The presence of a non competitive inhibitor (A) Leads to both an increase in the Vmax of a reaction and an increase in Km (B) Leads to a decrease in the observed Vmax (C) Leads to a decrease in Km and Vmax (D) Leads to an increase in Km without affecting Vmax

The presence of a non competitive inhibitor (A) Leads to both an increase in the Vmax of a reaction and an increase in Km (B) Leads to a decrease in the observed Vmax (C) Leads to a decrease in Km and Vmax (D) Leads to an increase in Km without affecting Vmax
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A competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases both Vmax and Km

Description : A competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases both Vmax and Km

Last Answer : Answer : A

In competitive enzyme activity inhibition (A) The structure of inhibitor generally resembles that of the substrate (B) Inhibitor decreases apparent Km (C) Km remains unaffective (E) Inhibitor decreases Vmax without affecting Km

Description : In competitive enzyme activity inhibition (A) The structure of inhibitor generally resembles that of the substrate (B) Inhibitor decreases apparent Km (C) Km remains unaffective (E) Inhibitor decreases Vmax without affecting Km

Last Answer : Answer : A

The kinetic effect of purely competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases Vmax without affecting Km

Description : The kinetic effect of purely competitive inhibitor of an enzyme (A) Increases Km without affecting Vmax (B) Decreases Km without affecting Vmax (C) Increases Vmax without affecting Km (D) Decreases Vmax without affecting Km

Last Answer : Answer : A

In competitive inhibition which of the following kinetic effect is true ? (A) Decreases both Km and Vmax (B) Increases both Km and Vmax (C) Decreases Km without affecting Vmax (D) Increases Km without affecting Vmax

Description : In competitive inhibition which of the following kinetic effect is true ? (A) Decreases both Km and Vmax (B) Increases both Km and Vmax (C) Decreases Km without affecting Vmax (D) Increases Km without affecting Vmax

Last Answer : Answer : D

Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax

Description : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax

Last Answer : Answer : C

Which of the following statements about an enzyme exhibiting allosteric kinetics with cooperative interaction is false? (A) A plot of V-Vk [s] has a sigmaidal shape (B) An inhibitor may increase the apparent Km (C) Line weaver Bnrk plot is useful for determining Km and Vmax (D) Removal of allosteric inhibitor may result in hyperbolic V-S [s] plot

Description : Which of the following statements about an enzyme exhibiting allosteric kinetics with cooperative interaction is false? (A) A plot of V-Vk [s] has a sigmaidal shape (B) An inhibitor may increase the ... Km and Vmax (D) Removal of allosteric inhibitor may result in hyperbolic V-S [s] plot

Last Answer : Answer : D

A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Description : A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Last Answer : Answer : D

In non-competitive enzyme action (A) Vmax is increased (B) Apparent km is increased (C) Apparent km is decreased (D) Concentration of active enzyme molecule is reduced

Description : In non-competitive enzyme action (A) Vmax is increased (B) Apparent km is increased (C) Apparent km is decreased (D) Concentration of active enzyme molecule is reduced

Last Answer : Answer : C

In reversible non-competitive enzyme activity inhibition (A) Vmax is increased (B) Km is increased (C) Km is decreased (D) Concentration of active enzyme is reduced

Description : In reversible non-competitive enzyme activity inhibition (A) Vmax is increased (B) Km is increased (C) Km is decreased (D) Concentration of active enzyme is reduced

Last Answer : Answer : D

In competitive inhibition of enzyme action (A) The apparent Km is decreased (B) The apparent Km is increased (C) Vmax is decreased (D) Apparent concentration of enzyme molecules decreased

Description : In competitive inhibition of enzyme action (A) The apparent Km is decreased (B) The apparent Km is increased (C) Vmax is decreased (D) Apparent concentration of enzyme molecules decreased

Last Answer : Answer : B

In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased

Description : In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased

Last Answer : Answer : B

In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km

Description : In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km

Last Answer : Answer : C

In reversible non-competitive enzyme activity inhibition (A) Inhibitor bears structural resemblance to substrate (B) Inhibitor lowers the maximum velocity attainable with a given amount of enzyme (C) Km is increased (D) Km is decreased

Description : In reversible non-competitive enzyme activity inhibition (A) Inhibitor bears structural resemblance to substrate (B) Inhibitor lowers the maximum velocity attainable with a given amount of enzyme (C) Km is increased (D) Km is decreased

Last Answer : Answer : B

Which one of the following statements is incorrect? (a) The competitive inhibitor does not affect the rate of breakdown of the enzyme-substrate complex. (b) The presence of the competitive inhibitor decreases the Km of the enzyme for the substrate. (c) A competitive inhibitor reacts reversibly with the enzyme to form an enzyme-inhibitor complex. (d) In competitive inhibition, the inhibitor molecule is not chemically changed by the enzyme.

Description : Which one of the following statements is incorrect? (a) The competitive inhibitor does not affect the rate of breakdown of the enzyme-substrate complex. (b) The presence of the competitive inhibitor ... . (d) In competitive inhibition, the inhibitor molecule is not chemically changed by the enzyme.

Last Answer : (b) The presence of the competitive inhibitor decreases the Km of the enzyme for the substrate

Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these

Description : Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these

Last Answer : Answer : D

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 described as (A) Independent of enzyme concentration (B) A constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

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

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

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

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

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

When the velocity of an enzymatic reaction equals Vmax, substrate concentration is (A) Half of Km (B) Equal to Km (C) Twice the Km (D) Far above the Km

Description : When the velocity of an enzymatic reaction equals Vmax, substrate concentration is (A) Half of Km (B) Equal to Km (C) Twice the Km (D) Far above the Km

Last Answer : Answer : D

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

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

Which inactivates an enzyme by occupying its active site? (A) Competitive inhibitor (B) Allosteric inhibitor (C) Non-competitive inhibitor (D) All of these

Description : Which inactivates an enzyme by occupying its active site? (A) Competitive inhibitor (B) Allosteric inhibitor (C) Non-competitive inhibitor (D) All of these

Last Answer : Answer : A

Lovastatin is a (A) Competitive inhibitor of acetyl CoA carboxylase (B) Competitive inhibitor of HMG CoA synthetase (C) Non-competitive inhibitor of HMG CoA reductase (D) Competitive inhibitor of HMG CoA reductase

Description : Lovastatin is a (A) Competitive inhibitor of acetyl CoA carboxylase (B) Competitive inhibitor of HMG CoA synthetase (C) Non-competitive inhibitor of HMG CoA reductase (D) Competitive inhibitor of HMG CoA reductase

Last Answer : Answer : D

The following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All of these

Description : The following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All of these

Last Answer : Answer : D

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

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

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

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

In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km

Description : In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km

Last Answer : Answer : B

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

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

All of the following statements about allopurinol are true except (A) It is a structural analogue of uric acid (B) It can prevent uric acid stones in the kidneys (C) It increases the urinary excretion of xanthine and hypoxanthine (D) It is a competitive inhibitor of xanthine oxidase

Description : All of the following statements about allopurinol are true except (A) It is a structural analogue of uric acid (B) It can prevent uric acid stones in the kidneys (C) It increases the urinary excretion of xanthine and hypoxanthine (D) It is a competitive inhibitor of xanthine oxidase

Last Answer : Answer : A

Physostigmine is a competitive inhibitor of (A) Xanthine oxidase (B) Cholinesterase (C) Carbonic anhydrase (D) Monoamine oxidase

Description : Physostigmine is a competitive inhibitor of (A) Xanthine oxidase (B) Cholinesterase (C) Carbonic anhydrase (D) Monoamine oxidase

Last Answer : Answer : B

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

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

In competitive inhibition, the inhibitor (A) Competes with the enzyme (B) Irreversibly binds with the enzyme (C) Binds with the substrate (D) Competes with the substrate

Description : In competitive inhibition, the inhibitor (A) Competes with the enzyme (B) Irreversibly binds with the enzyme (C) Binds with the substrate (D) Competes with the substrate

Last Answer : Answer : D

A substance unrelated to substrate but capable of reversibly changing activity of enzyme by binding to a site other than active site is called (a) Competitive inhibitor (b) Non-competitive inhibitor (c) Catalytic inhibitor (d) Allosteric modulator/inhibitor

Description : A substance unrelated to substrate but capable of reversibly changing activity of enzyme by binding to a site other than active site is called (a) Competitive inhibitor (b) Non-competitive inhibitor (c) Catalytic inhibitor (d) Allosteric modulator/inhibitor

Last Answer : Ans. ((d))

Which one of the following statements regarding enzyme inhibition is correct? (a) Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor protein. (b) Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzyme. (c) Non-competitive inhibition of an enzyme can be overcome by adding large amount of substrate. (d) Non-competitive inhibitors often bind to the enzyme irreversibly.

Description : Which one of the following statements regarding enzyme inhibition is correct? (a) Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor protein. (b ... large amount of substrate. (d) Non-competitive inhibitors often bind to the enzyme irreversibly.

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

Select the option which is not correct with respect to enzyme action. (a) Substrate binds with enzyme at its active site. (b) Addition of lot of succinate does not reverse the inhibition of succinic dehydrogenase by malonate. (c) A non-competitive inhibitor binds the enzyme at a site distinct from that which binds the substrate. (d) Malonate is a competitive inhibitor of succinic dehydrogenase.

Description : Select the option which is not correct with respect to enzyme action. (a) Substrate binds with enzyme at its active site. (b) Addition of lot of succinate does not reverse the inhibition ... from that which binds the substrate. (d) Malonate is a competitive inhibitor of succinic dehydrogenase.

Last Answer : (b) Addition of lot of succinate does not reverse the inhibition of succinic dehydrogenase by malonate.

Choose the correct statement about allopurinol: A. It is a purine antimetabolite with antineoplastic activity B. It is a competitive inhibitor of xanthine oxidase C. It is inactive itself, but its metabolite alloxanthine is a competitive inhibitor of xanthine oxidase D. Both allopurinol as well as its metabolite alloxanthine are noncompetitive inhibitors of xanthine oxidase

Description : Choose the correct statement about allopurinol: A. It is a purine antimetabolite with antineoplastic activity B. It is a competitive inhibitor of xanthine oxidase C. It is inactive itself ... D. Both allopurinol as well as its metabolite alloxanthine are noncompetitive inhibitors of xanthine oxidase

Last Answer : B. It is a competitive inhibitor of xanthine oxidase

What happens to an enzyme when a competitive inhibitor binds to it?

Description : What happens to an enzyme when a competitive inhibitor binds to it?

Last Answer : Need answer

A competitive inhibitor of succinic dehydrogenase is (a) α-ketoglutarate (b) malate (c) malonate (d) oxaloacetate.

Description : A competitive inhibitor of succinic dehydrogenase is (a) α-ketoglutarate (b) malate (c) malonate (d) oxaloacetate.

Last Answer : (c) malonate

Choose the correct statement about lovastatin: A. It markedly lowers plasma triglyceride with little effect on cholesterol level B. It is used as an adjuvant to gemfibrozil for type III hyperlipoproteinemia C. It is not effective in diabetes associated hypercholesterolemia D. It is a competitive inhibitor of the rate limiting step in cholesterol synthesis

Description : Choose the correct statement about lovastatin: A. It markedly lowers plasma triglyceride with little effect on cholesterol level B. It is used as an adjuvant to gemfibrozil for type III ... hypercholesterolemia D. It is a competitive inhibitor of the rate limiting step in cholesterol synthesis

Last Answer : D. It is a competitive inhibitor of the rate limiting step in cholesterol synthesis

The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline

Description : The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline

Last Answer : C. Physostigmine

The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline

Description : The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline

Last Answer : C. Physostigmine

The equilibrium constant of chemical reaction __________ in the presence of catalyst. (A) Increases (B) Decreases (C) Remain unaffected (D) Can either increase or decrease (depends on the type of catalyst)

Description : The equilibrium constant of chemical reaction __________ in the presence of catalyst. (A) Increases (B) Decreases (C) Remain unaffected (D) Can either increase or decrease (depends on the type of catalyst)

Last Answer : (C) Remain unaffected

An increase in the motion of the molecules of a gas confined in a steel tank will be observed in one of the following ways. Will it be observed as an increase in: w) the temperature of the gas only x) the pressure of the gas only y) both the temperature and pressure of the gas z) the temperature of the gas and a decrease in its pressure

Description : An increase in the motion of the molecules of a gas confined in a steel tank will be observed in one of the following ways. Will it be observed as an increase in: w) the temperature of the ... both the temperature and pressure of the gas z) the temperature of the gas and a decrease in its pressure 

Last Answer : ANSWER: Y -- BOTH THE TEMPERATURE AND PRESSURE OF THE GAS

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

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

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

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

In post-myocardial infarction and other high cardiovascular risk subjects but without hypertension or heart failure, prolonged ACE inhibitor medication has been found to: A. Increase the chances of sudden cardiac death B. Reduce the incidence of fatal as well as nonfatal myocardial infarction or stroke C. Lower the risk of developing heart failure and diabetes D. Both ‘B‘ and ‘C’

Description : In post-myocardial infarction and other high cardiovascular risk subjects but without hypertension or heart failure, prolonged ACE inhibitor medication has been found to: A. Increase the chances of sudden cardiac death ... Lower the risk of developing heart failure and diabetes D. Both B and C'

Last Answer : D. Both ‘B‘ and ‘C

Reversing any two of the three rotor leads on a wound-rotor induction motor will _____________. A. increase motor performance B. decrease motor performance C. reverse the motor rotation D. have no effect on the direction of rotation or motor performance

Description : Reversing any two of the three rotor leads on a wound-rotor induction motor will _____________. A. increase motor performance B. decrease motor performance C. reverse the motor rotation D. have no effect on the direction of rotation or motor performance

Last Answer : Answer: D

What will happen if a firm in perfect competitive market, increase its output by 50% (a)Total sales revenue will also increase by 50% ; (b) (b)Selling price will come down by 50%; (c)Total sales revenue will decrease by 50% ; (d)Profit will increase by 25%

Description : What will happen if a firm in perfect competitive market, increase its output by 50% (a)Total sales revenue will also increase by 50% ; (b) (b)Selling price will come down by 50%; (c)Total sales revenue will decrease by 50% ; (d)Profit will increase by 25%

Last Answer : (a)Total sales revenue will also increase by 50% ;

Two Commodities X and UY can be inferred as complementary to each other if (a) Increase in price of one leads to increase in demand of other and vice versa (b) Increase in price of one leads to decrease in demand of other and vice versa (c) Fall in price of one lead to fall in demand of other one (d) Increase in price of one leads to increase in demand of other one

Description : Two Commodities X and UY can be inferred as complementary to each other if (a) Increase in price of one leads to increase in demand of other and vice versa (b) Increase in price of one leads to decrease ... in demand of other one (d) Increase in price of one leads to increase in demand of other one

Last Answer : (b) Increase in price of one leads to decrease in demand of other and vice versa