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

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Answer :  D

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Description : All the following statements about primary gout are true except (A) Its inheritance is X-linked recessive (B) It can be due to increased activity of PRPP synthetase (C) It can be ... activity of hypoxanthine guanine phosphoribosyl transferase (D) De novo synthesis of purines is increased in it

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Description : In the pathway of de novo synthesis of purine nucleotides, all the following are allosteric enzymes except (A) PRPP glutamyl amido transferase (B) Adenylosuccinate synthetase (C) IMP dehydrogenase (D) Adenylosuccinase

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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

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Description : An allosteric inhibitor of PRPP glutamyl amido transferase is (A) AMP (B) ADP (C) GMP (D) All of these

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Description : Cytosolic carbamoyl phosphate synthetase is activated by (A) Glutamine (B) PRPP (C) ATP (D) Aspartate

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Description : Cytosolic carbamoyl phosphate synthetase is inhibited by (A) UTP (B) CTP (C) PRPP (D) TMP

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Description : The first reaction unique to purine nucleotide synthesis is catalysed by (A) PRPP synthetase (B) PRPP glutamyl amido transferase (C) Phosphoribosyl glycinamide synthetase (D) Formyl transferase

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Description : PRPP synthetase is allosterically inhibited by (A) AMP (B) ADP (C) GMP (D) All of these

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Description : All of the following enzymes are unique to purine nucleotide synthesis except (A) PRPP synthetase (B) PRPP glutamyl amido transferase (C) Adenylosuccinate synthetase (D) IMP dehydrogenase

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Description : An allosteric inhibitor of adenylosuccinate synthetase is (A) AMP (B) ADP (C) GMP (D) GDP

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Description : All of the following are allosteric enzymes except (A) Citrate synthetase (B) a-Ketoglutarate dehdrogenase (C) Succinate thiokinase (D) Succinate dehydrogenase

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Description : Cytosolic and mitochondrial carbamoyl phosphate synthetase have the following similarity: (A) Both use ammonia as a substance (B) Both provide carbamoyl phosphate for urea synthesis (C) Both require N-acetylglutamate as an activator (D) Both are allosteric enzymes

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

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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

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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

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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

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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

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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

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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

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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

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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

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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

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

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

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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

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

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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

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