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

1 Answer

Answer :

Answer :  C

Related questions

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

Last Answer : Answer : B

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 : Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Last Answer : Answer : C

Description : Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein

Last Answer : Answer : B

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 : 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 : 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

Last Answer : Answer : A

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

Last Answer : Answer : D

Description : Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Last Answer : Answer : C

Description : In Lineweaver-Burk plot, the y-intercept represents (A) Vmax (B) Km (C) Km (D) 1/Km

Last Answer : Answer : B

Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Last Answer : Answer : D

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

Last Answer : Answer : A

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

Last Answer : Answer : B

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

Last Answer : Answer : A

Description : Lineweaver – Burk double reciprocal plot is related to (A) Substrate concentration (B) Enzyme activity (C) Temperature (D) Both (A) and (B) ENZYMES 145

Last Answer : Answer : D

Description : What is Michaelis-Menten Theory ?

Last Answer : It is otherwise called enzyme-substrate complex theory. The enzyme combines with the substrate, to form an enzyme-substrate complex, which immediately breaks down to the enzyme and the product.

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 enzyme kinetics Vmax reflects (A) The amount of an active enzyme (B) Substrate concentration (C) Half the substrate concentration (D) Enzyme substrate complex

Last Answer : Answer : A

Description : What is Michaelis Menten constant? -Biology

Last Answer : answer:

Description : ........................ studied the kinetics of enzyme catalysis. a. Arrhenius b. Rutherford c. Micheal Faraday d. Michaelis & Menten

Last Answer : d. Michaelis & Menten

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

Last Answer : Answer : D

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

Last Answer : Answer : B

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

Last Answer : Answer : C

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 : 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

Last Answer : Answer : 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

Last Answer : Answer : B

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 following abnormality in PRPP synthetase can cause primary gout: (A) High Vmax (B) Low Km (C) Resistance to allosteric inihbition. (D) All of these

Last Answer : Answer : D

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

Last Answer : Answer : A

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

Last Answer : Answer : D

Description : Competitive inhibitors (A) Decrease the Km (B) Decrease the Vmax (C) Increase the Km (D) Increase the Vmax

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

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

Last Answer : Answer : A

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 : The velocity of a ball tossed vertically into the air is expressed by the equation v(t) = -32t + 4, where t is given in seconds. Give the velocity of the ball when it reaches its highest point. 

Last Answer : ANSWER: 0

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 : If the time required for half change is inversely proportional to the square of initial concentration and the velocity depends on the units in which the concentration term is expressed, then the order of reaction is (A) 0 (B) 1 (C) 2 (D) 3

Last Answer : (D) 3

Description : A bed of spherical particles (specific gravity 2.5) of uniform size 1500 μm is 0.5 m in diameter and 0.5 m high. In packed bed state, the porosity may be taken as 0.4. Ergun's equation for the above fluid-particle ... fluidisation velocity, VOM is (A) 12 mm/s (B) 16 mm/s (C) 24 mm/s (D) 28 mm/s

Last Answer : (B) 16 mm/s

Description : Rate of reaction can be expressed as –dc/dt where dc is small decreasing concentration in time dt seconds, (-) sign indicates that the concentration decreases with time. For every 10 degrees rise of temperature, the rate of reaction is generally. Doubled

Last Answer : Which equation gives the relation between specific rate (k) and Temperature ?

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

Last Answer : Answer : B

Description : For a reaction `2X(s)+2Y(s)rarr 2Cl(l)+D(g)` The `q_(p)` at `27^(@)C` is -28 K Cal. `mol^(-1)`. The `q_(V)` is ___________ K. Cal. `mol^(-1)` :-

Last Answer : For a reaction `2X(s)+2Y(s)rarr 2Cl(l)+D(g)` The `q_(p)` at `27^(@)C` is -28 K Cal. `mol^(-1)`. The `q_( ... . `-27.4` B. `+27.4` C. `-28.6` D. `28.6`

Description : Which of the points P(0, 3), Q(l, 0), R(0, – 1), S(-5, 0) and T(1, 2) do not lie on the X-axis ? -Maths 9th

Last Answer : (c) We know that, if a point is of the form (x, 0)i.e., its y-coordinate is zero, then it will lie on X-axis otherwise not. Here, y-coordinates of points P(0, 3), R (0, -1) and T (1,2) are not zero, so these points do not lie on the X-axis.

Description : Which of the points P(0, 3), Q(l, 0), R(0, – 1), S(-5, 0) and T(1, 2) do not lie on the X-axis ? -Maths 9th

Last Answer : (c) We know that, if a point is of the form (x, 0)i.e., its y-coordinate is zero, then it will lie on X-axis otherwise not. Here, y-coordinates of points P(0, 3), R (0, -1) and T (1,2) are not zero, so these points do not lie on the X-axis.

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

Last Answer : Answer : C

Description : In enzyme assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature

Last Answer : Answer : B

Description : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these

Last Answer : Answer : B

Description : The order of reaction is the number of moles whose concentrations determine the rate of a reaction at a given temperature Give the integrated equation for first order reaction. K = (2.303 / t) * log (a ... a' is the initial concentration of reactants x' is the amount reacted in time t seconds

Last Answer : What is Threshold energy ?

Description : If C is basic capacity per lane, V is velocity in km/hour, S is stopping distance plus length of the vehicles in metres, the formula C = 1000V/S is applicable to (A) District roads (B) Two lane roads (C) Two lane roads in one direction (D) None of these

Last Answer : Answer: Option C

Description : Different isoenzymes of an enzyme have the same (A) Amino acid sequence (B) Michaelis constant (C) Catalytic activity (D) All of these

Last Answer : Answer : C