An enzyme is a catalyst, which is a chemical agent that changes the rate of a reaction without being consumed by the reaction. The reactant that enzymes act on is called its substrate. While the enzyme is bound to the substrate, the catalytic action converts the substrate to the product. Because of its shape, each enzyme catalyzes a specific reaction, which is the molecular recognition. Only a certain region of the enzyme molecule actually binds to the substrate. This area is called the active site and is usually a groove on the surface of the enzyme. The shape of the active site and the shape of the substrate fits accordantly. When the substrate enters the active site, it induces the enzyme in a process called induced fit to change its shape to fit tightly around the substrate. The induced fit is very important during the catalytic cycle when the substrate enters the active site to form an enzyme-substrate complex. The enzymes emerge from the reaction in their original form and are ready to function over and over again. When a reaction rearranges the atoms of molecules, the bonds in the reactants must be broken and the new bonds in the products must be formed. This requires energy. The energy required to break the bonds in the reactant molecules is known as the activation energy. The bonds only break when the molecule has absorbed enough energy (usually in the form of heat) to become unstable. Heat speeds up a reaction, but the high temperature kills cells. Organisms must instead use a catalyst. Enzymes (mostly proteins) are biological catalysts. Enzymes speed up reactions by lowering the barrier of activation energy, so that the transition state is within reach at regular temperatures. A transition state occurs when reactants are in an unstable condition and are ready for the reaction to take place. An enzyme cannot changes the free energy of the reaction or the spontantinuity of the reaction. It can only accelerate the reactions that would occur normally. However, this increases the metabolism of the cell and determines which chemical process will be going on in the cell at a certain time. Enzymes are regulated by factors that effect their activity. Some of these factors are environmental conditions, cofactor, enzyme inhibitors, all osteric regulation, and cooperativity. Enzymes are sensitive to their environment and each enzyme has environmental conditions in which it works best. For example, a temperature change can disrupt the hydrogen bonds, ionic bonds, and other weak interactions that stabilize the protein so the molecule denatures. Other environmental factors that influence the shape of proteins are pH and salt concentration. Also, many enzymes require cofactor which are nonprotein helpers for catalytic activity. Some cofactors are inorganic like zinc and copper; however, organic cofactors are called coenzymes like vitamins. Another factor is allosteric regulation. Molecules that inhibit enzyme activity may bind to an allosteric site, a receptor site separate from the active site. Complex enzymes with two or more polypeptide bonds may have allosteric sites where the polypeptides join. Also, the entire unit may oscillate between two conformational states, and the inhibitor stabilizes the catalytic conformation. Cooperativity, another factor, occurs when the induced-fit binding of a substrate molecule to one polypeptide subunit can change the conformation such that the active sites of all subunits are more active. An experiment that you could do would be with the substrate and the enzyme. You could leave one test-tube in room temperature, one test-tube over heat and one test-tube over ice. If temperature influences enzyme activity, then the rate of reaction will increase or decrease with the changes in temperature.