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Tryptophan synthase: the workings of a channeling nanomachine

MPG-Autoren
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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Dunn, M. F., Niks, D., Ngo, H., Barends, T., & Schlichting, I. (2008). Tryptophan synthase: the workings of a channeling nanomachine. Trends in biochemical sciences, 33(6), 254-264. doi:10.1016/j.tibs.2008.04.008.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-79FB-2
Zusammenfassung
Substrate channeling between enzymes has an important role in cellular metabolism by compartmentalizing cytoplasmic synthetic processes. The bacterial tryptophan synthases are multienzyme nanomachines that catalyze the last two steps in L-tryptophan biosynthesis. The common metabolite indole is transferred from one enzyme to the other in each alphabeta-dimeric unit of the alpha2beta2 complex via an interconnecting 25-A-long tunnel. Recent solution studies of the Salmonella typhimurium alpha2beta2 complex coupled with X-ray crystal-structure determinations of complexes with substrates, intermediates and substrate analogs have driven important breakthroughs concerning the identification of the linkages between the bi-enzyme complex structure, catalysis at the alpha- and beta-active sites, and the allosteric regulation of substrate channeling.