Description : If a coenzyme is required in an enzyme reaction, the former usually has the function of (A) Acting as an acceptor for one of the cleavage products of the substrate (B) Enhancing the specificity ... C) Increasing the number of receptor sites of the apo enzyme (D) Activating the substrate ENZYMES 167
Last Answer : Answer : A
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
Last Answer : Answer : C
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
Last Answer : Answer : B
Description : Template/lock and key theory of enzyme action is supported by (A) Enzymes speed up reaction (B) Enzymes occur in living beings and speed up certain reactions (C) Enzymes determine the direction of reaction (D) Compounds similar to substrate inhibit enzyme activity
Last Answer : Answer : D
Description : An enzyme promotes a chemical reaction by (A) Lowering the energy of activation (B) Causing the release of heat which acts as a primer (C) Increasing molecular motion (D) Changing the free energy difference between substrate and product
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 : 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 : 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 : An allosteric enzyme is generally inhibited by (A) Initial substrate of the pathway (B) Substrate analogues (C) Product of the reaction catalysed by allosteric enzyme (D) Product of the pathway
Description : Give an example for group specificity.
Last Answer : trypsin can hydrolyse peptide bonds formed by carboxyl groups of arginine or lysine residues.
Description : Give an example for absolute specificity.
Last Answer : Urea is the only substrate for urease.
Description : The example of generation of a high energy phosphate at the substrate level in the citric acid cycle is the reaction: (A) Isocitrate α-Ketoglutarate (B) Succinate α-fumarate (C) Malate α-oxaloacetate (D) Succinyl CoA α-Succinate
Description : Regulator gene controls chemical synthesis (Operon concept) by (a) Inhibiting transcription of mRNA (b) Inhibiting enzymes (c) Inhibiting passage of mRNA (d) Inhibiting substrate enzyme reaction
Last Answer : Ans. ((a))
Description : The figure given Progress of Reaction Product Substrate B A C D below shows the conversion of a substrate into product by an enzyme. In which one of the four options (A-D ... enzyme enzyme (d) Activation Transition Activation Potential energy state energy energy with without enzyme enzyme
Last Answer : (b) Transition Potential Activation Activation state energy energy energy without with enzyme enzyme
Description : Which of the following describes the given graph correctly? Potential energy Reaction Product Substrate B A (a) Endothermic reaction with energy A in presence of enzyme and B in absence of enzyme. (b) ... . (d) Exothermic reaction with energy A in absence of enzyme and B in presence of enzyme.
Last Answer : (b) Exothermic reaction with energy A in presence of enzyme and B in absence of enzyme
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 : The ratio of enzyme to substrate molecules can be as low as (A) 1 : 100,000 (B) 1 : 500,000 (C) 1 : 10,000 (D) 1 : 1,000
Description : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
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 : Combination of apoenzyme and coenzyme produces (A) Prosthetic group (B) Holoenzyme (C) Enzyme substrate complex (D) Enzyme product complex
Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
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 : 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 : 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 : 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 : 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 : A substrate for the enzyme aldolase is (A) galactose-6-phosphate (B) isocitric acid (C) Glucose-1-phosphate (D) Fructose 1, 6 diphosphate
Description : In enzyme assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature
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 : The hypothesis to explain enzyme– substrate complex formation: (A) Lock and key model (B) Induced fit theory (C) Proenzyme theory (D) Both (A) and (B)
Description : If all the enzymes, intermediates and cofactors of the citric acid cycle as well as an excess of the starting substrate acetylCoA are present and functional in an organelle free solution at the appropriate ... oxygen (B) Half life of enzyme (C) Turnover of intermediates (D) Reduction of cofactors
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 : An enzyme which uses hydrogen acceptor as substrate is (A) Xanthine oxidase (B) Aldehyde oxidase (C) Catalase (D) Tryptophan oxygenase
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 : 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 : 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 : Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein
Description : Hormone receptors possess all the following properties except (A) All of them are proteins (B) They possess a recognition domain (C) They bind hormones with a high degree of specificity (D) Number of receptors in a target cell is constant
Description : Thyroid stimulating hormone is a dimer. The α-subunits of TSH, LH, FSH are identical. Thus the biological specificity must therefore be β subunit in which the number of amino acids is (A) 78 (B) 112 (C) 130 (D) 199
Description : At low blood glucose concentration, brain but not liver will take up glucose. It is due to the (A) Low Km of hexokinase (B) Low Km of glucokinase (C) Specificity of glucokinase (D) Blood brain barrier
Description : What are the types of specificity shown by enzymes?
Last Answer : Absolute specificity, group specificity and streospecificity.
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
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 : From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S