Description : Part of enzyme which combines with nonprotein part to form functional enzyme is (A) Apoenzyme (B) Coenzyme (C) Prosthetic group (D) None of these
Last Answer : Answer : C
Description : Consider the following statements. (A) Coenzyme or metal ion that is tightly bound to enzyme protein is called prosthetic group. (B) A complete catalytic active enzyme with its bound prosthetic group is called apoenzyme. Select the ... ) (A) is true but (B) is false. (d) Both (A) and (B) are false
Last Answer : (d) Both (A) and (B) are false.
Description : An organic substance bound to an enzyme and essential for the activity of enzyme is called (A) Holoenzyme (B) Apoenzyme (C) Coenzyme (D) Isoenzyme
Description : The active form of enzyme is A- apoenzyme B- coenzyme C- holoenzyme D- none of these
Last Answer : holoenzyme
Description : Which of the following statements is correct with reference to enzymes? (a) Holoenzyme = Apoenzyme + Coenzyme (b) Coenzyme = Apoenzyme + Holoenzyme (c) Holoenzyme = Coenzyme + Co-factor (d) Apoenzyme = Holoenzyme + Coenzyme
Last Answer : a) Holoenzyme = Apoenzyme + Coenzyme
Description : Which one of the following statements is correct , with reference to enzymes ? (1) Holoenzyme = Apoenzyme + Coenzyme (2) Coenzyme = Apoenzyme + Holoenzyme (3) Holoenzyme = Coenzyme + Co-factor (4) Apoenzyme = Holoenzyme + Coenzyme
Last Answer : (1) Holoenzyme = Apoenzyme + Coenzyme
Description : Protein part of enzyme is know as – (1) Isoenzyme (2) Holoenzyme (3) Apoenzyme (4) All the above
Last Answer : (3) Apoenzyme Explanation: Enzymes are defined as biological catalysts. Chemically all enzymes are globular proteins. Each enzyme catalyses only one chemical reaction. Protein part of enzyme is known as Apoenzyme.
Description : Protein portion of an enzyme when it is combined with organic molecule is termed as A- apoenzyme B- co-enzyme C- holoenzyme D- co-factors
Last Answer : apoenzyme
Description : Protein part of enzyme is know as (1) Isoenzyme (2) Holoenzyme (3) Apoenzyme (4) All the above
Last Answer : Apoenzyme
Description : Cofactor (Prosthetic group) is a part of holoenzyme, it is (A) Inorganic part loosely attached (B) Accessory non-protein substance attached firmly (C) Organic part attached loosely (D) None of these
Last Answer : Answer : B
Description : A Holoenzyme is (A) Functional unit (B) Apo enzyme (C) Coenzyme (D) All of these
Last Answer : Answer : D
Description : Apoenzyme + Prosthetic group
Last Answer : Ans. Holoenzyme
Description : Co-factor (prosthetic group) is a part of holoenzyme. It is (a) loosely attached organic part (b) loosely attached inorganic part (c) accessory non-protein substance attached firmly (d) none of these.
Last Answer : (c) accessory non-protein substance attached firmly
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 : difference between apoenzyme and holoenzyme -Biology
Last Answer : answer:
Description : Hormones (A) Act as coenzyme (B) Act as enzyme (C) Influence synthesis of enzymes (D) Belong to B-complex group
Description : Which of the following is not having an apoenzyme and coenzyme? (A) Lactate dehydrogenase (B) Succinate dehydrogenase (C) Malate dehydrogenase (D) Pepsin
Description : Zn is present as prosthetic group in this enzyme: (A) Carbonic anhydrase (B) Carboxy peptidase (C) Lactate dehydrogenase (D) All of these
Description : Of Which warburg’s yellow enzyme contains as a prosthetic group? (A) Thiamine pyrophosphate (B) Biotin (C) NAD+ (D) Riboflavin-5-phosphate
Description : Difference between apoenzyme and coenzyme -Biology
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 : 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 : 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 : Enzymes combine with a ___________at the___________ site to lower the activation energy. a. Substrate; Active b. Product; Noncompetitive c. Product; Active d. Coenzyme; Active
Last Answer : a. Substrate; Active
Description : Binding of RNA polymerase holoenzyme to the promoter region of lac operon is facilitated by (A) Catabolite gene activator protein (CAP) (B) cAMP (C) CAP-cAMP complex (D) None of these
Description : Consider the following statements: (1) Copper is present in cytochrome oxidane (2) Pantothenic acid is precursor of co-enzyme-A (3) Thiamine prohosphate is the prosthetic group in decarboxylases (4) Zinc is present in RNA and DNA polymerases
Last Answer : Ans. ((b))
Description : Enzyme without Prosthetic group
Last Answer : Ans. Apo enzyme
Description : Ribonucleotides of RNA primer are replaced by deoxyribonucleotides by the enzyme: (A) DNA polymerase I (B) DNA polymerase II (C) DNA polymerase III holoenzyme (D) 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 : 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 : 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 : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
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 : Glycoproteins are marked for destruction by removal of their (A) Oligosaccharide prosthetic group (B) Sialic acid residues (C) Mannose residues (D) N-terminal amino acids
Description : The half-life of a protein depends upon its (A) Signal sequence (B) N-terminus amino acid (C) C-terminus amino acid (D) Prosthetic group
Description : Iron-pophyrin is present as prosthetic group in (A) Cytochromes (B) Catalases (C) Peroxidase (D) None of these
Description : The prosthetic group of aerobic dehydrogenases is (A) NAD (B) NADP (C) FAD (D) Pantothenic acid
Description : Prosthetic group in cone cell phototreceptors is (A) Iodine (B) Opsin (C) 11-cis-retinal (D) all-trans-retinal
Description : In most metabolic pathways, all needed enzymes are arranged together in a multienzyme complex within a (A) Solution of ATP (B) Membrane (C) Quanternary protein (D) Coenzyme
Description : Prosthetic groups differ from co-enzymes in that (a) they require metal ions for their activity (b) they (prosthetic groups) are tightly bound to apoenzymes (c) their association with apoenzymes is transient (d) they can serve as co-factors in a number of enzyme-catalyzed reactions.
Last Answer : (b) they (prosthetic groups) are tightly bound to apoenzymes
Description : An inorganic ion required for the activity of an enzyme is known as (A) Activator (B) Cofactor (C) Coenzyme (D) None of these
Description : Biotin is a coenzyme of the enzyme (A) Carboxylase (B) Hydroxylase (C) Decarboxylase (D) Deaminase
Description : Riboflavin is a coenzyme in the reaction catalysed by the enzyme (A) Acyl CoA synthetase (B) Acyl CoA dehydrogenase (C) β-Hydroxy acyl CoA (D) Enoyl CoA dehydrogenase
Description : The following co-enzyme is needed for the oxidative decarboxylation of ketoacids: (A) NADP+ (B) TPP (C) Folate coenzyme (D) Biotin coenzyme
Last Answer : B
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 : Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric inhibition