Study Notes on Enzymes and Catalysts
Enzymes and Catalysts
Enzymes are proteins or RNA molecules that act as catalysts, increasing reaction rates without being consumed.
They facilitate reactions by lowering activation energy barriers.
Key Concepts
Activation Energy Barriers: Requires energy to reach transition states; spontaneous reactions may be slow due to high activation energy.
Transition States: Unstable configurations that reactants must achieve during reactions.
Enzymes change shape upon substrate binding through induced fit, optimizing interactions for catalysis.
Enzyme Activity
Enzymes do not change Gibbs free energy (∆G); they can accelerate reactions but cannot convert non-spontaneous reactions into spontaneous ones.
Enzymes exhibit specificity for substrates via active sites where substrate molecules bind.
Activity is influenced by environmental conditions such as temperature and pH.
Regulation of Enzymes
Cofactors: Non-protein helpers (e.g., vitamins) that enhance enzyme activity.
Inhibitors:
Competitive inhibitors compete with substrates for active site binding.
Noncompetitive inhibitors alter enzyme shape without direct competition.
Allosteric Regulation: Molecules bind to sites other than the active site, influencing activation state and activity.
Feedback Inhibition
Inhibition of enzymatic pathways by the final product (e.g., ATP inhibits catabolic enzymes).
This regulatory mechanism prevents overproduction of metabolites, maintaining cellular balance.