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 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
Description : 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) 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 : 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 : 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 : 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
Last Answer : Answer : C
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 : 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 : 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 : 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 : 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 : Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these
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 : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax
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 : 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 : 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 : 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 : In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km
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 inactivates an enzyme by occupying its active site? (A) Competitive inhibitor (B) Allosteric inhibitor (C) Non-competitive inhibitor (D) All of these
Description : A compression spring is made of music wire of 2 mm diameter having a shear strength and shear modulus of 800 Mpa and 80 Gpa respectively. The mean coil diameter is 20mm, free length is 40 mm, and the number ... by 8 times b. decreased by 2 times c. increased by 2 times d. decreased by 8 times
Last Answer : a. increased by 8 times
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 : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these
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))
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 : 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 : 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 : 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 : 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 : 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 : thresher causes more seed damage if: a speed is increased b clearance increased c speed is decreased d feed rate is reduced
Last Answer : a speed is increased
Description : If particle size is reduced then total surface area will be — a. Decreased b. Constant c. Increased d. None of these
Last Answer : c. Increased
Description : An ideal gas is maintained at constant temperature. If the pressure on the gas is doubled, the volume is a. increased fourfold b. doubled c. reduced by half d. decreased by a quarter
Last Answer : reduced by half
Description : Lock' and Key' model of enzyme action proposed by Fisher implies that (A) The active site is flexible and adjusts to substrate (B) The active site requires removal of PO4 group ( ... complementary in shape to that of the substrate (D) Substrates change conformation prior to active site interaction
Description : Fischer's lock and key' model of the enzyme action implies that (A) The active site is complementary in shape to that of substance only after interaction. (B) The active site is ... change conformation prior to active site interaction (D) The active site is flexible and adjusts to substrate
Description : Increased serum alanine during fasting is due to (A) Breakdown of muscle proteins (B) Decreased utilization of non essential amino acids (C) Leakage of aminoacids to plasma (D) Impaired renal function
Description : All of the following contribute to the antihypertensive action of propranolol except: A. Direct vasodilatation B. Decreased renin release from kidney C. Adaptation of blood vessels to reduced cardiac output D. Less noradrenaline release from sympathetic nerve endings
Last Answer : A. Direct vasodilatation