Description : Allosteric enzymes regulate the formation of products by (A) Feedback inhibition (B) Non-competitive inhibition (C) Competitive inhibition (D) Repression-derepression
Last Answer : Answer : A
Description : Allosteric inhibition is also known as (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) None of these
Last Answer : Answer : C
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 : 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 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 : 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 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 : 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 sulfa drugs work by _______ with PABA in making folic acid. a. Positive Feedback b. Negative Feedback c. Competitive Inhibition d. Allosteric Inhibition
Last Answer : c. Competitive Inhibition
Description : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate
Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these
Description : Competitive inhibition can be relieved by raising the (A) Enzyme concentration (B) Substrate concentration (C) Inhibitor concentration (D) None of these
Description : In competitive inhibition, the inhibitor (A) Competes with the enzyme (B) Irreversibly binds with the enzyme (C) Binds with the substrate (D) Competes with the substrate
Last Answer : Answer : D
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 : Which one of the following statements regarding enzyme inhibition is correct? (a) Competitive inhibition is seen when a substrate competes with an enzyme for binding to an inhibitor protein. (b ... large amount of substrate. (d) Non-competitive inhibitors often bind to the enzyme irreversibly.
Last Answer : (b) Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzyme
Description : Select the option which is not correct with respect to enzyme action. (a) Substrate binds with enzyme at its active site. (b) Addition of lot of succinate does not reverse the inhibition ... from that which binds the substrate. (d) Malonate is a competitive inhibitor of succinic dehydrogenase.
Last Answer : (b) Addition of lot of succinate does not reverse the inhibition of succinic dehydrogenase by malonate.
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 : 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 : 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 : An example of feedback inhibition is (A) Allosteric inhibition of hexokinase by glucose6-phosphate (B) Cyanide action on cytochrome (C) Sulpha drug on folic acid synthesizer bacteria (D) Reaction between succinic dehydrogenase and succinic acid
Description : The inhibition of succinate dehydrogenase by malonate by (A) Competitive inhibition (B) Non-competitive inhibition (C) Uncompetitive inhibition (D) Feedback inhibition
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 : 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 : 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 : 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 : An example of enzyme inhibition: (A) Reversible inhibition (B) Irreversible inhibition (C) Allosteric inhibition (D) All of these ENZYMES 151
Description : Difference between competitive and allosteric inhibition -Biology
Last Answer : answer:
Description : In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km
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 : 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 : The organophosphates produce irreversible inhibition of cholinesterase because: A. They bind to an allosteric site of the enzyme resulting in unfavourable conformation of esteratic site to bind ... degradation of enzyme molecules D. They are neither metabolized nor excreted from the body
Last Answer : B. Regeneration time of the phosphorylated enzyme is longer than the turnover time of the enzyme molecules
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 : 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
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 : If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is (A) A (B) B (C) C (D) D
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 : 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
Description : ATP is a co-substrate as well as an allosteric inhibitor of (A) Phosphofructokinase (B) Hexokinase (C) Glucokinase (D) None of these
Description : Give examples for allosteric inhibition.
Last Answer : ALA synthase, aspartyl trans-carbamoylase, HMG CoA reductase
Description : What are the salient features of allosteric inhibition?
Last Answer : (1) The inhibitor is not a substrate analogue. (2) It is partially reversible when excess substrate is added. (3) Km is usually increased. (4) Vmax is reduced. (5) Most allosteric enzymes possess quaternary structure. They are made up of subunits.
Description : What is allosteric inhibition?
Last Answer : Allosteric enzyme has one catalytic site where the substrate binds and another separate allosteric site where the modifier binds.
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
Description : The ability of CTP to bind to aspartate carbamoyltransferase and shut down the synthesis of more A- enzyme induction B- enzyme repression C- feedback inhibition of enzyme activity D- none of these
Last Answer : feedback inhibition of enzyme activity
Description : Give examples of non-competitive inhibition.
Last Answer : Di-isopropyl fluoro phosphate inhibits trypsin, fluoride inhibits and enolase.
Description : What are the salient features of non-competitive inhibition?
Last Answer : Non-competitive inhibitor has no structural similarity with the substrate. 2. It is generally not reversible 3. Km is not changed. 4. Vmax is reduced.
Description : An example of competitive inhibition of an enzyme is the inhibition of a. Succinic dehydrogenase by malonic acid b. Cytochrome oxidase by cyanide c. Hexokinase by glucose-6-phosphate d. Carbonic anhydrase by carbon dioxide
Last Answer : Ans: A
Description : If an enzyme‘s active site becomes deformed, inhibition was likely responsible. a. Metabolic b. Competitive c. Noncompetitive d. Cellular
Last Answer : c. Noncompetitive
Description : Negative regulation of protein synthesis is accomplished by A- allosteric inhibition B- the binding of RNA polymerase to the promoter C- the binding of a repressor to the DNA D- the binding of a repressor to the RNA polymerase
Last Answer : the binding of a repressor to the DNA
Description : Regulation of ACTH secretion occurs through (A) Corticotropin releasing hormone (CRH) and corticotropin release inhibiting hormone (CRIH) of hypothalamus (B) Feedback inhibition by cortisol (C) CRH and feedback inhibition by cortisol (D) CRIH and feedback inhibition by cortisol