Enzymes catalyze reactions?
They accelerate reaction rates in biological systems.
Enzyme specificity — role?
Ensures catalysis of specific substrates or reactions.
Isozymes — definition?
Variants of enzymes with different properties for same reaction.
Rapid equilibrium hypothesis — meaning?
Assumes quick formation/dissociation of enzyme-substrate complex.
Reaction velocity equations — basis?
Derived from Michaelis-Menten assumptions and rate constants.
Temperature effects — enzyme activity?
Increases to an optimum, then declines due to denaturation.
pH influence — enzyme activity?
Maximized at optimal pH; declines outside this range.
Michaelis-Menten model — assumption?
Steady-state of enzyme-substrate complex during initial rate.
Lineweaver-Burk plot — purpose?
Linearizes Michaelis-Menten for parameter determination.
Activation energy — role?
Energy barrier that must be overcome for reaction.
Collision theory — explanation?
Reactions occur when molecules collide with proper energy and orientation.
Enzyme denaturation — cause?
High temperature, pH extremes, or chemicals disrupt structure.
Optimal temperature — definition?
Temperature at which enzyme activity is highest.
pH effect — enzyme stability?
Depends on ionization of amino acids; too high or low causes denaturation.
Vmax — meaning?
Maximum reaction velocity at enzyme saturation.
Km — significance?
Substrate concentration at half Vmax, indicates affinity.
Lineweaver-Burk — slope?
Km/Vmax, used to calculate kinetic parameters.
Enzyme specificity — models?
Lock-and-key and induced fit models.
Activation energy — lowered by?
Enzymes stabilize transition state, reducing Ea.
Collision theory — temperature effect?
Higher temperature increases collision frequency and energy.
Testez vos connaissances avec un QCM de 10 questions sur Enzyme Kinetics and Catalysis Fundamentals.
1. What does the Michaelis constant (Km) represent in enzyme kinetics?
2. Who are the authors and the year associated with the development of the Michaelis-Menten reaction velocity model?
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