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
Last Answer : Answer : D
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
Last Answer : Answer : C
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
Last Answer : Answer : A
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 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 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 : 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 : 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
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 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 : 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 : 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 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 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 : 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 : In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased
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 : 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 : 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 : 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 : 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 : 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 : 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 : Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145
Description : Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein
Description : The following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All 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 : 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 : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax
Description : In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km
Description : Vmax of an enzyme may be affected by (A) pH (B) Temperature (C) Non-competitive inhibitors (D) All of these
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 : What is the effect of substrate concentration on enzyme activity? -Biology
Last Answer : answer:
Description : Concentration of substrate on enzyme activity. -Biology
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 : A specific fructokinase present in liver has a very high affinity for its substrate because (A) Km for fructose is very high (B) Km for fructose is very low (C) Activity is affected by fasting (D) Activity is affected by insulin
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 : 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
Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
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 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 : 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 : 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 : 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
Description : A substrate for the enzyme aldolase is (A) galactose-6-phosphate (B) isocitric acid (C) Glucose-1-phosphate (D) Fructose 1, 6 diphosphate