubMedGoogle Scholar
  14. 14.
    Kaufman, K. A., and Harper, C. (2009) Int. J. Biochem. Cell Biol., 41, 717–720.CrossRefGoogle Scholar
  15. 15.
    Coy, J. F., Dressler, D., Wilde, J., and Schubert, P. (2005) Clin. Lab., 51, 257–273.PubMedGoogle Scholar
  16. 16.
    Zerilli, M., Amato, M. C., Martorana, A., Cabibi, D., Coy, J. F., Cappello, F., Pompei, G., Russo, A., Giordano, C., and Rodolico, V. (2008) Cancer, 113, 936–944.PubMedCrossRefGoogle Scholar
  17. 17.
    Xiaojun, X., Zur Hausen, A., Coy, J. F., and Lochelt, M. (2009) Int. J. Cancer, 124, 1330–1337.CrossRefGoogle Scholar
  18. 18.
    Meshalkina, L. E., Solovjeva, O. N., Khodak, Yu. A., Drutsa, V. L., and Kochetov, G. A. (2010) Biochemistry (Moscow), 75, 873–880.CrossRefGoogle Scholar
  19. 19.
    Mitschke, L., Parthier, C., Schroder-Tittmann, K., Coy, J., Ludtke, S., and Tittmann, K. (2010) J. Biol. Chem., 285, 31559–31570.PubMedCrossRefGoogle Scholar
  20. 20.
    Solovjeva, O. N., and Kochetov, G. A. (2008) J. Mol. Cat.: B Enzymatic, 54, 90–92.CrossRefGoogle Scholar
  21. 21.
    Gasteiger, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., and Bairoch, A. (2005) The Proteomics. Protocols Handbook, Humana Press, Totowa, New Jersey, pp. 571–607.CrossRefGoogle Scholar
  22. 22.
    Usmanov, R. A., and Kochetov, G. A. (1981) Biochem. Int., 3, 33–39.Google Scholar
  23. 23.
    Singleton, C. K., Wang, J. J., Shan, L., and Martin, P. R. (1996) Biochemistry, 35, 15865–15869.PubMedCrossRefGoogle Scholar
  24. 24.
    Takeuchi, T., Nishimo, K., and Itokawa, Y. (1986) Biochim. Biophys. Acta, 872, 24–32.PubMedCrossRefGoogle Scholar
  25. 25.
    Paoletti, F., Mocali, A., Marchi, M., and Truchi, F. (1989) Biochem. Biophys. Res. Commun., 161, 150–155.PubMedCrossRefGoogle Scholar
  26. 26.
    Tate, J. R., and Nixon, P. F. (1987) Anal. Biochem., 160, 78–87.PubMedCrossRefGoogle Scholar
  27. 27.
    Solovjeva, O. N., Meshalkina, L. A., Kovina, M. V., Selivanov, V. A., Bykova, I. A., and Kochetov, G. A. (2000) Biochemistry (Moscow), 65, 1202–1205.Google Scholar
  28. 28.
    Hanes, C. S. (1932) Biochem. J., 26, 1406–1421.PubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • L. E. Meshalkina
    • 1
    Email author
  • O. N. Solovjeva
    • 1
  • G. A. Kochetov
    • 1
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

Personalised recommendations