Enzyme modes of action
Lower activation energy via substrate binding.
Enzyme-substrate complex
Intermediate formed during catalysis.
Lock-and-key model
Active site and substrate are complementary.
Induced fit model
Enzyme changes shape upon substrate binding.
Factors influencing activity
Substrate, temperature, pH, inhibitors.
Substrate saturation
All active sites occupied; max rate.
Optimal temperature
Temperature at which enzyme activity peaks.
Enzyme concentration effect
Increases reaction rate until saturation.
Enzyme inhibition types
Reversible and irreversible.
Competitive inhibitors
Bind active site, resemble substrate.
Non-competitive inhibitors
Bind allosteric site, change shape.
Enzyme cofactors
Non-protein helpers for activity.
Coenzymes
Organic cofactors derived from vitamins.
Metal ion cofactors
Inorganic helpers like zinc, iron.
Effects of pH
Optimal pH maintains enzyme shape.
Denaturation
Loss of enzyme structure and activity.
Activation energy
Energy barrier lowered by enzymes.
Transition state
High-energy intermediate in reactions.
Enzyme properties
Reusable, specific, sensitive to environment.
Metabolic pathways
Series of interconnected reactions.
Test your knowledge with 10 questions on Enzyme Function and Regulation.
1. Who is credited with proposing the induced fit model of enzyme action?
2. When was the lock-and-key model of enzyme action first proposed?
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