Lectures

Enzymes and Enzyme Kinetics: Enzyme Catalysis

by Kevin Ahern, PhD
(2)

Questions about the lecture
My Notes
  • Required.
Save Cancel
    Learning Material 2
    • PDF
      01 Advanced Enzymes&Kinetics1.pdf
    • PDF
      Download Lecture Overview
    Report mistake
    Transcript

    About the Lecture

    The lecture Enzymes and Enzyme Kinetics: Enzyme Catalysis by Kevin Ahern, PhD is from the course Enzymes and Enzyme Kinetics. It contains the following chapters:

    • Background of Enzymatic Reactions
    • Enzymes - Activation Energy & Mechanistics
    • Serine Proteases
    • Kinetic Considerations
    • Michaelis-Menten Kinetics

    Included Quiz Questions

    1. Catalysis only occurs in reactions with more than one substrate.
    2. The enzyme in the ES complex has a different structure than the enzyme alone.
    3. Binding of substrate induces a change in enzyme structure.
    4. When product is released, the enzyme reverts to its original structure.
    1. ...it lowers the energy of activation of a reaction.
    2. ...it changes the Gibbs free energy change of a reaction.
    3. ...it changes the standard Gibbs free energy change of a reaction.
    4. ...it only allows reactions to go forward.
    1. ...use serine for catalysis in their active sites.
    2. ...cut target proteins at serine residues.
    3. ...bind serine during catalysis.
    4. ...are misnamed because they do not involve serine at all.
    1. ...aspartic acid and histidine play important roles.
    2. ...the alkoxide ion forms on aspartic acid.
    3. ...electrophilic attack is at the core of the reaction mechanism.
    4. ...the slow step is the first one.
    1. ...determines the binding/cutting specificity of the enzyme.
    2. ...stabilizes an unstable tetrahedral intermediate.
    3. ...is the location of the catalytic triad.
    4. ...requires serine for binding.
    1. ...the velocity of a reaction is related to the concentration of substrate used.
    2. ...the velocity of a reaction is measured as the quantity of product per time.
    3. ...there is an inverse relationship between substrate concentration and reaction velocity.
    4. ...the velocity of a reaction is unrelated to enzyme concentration.
    1. ...occur when ES and Enzyme are not varying rapidly.
    2. ...are usually measured when there is a saturating amount of enzyme for the substrate.
    3. ...require product to be abundant when measuring velocity.
    4. ...are measured best when substrate concentration is low.

    Author of lecture Enzymes and Enzyme Kinetics: Enzyme Catalysis

     Kevin Ahern, PhD

    Kevin Ahern, PhD


    Customer reviews

    (2)

    5,0 of 5 stars
    5 Stars
    2
    4 Stars
    0
    3 Stars
    0
    2 Stars
    0
    1  Star
    0
     
    Great explanation of steady state using a graph
    By Alina B. on 23. November 2016 for Enzymes and Enzyme Kinetics: Enzyme Catalysis

    Thank you so much! The part at the end where the steady state was explained with a graph was especially useful.

     
    Thank you for this …
    By Hilda M. on 30. April 2016 for Enzymes and Enzyme Kinetics: Enzyme Catalysis

    Thank you for this class of enzyme catalysis,it's really helpful.