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Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution

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Abstract

The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure of triosephosphate isomerase. Another domain shows similarities to many other nucleotide binding proteins. We discuss these similarities and their implications for current arguments on protein taxonomy and evolution.

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Author notes

  1. Michael Levine

    Present address: Department of Physiology, University of Bristol, Bristol, UK

  2. David K. Stammers

    Present address: The Wellcome Research Laboratories, Beckenham, Kent, UK

Authors and Affiliations

  1. Molecular Enzymology Laboratory, Department of Biochemistry, University of Bristol, Bristol, UK

    Michael Levine, Hilary Muirhead, David K. Stammers & David I. Stuart

Authors
  1. Michael Levine
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  2. Hilary Muirhead
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  3. David K. Stammers
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  4. David I. Stuart
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Levine, M., Muirhead, H., Stammers, D. et al. Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution. Nature 271, 626–630 (1978). https://doi.org/10.1038/271626a0

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  • DOI: https://doi.org/10.1038/271626a0

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