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  • Title: Tryptophan synthase: the workings of a channeling nanomachine.
    Author: Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I.
    Journal: Trends Biochem Sci; 2008 Jun; 33(6):254-64. PubMed ID: 18486479.
    Abstract:
    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.
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