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Salt Bridging and Movalent Cation Binding Regulate Catalysis and Channeling in Tryptophan Synthase

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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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References

  1. Pan, P., Woehl, E., & Dunn, M. F. (1997) Trends in Biochemical Sciences 22, 22–27.

    Article  PubMed  CAS  Google Scholar 

  2. Miles, E. W., Rhee, S., & Davies, D. R. (1999) J Biol. Chem. 274, 12193–12196.

    CAS  Google Scholar 

  3. Rowlett, R., Yang, L. H., Ahmed, S. A., McPhie, P., Jhee, K. H., & Miles, E. W. (1998) Biochemistry 37, 2961–2968).

    Article  PubMed  CAS  Google Scholar 

  4. Yang, X-J. & Miles, E. W. (1993) J. Biol. Chem. 268, 22269–22272.

    CAS  Google Scholar 

  5. Ahmed, S. A., Ruvinov, S. B., Kayastha, A. M., & Miles, E. W. (1991) J. Biol. Chem. 266 21548–21557.

    CAS  Google Scholar 

  6. Peracchi, A., Mozzarelli, A., & Rossi, G. L. (1995) Biochemistry 34, 945–9465.

    Article  Google Scholar 

  7. Woehl, E.U., & Dunn, M.F. (1995) Biochemistry, 34, 9466–9476.

    Article  PubMed  CAS  Google Scholar 

  8. Woehl, E.U., & Dunn, M.F. (1999) Biochemistry, 38, 7118–7130.

    Article  PubMed  CAS  Google Scholar 

  9. Woehl, E.U., & Dunn, M.F. (1999) Biochemistry, 38, 7131–7141.

    Article  PubMed  CAS  Google Scholar 

  10. Rhee, S. Parris, K. D., Hyde, C. C., Ahmed, S. A., Miles, E. W., & Davies, D. R. (1997) Biochemistry 36, 7664–7680.

    Article  PubMed  CAS  Google Scholar 

  11. Brzovic, P. S., Sawa, Y., Hyde, C. C., Miles, E. W., & Dunn, M. F. (1992) J Biol. Chem. 267, 13028–13038.

    CAS  Google Scholar 

  12. Drewe, W. F., Jr., & Dunn, M. F. (1985) Biochemistry 24, 3977–3987.

    Article  PubMed  CAS  Google Scholar 

  13. Drewe, W. F., Jr., & Dunn, M. F. (1986) Biochemistry 25, 2494–2501.

    Article  PubMed  CAS  Google Scholar 

  14. Pan, P. & Dunn, M. F. (1996) Biochemistry 35, 5002–5015.

    Article  PubMed  CAS  Google Scholar 

  15. Roy, M., Keblawi, S., & Dunn, M. F. (1988a) Biochemistry 27, 6698–6704.

    Article  PubMed  CAS  Google Scholar 

  16. Brzovic, P. S., Ngo, K., & Dunn, M. F. (1992) Biochemistry 31, 3831–3839.

    Article  PubMed  CAS  Google Scholar 

  17. Leja, C. A., Woehl, E. U., & Dunn, M. F. (1995) Biochemistry 34, 6552–6561.

    Article  PubMed  CAS  Google Scholar 

  18. Dunn, M. F., Aguilar, V., Brzovic, P. S., Drewe, W. F., Jr., Houben, D. F., Leja, C. A., & Roy, M. (1990) Biochemistry 29, 8598–8607.

    Article  PubMed  CAS  Google Scholar 

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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

  • Print ISBN: 978-3-0348-9549-1

  • Online ISBN: 978-3-0348-8397-9

  • eBook Packages: Springer Book Archive

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