Topic 3 Vocabulary

  • Activation Energy: The amount of energy needed for a reaction to happen.

  • Active Site: A specific region on an enzyme where the substrate binds and the reaction takes place.

  • Amylase: An enzyme that catalyzes the extracellular breakdown of starch.

  • Catalase: An enzyme that catalyzes the intracellular breakdown of hydrogen peroxide into oxygen and water.

  • Catalyst: A substance that increases the rate of reaction, often by offering an alternative reaction pathway with a lower activation energy. It is unchanged at the end of the reaction.

  • Colorimeter: A light-sensitive device that measures the absorbance or transmission of certain wavelengths of light by a solution. A colorimeter can be used to investigate the rate of a reaction that involves color changes.

  • Competitive Inhibitor: A molecule that binds to the active site of an enzyme and prevents the substrate from binding.

  • Enzyme: A globular protein molecule that acts as a biological catalyst and increases the rate of biochemical reactions. Some enzymes work intracellularly, and others work extracellularly.

  • Enzyme/Substrate Complex: The temporary complex formed when the substrate binds to the active site of the enzyme.

  • Extracellular Enzyme: An enzyme that is secreted by cells and functions outside of cells, e.g., amylase.

  • Extracellular Reaction: A reaction that occurs outside of cells, e.g., in the tissue fluid.

  • Immobilized Enzymes: Enzymes that are attached to an inert, insoluble material over which the substrate passes and the reaction takes place.

  • Induced-Fit Hypothesis: A model of enzyme action that describes how enzymes undergo subtle conformational changes which exert a strain on bonds in the substrate.

  • Intracellular Enzyme: An enzyme that acts within cells, e.g., catalase.

  • Intracellular Reaction: A reaction that occurs within cells.

  • Lock and Key Hypothesis: A model of enzyme action that describes how the enzyme will only fit a substrate that has the correct complementary shape to the active site.

  • Michaelis-Menten Constant (Km): A value that indicates how strong the affinity between an enzyme and its substrate is.

  • Non-Competitive Inhibitor: An inhibitor that binds to a part of an enzyme that is not the active site (an allosteric site) and prevents the enzyme from functioning.

  • Substrate Specificity: The ability of an enzyme to catalyze only a specific reaction or set of reactions which have substrates complementary to the active site of the enzyme.

  • Vmax: The maximum reaction rate.