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The velocity of an enzyme-catalysed reaction following Michaelis–Menten kinetics, at the substrate concentration equal to 0.3×Km, is equal to ____ × Vmax (round off to 2 decimal places)
Correct answer is '0.22 to 0.24'. Can you explain this answer?
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The velocity of an enzyme-catalysed reaction following Michaelis&ndash...
-Menten kinetics can be described by the following equation:
V = (Vmax [S]) / (Km + [S])
where V is the velocity of the reaction, Vmax is the maximum velocity of the reaction, [S] is the substrate concentration, and Km is the Michaelis constant.
The Michaelis constant (Km) is a measure of the affinity of the enzyme for its substrate. It is defined as the substrate concentration at which the reaction velocity is half of its maximum value. Enzymes with low Km values have high affinity for their substrates and are able to catalyze reactions at low substrate concentrations. Conversely, enzymes with high Km values have low affinity for their substrates and require higher substrate concentrations to achieve maximum velocity.
The equation above shows that as substrate concentration increases, the velocity of the reaction increases until it reaches a maximum value (Vmax). At high substrate concentrations, the enzyme becomes saturated with substrate and the reaction velocity levels off, approaching Vmax. At low substrate concentrations, the enzyme is not saturated and the reaction velocity is limited by the enzyme-substrate complex formation, resulting in a lower reaction velocity.
V = (Vmax [S]) / (Km + [S])
where V is the velocity of the reaction, Vmax is the maximum velocity of the reaction, [S] is the substrate concentration, and Km is the Michaelis constant.
The Michaelis constant (Km) is a measure of the affinity of the enzyme for its substrate. It is defined as the substrate concentration at which the reaction velocity is half of its maximum value. Enzymes with low Km values have high affinity for their substrates and are able to catalyze reactions at low substrate concentrations. Conversely, enzymes with high Km values have low affinity for their substrates and require higher substrate concentrations to achieve maximum velocity.
The equation above shows that as substrate concentration increases, the velocity of the reaction increases until it reaches a maximum value (Vmax). At high substrate concentrations, the enzyme becomes saturated with substrate and the reaction velocity levels off, approaching Vmax. At low substrate concentrations, the enzyme is not saturated and the reaction velocity is limited by the enzyme-substrate complex formation, resulting in a lower reaction velocity.
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The velocity of an enzyme-catalysed reaction following Michaelis–Menten kinetics, at the substrate concentration equal to 0.3×Km, is equal to ____ × Vmax (round off to 2 decimal places)Correct answer is '0.22 to 0.24'. Can you explain this answer?
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The velocity of an enzyme-catalysed reaction following Michaelis–Menten kinetics, at the substrate concentration equal to 0.3×Km, is equal to ____ × Vmax (round off to 2 decimal places)Correct answer is '0.22 to 0.24'. 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 The velocity of an enzyme-catalysed reaction following Michaelis–Menten kinetics, at the substrate concentration equal to 0.3×Km, is equal to ____ × Vmax (round off to 2 decimal places)Correct answer is '0.22 to 0.24'. 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 The velocity of an enzyme-catalysed reaction following Michaelis–Menten kinetics, at the substrate concentration equal to 0.3×Km, is equal to ____ × Vmax (round off to 2 decimal places)Correct answer is '0.22 to 0.24'. Can you explain this answer?.
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