Enzyme Kinetics Quiz

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Questions and Answers

What is the formula for an enzyme-catalyzed reaction?

E + S → [E-S] ⇌ E + P

E + S ⇌ [E-S] → E + P (correct)

E + S → [E-S] → P + E

E + S → E-S → E + P

What does Vmax represent in enzyme kinetics?

The initial rate of the reaction

The rate when the enzyme is saturated with substrate

The rate when the enzyme is not bound to the substrate

The theoretical maximal rate of the reaction (correct)

What does a small Km value indicate about substrate affinity?

Low affinity of enzyme to substrate

High amount of substrate needed to obtain ES complex

Weak binding between enzyme and substrate

Tight binding and high affinity of enzyme to substrate (correct)

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

When the enzyme is saturated with substrate Signup and view all the answers

What does the Michaelis constant (Km) measure?

Substrate concentration that produces half maximal velocity Signup and view all the answers

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

The maximum point on the plot, representing saturation of the enzyme with substrate Signup and view all the answers

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

Double-Displacement (Ping-Pong) Reaction Signup and view all the answers

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

Sequential Ordered Reaction Signup and view all the answers

Which enzyme type displays cooperative substrate binding?

Allosteric Enzymes Signup and view all the answers

Which enzyme kinetics do allosteric enzymes not obey?

Michaelis-Menten kinetics Signup and view all the answers

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

Sequential Ordered Reaction Signup and view all the answers

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

Lineweaver-Burke Equation Signup and view all the answers

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

Ordered mechanism Signup and view all the answers

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

Double-Displacement (Ping-Pong) Reaction Signup and view all the answers

What is the function of allosteric enzymes?

Display cooperative substrate binding Signup and view all the answers

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

Double-Displacement (Ping-Pong) Reaction Signup and view all the answers

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

Sequential Random Reaction Signup and view all the answers

Match the type of multiple substrate reaction with its characteristics:

Sequential (single displacement) reactions = Include two classes: ordered and random Double-displacement (ping-pong) reactions = One or more products are released before all substrates bind the enzyme Signup and view all the answers

Match the type of sequential reaction with its characteristics:

Ordered = The substrates bind the enzyme in a defined sequence Random = The order of events is random Signup and view all the answers

Match the enzyme type with its characteristic:

Allosteric enzymes = Can bind to inhibitors or activators at the allosteric site Signup and view all the answers

Match the enzyme kinetics equation with its characteristic:

Michaelis-Menten Equation = Accounts for the kinetic properties of many enzymes Lineweaver-Burke Equation = "Double reciprocal" plot useful for quantitation, use to determine Km and Vmax graphically Signup and view all the answers

Match the enzyme kinetic parameter with its definition:

Vmax = Maximum velocity obtained when ALL of the enzyme is in the E-S complex Michaelis constant (Km) = The substrate concentration that produces half maximal velocity Enzyme-catalyzed reaction = E + S ⇌ [E-S] → E + P Relation between Vo and [Substrate] = The values of Vo vs [S] plotted to reveal the relationship of Vo to substrate concentration Signup and view all the answers

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

Tight binding = Small amount of substrate needed to obtain ES complex High affinity of enzyme to substrate = Small Km value Liver glucokinase and hexokinase both bind glucose as substrate = Example of small Km values Km of glucokinase = 10.0 mM glucose = Example of small Km values Signup and view all the answers

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

Fastest rate occurs when the enzyme is saturated with substrate = Characteristic of an enzyme-catalyzed reaction Dependence on substrate concentration for reaction rate = Characteristic of an enzyme-catalyzed reaction E + S ⇌ [E-S] → E + P = Formula for an enzyme-catalyzed reaction Constant amount of enzyme used in saturation kinetic experiments = Characteristic of an enzyme-catalyzed reaction Signup and view all the answers

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

Small Km = High affinity of enzyme to substrate Large Km = Low affinity of enzyme to substrate Tight binding = Implication of small Km value Loose binding = Implication of large Km value Signup and view all the answers

Match the enzyme kinetic parameter with its description:

Vmax = Theoretical maximal rate of the reaction Michaelis constant (Km) = A constant and measure of substrate affinity Saturation kinetic experiments = Reaction rate measured at increasing substrate concentration using a constant amount of enzyme Relation between Vo and [Substrate] = Assay repeated at about ten different substrate concentrations and plotted to reveal the relationship of Vo to substrate concentration Signup and view all the answers