Biochemistry (Moscow)

, Volume 74, Issue 7, pp 789–792

Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae

  • I. A. Sevostyanova
  • V. A. Selivanov
  • V. A. Yurshev
  • O. N. Solovjeva
  • S. V. Zabrodskaya
  • G. A. Kochetov
Article

DOI: 10.1134/S0006297909070128

Cite this article as:
Sevostyanova, I.A., Selivanov, V.A., Yurshev, V.A. et al. Biochemistry Moscow (2009) 74: 789. doi:10.1134/S0006297909070128

Abstract

Catalytic activity of two active sites of transketolase and their affinity towards the substrates (xylulose-5-phosphate and ribose-5-phosphate) has been studied in the presence of Ca2+ and Mg2+. In the presence of Ca2+, the active sites exhibit negative cooperativity in binding both xylulose-5-phosphate (donor substrate) and ribose-5-phosphate (acceptor substrate) and positive cooperativity in the catalytic transformation of the substrates. In the presence of Mg2+, nonequivalence of the active sites is not observed.

Key words

transketolase nonequivalence of active sites bivalent cations xylulose-5-phosphate ribose-5-phosphate 

Abbreviations

DTT

dithiothreitol

GAPD

glyceraldehyde-3-phosphate dehydrogenase

R5P

ribose-5-phosphate

TDP

thiamine diphosphate

TK

transketolase

X5P

xylulose-5-phosphate

Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • I. A. Sevostyanova
    • 1
  • V. A. Selivanov
    • 2
  • V. A. Yurshev
    • 3
  • O. N. Solovjeva
    • 1
  • S. V. Zabrodskaya
    • 4
  • G. A. Kochetov
    • 1
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Barcelona UniversityBarcelonaSpain
  3. 3.Faculty of Bioengineering and BioinformaticsLomonosov Moscow State UniversityMoscowRussia
  4. 4.Institute of BiochemistryNational Academy of Sciences of BelarusGrodnoBelarus