發布於 2018-10-10
觀看次數: 25
  • 00:30 1.
    index 1
  • 01:13 2.
    Slide 2
  • 02:48 3.
    There are three ways to increase the rate of a chemical reaction.
  • 01:14 4.
    Enzymes are catalysts.
  • 01:45 5.
    Enzymes speed up biochemical reactions.
  • 02:40 6.
    Enzymes have an active site.
  • 03:19 7.
    Most enzymes are highly specific for their substrates.
  • 00:05 8.
    Enzymes are usually named after the reaction they catalyze.
  • 00:33 9.
    Most enzymes are highly specific for their substrates.
  • 03:54 10.
    Enzymes are usually named after the reaction they catalyze.
  • 04:33 11.
    There are six major classifications of enzymes.
  • 00:58 12.
    What is the enzyme classification for pyruvate decarboxylase?
  • 02:48 13.
    Slide 11
  • 02:33 14.
    The height of the activation energy barrier determines the rate of a reaction.
  • 01:03 15.
    The sign of ΔG indicates the spontaneity of a reaction.
  • 01:33 16.
    Enzymes work by lowering the activation energy for a reaction.
  • 01:20 17.
    Enzymes often use cofactors to aid in catalysis.
  • 02:32 18.
    There are three fundamental mechanisms for enzyme catalysis.
  • 01:23 19.
    Essential BiochemistryPratt (Third Edition)
  • 01:27 20.
    KEY CONCEPTS: Section 7-1
  • 03:33 21.
    index 2
  • 02:31 22.
    Consider the reaction catalyzed by triose phosphate isomerase.
  • 01:04 23.
    Reaction velocity can be thought of as concentration vs. time.
  • 04:08 24.
    Many enzymes react with substrates in a nonlinear fashion.
  • 01:27 25.
    KEY CONCEPTS: Section 7-2
  • 01:45 26.
    Rate equations describe chemical processes.
  • 01:22 27.
    Rate equations describe chemical processes.
  • 03:40 28.
    Many enzymes obey Michaelis-Menten kinetics.
  • 01:40 29.
    Try to re-express the rate.
  • 02:18 30.
    The Michaelis-Menten Equation
  • 02:19 31.
    The Michaelis-Menten equation is hyperbolic.
  • 02:12 32.
    KM is the substrate concentration at which velocity is half-maximal
  • 02:14 33.
    The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data.
  • 01:58 34.
    The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data.
  • 01:45 35.
    KEY CONCEPTS: Section 7-3
  • 01:59 36.
    KEY CONCEPTS: Section 7-3
  • 01:36 37.
    Competitive inhibitors bind to the same site as the substrate.
  • 01:12 38.
    Competitive inhibitors increase KM, but do not affect Vmax.
  • 02:03 39.
    A Lineweaver-Burk plot for competitive inhibition
  • 01:59 40.
    Noncompetitive inhibitors appear to decrease Vmax.
  • 01:01 41.
    Noncompetitive inhibitors appear to decrease Vmax.
  • 01:09 42.
    Uncompetitive inhibitors reduce Vmax and KM by roughly the same amount.
  • 00:54 43.
    Uncompetitive inhibitors reduce Vmax and KM
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1:24:22, 發布於 2018-10-10 by 梅書瑄