The Protein Journal

, Volume 31, Issue 2, pp 137–140 | Cite as

Effects of Free Ca2+ on Kinetic Characteristics of Holotransketolase

  • Olga N. Solovjeva
  • Irina A. Sevostyanova
  • Vladimir A. Yurshev
  • Vitalii A. Selivanov
  • German A. Kochetov


Catalytic activity has been demonstrated for holotransketolase in the absence of free bivalent cations in the medium. The two active centers of the enzyme are equivalent in both the catalytic activity and the affinity for the substrates. In the presence of free Ca2+ (added to the medium from an external source), this equivalence is lost: negative cooperativity is induced on binding of either xylulose 5-phosphate (donor substrate) or ribose 5-phosphate (acceptor substrate), whereupon the catalytic conversion of the bound substrates causes the interaction between the centers to become positively cooperative. Moreover, the enzyme total activity increase is observed.


Calcium ions Kinetic parameters Negative cooperativity Positively cooperative Transketolase 





Thiamine diphosphate


Ribose 5-phosphate


Xylulose 5-phosphate



This work was supported by a grant from the Russian Foundation for Basic Research (projects No. 09-04-00544).


  1. 1.
    Esakova OA, Meshalkina LE, Kochetov GA (2005) Life Sci 78:8–13CrossRefGoogle Scholar
  2. 2.
    Heinrich CP, Noack K, Wiss O (1972) Biochem Biophys Res Commun 49:1427–1432CrossRefGoogle Scholar
  3. 3.
    Heinrich C, Schmidt D (1973) Experientia 29:1226–1227CrossRefGoogle Scholar
  4. 4.
    Heinrich H, Steffen H, Janser P, Wiss O (1972) Eur J Biochem 30:533–541CrossRefGoogle Scholar
  5. 5.
    Kochetov GA (1982) Methods Enzym 90:209–223CrossRefGoogle Scholar
  6. 6.
    Kochetov GA, Philippov PP (1970) Biochem Biophys Res Commun 38:930–933CrossRefGoogle Scholar
  7. 7.
    Kochetov GA, Philippov PP (1970) Dokl Acad Nauk USSR 19:1234–1236Google Scholar
  8. 8.
    Kochetov GA, Meshalkina LE, Usmanov RA (1976) Biochem Biophys Res Commun 69:836–843CrossRefGoogle Scholar
  9. 9.
    Kochetov GA, Tikhomirova NK, Philippov PP (1975) Biochem Biophys Res Commun 63:924–930CrossRefGoogle Scholar
  10. 10.
    Lindqvist Y, Schneider G, Ermler V, Sundström M (1992) EMBO J 11:2373–2379Google Scholar
  11. 11.
    Meshalkina LE, Kochetov GA (1979) Dokl Acad Nauk USSR 248:1482–1486Google Scholar
  12. 12.
    Nikkola M, Lindqvist Y, Schneider G (1994) J Mol Biol 238:387–404CrossRefGoogle Scholar
  13. 13.
    Philippov PP, Tikhomirova NK, Kochetov GA (1978) Physico-Chem Methods of Mol Biol pp 57–64, Moscow State University, MoscowGoogle Scholar
  14. 14.
    Selivanov VA, Kovina MV, Kochevova NV, Meshalkina LE, Kochetov GA (2004) FEBS Lett 567:270–274CrossRefGoogle Scholar
  15. 15.
    Selivanov VA, Kovina MV, Kochevova NV, Meshalkina LE, Kochetov GA (2003) J Mol Catal. B Enzym 26:33–40CrossRefGoogle Scholar
  16. 16.
    Schneider G, Lindqvist Y (1998) Biochim Biophys Acta 1385:387–398CrossRefGoogle Scholar
  17. 17.
    Schenk G, Duggleby RG, Nixon PF (1998) Int J Biochem Cell Biol 30:1297–1318CrossRefGoogle Scholar
  18. 18.
    Solovieva ON (2002) Biochemistry (Moscow) 67:667–671CrossRefGoogle Scholar
  19. 19.
    Solovieva ON, Bykova IA, Meshalkina LE, Kovina MV, Kochetov GA (2001) Biochemistry (Moscow) 66:932–936CrossRefGoogle Scholar
  20. 20.
    Solovieva ON, Kochetov GA (2008) J Mol Catal B Enzym 54:90–92CrossRefGoogle Scholar
  21. 21.
    Sundström M, Lindqvist Y, Schneider G, Hellman U, Ronne H (1993) J Biol Chem 268:24346–24352Google Scholar
  22. 22.
    Yonatt J (1993) Critical Rev Microbiol 19:83–97CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Olga N. Solovjeva
    • 1
  • Irina A. Sevostyanova
    • 1
  • Vladimir A. Yurshev
    • 1
  • Vitalii A. Selivanov
    • 1
  • German A. Kochetov
    • 1
  1. 1.A.N. Belozersky Institute of Physico-chemical BiologyMoscow State UniversityMoscowRussia

Personalised recommendations