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 : 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 : 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 : 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
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 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
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 : 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 : 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 : 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 : 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 : 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 : 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 : 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 : 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 : What holds substrates in position during an enzyme catalyzed reaction?
Last Answer : the acive site
Description : Pick out the wrong statement. (A) Catalytic activity of enzyme catalysed reactions which is affected by temperature, pH value & chemical agents, is maximum at a temperature of about 45°C ... in enzyme catalysed reactions can be calculated by using the thermodynamic properties of substrates & prod
Last Answer : (C) Enzymes help in increasing the activation energy of the reaction
Description : Which one of the following statements regarding a catalyst is not correct? A An enzyme is a catalyst that only binds certain substrates. B An enzyme is a protein that is a highly ... increasing the activation energy. D Catalysts do not alter the equilibrium constant for a chemical reaction.
Last Answer : C Catalysts increase the rate of a reaction by altering the mechanism, thereby increasing the activation energy.
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 : Enzyme involved in joining together two substrates is (A) Glutamine synthetase (B) Aldolase (C) Gunaine deaminase (D) Arginase
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 : 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 : 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 : 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 : 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 : 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 : Draw the following bar graph representing the number of students in each class. -Technology
Last Answer : import matplotlib.pyplot as pltClasses = ['VII','VIII','IX','X']Students = [40,45,35,44]plt.bar(classes, students)plt.show()
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 : An example of enzyme inhibition: (A) Reversible inhibition (B) Irreversible inhibition (C) Allosteric inhibition (D) All of these ENZYMES 151
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 : The curve given below shows enzymatic activity in relation to three conditions (pH, temperature and substrate concentration). What do the two axes (X and Y) represent? X-axis ... (b) Temperature Enzyme activity (c) Substrate Enzymatic concentration activity (d) Enzymatic activity Temperature
Last Answer : (b) Temperature Enzyme activity
Description : What is Competitive Inhibition -Biology
Last Answer : answer:
Description : What is non-competitive Inhibition? -Biology
Description : Difference between competitive and allosteric inhibition -Biology
Description : The sulfa drugs work by _______ with PABA in making folic acid. a. Positive Feedback b. Negative Feedback c. Competitive Inhibition d. Allosteric Inhibition
Last Answer : c. Competitive Inhibition
Description : All of the following statements about thioredoxin reductase are true except: (A) It requires NADH as a coenzyme (B) Its substrates are ADP, GDP, CDP and UDP (C) It is activated by ATP (D) It is inhibited by dADP
Description : Which of the following graph of potential energy represents the unimolecular elimination reaction ?
Last Answer : Which of the following graph of potential energy represents the unimolecular elimination reaction ? A. B. C. D.
Description : The chemical forces that bind most coenzymes and substrates to enzymes such as LDH are (A) Hydrogen bonds (B) Peptide bonds (C) Coordinate bonds (D) Covalent bonds
Description : Enzymes which catalyse binding of two substrates by covalent bonds are known as (A) Lyases (B) Hydrolases (C) Ligases (D) Oxidoreductases
Description : Enzymes leading to the high energy phosphorylation of substrates during glycolysis include which of the following? (A) Phosphoglycerate kinase (B) Enolase (C) Pyruvate Kinase (D) Glyceraldehyde-3-phosphate dehydrogenase
Description : Most amino acids are substrates for transamination except (A) Alanine (B) Threonine (C) Serine (D) Valine