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
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
Last Answer : Answer : B
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 : 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 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 : Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric 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 : 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 : 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 : 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 : 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 : 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 : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
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 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 : 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 enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased
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 : Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these
Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax
Description : Feedback term refers to (A) Effect of substrate on rate of enzymatic reaction (B) Effect of end product on rate reaction (C) Effect of enzyme concentration on rate of reaction (D) Effect of external compound on rate of reaction
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 : Enzymes activity is controlled by (A) pH of the solution (B) Temperature (C) Concentration of the enzyme (D) Concentration of the substrate (E) All of these
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 : The Michaehis-Menten hypothesis: (A) Postulates the formation of an enzyme substrate complex (B) Enables us to calculate the isoelectric point of an enzyme (C) States that the ... independent of substrate concentration (D) States that the reaction rate is proportional to substrate concentration
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 : 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 assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature
Description : Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145
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 enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex
Description : Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein
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 : 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 : ATP is a co-substrate as well as an allosteric inhibitor of (A) Phosphofructokinase (B) Hexokinase (C) Glucokinase (D) None of these
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 blood sugar raising action of the hormone of suprarenal cortex is due to (A) Glyconeogenesis (B) Glycogenolysis (C) Glucagon like activity (D) due to inhibition of glomerular filtration of glucose
Description : The blood sugar raising action of the hormones of suprarenal cortex is due to (A) Gluconeogenesis (B) Glycogenolysis (C) Glucagon-like activity (D) Due to inhibition of glomerular filtration
Last Answer : A
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 : What is the effect of substrate concentration on enzyme activity? -Biology
Last Answer : answer:
Description : Concentration of substrate on enzyme activity. -Biology