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Interaction of pyruvate kinase with isatin and deprenyl

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Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry Aims and scope Submit manuscript

Abstract

The key glycolytic enzyme, pyruvate kinase, exhibits moderate affinity [3H]isatin binding (KD ∼10 μM) which is inhibited by ATP (IC50 25 μM) and deprenyl (IC50 5 μM). Interaction of pyruvate kinase with isatin and its inhibition by ATP and deprenyl has also been confirmed using an independent biosensor technique and the immobilized isatin analogue, aminoisatin. This effect has some specificity because the enzyme, creatine phosphokinase, does not exhibit specific isatin-binding. It is suggested that interaction of pyruvate kinase with isatin may reflect some non-glycolytic functions of this enzyme.

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Authors and Affiliations

  1. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya ul. 10, Moscow, 119121, Russia

    O. A. Buneeva, O. V. Gnedenko, Yu. D. Ivanov & A. E. Medvedev

  2. School of Biology, Moscow State University, Leninskie gory 1-12, Moscow, 119992, Russia

    M. V. Medvedeva

  3. Imperial College London, IRDB, Hammersmith Campus, Du Cane Road, London, W12 0NN, UK

    V. Glover

Authors
  1. O. A. Buneeva
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  2. O. V. Gnedenko
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  3. M. V. Medvedeva
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  4. Yu. D. Ivanov
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  5. V. Glover
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  6. A. E. Medvedev
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Correspondence to O. A. Buneeva.

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Original Russian Text © O.A. Buneeva, O.V. Gnedenko, M.V. Medvedeva, Yu.D. Ivanov, V. Glover, A.E. Medvedev, 2007, published in Biomeditsinskaya Khimiya.

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Buneeva, O.A., Gnedenko, O.V., Medvedeva, M.V. et al. Interaction of pyruvate kinase with isatin and deprenyl. Biochem. Moscow Suppl. Ser. B 1, 143–146 (2007). https://doi.org/10.1134/S1990750807020060

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  • DOI: https://doi.org/10.1134/S1990750807020060

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