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An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?
- a)A protonated Asp
- b)A deprotonated Asp
- c)A deprotonated Asn
- d)A protonated Asn
Correct answer is option 'A'. Can you explain this answer?
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Most Upvoted Answer
An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 ...
Explanation:
The pH at which an enzyme shows maximum activity is called its optimal pH. The activity of an enzyme decreases as the pH deviates from its optimal pH. This is because the pH affects the charge of amino acid residues at the active site of the enzyme, which in turn affects the enzyme-substrate interaction.
The given enzyme shows the highest activity in the pH range of 2.0-3.0. At pH 4.0 and pH 7.0, the enzyme exhibits only 50% and 1% of its highest activity, respectively. This indicates that the active site of the enzyme has an acidic amino acid residue that is responsible for its activity profile.
The correct answer is option 'A', which states that a protonated Asp residue is most responsible for the enzyme's activity profile. This means that the carboxyl group of Asp is protonated at the optimal pH, and it interacts with the substrate to catalyze the reaction.
At pH 4.0, the protonated Asp residue starts to deprotonate, reducing the enzyme's activity. At pH 7.0, the Asp residue is completely deprotonated and loses its ability to interact with the substrate, resulting in very low enzymatic activity.
In summary, the pH affects the charge of amino acid residues at the active site of the enzyme, which in turn affects the enzyme-substrate interaction. The given enzyme shows the highest activity in the pH range of 2.0-3.0, indicating that the active site of the enzyme has a protonated Asp residue that is responsible for its activity profile.
The pH at which an enzyme shows maximum activity is called its optimal pH. The activity of an enzyme decreases as the pH deviates from its optimal pH. This is because the pH affects the charge of amino acid residues at the active site of the enzyme, which in turn affects the enzyme-substrate interaction.
The given enzyme shows the highest activity in the pH range of 2.0-3.0. At pH 4.0 and pH 7.0, the enzyme exhibits only 50% and 1% of its highest activity, respectively. This indicates that the active site of the enzyme has an acidic amino acid residue that is responsible for its activity profile.
The correct answer is option 'A', which states that a protonated Asp residue is most responsible for the enzyme's activity profile. This means that the carboxyl group of Asp is protonated at the optimal pH, and it interacts with the substrate to catalyze the reaction.
At pH 4.0, the protonated Asp residue starts to deprotonate, reducing the enzyme's activity. At pH 7.0, the Asp residue is completely deprotonated and loses its ability to interact with the substrate, resulting in very low enzymatic activity.
In summary, the pH affects the charge of amino acid residues at the active site of the enzyme, which in turn affects the enzyme-substrate interaction. The given enzyme shows the highest activity in the pH range of 2.0-3.0, indicating that the active site of the enzyme has a protonated Asp residue that is responsible for its activity profile.
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An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer?
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An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? for IIT JAM 2024 is part of IIT JAM preparation. The Question and answers have been prepared according to the IIT JAM exam syllabus. Information about An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? covers all topics & solutions for IIT JAM 2024 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer?.
An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? for IIT JAM 2024 is part of IIT JAM preparation. The Question and answers have been prepared according to the IIT JAM exam syllabus. Information about An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? covers all topics & solutions for IIT JAM 2024 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer?.
Solutions for An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? in English & in Hindi are available as part of our courses for IIT JAM.
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ample number of questions to practice An enzyme shows highest activity in the pH range 2.0 - 3.0. At pH 4.0 and pH 7.0, the enzyme exhibits 50% and 1%, respectively, of its highest activity. Which of the following states of an amino acid residue in the catalytic site is most responsible for its activity profile ?a)A protonated Aspb)A deprotonated Aspc)A deprotonated Asnd)A protonated AsnCorrect answer is option 'A'. Can you explain this answer? tests, examples and also practice IIT JAM tests.
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