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C1.1 Factors Affecting Enzyme Reaction Rate

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Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

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#1
Front (Question)

What is activation energy (Eₐ)?

Back (Answer)

The minimum energy required for a reaction to occur.

#2
Front (Question)

How do enzymes lower activation energy?

Back (Answer)

By destabilizing substrate bonds and stabilizing the transition state.

#3
Front (Question)

What is the transition state?

Back (Answer)

An unstable intermediate formed during a reaction before products appear.

#4
Front (Question)

What are exergonic and endergonic reactions?

Back (Answer)

Exergonic: releases energy (catabolic) Endergonic: requires energy input (anabolic)

#5
Front (Question)

What are the main factors affecting enzyme activity?

Back (Answer)

Temperature, pH, enzyme concentration, substrate concentration.

#6
Front (Question)

What is the optimum temperature?

Back (Answer)

The temperature at which enzyme activity is maximum.

#7
Front (Question)

What happens below the optimum temperature?

Back (Answer)

Molecular motion slows → fewer effective collisions → lower reaction rate.

#8
Front (Question)

What happens above the optimum temperature?

Back (Answer)

Enzyme denatures as hydrogen bonds break, changing active site shape.

#9
Front (Question)

Why is denaturation irreversible?

Back (Answer)

Disruption of tertiary structure prevents the enzyme from refolding properly.

#10
Front (Question)

What is the Q₁₀ temperature coefficient?

Back (Answer)

Measures rate change for a 10°C increase in temperature (usually 2–3× faster until denaturation).

#11
Front (Question)

What is the optimum pH?

Back (Answer)

The pH at which ionic and hydrogen bonds in the enzyme are most stable and active site shape is ideal.

#12
Front (Question)

What happens when pH deviates from optimum?

Back (Answer)

Changes in H⁺ concentration alter charge distribution → active site shape changes → enzyme denatures.

#13
Front (Question)

Example: Pepsin vs Trypsin vs Urease

Back (Answer)

Pepsin: pH 1–2 (stomach, acidic) Trypsin: pH 7.5–8.5 (small intestine, alkaline) Urease: pH 6.5–7.0 (neutral)

#14
Front (Question)

What is enzyme concentration’s effect on rate?

Back (Answer)

Rate increases linearly with enzyme concentration if substrate is not limiting.

#15
Front (Question)

What happens when enzyme concentration increases but substrate is limited?

Back (Answer)

Rate increases then plateaus — active sites saturated.

#16
Front (Question)

What is substrate saturation?

Back (Answer)

When all enzyme active sites are occupied — reaction rate cannot increase further.

#17
Front (Question)

How can cells control enzyme concentration?

Back (Answer)

By regulating gene expression (transcription and translation).

#18
Front (Question)

What is substrate concentration’s effect on rate?

Back (Answer)

Rate increases until enzyme saturation; then it levels off.

#19
Front (Question)

Why does reaction rate slow down over time?

Back (Answer)

Substrate is used up, product accumulates, fewer effective collisions.

#20
Front (Question)

What does “optimum conditions” mean?

Back (Answer)

The specific pH, temperature, and substrate concentration where enzyme rate is maximal.

#21
Front (Question)

What happens to enzymes at low temperature?

Back (Answer)

Reactions are too slow but reversible — enzyme not denatured.

#22
Front (Question)

Why are enzymes specific to their environments?

Back (Answer)

Evolutionary adaptation of enzyme structure to suit organism’s conditions (e.g., icefish enzymes optimal at -2°C).

#23
Front (Question)

What is the effect of extreme temperature on enzyme bonds?

Back (Answer)

Breaks hydrogen and ionic bonds, destabilizing tertiary structure.

#24
Front (Question)

What is the difference between enzyme-catalyzed and uncatalyzed reactions?

Back (Answer)

Catalyzed reactions have lower activation energy and faster reaction rate.