Topic 12: Enzyme Kinetics

The maximum reaction rate ( $$V_{max}$$ )

The Michaelis constant ( $$K_m$$ )

The inverse of the maximum reaction rate ( $$\frac{1}{V_{max}}$$ )

The inverse of the Michaelis constant ( $$\frac{1}{K_m}$$ )

The inhibitor binds to the enzyme-substrate complex

The inhibitor binds to the active site of the enzyme

The inhibitor binds to an allosteric site

The inhibitor permanently deactivates the enzyme

It increases $$V_{max}$$

It decreases $$V_{max}$$

It has no effect on $$V_{max}$$

It increases the $$K_m$$

It increases $$K_m$$

It decreases $$K_m$$

It has no effect on $$K_m$$

It increases $$V_{max}$$

Noncompetitive inhibitor

Irreversible inhibitor

Competitive inhibitor

Allosteric inhibitor

It temporarily reduces enzyme activity

It permanently inactivates the enzyme

It increases enzyme activity

It changes the enzyme's substrate specificity

The maximum reaction rate

The substrate concentration at half-maximum velocity

The enzyme concentration

The inhibitor concentration

The inhibitor competes with the substrate for the active site

The inhibitor binds only to the enzyme-substrate complex

The inhibitor can bind to both the enzyme and the enzyme-substrate complex

The inhibitor increases the $$K_m$$

It increases the slope and changes the y-intercept

It decreases the slope and changes the x-intercept

It increases the slope without changing the x-intercept

It decreases the slope without changing the y-intercept

Enzyme kinetics is independent of substrate concentration

Enzyme kinetics can be described by the Michaelis–Menten equation

Enzyme kinetics is only applicable to irreversible reactions

Enzyme kinetics is not affected by enzyme concentration