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Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

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Abstract

Studies of the self-assembly of pyruvate dehydrogenase of Escherichia coli show that the catalytic activity is proportional to the state of assembly and uncover a novel functional connection of active sites in this multienzyme complex.

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Author notes

  1. David L. Bates

    Present address: Department of Biochemistry, Stanford University Medical Center, Stanford, California, 94305, USA

Authors and Affiliations

  1. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK

    David L. Bates, Michael J. Danson, Geoffrey Hale, Elizabeth A. Hooper & Richard N. Perham

Authors
  1. David L. Bates
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  2. Michael J. Danson
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  3. Geoffrey Hale
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  4. Elizabeth A. Hooper
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  5. Richard N. Perham
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Bates, D., Danson, M., Hale, G. et al. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Nature 268, 313–316 (1977). https://doi.org/10.1038/268313a0

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  • DOI: https://doi.org/10.1038/268313a0

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