title: Unsymmetrical and concerted examples of the effect of enzyme--enzyme interactions on steady-state enzyme kinetics.
abstract: In previous papers of this series, emphasis has been placed on the steady-state phase transition and critical properties of large lattices of interacting, symmetrical, and identical enzyme molecules. The present paper is concerned with a number of examples of enzyme--enzyme interactions that do not belong to the class of models of the earlier papers. These are more biochemically oriented and include heterologous dimers, a linear chain with unsymmetrical interactions, and concerted isologous dimers (half-the-sites reactivity).
mesh_terms: D002384:Catalysis; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008954:Models, Biological
chemical_list: D004798:Enzymes; D046911:Macromolecular Substances
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references.pmid: 269419
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references.pmid: 271948
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references.pmid: 4366378