Lesson 3.1.4.2.2
3.1.4.2.2 Factors affecting enzyme-controlled reactions Quiz: AQA Biology, Unit 1
20 questions
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Lesson 3.1.4.2.2, Factors affecting enzyme-controlled reactions: 20 multiple choice questions for the AQA Biology (7402), Unit 1: Biological molecules, written with Revision Ninja.
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The 20 questions
-
Where does a competitive inhibitor bind to an enzyme?
- Allosteric site
- Substrate site
- Peptide backbone
- Active site
-
Where does a non-competitive inhibitor bind to an enzyme?
- Active site
- Reactive site
- Allosteric site
- Substrate site
-
How does increasing substrate concentration affect a reaction with a competitive inhibitor?
- Reduces inhibition
- Increases inhibition
- Denatures the enzyme
- Has no effect
-
Why does the reaction rate plateau at high substrate concentrations with fixed enzyme concentration?
- Enzymes denatured
- Active sites saturated
- Inhibitors bound
- Substrate exhausted
-
Why does the reaction rate fall rapidly above an enzyme's optimum temperature?
- Enzyme concentration drops
- Enzyme denatures
- Activation energy rises
- Substrate breaks down
-
How does a change in pH affect the structure of an enzyme's active site?
- Denatures substrate molecules
- Alters R-group ionisation
- Hydrolyses polypeptide chain
- Breaks peptide bonds
-
Which factor limits the reaction rate when substrate concentration is very high?
- Enzyme concentration
- Activation energy
- Substrate concentration
- Competitive inhibitor
-
Why does reaction rate increase as temperature rises towards the optimum?
- Less enzyme denaturation
- More active sites
- More kinetic energy
- Lower activation energy
-
Why can increasing substrate concentration not overcome non-competitive inhibition?
- Active site altered
- Inhibitor is consumed
- Substrate is blocked
- Enzyme is broken
-
In an iodine clock experiment, a colour change takes 40 s. What is the rate of reaction in s^-1?
- 2.5 s^-1
- 40 s^-1
- 0.4 s^-1
- 0.025 s^-1
-
An enzyme with optimum pH 7 shows lower activity at pH 5. What caused this?
- Activation energy doubled
- Substrate fully consumed
- Enzyme destroyed completely
- Active site altered
-
What happens to reaction rate when competitive inhibitor concentration is doubled with constant substrate?
- It stays constant
- It decreases
- It doubles
- It increases
-
A student measures the rate of an enzyme-controlled reaction at 30 C and at 40 C. The rate doubles between these temperatures. What is the Q10 value for this range?
- 1
- 2
- 10
- 4
-
Which change increases the maximum rate (Vmax) of an enzyme-catalysed reaction?
- Increase substrate concentration
- Decrease reaction temperature
- Add competitive inhibitor
- Increase enzyme concentration
-
Why does doubling substrate concentration not always double the rate of reaction?
- Activation energy rises
- Substrate denatures
- Active sites saturate
- Enzymes are consumed
-
Which type of enzyme inhibition can be overcome by increasing substrate concentration?
- Irreversible inhibition
- End-product inhibition
- Competitive inhibition
- Non-competitive inhibition
-
Which bonds in an enzyme's tertiary structure are disrupted by changes in pH?
- Glycosidic and ester
- Disulphide and peptide
- Hydrogen and ionic
- Peptide and phosphodiester
-
What type of variable must be kept constant during an enzyme activity investigation?
- Independent variable
- Categorical variable
- Dependent variable
- Control variable
-
What term describes the temperature at which an enzyme-catalysed reaction occurs fastest?
- Critical temperature
- Optimum temperature
- Denaturation temperature
- Maximum temperature
-
What pH environment is optimal for stomach enzymes such as pepsin?
- Neutral
- Basic
- Acidic
- Alkaline
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