What are the salient features of non-competitive inhibition?

What are the salient features of non-competitive inhibition? 
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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.
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What are salient features of competitive inhibition?

Description : What are salient features of competitive inhibition?

Last Answer : Competitive inhibitor is a structural analogue. 2. It is reversible. 3. Km is increased. 4. Vmax is not changed.

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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.

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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

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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

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The inhibition of succinate dehydrogenase by malonate by (A) Competitive inhibition (B) Non-competitive inhibition (C) Uncompetitive inhibition (D) Feedback inhibition

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Allosteric inhibition is also known as (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) None of these

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

In non competitive enzyme activity inhibition, inhibitor (A) Increases Km (B) Decreases Km (C) Does not effect Km (D) Increases Km

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Last Answer : Answer : C

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

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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

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Last Answer : Di-isopropyl fluoro phosphate inhibits trypsin, fluoride inhibits and enolase.

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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

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

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Last Answer : Answer : B

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

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In competitive enzyme activity inhibition (A) Apparent Km is decreased (B) Apparent Km is increased (C) Vmax is increased (D) Vmax is decreased

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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

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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

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