Enzymes

• Active sites have specific shapes to fit their corresponding substrates.
• Non-competitive enzyme inhibition involves binding of the inhibitor at another location on the enzyme, which changes its shape and prevents substrates from reaching the active site.
• Competitive enzyme inhibition occurs when the substrate is bound to the active site, but an inhibitor molecule binds to it instead.
• The Km (Michaelis constant) of an enzyme indicates its affinity for a substrate when the enzyme concentration is constant.
• Michaelis-Menten kinetics is the most common mathematical model used to describe the enzyme kinetics of a single-substrate reaction.
• Enzyme kinetics studies how the rate of an enzyme-catalyzed reaction depends on the concentration of the enzyme and the substrates.
• Enzyme inhibitors can be competitive or non-competitive.
• The active site is the part of an enzyme where substrate molecules bind, while other parts of the enzyme do not interact with the substrates.
• Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions.
• The rate at which an enzymatic reaction occurs depends on several factors, including temperature, pH, concentration of reactants, and presence of inhibitors or activators.
• Enzyme-substrate complex formation is reversible, with the enzyme releasing its product(s) when it reaches equilibrium.
• Temperature affects enzyme activity by altering the shape of active sites and causing denaturation above optimal temperatures.
• Competitive inhibitors bind to the same site as the substrate but do not react with it.