Abstract
A growing body of experimental evidence supports the view that many consecutive enzymes in metabolic pathways form aggregates which transfer their common intermediate metabolite(s) directly, without its escape into a bulk phase1. These enzyme-enzyme interactions may be classified in terms of the lifetime of the multienzyme complexes: static channels persist over long periods of time and are destroyed only by processes as drastic as proteolysis; dynamic channels have a short lifetime and dissociate very easily2. Several examples of the former type have been found and in the case of tryptophan synthase, pictures of the multienzyme complex with the channeled intermediate bound in several positions have been reconstructed from X-ray diffraction patterns3. Due to their dissociable nature, channels of the latter type have not been detected in this way; evidence for their existence has therefore been gathered by other methods4.
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Mendes, P., Kell, D.B. (1993). Control Analysis of Metabolic Channeling. In: Schuster, S., Rigoulet, M., Ouhabi, R., Mazat, JP. (eds) Modern Trends in Biothermokinetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2962-0_34
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DOI: https://doi.org/10.1007/978-1-4615-2962-0_34
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