2.4 Enzymes

• Non-competitive enzyme inhibition involves binding of the inhibitor at another location on the enzyme, which changes its shape and prevents the substrate from being able to bind.
• 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.
• Enzyme inhibitors can be competitive or non-competitive.
• Enzyme inhibitors are substances that reduce the activity of an enzyme.
• Denaturing is the process of changing the shape of a protein, making it less stable.
• Activation energy is the minimum amount of energy needed for a reaction to occur.
• The induced fit hypothesis is the idea that the active site of an enzyme is shaped by the substrate and when joined together slight moulding of the enzyme around the substrate.
• The lock and key theory is a model of enzyme-substrate interactions that describes how the shape of the active site of an enzyme is complementary to the shape of the substrate.
• The active site is the part of the enzyme that binds to the substrate.
• A coenzyme is a molecule that is involved in the metabolic reactions of an enzyme that binds temporarily to help an enzyme and substrate bind efficiently.
• Enzymes are a substance that acts as a catalyst to bring about a biological reaction, speeding up reactions without being used up.
• Enzymes: Biological catalysts that speed up chemical reactions in the body.
• Catalyst: A substance that increases the rate of a chemical reaction without being used up in the reaction
• extracellular: outside the cell
• Intracellular: within the cell
• Cofactor: A molecule that is required for the enzyme to function.
• Enzyme-substrate complex: A complex formed when an enzyme and a substrate bind together
• Activation energy: The minimum amount of energy needed for a reaction to occur.
• Optimum temperature: The temperature at which the rate of reaction is at its maximum.