An enzyme is a catalysis that speeds up a reaction. Some enzymes are non-specific and some are highly specific. The active site on an enzyme is where the chemical reactions occur. Substrates, which are the reactants, bind to the active site. For specific enzymes, only substrates that fit the three-dimensional shape and structure of the active site can bind with it. When a substrate binds with an active site an enzyme-substrate complex (ES) is made. Only the substrates undergo chemical changes while the enzymes remain the same and are used again. The lock-and-key model is that the active site and substrate fit perfectly. The induced-fit model is that both the substrate and active site alter their shape to fit together. Temperature, pH, activator, …show more content…
When a reversible inhibitor unbinds from an enzyme, the enzyme can function as it did before. A few types of reversible inhibitors are competitive inhibitors, uncompetitive inhibitors, and noncompetitive inhibitors. A competitive inhibitor prevents substrate binding by attaching to the active site. An uncompetitive inhibitor binds to the ES and doesn’t allow for any products to be released. Lastly, the noncompetitive inhibitor binds to the enzyme at a different location other than the active site and changes the shape of the enzyme. However, an irreversible inhibitor can make an enzyme permanently inactive by changing the enzymes shape. An example of an irreversible inhibitor is nerve gas, which blocks the enzyme acetylcholinesterase. This enzyme is important in the proper functioning of the nervous system. The enzyme being used during our lab today is amylase. Amylase is a type of enzyme that is found in human saliva and begins the digestion process. After food gets chewed up, the amylase breaks down the bonds that are linked together to make starch molecules and converts it into sugars. The starch is broken down into disaccharides and trisaccharides. These are then turned into