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Enzyme-Enzyme Interactions in Tryptophan Synthetase from E. coli

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Protein-Protein Interactions

Abstract

Multienzyme complexes are multifunctional in the sense of being able to catalyze two or more different metabolic reactions [1, 2, 3]. In the majority of known examples (e.g. pyruvate dehydrogenase [4] and yeast fatty acid synthetase [5]) the different catalytic functions associated with the complex represent the members of a complete or partial metabolic chain. Physically speaking, multienzyme complexes are stable aggregates of different polypeptide chains (i.e. protein subunits assembled in well-defined proportions). To the extent that there are no covalent bonds between the constituent subunits, these statements describe the quaternary structure of multienzyme complexes. It is reasonable to conclude that the evolution of these organized enzymes utilized the inherent advantages offered by subunit — subunit (or quaternary) interactions between different proteins. What are these advantages ?

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Author information

Authors and Affiliations

  1. Abt. für Biophysikalische Chemie, Biozentrum der Universität Basel, Basel, Switzerland

    K. Kirschner & R. Wiskocil

Authors
  1. K. Kirschner
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  2. R. Wiskocil
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Editor information

Editors and Affiliations

  1. Biochemie II, Fachbereich Biologie, Universität Regensburg, D-8400, Regensburg, Universitätsstr. 31, Deutschland

    R. Jaenicke

  2. Physiologisch-Chemischen Institutes, Universität Würzburg, D-8700, Würzburg, Koellikerstr. 2, Deutschland

    E. Helmreich (Direktor) (Direktor)

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Kirschner, K., Wiskocil, R. (1972). Enzyme-Enzyme Interactions in Tryptophan Synthetase from E. coli. In: Jaenicke, R., Helmreich, E. (eds) Protein-Protein Interactions. Colloquium der Gesellschaft für Biologische Chemie 13.–15. April 1972 in Mosbach/Baden, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65456-5_12

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  • DOI: https://doi.org/10.1007/978-3-642-65456-5_12

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-65458-9

  • Online ISBN: 978-3-642-65456-5

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