Sandbox Reserved 983

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The structure of Tryptophan Synthase is in an alpha-beta-beta-alpha complex with two binding sites: an indole 3-glycerol binding site and an indole and serine binding site.In <i>Salmonella typhimurium</i>, studies have shown the relevance of its monovalent cation site (MVC), which is necessary for catalysis and regulation of substrate channeling <ref>Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.</ref>. This site is also directly related to the reaction between the &#945;2&#946;2 complex of tryptophan synthase and the L-serine by regulating the distribution of intermediates within this reaction.It activates Tryptophan synthase by binding to its allosteric site which is positioned near the PLP cofactor of the enzyme <ref>Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.</ref>. Examples of these cations bounded by the enzyme <i>in vitro</i> include Sodium, Potassium, Cesium, Lithium, Rubidium, Ammonium, and Guanidinium ions.
The structure of Tryptophan Synthase is in an alpha-beta-beta-alpha complex with two binding sites: an indole 3-glycerol binding site and an indole and serine binding site.In <i>Salmonella typhimurium</i>, studies have shown the relevance of its monovalent cation site (MVC), which is necessary for catalysis and regulation of substrate channeling <ref>Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.</ref>. This site is also directly related to the reaction between the &#945;2&#946;2 complex of tryptophan synthase and the L-serine by regulating the distribution of intermediates within this reaction.It activates Tryptophan synthase by binding to its allosteric site which is positioned near the PLP cofactor of the enzyme <ref>Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.</ref>. Examples of these cations bounded by the enzyme <i>in vitro</i> include Sodium, Potassium, Cesium, Lithium, Rubidium, Ammonium, and Guanidinium ions.
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<scene name='68/687333/Nick01/1'>Tunnel</scene>between active site and indole binding site, blah, blah, blah...

Revision as of 14:31, 24 April 2015

This Sandbox is Reserved from 15-Jan-2015, through 30-May-2015 for use in the course "Biochemistry" taught by Jason Telford at the Maryville University. This reservation includes Sandbox Reserved 977 through Sandbox Reserved 986.
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Tryptophan Synthase

PDB ID 1wbj

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References

1. Dunn, Michael F., Dimitri Niks, Huu Ngo, Thomas R.m. Barends, and Ilme Schlichting. "Tryptophan Synthase: The Workings of a Channeling Nanomachine."Trends in Biochemical Sciences 33.6 (2008): 254-64. Science Direct. Web. 25 Jan. 2015. <http://www.sciencedirect.com/science/article/pii/S0968000408000923>.

2. "Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>.

  1. ↑ "Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>. <references/>
  2. ↑ Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.
  3. ↑ Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.
  4. ↑ Dierkers, Adam T., et al. "Tryptophan synthase: structure and function of the monovalent cation site." Biochemistry 48.46 (2009): 10997-11010.

3. Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.

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