Lecture 10- Enzyme Kinetics Quiz

What is the enzyme-substrate complex called?

• E

• S

• ES

• P

What determines the rate of an enzyme reaction?

• Formation of the product from the ES complex

• Formation of the ES complex

• Formation of the enzyme-substrate complex

• Formation of the enzyme and product

What is the Michaelis-Menten equation used for?

• To measure the concentration of free enzyme

• To determine the rate of the reaction

• To calculate the maximum velocity of the reaction

• To understand the relationship between substrate concentration and reaction rate

What does the Michaelis constant (Km) measure?

• The concentration of the substrate at which the reaction rate is half of the maximum velocity

• The concentration of the enzyme at which the reaction rate is half of the maximum velocity

• The equilibrium constant of the reaction

• The rate constant for the formation of the enzyme-substrate complex

What does the Michaelis-Menten equation graphically produce when plotting reaction rate against substrate concentration?

• A linear curve

• A parabolic curve

• A hyperbolic curve

• An exponential curve

At high substrate concentrations, the reaction becomes:

• Zero order

• First order

• Second order

• Third order

At low substrate concentrations, the reaction follows:

• Zero order kinetics

• First order kinetics

• Second order kinetics

• Third order kinetics

When the substrate concentration is equal to the Michaelis constant, the rate is:

• Equal to zero

• Equal to the maximum velocity

• Half of the maximum velocity

• Double the maximum velocity

What is the rate determining step in the reaction scheme?

• Formation of the enzyme-substrate complex

• Breakdown of the enzyme-substrate complex to form the product

• Formation of the enzyme and product

• Breakdown of the enzyme and substrate

What does the steady-state approximation state?

• The rate of formation of the enzyme-substrate complex is relatively constant

• The rate of formation of the enzyme-substrate complex is greater than the rate of its breakdown

• The rate of formation of the enzyme-substrate complex is less than the rate of its breakdown

• The rate of formation of the enzyme-substrate complex is zero