Kinetic Considerations – Enzyme Catalysis
About the Lecture
The lecture Kinetic Considerations – Enzyme Catalysis by Kevin Ahern, PhD is from the course Enzymes and Enzyme Kinetics.
Included Quiz Questions
Kcat in an enzymatic reaction refers to what?
- The rate of formation of the product.
- The rate of formation of the enzyme-substrate complex.
- The rate of formation of the enzyme-product complex.
- The rate of disappearance of product from the reaction mixture.
- The rate of backward reaction.
With time, the linear curve of a graph showing the relation between time and product concentration of an enzymatic reaction starts flattening. What can be the cause of the flattening?
- At the equilibrium state, the concentrations of the product and the reactant do not change.
- The longer an enzymatic reaction goes, the less the reverse reaction from product to substrate occurs.
- The enzyme gets tired of working over and over with the substrate molecules.
- The enzyme undergoes conformational changes, so it is unable to bind to the substrate anymore.
- The enzyme starts to build up.
In enzyme catalysis, which of the following is true?
- The velocity of a reaction is related to the concentration of the substrate used.
- There is an inverse relationship between substrate concentration and reaction velocity.
- The velocity of a reaction is unrelated to enzyme concentration.
- The reverse reaction rate can be different from the forward reaction rate.
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Author of lecture Kinetic Considerations – Enzyme Catalysis
Kevin Ahern, PhD
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This lecture provided me with so much clarity. Thank you
I really like the video, makes medical biochemistry easier to understand
