Unit 3 · Cellular Energetics
Lesson 19 of 65

3.2 Enzyme Catalysis

01Lowering activation energy

Every reaction needs an energy push to start: the activation energy (Eₐ). Enzymes lower Eₐ by orienting substrates, straining bonds, or providing a favorable microenvironment.

Enzymes do not change ΔG — the energy difference between reactants and products stays the same. They only change how fast equilibrium is reached.

02Reading the energy diagram

On an energy-vs-reaction-progress graph, the catalyzed curve has a lower hump, but starts and ends at the same heights as the uncatalyzed curve.

Exergonic reactions end lower than they start (release energy, ΔG < 0); endergonic reactions end higher (ΔG > 0).

03Notebook box

Enzyme changes: Eₐ ↓, rate ↑. Enzyme does NOT change: ΔG, equilibrium position, products.

Worked example: A graph shows two curves with the same start and end but different peaks. Which is enzyme-catalyzed and what is the same? → The lower peak; ΔG is identical.

Key takeaways
  • ✦Enzymes lower activation energy only.
  • ✦ΔG unchanged by enzymes.
  • ✦Lower hump on graph = catalyzed.
Watch out'Spontaneous' (ΔG < 0) doesn't mean fast. Without enzymes, many favorable reactions take years.
Quick check

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1.Enzymes speed reactions by…

2.On an energy diagram, the enzyme changes the…

3.A reaction with ΔG < 0 is…