Michaelis-Menten Kinetics: Parameters – Enzyme Classification
About the Lecture
The lecture Michaelis-Menten Kinetics: Parameters – Enzyme Classification by Kevin Ahern, PhD is from the course Enzymes and Enzyme Kinetics.
Included Quiz Questions
What is true of the Km value of an enzyme?
- Low Km suggests that an enzyme has a high affinity for a particular substrate.
- It is directly proportional to the affinity of the enzyme for substrate.
- It varies with substrate concentration.
- It increases as the number of enzymes decreases.
Which of the following is true of enzymes that obey Michaelis-Menten kinetics?
- They give hyperbolic plots of the velocity of a reaction versus substrate.
- They are ones where the substrate changes the enzyme’s binding affinity when it is bound.
- The Km of an enzyme might vary.
- They have constant Vmax values.
Km measures which of the following?
- An enzyme’s affinity for its substrate.
- The amount of enzyme required to get to Vmax/2.
- The substrate necessary for Vmax.
- The amount of enzyme necessary to get to Kcat.
Why is Kcat more useful for comparing enzymes than Vmax?
- Kcat is independent of the amount of enzyme used in a reaction.
- Vmax requires the calculation of Km/2.
- Kcat is directly related to the amount of enzyme used.
- Kcat/2 gives a more accurate measure of Km.
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Author of lecture Michaelis-Menten Kinetics: Parameters – Enzyme Classification
Kevin Ahern, PhD
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such a hard concept explained so easy and well. such an amazing work sir
THANK YOU Pro Ahern you're amazing! very well explained!
