13 Questions
What type of inhibitors bind permanently to the enzyme and stop the whole pathway?
Irreversible inhibitors
What type of inhibition involves the inhibitor binding at either the enzyme or the enzyme-substrate complex?
Mixed inhibition
What is the rate constant (k) for a first-order reaction involving only 1 reactant?
k
What do reversible inhibitors do to the enzyme pathway?
Slow down the EZ pathway
What is the rate expression for a second-order reaction involving 2 reactants?
v=k[A][B]
What assumption is made in the steady-state assumption for enzyme kinetics?
Assume that over most of the reaction course [ES] is small & does not change, d[ES]/dt=0
What does the turnover number (kcat) represent?
Max velocity per enzyme molecule per unit of time
What is the nature of the R1 side chain critical for in the hydrolysis of a peptide bond by proteolytic enzymes?
The nature of the R1 side chain is critical for the hydrolysis of a peptide bond by proteolytic enzymes.
How can enzyme activity be controlled?
Enzyme activity can be controlled by allosteric regulation, covalent modification, and inhibitors.
What is the function of allosteric effectors in enzyme regulation?
Allosteric effectors can bind at allosteric sites to either activate (favor R state) or inhibit (favor T state) enzyme activity.
What is the mechanism of action of competitive inhibitors?
Competitive inhibitors compete with the substrate for binding at the active site of the enzyme.
How do non-allosteric site inhibitors affect enzyme activity?
Non-allosteric site inhibitors decrease the velocity and Vmax of the reaction by decreasing the kcat.
What is the role of reversible covalent modification in enzyme regulation?
Reversible covalent modification, such as phosphorylation and dephosphorylation, is a common mechanism to regulate enzyme activity.
Test your understanding of kinetics, rate constants, and enzyme efficiency with this quiz. Explore topics such as first and second-order reactions, the steady-state assumption, turnover number (kcat), and enzyme efficiency (kcat/KM).
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