NEW
Font size
WorksheetsEnzyme Inhibition Quiz
Total questions: 10
Worksheet time: 5mins
A competitive inhibitor slows down an enzyme-catalysed reaction because it...
Binds to an allosteric site, changing the shape of the enzyme.
Has a similar structure to the substrate and binds to the active site.
Permanently destroys the enzyme's tertiary structure.
Increases the enzyme's affinity for the substrate.
Which statement best describes a non-competitive inhibitor?
It competes with the substrate for the active site.
Its effect is reduced when the substrate concentration is increased.
It binds to a site other than the active site, altering the active site's shape.
It has a molecular structure that is very similar to the substrate.
What is the effect of a competitive inhibitor on the Vmax and Km of an enzyme?
Vmax decreases, Km remains the same.
Vmax remains the same, Km increases.
Vmax decreases, Km increases.
Vmax remains the same, Km decreases.
When a non-competitive inhibitor is added to an enzyme-catalysed reaction, what happens to Vmax and Km?
Vmax decreases, Km remains the same.
Vmax remains the same, Km increases.
Vmax and Km both decrease.
Vmax and Km both remain the same.
How can the effect of a competitive inhibitor be overcome?
By increasing the temperature significantly.
By adding a non-competitive inhibitor.
By significantly increasing the substrate concentration.
By decreasing the enzyme concentration.
In the "Enzyme Musical Chairs" analogy, a student tying a rope across a chair to make it unusable models which concept?
A normal enzyme-substrate reaction.
Competitive inhibition, where the inhibitor blocks the active site.
The denaturation of an enzyme by high pH.
Non-competitive inhibition, where the active site's shape is changed.
A non-competitive inhibitor decreases the Vmax because...
It lowers the activation energy of the reaction.
It effectively removes some enzyme molecules from being able to react.
It increases the enzyme's affinity for the substrate.
It competes directly with the substrate for binding.
An inhibitor binds to a location on an enzyme called the allosteric site. What type of inhibitor is this?
Competitive
Reversible
Non-competitive
Substrate-like
Why does the Km value increase in the presence of a competitive inhibitor?
The inhibitor permanently damages the enzyme.
The enzyme's affinity for the substrate is unchanged.
The Vmax is lowered, so it takes longer to reach the halfway point.
A higher substrate concentration is needed to achieve half the Vmax.
An experiment shows that adding a chemical to an enzyme-catalysed reaction reduces the maximum rate of reaction, but does not change the affinity of the functioning enzymes for the substrate. This chemical is likely a...
Competitive inhibitor.
Non-competitive inhibitor.
Substrate analogue.
Product of the reaction.
