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
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
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
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
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
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
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
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
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
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
Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax
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
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
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
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
Description : In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km
Description : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these
Description : 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
Description : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax
Description : Down regulation is (A) Increased destruction of a hormone (B) Feed back inhibition of hormone secretion (C) Decreased concentration of a hormone in blood (D) Decrease in number of receptors for a hormone
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
Description : Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these
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
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
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
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
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.
Description : Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric inhibition
Description : Which one of the following regulatory actions involves a reversible covalent modification of the enzyme? (A) Phosphorylation of ser-OH on the enzyme (B) Allosteric modulation (C) Competitive inhibition (D) Non-competitive inhibition
Description : Which of the following regulatory reactions involves a reversible covalent modification of an enzyme? (A) Phosphorylation of serine OH on the enzyme (B) Allosteric modulation (C) Competitive inhibition (D) Non-competitive inhibition
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
Description : If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is (A) A (B) B (C) C (D) D
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
Description : At the adrenergic synapse, the concentration of adrenaline in synaptic cleft: a. increased by cocaine which inhibit reuptake of adrenaline b. decreased by MAO (monoamine oxidase) - inhibitors c. controlled chiefly by the activity of the enzyme COMT d. increased by noradrenaline receptor blockers
Last Answer : increased by cocaine which inhibit reuptake of adrenaline
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
Description : In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km
Description : An example of competitive inhibition of an enzyme is the inhibition of a. Succinic dehydrogenase by malonic acid b. Cytochrome oxidase by cyanide c. Hexokinase by glucose-6-phosphate d. Carbonic anhydrase by carbon dioxide
Last Answer : Ans: A
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
Description : What is it called when an enzyme is blocked at its active site so the normal substrate can't bind? a. Competitive Inhibition b. Feedback Inhibition c. Noncompetitive Inhibition d. Pathway Modulation
Last Answer : a. Competitive Inhibition
Description : If an enzyme‘s active site becomes deformed, inhibition was likely responsible. a. Metabolic b. Competitive c. Noncompetitive d. Cellular
Last Answer : c. Noncompetitive
Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
Description : Answer: a, b, c, d Free oxygen radicals are chemical species that are intermediates in the normal process of cellular respiration. Oxidants that are free radicals have been implicated as initiators of ... a. C-reactive protein b. Serum amyloid c. a -Proteinase inhibitor d. Fibrinogen e. Albumin
Last Answer : Answer: a, b, c, d The acute-phase response is a series of homeostatic responses of the organism to tissue injury in infection and inflammation. After an inflammatory stimulus occurs, a number ... 30% to 50% of the level before injury. The reason for the decrease in production is poorly understood
Description : The organophosphates produce irreversible inhibition of cholinesterase because: A. They bind to an allosteric site of the enzyme resulting in unfavourable conformation of esteratic site to bind ... degradation of enzyme molecules D. They are neither metabolized nor excreted from the body
Last Answer : B. Regeneration time of the phosphorylated enzyme is longer than the turnover time of the enzyme molecules
Description : One of the potent st imu lators of aldosterone secretion is (A) Increased sodium concentration (B) Decreased potassium concentration (C) Increased potassium concentration (D) Increased ECF volume
Description : Compared to the resting state, vigorously contracting muscle shows (A) An increased conversion of pyruvate to lactate (B) Decreased oxidation of pyruvate of CO2 and water (C) A decreased NADH/NAD+ ratio (D) Decreased concentration of AMP CARBOHYDRATES AND CARBOHYDRATE METABOLISM 21
Last 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
Description : The inhibition of succinate dehydrogenase by malonate by (A) Competitive inhibition (B) Non-competitive inhibition (C) Uncompetitive inhibition (D) Feedback inhibition
Description : Allosteric enzymes regulate the formation of products by (A) Feedback inhibition (B) Non-competitive inhibition (C) Competitive inhibition (D) Repression-derepression
Description : Allosteric inhibition is also known as (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) None of these