Birrer Sandbox 2: Difference between revisions
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Zn plays an important role in the catalysis. It funtions by electrostatically stabilizing the oxygen in alcohol during ADH's catalysis, which causes the alcohol to be more acidic. At the <scene name='Birrer_Sandbox_2/Zinc_binding_site/1'>Zinc Binding Site</scene>, Zinc coordinates with Cys 146, Cys 174, and His 67.<ref>''Protein: Alcohol Dehydrogenase''. The College of Saint Benedict and Saint John's University. 1 March 2010 < http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm></ref> | Zn plays an important role in the catalysis. It funtions by electrostatically stabilizing the oxygen in alcohol during ADH's catalysis, which causes the alcohol to be more acidic. At the <scene name='Birrer_Sandbox_2/Zinc_binding_site/1'>Zinc Binding Site</scene>, Zinc coordinates with Cys 146, Cys 174, and His 67.<ref>''Protein: Alcohol Dehydrogenase''. The College of Saint Benedict and Saint John's University. 1 March 2010 < http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm></ref> | ||
NAD functions as a cosubstrate in the dehydration. NAD binds to numerous residues in a series of beta-alpha-beta folds. <scene name='Birrer_Sandbox_2/Nad_binding_site/1'>NAD Binding Region</scene> shows the domain where NAD binds, and many of the residues with which it interacts are selected. | |||
<ref>''Protein: Alcohol Dehydrogenase''. The College of Saint Benedict and Saint John's University. 1 March 2010 < http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm></ref> | |||
