Enzymes

• Enzyme-substrate complex is formed when the substrate binds to an enzyme.
• When the substrate enters the active site, it undergoes chemical changes to form products.
• Products are released from the enzyme's active site once they have been produced.
• The active site of an enzyme has a specific shape that fits only one type of molecule, called the substrate.
• Non-competitive enzyme inhibition occurs when the inhibitor binds to another part of the enzyme, blocking its activity even if there are free active sites available.
• Competitive enzyme inhibition occurs when the substrate is bound to the active site, but an inhibitor molecule binds to it instead.
• Enzyme inhibitors can be competitive or non-competitive.
• The active site is where the reaction occurs, with the substrate being converted into product(s).
• Enzymes are proteins that act as biological catalysts, speeding up chemical reactions in living organisms.
• The product dissociates from the enzyme, leaving the free enzyme ready to catalyze another reaction.
• Inhibitors can either compete with the substrate for binding to the active site or block the active site in some other way.
• An example of a reversible reaction is the hydrolysis of sucrose (a disaccharide) into glucose and fructose.
• Enzymes increase the rate of a reaction without changing the position of equilibrium.
• Enzymes lower the activation energy required for a reaction by providing a pathway for reactants to follow.
• Enzymes have a unique three-dimensional structure that allows them to function effectively.
• Inhibitors block the action of enzymes by binding to them at different locations than the active site.
• Inhibitors compete with the substrate for binding to the active site of the enzyme.
• Non-competitive inhibitors bind to the enzyme at a different location than the active site, blocking its activity without competing with the substrate.
• Competitive inhibition involves an inhibitor molecule competing with the substrate for binding to the active site on the enzyme.
• Non-competitive inhibition involves an inhibitor molecule blocking the active site even when it's not bound to the enzyme.
• Enzymes have an optimum temperature range where they function best.
• Enzymes work best under optimal conditions such as pH and temperature.
• High temperatures cause denaturation, while low temperatures slow down the reaction.
• Enzymes are specific to certain reactions because they only fit one type of molecule at their active sites.
• Temperature affects the shape of the protein molecule, which can affect its activity.
• Denaturation occurs when an enzyme's shape changes due to unfavorable environmental factors like high temperatures or extreme pH levels.
• Enzymes are globular proteins.
• An anabolic reaction is where small molecules are joined to make bigger ones
• Catabolic reactions are reactions that split large molecules to make smaller ones
• Reactions rarely occur in single steps and are generally a series of smaller reactions.
• The series of smaller reactions are all controlled by a specific enzyme and this forms the metabolic pathway.
• In the induced fit model, the shape of the active site changes slightly to accommodate the shape of the substrate.
• Enzymes act in 1 of 3 distinct sites.
• Extracellular enzymes are secreted from cells by exocytosis.
• Extracellular enzymes catalyse extracellular reactions such as digestive enzymes like amylase.
• Intracellular enzymes in solution act inside the solution in cells.
• Membrane-bound intracellular enzymes are attached to membranes such as ATP synthesis.
• Examples of enzymes include maltase, catalase, amylase, lipase, protease.
• A substrate is a molecule that an enzyme reacts with.
• Activation energy is the amount of energy needed to initiate a reaction.