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Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae

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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.

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Abbreviations

DTT:

dithiothreitol

GAPD:

glyceraldehyde-3-phosphate dehydrogenase

R5P:

ribose-5-phosphate

TDP:

thiamine diphosphate

TK:

transketolase

X5P:

xylulose-5-phosphate

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Authors and Affiliations

  1. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991, Moscow, Russia

    I. A. Sevostyanova, O. N. Solovjeva & G. A. Kochetov

  2. Barcelona University, Barcelona, 08028, Spain

    V. A. Selivanov

  3. Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991, Moscow, Russia

    V. A. Yurshev

  4. Institute of Biochemistry, National Academy of Sciences of Belarus, Bulvar Leninskogo Komsomola 50, 230017, Grodno, Belarus

    S. V. Zabrodskaya

Authors
  1. I. A. Sevostyanova
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  2. V. A. Selivanov
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  3. V. A. Yurshev
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  4. O. N. Solovjeva
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  5. S. V. Zabrodskaya
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  6. G. A. Kochetov
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Corresponding author

Correspondence to G. A. Kochetov.

Additional information

Original Russian Text © I. A. Sevostyanova, V. A. Selivanov, V. A. Yurshev, O. N. Solovjeva, S. V. Zabrodskaya, G. A. Kochetov, 2009, published in Biokhimiya, 2009, Vol. 74, No. 7, pp. 972–976.

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Sevostyanova, I.A., Selivanov, V.A., Yurshev, V.A. et al. Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae . Biochemistry Moscow 74, 789–792 (2009). https://doi.org/10.1134/S0006297909070128

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  • DOI: https://doi.org/10.1134/S0006297909070128

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