Summary
Control of indole channeling between the α-and β-sites of tryptophan synthase involves allosteric signals that switch αβ-dimeric units between open and closed conformations of low and high activity. Signaling is triggered by covalent bonding at the β-site and ligand binding to the α -site, and is postulated to be transmitted between sites via a scaffolding that includes a monovalent cation (MVC) site and the side chain of βLys 167 in alternating salt bridges with βAsp 305 or αAsp 56. Via site-directed mutation and MVC-substitutions, we have explored the roles of the MVC site and salt bridging in the regulation of channeling. From these experiments, we conclude the βK167-αD56 salt bridge plays an important role in substrate channeling.
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© 2000 Springer Basel AG
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Dunn, M.F. et al. (2000). Salt Bridging and Movalent Cation Binding Regulate Catalysis and Channeling in Tryptophan Synthase. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_24
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_24
Publisher Name: Birkhäuser, Basel
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