Enzyme Kinetics Quiz

What is the formula for an enzyme-catalyzed reaction?

What does Vmax represent in enzyme kinetics?

What does a small Km value indicate about substrate affinity?

In saturation kinetic experiments, when does the fastest rate occur?

What does the Michaelis constant (Km) measure?

What does Vmax represent on a Vo vs [S] plot?

What type of reaction is characterized by the formation of a substituted enzyme intermediate?

Which type of multiple substrate reaction is characterized by the formation of a ternary ES complex?

Which enzyme type displays cooperative substrate binding?

Which enzyme kinetics do allosteric enzymes not obey?

In which type of sequential reaction must all substrates bind to the enzyme before any product is released?

Which equation is an algebraically rearranged form of the Michaelis-Menten equation and is useful for quantitation?

Which substrate binding mechanism has a defined sequence for substrate binding to the enzyme?

What type of reaction is characterized by the formation of a substituted enzyme intermediate?

What is the function of allosteric enzymes?

What type of reaction involves one or more products being released before all substrates bind the enzyme?

What type of multiple substrate reaction has a random order for substrate addition and product release?

Match the type of multiple substrate reaction with its characteristics:

Match the type of sequential reaction with its characteristics:

Match the enzyme type with its characteristic:

Match the enzyme kinetics equation with its characteristic:

Match the enzyme kinetic parameter with its definition:

Match the characteristic of a small Km value with its implication on substrate affinity:

Match the statement with the correct characteristic of an enzyme-catalyzed reaction:

Match the kinetic parameter with its implication on enzyme affinity to substrate:

Match the enzyme kinetic parameter with its description:

Enzyme kinetics study provides information on enzyme specificities and mechanisms.

The Michaelis constant (Km) is a measure of the enzyme's maximum velocity.

A small Km value indicates a high substrate affinity for the enzyme.

The Vmax is obtained when none of the enzyme is in the E-S complex.

The enzyme type displaying cooperative substrate binding is allosteric.

The formula for an enzyme-catalyzed reaction is E + S ⇌ [E-S] → E + P.

Fastest reaction rate occurs when the enzyme is unsaturated with the substrate.

Allosteric enzymes do not obey Michaelis-Menten kinetics.

The Michaelis-Menten equation is an algebraically rearranged form of the Lineweaver-Burk plot.

The Vmax is a measure of the theoretical maximal rate of the reaction.

Allosteric enzymes can be accurately described using Michaelis-Menten kinetics.

The Lineweaver-Burke Equation is a 'double reciprocal' plot that is useful for quantitation and can be used to determine Km and Vmax graphically.

Sequential ordered reactions are characterized by the formation of a ternary ES complex consisting of the enzyme and both substrates.

Allosteric enzymes display cooperative substrate binding, which is evident as a sigmoidal reaction velocity curve.

In sequential random reactions, the order of substrate addition and product releasing are random.

Double-displacement (ping-pong) reactions involve the formation of a substituted enzyme intermediate and temporarily modified enzyme.

Allosteric enzymes have only one binding site for substrates.

The Michaelis constant (Km) measures the substrate concentration at which the reaction rate is half of Vmax.

The Lineweaver-Burke Equation is difficult to fit the best hyperbola through points determined in experiments.

Allosteric enzymes have multiple binding sites, including an active site for substrate binding and an allosteric site for inhibitor or activator binding.

Double-displacement (ping-pong) reactions involve the release of one or more products before all substrates bind the enzyme.