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 : 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 : 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 : Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric inhibition
Last Answer : Answer : A
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 : 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
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
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
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 : 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 : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these
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 : 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 : 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 : 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
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
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
Description : AMP is an allosteric inhibitor of (A) PRPP synthetase (B) Adenylosucciante synthetase (C) Both (A) and (B) (D) None of these
Description : GMP is an allosteric inhibitor of all the following except (A) PRPP synthetase (B) PRPP glutamyl amido synthetase (C) IMP dehydrogenase (D) Adenylosuccinate synthetase
Description : An allosteric inhibitor of IMP dehydrogenase is (A) AMP (B) ADP (C) GMP (D) GDP
Description : An allosteric inhibitor of adenylosuccinate synthetase is (A) AMP (B) ADP (C) GMP (D) GDP
Description : An allosteric inhibitor of PRPP glutamyl amido transferase is (A) AMP (B) ADP (C) GMP (D) All of these
Description : ATP is a co-substrate as well as an allosteric inhibitor of (A) Phosphofructokinase (B) Hexokinase (C) Glucokinase (D) None of these
Description : Glucose-6-phosphate is an allosteric inhibitor of (A) Glucokinase (B) Hexokinase (C) Phosphohexose isomerase (D) None of these
Description : An allosteric inhibitor of pyruvate dehydrogenase is (A) Acetyl CoA (B) ATP (C) NADH (D) Pyruvate
Description : Allosteric inhibitor of glutamate dehydrogenase is (A) ATP (B) ADP (C) AMP (D) GMP
Description : An allosteric enzyme influences the enzyme activity by (A) Competiting for the catalytic site with the substrate (B) Changing the specificity of the enzyme for the substrate (C) Changing the conformation ... binding to a site other than catalytic site (D) Changing the nature of the products formed
Description : Allosteric inhibition (A) Makes active site unifit for substrate (B) Controls excess formation and end product (C) Both (A) and (B) (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 : 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 : What happens to an enzyme when a competitive inhibitor binds to it?
Last Answer : Need answer
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 : The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline
Last Answer : C. Physostigmine
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 : 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 : What will happen if the secretion of parietal cells of gastric glands is blocked with an inhibitor? (a) In the absence of HCl secretion, inactive pepsinogen is not converted into the active ... c) Gastric juice will be deficient in chymosin. (d) Gastric juice will be deficient in pepsinogen.
Last Answer : (a) In the absence of HCl secretion, inactive pepsinogen is not converted into the active enzyme pepsin.
Description : The nucleophilic attack on the esterified carboxyl group of the peptidyl-tRNA occupying the P site and the α-amino group of the new amino acyl tRNA, the number of ATP required by the amino acid on the charged tRNA is (A) Zero (B) One (C) Two (D) Four
Description : The α-amino group of the new amino acyl tRNA in the A site carries out a nucleophilic attack on the esterified carboxyl group of the peptidyl tRNA occupying the P site. This reaction is catalysed by (A) DNA polymerase (B) RNA polymerase (C) Peptidyl transferase (D) DNA ligase
Description : The shape of an enzyme and consequently its activity can be reversibly altered from moment to moment by (A) Heat (B) Amino acid substrate (C) Allosteric subunits (D) Sulfur substitutions
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
Description : Physostigmine is a competitive inhibitor of (A) Xanthine oxidase (B) Cholinesterase (C) Carbonic anhydrase (D) Monoamine oxidase
Description : An enzyme of pyrimidine nucleotide biosynthesis sensitive to allosteric regulation is (A) Aspartate transcarbamoylase (B) Dihydroorotase (C) Dihydroorotate dehydrogenase (D) Orotidylic acid decarboxylase
Description : An enzyme which acts as allosteric regulator and sensitive to both phosphate concentration and to the purine nucleotides is (A) PRPP synthetase (B) PRPP glutamyl midotransferase (C) HGPR Tase (D) Formyl transferase
Description : In which of the following types of enzymes an inducer is not required? (A) Inhibited enzyme (B) Cooperative enzyme (C) Allosteric enzyme (D) Constitutive enzyme
Description : Which of the following is an allosteric enzyme? (A) Phosphohexose isomerase (B) Phosphotriose isomerase (C) Lactate dehydrogenase (D) Phosphofructokinase