The of chemical reactions, maiking energy molecules
The Effect of Temperature, pH, and Enzyme concentration on the rate of enzyme activity using Turnip (Brassica rapa subsp. rapa) and Hydrogen peroxide.Living cells are capable of undergoing a multitude of chemicals very rapidly because of the participation of enzymes. Enzyme are biological catalysts. They are involved in increasing the efficiency of chemical reactions, maiking energy molecules called ATP, moving components of the cell and other substances, anabolism and catabolism of molecules.
(Biology Reference enzymes 2018). By lowering the activation energy in a chemical reaction, they speed up the rate of a reaction without themselves being altered in the reaction. Proteins which perform catalytic functions have a globular tertiary structure. Globular proteins have a globular shape which have regions alpha and beta sheet arrangements depending upon the particular amino acids in the primary structure.
The polypeptide of a globular protein folds and twist into a tertiary structure and this structure is maintained by various types of bonding between R groups of amino acids. Sometimes an enzyme incorporates an important nonprotein component into its structure. When attached covalently to the enzyme’s protein, it is called a prosthetic group. If it is held more loosely by other types of bonds, it is a cofactor. Examples of cofactors are inorganic ions and organic coenzymes.
A substrate is the substance an enzyme act upon. The substrate is changed during the reaction to form a new product. The enzyme leaves the reaction unchanged and ready to bind with another substrate molecule. A small amount of enzyme can alter a relatively large amount of substrate.
The active site of an enzyme will bind with a substrate and form an enzyme substrate complex. In here, catalysis takes place and when it is complete, the complex dissociates into enzymes and product(s) in biochemical reactions. According to a model called induced fit, binding of the substrate causes a confrontational change in the active site of the enzyme, making the two molecules perfectly complementary. Each enzyme is specific for a certain reaction because its unique amino acid sequence causes it to have a unique three-dimensional structure. The active site also has a specific shape so that only one or a few of the thousands of compounds present in the cell can interact with it. If there is a prosthetic group on the enzyme, it will form part of the active site.
Any substance that blocks or changes the shape of the active site will interfere with the activity and efficiency of the enzyme.