Study the reaction given below

CO2+H2OEnzymeH2CO3

In absence of any enzyme this reaction is very slow, with 200 molecules of H2CO3 formed in one hour. In presence of an enzyme the reaction speeds up dramatically with about 600,000 molecules formed every second. Name the enzyme which has accelerated up the reaction by 10 million times.

1. Ribozyme

2. Carbonic anhydrase

3. Catalase

4. Peroxidase

Subtopic:  Enzyme Inhibition |
 95%
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The competitive inhibitor of enzyme succinic dehydrogenase is

1. succinate

2. malonate

3. malate

4. mannose

Subtopic:  Enzyme Inhibition |
 91%
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Which of the following set of coenzymes are nucleotides of vitamin niacin ?

1. NAD, NADP

2. FMN, FAD

3. ATP, ADP

4. ATP, FAD

Subtopic:  Enzyme Inhibition |
 94%
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In competitive inhibition:

(1) Inhibitor resembles the substrate in molecular structure

(2) Competition between substrates and inhibitors to occupy active sites

(3) Binding the inhibitors to activities sites declines the enzyme action

(4) All are correct

Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
 92%
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The inhibition of succinic dehydrogenase by malonate is an example of

1. competitive inhibition

2. non-competitive inhibition

3. allosteric modulation

4. none of the above

Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
 92%
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The adjoining graph shows change in conc. of substrate on enzyme activity. Identify A, B and C:

 

A

B

C

(1)

Ki

Km

Vmax

(2)

Vmax2

Km

Ki

(3)

Vmax

Km

Vmax2

(4)

Km

Vmax

Vmax2
Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
 87%
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Which of the following class of enzyme catalyse removal of groups from substrates by mechanism other than hydrolysis leaving double bonds?

1. Lyases

2. Ligases

3. Isomerases

4. Hydrolases

Subtopic:  Enzyme Inhibition |
 83%
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Select the option which is not correct with respect to enzyme action.

1. Substrate binds with enzyme as its active site

2. Addition of lot of succinate does not reverse the inhibition of succinic dehydogenase by malonate.

3. A non-competitive inhibitor binds the enzyme at a site distinct from that which binds the substrate

4. Malonate is a competitive inhibitor of succinic dehydrogenase

Subtopic:  Enzyme Inhibition: Introduction | Enzyme Inhibition |
 68%
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Given below is the graph showing the effect of substrate concentration on enzyme activity. In the presence of a competitive inhibitor, when the concentration of the substrate is progressively increased:

 

1. The Km value increases but the reaction will not achieve Vmax
2. The Km value increases but the reaction can ultimately achieve  Vmax
3. The Km value decreases but the reaction will not achieve Vmax
4. The Km value decreases but the reaction can ultimately achieve  Vmax
Subtopic:  Enzyme Inhibition |
 60%
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In non-competitive inhibition:

1. the substrate and inhibitor cannot bind to the enzyme at the same time

2. the inhibitor binds only to the substrate-enzyme complex

3. the inhibitor can bind to the enzyme at the same time as the enzyme's substrate

4. the binding of the inhibitor to the enzyme reduces its activity but does not affect the binding of substrate

Subtopic:  Enzyme Inhibition |
 53%
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