ch 7,8 - Enzymes Wednesday, October 06, 2010 11:16 AM...

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Enzymes Audio recording started: 11:41 AM Friday, October 08, 2010 Enzyme-substrate complex Reaction rate increases(substrate) at constant (enzyme) High resolution images from X-ray crystallography Tryptophan synthase (pg. 211) Change in spectroscopic characteristics of enzymes (E) and substrates (S) in ES complex Active site -3D cleft or crevice Just a small portion maybe containing 4 to 5 amino acids Small part compared to the entire enzyme molecule Unique microenvironment S bind to E by multiple weak interactions Specific bind of Substrate and Enz is dependent on arrangement of atoms in an active site Lock and key Induce fit Also look at graph 8- 12 Equation on 211 is important Pg. 215 Common features of Enzyme active site Reversible Inhibition: can be competitive, non-competitive, or uncompetitive The enzyme such that when inhibitor is removed, inhibitions persists (e.g. erythromycin) Synthesis of enzyme decreased or degradation of enzyme increased (e.g. interferon) No matter how high the (S), this type of inhibitor will affect the metabolic rate Duration of inhibition reflects time to synthesize new E
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This note was uploaded on 05/30/2011 for the course BIOCHEMIST 4033 taught by Professor Dorristerry during the Fall '10 term at Florida A&M.

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ch 7,8 - Enzymes Wednesday, October 06, 2010 11:16 AM...

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