Study Guide 5 - Study Guide 5 Proteins/ Enzymes (Kopachik)...

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Study Guide 5 Proteins/ Enzymes (Kopachik) Terms to know: Enzyme Activation energy E a Catalyst Active site Transition state Cofactor Coenzyme Competitive inhibitor Noncompetitive inhibitor Allosteric regulation Feedback regulation cooperativity Summary of main points: 1. The reaction rate of an exergonic reaction is determined by the E a. which is dependent on the covalent and other bonds which must be broken to get to the transition state. Enzymes are biological catalysts that speed up reactions by lowering the E a . The enzyme is neither used up in the reaction nor permanently changed. 2. The enzyme specificity of binding to a substrate is dependent on complementary shape of the active site, usually a small pocket or groove on the surface. Enzyme and substrate have a lock and key –like relationship. Binding of the substrate creates a favorable orientation for stressing bonds so the rearrangement is done at lower energy. Enzymes are highly specific for their substrate. Many enzymes require cofactors (ions or coenzymes). 3. Enzymes work incredibly fast in creating product from reactant but they all have a characteristic maximum rate. Enzyme kinetic studies show that at low reactant concentration the speed of the product formation is dependent on the amount of reactant because the enzyme rate is not limiting (substrate is). The kinetic curve is a straight line up until at some reactant concentration the enzyme begins working at its maximum rate and this, not the reactant concentration, determines the rate of
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This note was uploaded on 05/25/2011 for the course BS 111 taught by Professor Patterson during the Winter '05 term at Michigan State University.

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Study Guide 5 - Study Guide 5 Proteins/ Enzymes (Kopachik)...

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