Description : A substance unrelated to substrate but capable of reversibly changing activity of enzyme by binding to a site other than active site is called (a) Competitive inhibitor (b) Non-competitive inhibitor (c) Catalytic inhibitor (d) Allosteric modulator/inhibitor
Last Answer : Ans. ((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 : 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 : 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 : 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 : 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
Last Answer : Answer : D
Description : Allosteric enzymes contain (A) Multiple subunits (B) Single chain (C) Two chains (D) Three chains
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 : 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 : ATP is a co-substrate as well as an allosteric inhibitor of (A) Phosphofructokinase (B) Hexokinase (C) Glucokinase (D) None of these
Description : The active site of an enzyme is formed by a few of the enzymes: (A) R groups of the amino acids (B) Amino groups of the amino acids (C) Carboxyl group of the amino acids (D) Exposed sulfur bonds
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 : 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
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
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 : 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 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 : An enzyme of pyrimidine nucleotide biosynthesis sensitive to allosteric regulation is (A) Aspartate transcarbamoylase (B) Dihydroorotase (C) Dihydroorotate dehydrogenase (D) Orotidylic acid decarboxylase
Description : The rate of citric acid cycle is controlled by the allosteric enzyme: (A) Aconitase (B) Fumarase (C) Fumarase (D) Malate dehydrogenase
Description : Different isoenzymes of an enzyme have the same (A) Amino acid sequence (B) Michaelis constant (C) Catalytic activity (D) All of these
Description : Tetracyclines inhibit binding of amino acyl tRNAs to (A) 30 S ribosomal subunits (B) 40 S ribosomal subunits (C) 50 S ribosomal subunits (D) 60 S ribosomal subunits
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 : 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 : Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation
Last Answer : C. Alter its folding or alignment of subunits
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 : Select the drug that reversibly inhibits the enzyme COMT and is useful as an adjuvant medication in advanced parkinson's disease: A. Pramipexole B. Entacapone C. Pergolide D. Piribedil
Last Answer : B. Entacapone
Description : Peptidyl transferase activity of 50 S ribosomal subunits is inhibited by (A) Rifampicin (B) Cycloheximide (C) Chloramphenicol (D) Erythromycin
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 : 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 : 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 : Which inactivates an enzyme by occupying its active site? (A) Competitive inhibitor (B) Allosteric inhibitor (C) Non-competitive inhibitor (D) All of these
Description : An enzyme which acts as allosteric regulator and sensitive to both phosphate concentration and to the purine nucleotides is (A) PRPP synthetase (B) PRPP glutamyl midotransferase (C) HGPR Tase (D) Formyl transferase
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 which of the following types of enzymes an inducer is not required? (A) Inhibited enzyme (B) Cooperative enzyme (C) Allosteric enzyme (D) Constitutive enzyme
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 : Which of the following is an allosteric enzyme? (A) Phosphohexose isomerase (B) Phosphotriose isomerase (C) Lactate dehydrogenase (D) Phosphofructokinase
Description : Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these
Description : An example of enzyme inhibition: (A) Reversible inhibition (B) Irreversible inhibition (C) Allosteric inhibition (D) All of these ENZYMES 151
Description : In gluconeogensis, an allosteric activator required in the synthesis of oxaloacetate from bicarbonate and pyruvate, which is catalysed by the enzyme pyruvate carboxylase is (A) Acetyl CoA (B) Succinate (C) Isocitrate (D) Citrate
Description : A demonstrable inducer is absent in (A) Allosteric enzyme (B) Constitutive enzyme (C) Inhibited enzyme (D) Co-operative enzyme ENZYMES 141
Description : An inducer is absent in the type of enzyme: (A) Allosteric enzyme (B) Constitutive enzyme (C) Co-operative enzyme (D) Isoenzymic enzyme
Description : An allosteric enzyme responsible for controlling the rate of T.C.A cycle is (A) Malate dehydrogenase (B) Isocitrate dehydrogenase (C) Fumarase (D) Aconitase
Last Answer : B
Description : Which of the following compound is a positive allosteric modifier of the enzyme pyruvate carboxylase? (A) Biotin (B) Acetyl CoA (C) Oxaloacetate (D) ATP
Last Answer : A
Description : When amino acids are treated with neutral formaldehyde, the pH of the mixture (A) Is not altered (B) Increases (C) Decreases (D) First increases then decreases
Description : 1m3 of an ideal gas at 500 K and 1000 kPa expands reversibly to 5 times its initial volume in an insulated container. If the specific heat capacity (at constant pressure) of the gas is 21 J/mole . K, the final temperature will be (A) 35 K (B) 174 K (C) 274 K (D) 154 K
Last Answer : (C) 274 K
Description : A system absorbs reversibly 600 J of heat and performs 250 J of work. The increase in the internal energy of system is :-
Last Answer : A system absorbs reversibly 600 J of heat and performs 250 J of work. The increase in the internal energy of system ... J B. 250 J C. 600 J D. 350 J