Description : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
Last Answer : Answer : C
Description : Which factor is responsible for inhibition of enzymatic process during feedback? (a) Substrate (b) Enzymes (c) End product (d) Temperature
Last Answer : (c) End product
Description : $ Coenzymes are usually proteins ! The term feedback refers to the effect of enzyme concentration on its rate of reaction.
Last Answer : $ Coenzymes are usually proteins ! The term feedback refers to the effect of enzyme concentration on its rate ... wrong D. If both As and R are wrong.
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 : 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 : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
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 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 : 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
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 : 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 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 : Transition state structure of the substrate formed during an enzymatic reaction is (a) transient and unstable (b) permanent and stable (c) transient but stable (d) permanent but unstable.
Last Answer : (a) transient and unstable
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 : 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 : What is the effect of substrate concentration on enzyme activity? -Biology
Last Answer : answer:
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 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 : 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 : 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 : 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 : 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 : Which of the following is the correct matchin of the site of action on the given substrate, the enzyme acting state upon it and the end product
Last Answer : Which of the following is the correct matchin of the site of action on the given substrate, the ... alpha`-amylase `rarr` Disac- charide (Maltose)
Description : Which one of the following is the correct matching of the site of action on the given substrate, the enzyme acting upon it and the end product? (a) Small intestine : Proteins Pepsin → ... Trypsin → Monoglycerides (d) Small intestine : Starch α-Amylase → Disaccharide (maltose)
Last Answer : (d) Small intestine : Starch α-Amylase → Disaccharide
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 : 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 : Example of enzyme specificity: (A) Stereo specificity (B) Reaction specificity (C) Substrate specificity(D) All of these
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 : 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
Description : Combination of apoenzyme and coenzyme produces (A) Prosthetic group (B) Holoenzyme (C) Enzyme substrate complex (D) Enzyme product complex
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 : Concentration of substrate on enzyme activity. -Biology
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 energy required to start an enzymatic reaction is called (A) Chemical energy (B) Metabolic energy (C) Activation energy (D) Potential energy
Description : Isoenzymes can be characterized by (A) Proteins lacking enzymatic activity that are necessary for the activation of enzymes (B) Proteolytic enzymes activated by hydrolysis (C) Enzymes with identical primary structure (D) Similar enzymes that catalyse different reaction
Description : Which one of the following is the correct mathcing of the site of action on the given substrate, the enzyme acting upon it and the end producrt?
Last Answer : Which one of the following is the correct mathcing of the site of action on the given substrate, ... ( prop "Amylas")(rarr)` Disaccharie (Maltose)
Description : The reaction catalysed by phosphofructokinase (A) Is activated by high concentrations of ATP and citrate (B) Uses fruitose-1-phosphate as substrate (C) Is the rate-limiting reaction of the glycolytic pathway (D) Is inhibited by fructose 2, 6-bisphosphate
Last Answer : C
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 : Ribozyme is: (a) enzyme (b) RNA with enzymatic activity (c) Hormone (d) Protein
Last Answer : Ans. ((b))
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 : 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