Investigation of substrate channeling in multi-enzyme complexes

Nature has generated a wide variety of enzymes, all sharing the common objective of catalyzing specific reactions. Yet, enzymes have evolved and developed numerous strategies and structural features to complete their tasks. Along an enzymatic pathway, several frequently assemble into multi-enzyme complexes for efficient transport of substrates from one active site to another using different strategies, including substrate channeling, where intermediates are directly transferred to the second active site via a tunnel, without being released into the surrounding solution. Channeling enhances the efficiency of enzymatic pathways, and prevents the release of unstable, reactive or toxic intermediates.
In this experiment, tryptophan synthase will be used as a model to investigate substrates channeling. We aim to uncover the mechanism of efficient substrates transport, and to understand how enzyme catalysis is controlled by conformational changes upon substrate binding and transport.