Practice: Enzyme affinity and immobilizing enzymes

Competitive enzyme inhibitors limit the formation of enzyme-substrate complexes. True or false?

• True

• False

Which line represents the enzyme with the COMPETITIVE inhibitor?

• X

• Y

• Z

Which two curves have the same Km value? Tick two.

• X

• Y

• Z

In the presence of a non-competitive inhibitor, Vmax is overcome by increasing the substrate concentration. True or false?

• True

• False

Which can be inferred from this graph?

• Inhibitor A has the same affinity compared to without the inhibitor.

• Inhibitor B has the same affinity compared to without the inhibitor.

• Inhibitor A has a lower Vmax compared to without the inhibitor.

• Inhibitor B has a higher Vmax compared to without the inhibitor.

When the substrate is not competing with the inhibitor for the active site...

• ...the affinity is the same

• ...the affinity increases

What can be used to find the rate of an enzyme-catalyzed reaction? Tick two.

• increase in product concentration

• decrease in substrate concentration

• Michaelis-menten constant

What do you call the substrate concentration at which the reaction rate is half of Vmax?

• Michaelis-menten constant

• Enzyme affinity

• Immoblization

• Substrate concentration

Which is CORRECT about this graph?

• The two lower curves are both with competitive inhibitors.

• The dotted curve is with a non-competitive inhibitor.

• The thinner curve is with a competitive inhibitor.

When the value of km increases...

• ...the enzyme affinity decreases.

• ...the Vmax increases.

• ...the enzyme affinity increases.

• ...the Vmax decreases.