Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein

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Answer :

Answer : B

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Description : From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S

Last Answer : Answer : C

Description : A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition

Last Answer : Answer : B

Description : Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Last Answer : Answer : C

Description : Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Last Answer : Answer : C

Description : The Michaehis-Menten hypothesis: (A) Postulates the formation of an enzyme substrate complex (B) Enables us to calculate the isoelectric point of an enzyme (C) States that the ... independent of substrate concentration (D) States that the reaction rate is proportional to substrate concentration

Last Answer : Answer : A

Description : Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these

Last Answer : Answer : B

Description : The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Last Answer : Answer : D

Description : ........................ studied the kinetics of enzyme catalysis. a. Arrhenius b. Rutherford c. Micheal Faraday d. Michaelis & Menten

Last Answer : d. Michaelis & Menten

Description : What is Michaelis-Menten Theory ?

Last Answer : It is otherwise called enzyme-substrate complex theory. The enzyme combines with the substrate, to form an enzyme-substrate complex, which immediately breaks down to the enzyme and the product.

Description : An enzyme is a (A) Carbohydrate (B) Lipid (C) Protein (D) Nucleic acid ENZYMES 171

Last Answer : Answer : C

Description : What is Michaelis Menten constant? -Biology

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Description : Choose the correct enzyme - substrate pair. (a) Carbohydrate - Lipase (b) Maltase - Lactose (c) Rennin - Casein (d) Protein - Amylase

Last Answer : (c) Rennin - Casein

Description : Feedback term refers to (A) Effect of substrate on rate of enzymatic reaction (B) Effect of end product on rate reaction (C) Effect of enzyme concentration on rate of reaction (D) Effect of external compound on rate of reaction

Last Answer : Answer : B

Description : Humans most easily tolerate a lack of the nutrient: (A) Protein (B) Lipid (C) Iodine (D) Carbohydrate

Last Answer : Answer : D

Description : Humans most easily tolerate a lack of which of the following nutrients? (A) Protein (B) Iodine (C) Carbohydrate (D) Lipid

Last Answer : Answer : C

Description : The building up and breaking down of protoplasm are concerned with the metabolism of (A) Carbohydrate (B) Lipid (C) Protein (D) Minerals

Last Answer : Answer : C

Description : What is the effect of substrate concentration on enzyme activity? -Biology

Last Answer : answer:

Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Last Answer : Answer : D

Description : The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be ... constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Last Answer : Answer : C

Description : Enzymes activity is controlled by (A) pH of the solution (B) Temperature (C) Concentration of the enzyme (D) Concentration of the substrate (E) All of these

Last Answer : Answer : C

Description : When [s] is equal to Km, which of the following conditions exist? (A) Half the enzyme molecules are bound to substrate (B) The velocity of the reaction is equal to Vmax (C) The velocity of the reaction is independent of substrate concentration (D) Enzyme is completely saturated with substrate

Last Answer : Answer : A

Description : Velocity maximum for an enzyme at half the substrate concentration gives (A) The molecular weight of the enzyme (B) Km value (C) Isoelectric pH (D) Pk value

Last Answer : Answer : B

Description : If the substrate concentration is much below the km of the enzyme, the velocity of the reaction is (A) Directly proportional to substrate concentration (B) Not affected by enzyme concentration (C) Nearly equal to Vmax (D) Inversely proportional to substrate concentration

Last Answer : Answer : A

Description : In enzyme assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature

Last Answer : Answer : B

Description : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these

Last Answer : Answer : B

Description : Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145

Last Answer : Answer : D

Description : In enzyme kinetics Km implies (A) The substrate concentration that gives one half Vmax (B) The dissocation constant for the enzyme substrate comples (C) Concentration of enzyme (D) Half of the substrate concentration required to achieve Vmax

Last Answer : Answer : A

Description : In enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex

Last Answer : Answer : A

Description : Different isoenzymes of an enzyme have the same (A) Amino acid sequence (B) Michaelis constant (C) Catalytic activity (D) All of these

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Last Answer : b) lipid

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Last Answer : (a) protein

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Description : Concentration of substrate on enzyme activity. -Biology

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Description : Define Michaelis constant of an enzyme. -Biology

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Last Answer : (b) Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzyme

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Description : The hypothesis to explain enzyme– substrate complex formation: (A) Lock and key model (B) Induced fit theory (C) Proenzyme theory (D) Both (A) and (B)

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