18 Questions
What is the effect of a competitive inhibitor on the apparent Km of an enzyme?
It is increased
What happens to the reaction velocity when the concentration of substrate is increased in the presence of a competitive inhibitor?
It reaches Vmax
What is the effect of non-competitive inhibitors on the binding of substrate to enzyme?
They have no effect on the binding of substrate to enzyme
What is the point of intersection between the plots of inhibited and uninhibited reactions in a Lineweaver-Burk plot?
The y-axis at 1/Vmax
What is the result of increasing the substrate concentration in the presence of uncompetitive inhibitors?
The inhibition is increased
What is a potential limitation of enzyme activity measurements?
All of the above
What is the purpose of maintaining a constant pH during enzyme concentration measurements?
To ensure accurate enzyme activity measurements
What is the effect of non-competitive inhibitors on Vmax?
It is decreased
What is the effect of non-competitive inhibitors on Km?
It is unchanged
What is the principle of the fixed-time assay method?
Reactants are combined, reaction proceeds for a designated time, and then the reaction is stopped
How do uncompetitive inhibitors differ from competitive inhibitors?
Uncompetitive inhibitors are not overcome by increasing substrate concentration, while competitive inhibitors are
What is the advantage of continuous-monitoring or kinetic assays?
They can be used to measure substrate depletion
What is the effect of increasing substrate concentration on competitive inhibition?
Inhibition is partially reversed
What type of bond is formed between a reversible inhibitor and an enzyme?
Noncovalent bond
What happens when the concentration of substrate is significantly higher than the concentration of a competitive inhibitor?
Inhibition is partially reversed
What is the characteristic of non-competitive inhibitors?
They bind to an allosteric site
What is the effect of increasing substrate concentration on uncompetitive inhibition?
Inhibition is increased
What is the characteristic of mixed inhibitors?
They bind to either E or ES complex
This quiz covers the different types of enzyme inhibitors, their effects on Vmax and Km, and how they are represented on Lineweaver-Burk plots. It also discusses the characteristics of competitive inhibitors and how they interact with substrates.
Make Your Own Quizzes and Flashcards
Convert your notes into interactive study material.
Get started for free