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Which one of the following statements is NOT true?
- a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzyme
- b)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibition
- c)A transition state analogue in enzyme catalyzed reaction increases the rate of product formation
- d)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increases
Correct answer is option 'C'. Can you explain this answer?
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Which one of the following statements is NOT true?a)In competitive inh...
Transition state analogs (transition state analogues), are chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in anenzyme-catalyzed chemical reaction. Enzymes interact with a substrate by means of strain or distortions, moving the substrate towards the transition state.[1] Theory suggests that enzyme inhibitors which resembled the transition state structure would bind more tightly to the enzyme than the actual substrate.[2] Transition state analogs can be used as inhibitors in enzyme catalyzed reactions by blocking the active site of the enzyme. Examples of drugs that are transition state analog inhibitors include flu medications such as the neuraminidase inhibitor oseltamivir and the HIV protease inhibitors saquinavir in the treatment of AIDS.
In non-competitive inhibition, the Km does not change. This is because Km is a measure of the affinity of the enzyme for its substrate and this can only be measured by active enzyme. The fixed amount of inactive enzyme in non-competitive inhibition does not affect the Km and the Km, therefore is unchanged
In non-competitive inhibition, the Km does not change. This is because Km is a measure of the affinity of the enzyme for its substrate and this can only be measured by active enzyme. The fixed amount of inactive enzyme in non-competitive inhibition does not affect the Km and the Km, therefore is unchanged
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Which one of the following statements is NOT true?a)In competitive inh...
Introduction:
In enzyme catalyzed reactions, various types of enzyme inhibition can occur. In this question, we are asked to identify the statement that is NOT true regarding enzyme inhibition.
Competitive Inhibition:
In competitive inhibition, the inhibitor molecule competes with the substrate molecule for the same active site on the enzyme. Both the substrate and the inhibitor can bind to the active site, but they cannot bind simultaneously. As a result, the presence of the inhibitor reduces the effective concentration of the substrate that can bind to the enzyme. This type of inhibition can be overcome by adding a large amount of substrate because the increased substrate concentration increases the chances of substrate molecules outcompeting the inhibitor for the active site.
Uncompetitive Inhibition:
Uncompetitive inhibition occurs when the inhibitor binds to the enzyme-substrate complex, forming an enzyme-inhibitor-substrate ternary complex. The inhibitor only binds to the enzyme-substrate complex and does not compete with the substrate for the active site. Addition of a large amount of substrate cannot overcome uncompetitive inhibition because the inhibitor specifically binds to the enzyme-substrate complex, preventing the release of the product and inhibiting the overall reaction.
Transition State Analogue:
A transition state analogue is a molecule that mimics the transition state of a reaction. It binds to the active site of the enzyme with high affinity and specificity, resembling the transition state structure. The presence of a transition state analogue in an enzyme-catalyzed reaction can increase the rate of product formation by stabilizing the transition state and lowering the activation energy required for the reaction.
Non-competitive Inhibition:
In non-competitive inhibition, the inhibitor binds to a site on the enzyme other than the active site, known as an allosteric site. This binding does not directly interfere with the substrate binding to the active site. As the concentration of the inhibitor increases, it reduces the maximum velocity (Vmax) of the reaction, but the Km (Michaelis constant) remains constant.
Conclusion:
The statement that is NOT true is option 'C'. A transition state analogue in enzyme-catalyzed reactions increases the rate of product formation by mimicking the transition state and stabilizing it, thereby lowering the activation energy required for the reaction.
In enzyme catalyzed reactions, various types of enzyme inhibition can occur. In this question, we are asked to identify the statement that is NOT true regarding enzyme inhibition.
Competitive Inhibition:
In competitive inhibition, the inhibitor molecule competes with the substrate molecule for the same active site on the enzyme. Both the substrate and the inhibitor can bind to the active site, but they cannot bind simultaneously. As a result, the presence of the inhibitor reduces the effective concentration of the substrate that can bind to the enzyme. This type of inhibition can be overcome by adding a large amount of substrate because the increased substrate concentration increases the chances of substrate molecules outcompeting the inhibitor for the active site.
Uncompetitive Inhibition:
Uncompetitive inhibition occurs when the inhibitor binds to the enzyme-substrate complex, forming an enzyme-inhibitor-substrate ternary complex. The inhibitor only binds to the enzyme-substrate complex and does not compete with the substrate for the active site. Addition of a large amount of substrate cannot overcome uncompetitive inhibition because the inhibitor specifically binds to the enzyme-substrate complex, preventing the release of the product and inhibiting the overall reaction.
Transition State Analogue:
A transition state analogue is a molecule that mimics the transition state of a reaction. It binds to the active site of the enzyme with high affinity and specificity, resembling the transition state structure. The presence of a transition state analogue in an enzyme-catalyzed reaction can increase the rate of product formation by stabilizing the transition state and lowering the activation energy required for the reaction.
Non-competitive Inhibition:
In non-competitive inhibition, the inhibitor binds to a site on the enzyme other than the active site, known as an allosteric site. This binding does not directly interfere with the substrate binding to the active site. As the concentration of the inhibitor increases, it reduces the maximum velocity (Vmax) of the reaction, but the Km (Michaelis constant) remains constant.
Conclusion:
The statement that is NOT true is option 'C'. A transition state analogue in enzyme-catalyzed reactions increases the rate of product formation by mimicking the transition state and stabilizing it, thereby lowering the activation energy required for the reaction.
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Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer?
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Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? for GATE 2024 is part of GATE preparation. The Question and answers have been prepared according to the GATE exam syllabus. Information about Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? covers all topics & solutions for GATE 2024 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer?.
Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? for GATE 2024 is part of GATE preparation. The Question and answers have been prepared according to the GATE exam syllabus. Information about Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? covers all topics & solutions for GATE 2024 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer?.
Solutions for Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? in English & in Hindi are available as part of our courses for GATE.
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ample number of questions to practice Which one of the following statements is NOT true?a)In competitive inhibition, substrate and inhibitor compete for the same active site of an enzymeb)Addition of a large amount of substrate to an enzyme cannot overcome uncompetitive inhibitionc)A transition state analogue in enzyme catalyzed reaction increases the rate of product formationd)In non-competitive inhibition, Km of an enzyme for its substrate remains constant as the concentration of the inhibitor increasesCorrect answer is option 'C'. Can you explain this answer? tests, examples and also practice GATE tests.
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