L9 Enzymes Part 2 of 3

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A  Vo

B  Keq

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A  KM for the substrate

B  initial velocity of the catalyzed reaction at low [S]

C  enzyme concentration

D  initial velocity of the catalyzed reaction at [S] >> KM

E  two of these

A  An increase in the substrate concentration (at constant enzyme concentration) leads to proportional increases in the rate of the reaction.

B  An enzyme–substrate complex can either form a product or dissociate back into the enzyme and substrate.

C  Most enzymes operating in the human body work best at a temperature of 37°C.

D  Maximal activity of many human enzymes occurs around pH 7.4.

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A  Michaelis-Menten kinetics assume covalent binding occurs between enzyme and substrate

B  Michaelis-Menten kinetics apply only to reaction rates before the product is formed.

C  Michaelis-Menten kinetics assume the enzyme and substrate first bind to form an enzyme-substrate complex.

A  A high Michaelis constant (Km) indicates a high affinity of an enzyme for its substrate.

B  The Michaelis constant (Km) of an enzyme increases when the enzyme concentration is increased.

C  A low Michaelis constant (Km) indicates a high affinity of an enzyme for its substrate.

A  usually catalyze several different reactions within a metabolic pathway

B  usually show strict Michaelis-Menten kinetics

C  usually have more than one polypeptide chain

D  are regulated primarily by covalent modification

A  extrapolate for the value of reaction rate at infinite enzyme concentration

B  determine the equilibrium constant for an enzymatic reaction

C  solve, graphically, for the rate of an enzymatic reaction at infinite substrate concentration

D  solve, graphically, for the ratio of products to reactants for any starting substrate concentration

E  illustrate the effect of temperature on an enzymatic reaction

A  Michaelis-Menten number

B  dissociation constant

C  half-saturation constant

D  turnover number

E  maximum velocity

A  Km, the Michaelis constant, is expressed in terms of the reaction velocity.

B  Km, the Michaelis constant, is defined as the dissociation constant of the enzyme-substrate complex.

C  Km, the Michaelis constant, is defined as the concentration of substrate required for the reaction to reach maximum velocity.

D  Km, the Michaelis constant, is a measure of the affinity the enzyme has for its substrate.

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A  Allosteric enzymes control metabolism.

B  Allosteric enzymes display Michaelis-Menten kinetics.

C  Allosteric enzymes display hyperbolic kinetics in response to changes in substrate concentration.

D  Allosteric enzymes are usually single subunit enzymes.

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