Properties of Enzymes: Peroxidase

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Properties of Enzymes: Peroxidase, A Case Study Objectives Name the class of macromolecules to which peroxidase belongs and the monomers that make it up. Name the substrates and products of the peroxidase catalyzed reaction. Explain the role of guaiacol in this experiment. Define enzyme, activation energy, active site, pH, and denaturation. Distinguish between oxidation/reduction, activation energy/catalysis, substrate/product, and hydrogen peroxide/peroxidase. Describe how temperature, pH, enzyme concentration, and substrate concentration affect the reaction rate. Explain why peroxidase is a necessary enzyme for all aerobic or oxygen-using cells. Background Information The thousands of chemical reactions that occur in a cell at any given time do not occur randomly, but are highly under the control of biological catalysts called enzymes. A catalyst is a substance that speeds up a chemical reaction without being consumed by the reaction. Enzymes speed up reactions by lowering the activation energy of a reaction, which is that initial amount of energy necessary to bring reactants together with the proper amount of energy and in the proper orientation so that the products can be formed. Most enzymes are proteins with particular primary structures dictated by genes. As proteins, upon their synthesis, enzymes assume particular shapes. This shape, especially in its “active site”, determines its catalytic effects. The active site of each enzyme binds to specific molecules – for example, the enzyme sucrase binds to sucrose but not to lactose, even though both are disaccharides. The reactant molecule that binds with to the active site of an enzyme and undergoes chemical modification is called the substrate of that enzyme. Some enzymes bind to two substrates to form products. Certain enzymes have metallic ions (such as Cu2+, Fe2+, Mn2+ ) as part of their active site

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