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
Last Answer : Answer : B
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 : 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 : 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 : 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 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 enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased
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 : 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 : 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 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 : 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 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 : 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 : Which inactivates an enzyme by occupying its active site? (A) Competitive inhibitor (B) Allosteric inhibitor (C) Non-competitive inhibitor (D) All of these
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 : 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 : 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 : 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 : 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 : 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 : 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
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 : Give examples of non-competitive inhibition.
Last Answer : Di-isopropyl fluoro phosphate inhibits trypsin, fluoride inhibits and enolase.
Description : What are the salient features of non-competitive inhibition?
Last Answer : Non-competitive inhibitor has no structural similarity with the substrate. 2. It is generally not reversible 3. Km is not changed. 4. Vmax is reduced.
Description : What happens to an enzyme when a competitive inhibitor binds to it?
Last Answer : Need answer
Description : The following is a competitive type of enzyme inhibitor: A. Acetazolamide B. Disulfiram C. Physostigmine D. Theophylline
Last Answer : C. Physostigmine
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 : 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 : 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
Description : Pasteur effect is (A) Inhibition of glycolysis (B) Oxygen is involved (C) Inhibition of enzyme phosphofructokinase (D) All of these
Last Answer : D
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
Description : Photosynthetic inhibition by 02 is called: (A) Reaction (B) Warburg’s effect (C) Back inhibition (D) Competitive effect
Last Answer : (B) Warburg’s effect
Description : Physostigmine is a competitive inhibitor of (A) Xanthine oxidase (B) Cholinesterase (C) Carbonic anhydrase (D) Monoamine oxidase
Description : Give examples of clinical application of competitive inhibition.
Last Answer : Sulfonamide inhibits PABA incorporation in bacteria, and so acts as an antibacterial agent. Methotrexate inhibits folate reductase system, dicoumarol inhibits vitamin K.
Description : Give examples of competitive inhibition.
Last Answer : Malonate inhibits succinate dehydrogenase.
Description : What are salient features of competitive inhibition?
Last Answer : Competitive inhibitor is a structural analogue. 2. It is reversible. 3. Km is increased. 4. Vmax is not changed.
Description : The ability of CTP to bind to aspartate carbamoyltransferase and shut down the synthesis of more A- enzyme induction B- enzyme repression C- feedback inhibition of enzyme activity D- none of these
Last Answer : feedback inhibition of enzyme activity
Description : What is non-competitive Inhibition? -Biology
Last Answer : answer:
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 : Which of the following is/are true of the actions of transforming growth factor beta (TGF-b) during wound repair? A. Increased matrix and proteoglycan synthesis. B. Inhibition of proteases. ... of plasminogen inhibitor. D. Chemotaxis for fibroblasts and macrophages. E. Autoinduction of TGF-b.
Last Answer : Answer: ABDE DISCUSSION: Through autocrine and paracrine mechanisms TGF-b stimulates the deposition of collagen and other matrix components by fibroblasts, inhibits proteases, blocks plasminogen inhibitor, ... effects. The sustained production of TGF-b at the wound site leads to tissue fibrosis
Description : The mode of action of Isoproturon is a). Root inhibitor b). Shoot inhibitor c). Photosynthesis inhibition d). Amino acid inhibition
Last Answer : c). Photosynthesis inhibition