Advertisement

Biochemistry (Moscow)

, Volume 75, Issue 8, pp 1014–1016 | Cite as

Inhibition of transketolase by hexacyanoferrate(III)

  • V. A. Yurshev
  • I. A. Sevostyanova
  • O. N. Solovjeva
  • G. A. KochetovEmail author
Article
  • 55 Downloads

Abstract

The effect of hexacyanoferrate(III) on the catalytic activity of transketolase has been studied. This oxidant inactivates only one of two active sites of the enzyme, the one with a higher affinity to the coenzyme (thiamine diphosphate). The second active site does not lose its catalytic activity. These observations indicate that the active sites of holotransketolase, being indiscernible by data of X-ray analysis, exhibit functional nonequivalence.

Key words

transketolase nonequivalence of active sites inhibitors hexacyanoferrate 

Abbreviations

TK

transketolase

TDP

thiamine diphosphate

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Horecker, B. L. (2002) J. Biol. Chem., 277, 47965–47971.CrossRefPubMedGoogle Scholar
  2. 2.
    Kochetov, G. A. (1982) Meth. Enzymol., 90, 209–223.CrossRefPubMedGoogle Scholar
  3. 3.
    Schenk, G., Duggleby, R., and Nixon, P. (1998) Int. J. Biochem. Cell. Biol., 30, 1297–1318.CrossRefPubMedGoogle Scholar
  4. 4.
    Kochetov, G. A., Meshalkina, L. E., and Usmanov, R. A. (1976) Biochem. Biophys. Res. Commun., 69, 836–843.CrossRefGoogle Scholar
  5. 5.
    Meshalkina, L. E., and Kochetov, G. A. (1979) Biochim. Biophys. Acta, 571, 218–223.PubMedGoogle Scholar
  6. 6.
    Lindqvist, Y., Schneider, G., Ermler, U., and Sundstrom, M. (1992) EMBO J., 11, 2373–2379.PubMedGoogle Scholar
  7. 7.
    Nikkola, M., Lindqvist, Y., and Schneider, G. (1994) J. Mol. Biol., 238, 387–404.CrossRefPubMedGoogle Scholar
  8. 8.
    Kochetov, G. A., and Philippov, P. P. (1970) Biochem. Biophys. Res. Commun., 38, 930–933.CrossRefPubMedGoogle Scholar
  9. 9.
    Datta, A., and Racker, E. (1961) J. Biol. Chem., 236, 617–623.PubMedGoogle Scholar
  10. 10.
    Esakova, O. A., Meshalkina, L. E., and Kochetov, G. A. (2005) Life Sci., 78, 8–13.CrossRefPubMedGoogle Scholar
  11. 11.
    Schneider, G., and Lindqvist, Y. (1998) Biochim. Biophys. Acta, 1385, 387–398.PubMedGoogle Scholar
  12. 12.
    Christen, Ph., Cogoli-Greuter, M., Healy, M., and Lubini, D. (1976) Eur. J. Biochem., 63, 223–231.CrossRefPubMedGoogle Scholar
  13. 13.
    Solovjeva, O. N. (2002) Biochemistry (Moscow), 67, 667–671.CrossRefGoogle Scholar
  14. 14.
    Heinrich, C., Noack, K., and Wiss, O. (1972) Biochem. Biophys. Res. Commun., 49, 1427–1432.CrossRefPubMedGoogle Scholar
  15. 15.
    Solovjeva, O. N., and Kochetov, G. A. (2008) J. Mol. Catal. B-Enzym., 54, 90–92.CrossRefGoogle Scholar
  16. 16.
    Kovina, M. V., and Kochetov, G. A. (1998) FEBS Let., 440, 81–84.CrossRefGoogle Scholar
  17. 17.
    Kovina, M. V., de Kok, A., Sevostyanova, I. A., Khailova, L. S., Belkina, N. V., and Kochetov, G. A. (2004) PROTEINS: Structure Function and Bioinformatics, 56, 338–345.CrossRefGoogle Scholar
  18. 18.
    Schellenberger, A. (1998) Biochim. Biophys. Acta, 1385, 177–186.PubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • V. A. Yurshev
    • 1
  • I. A. Sevostyanova
    • 1
  • O. N. Solovjeva
    • 1
  • G. A. Kochetov
    • 1
    Email author
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

Personalised recommendations