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Structure, Function, and Regulation of Mammalian Pyruvate Dehydrogenase Complex

  • Conference paper
Metabolic Interconversion of Enzymes 1980

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

The mammalian pyruvate dehydrogenase complex consists of three catalytic components — pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). These three enzymes, acting in sequence, catalyze the reactions shown in Fig. 1 (Reed 1974). E1 catalyzes both the decarboxylation of pyruvate (reaction 1) and the subsequent reductive acetylation of the lipoyl moiety (reaction 2) which is covalently bound to E2. E2 catalyzes the transacetylation step (reaction 3), and E3 catalyzes the reoxidation of the dihydrolipoyl moiety NAD+ as the ultimate electron acceptor (reactions 4 and 5). The mammalian complex also contains small amounts of two regulatory enzymes, a kinase and a phosphatase, which modulate the activity of E1 by phosphorylation and dephosphorylation, respectively (Linn et al. 1969). This paper discusses some aspects of the structural organization of the mammalian pyruvate dehydrogenase complex and regulation of its activity by a phosphorylation-dephosphorylation cycle.

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Authors and Affiliations

  1. Clayton Foundation Biochemical Institute and Department of Chemistry, The University of Texas at Austin, Austin, TX, 78712, USA

    T.-L. Wu

Authors
  1. L. J. Reed
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  2. F. H. Pettit
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  3. D. M. Bleile
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  4. T.-L. Wu
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Editor information

Editors and Affiliations

  1. Biochemisches Institut, Albert-Ludwigs-Universität, Hermann-Herder-Str. 7, 7800, Freiburg, Germany

    Helmut Holzer

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© 1981 Springer-Verlag, Berlin Heidelberg

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Reed, L.J., Pettit, F.H., Bleile, D.M., Wu, TL. (1981). Structure, Function, and Regulation of Mammalian Pyruvate Dehydrogenase Complex. In: Holzer, H. (eds) Metabolic Interconversion of Enzymes 1980. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68211-7_12

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  • DOI: https://doi.org/10.1007/978-3-642-68211-7_12

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-68213-1

  • Online ISBN: 978-3-642-68211-7

  • eBook Packages: Springer Book Archive

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