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WorksheetsIB biology 2.5 and 8.1 (enzymes and metabolism)
Total questions: 11
Worksheet time: 7mins
What is an advantage of using lactase in an immobilised state in the food manufacturing industry?
It functions within cells
It dissolves in multiple solvents
It converts cellulose to glucose
It is less likely to become denatured
Metabolic pathways are dependent on enzyme-catalysed reactions. Which term corresponds with the description?
Allosteric inhibition: The inhibitor binds to the active site of the enzyme
Competitive inhibition: The maximum rate of a reaction is lowered as the substrate concentration increases
Non-competitive inhibition: raises the maximum rate of reaction of a given enzyme reaction
End-product inhibition: The end-product in a metabolic pathway binds to an allosteric site of the first enzyme
Which enzyme does isoleucine inhibit?
Enzyme E1
Enzyme E2
Enzyme E3
Enzyme E5
The graph shows the effect of changing the substrate concentration on the early stages of an enzyme-catalysed reaction. What can be interpreted about the rate of reaction from the graph?
Rate of reaction increases up to a point and then stays constant
Rate of reaction increases linearly with increasing substrate concentration
Rate of reaction increases non-linearly with increasing substrate concentration
Rate of reaction is not affected by the substrate concentration
Living organisms control pH within their tissues. What is the reason for regulating pH?
All parts of the body must have the same pH in order to survive
Many reactions can only happen at specific pH levels
pH affects osmosis
Control of active transport is achieved by pH
The graph shows the effect of substrate concentration on the rate of an enzyme-catalysed reaction with and without an inhibitor. What do curves J, K and L on the graph indicate?
J: Competitive inhibitor, K: Non-competitive inhibitor, L: Normal enzyme activity
J: Normal enzyme activity, K: Competitive inhibitor, L: Non-competitive inhibitor
J: Non-competitive inhibitor, K: Normal enzyme activity, L: Competitive inhibitor
J: Normal enzyme activity, K: Non-competitive inhibitor, L: Competitive inhibitor
The graph shows the results of an investigation into the activity of turnip peroxidase. The accumulation of the product of the reaction catalysed by the enzyme is shown at different pH values. Based on the data, what is the optimum pH for this enzyme?
Between 3 and 5
Between 10 and 11
Between 7 and 8
Between 9 and 10
The first enzyme in the metabolic pathway that produces isoleucine is threonine deaminase. Which graph illustrates the relationship between threonine deaminase activity and threonine concentration?
A
B
C
D
In which processes are macromolecules broken down into monomers?
Anabolism and catabolism
Catabolism and hydrolysis
Hydrolysis and reduction
Reduction and anabolism
What effect do changes in pH have on enzymes?
All enzymes increase in activity as pH increases
The activity of all enzymes is reduced by a pH below or above 7
Low pH causes irreversible denaturation in all enzymes
Extreme pH can alter the active site of all enzymes
The grey line in each graph represents the rate of reaction catalysed by an uninhibited enzyme as substrate concentration is increased. Which graph shows the expected results if a competative inhibitor was added to the reaction.
A
B
C
D
