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20190307 Ch6 & 7 Enzyme and Enzyme kinetics
(1:43:18)
by 邱奕霖, 2019-03-08 11:02, Views(868)
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Title
1.
index 1
2.
Enzyme 酶
3.
There are three ways to increase the rate of a chemical reaction.
4.
Enzymes are catalysts.
5.
Enzymes speed up biochemical reactions.
6.
** after ch06 How enzymes work & ch07 Enzyme kinetics and inhibition (108-3-7).ppt
7.
Enzymes speed up biochemical reactions.
8.
** after ch06 How enzymes work & ch07 Enzyme kinetics and inhibition (108-3-7).ppt
9.
index 2
10.
Most enzymes are highly specific for their substrates.
11.
Enzymes are usually named after the reaction they catalyze.
12.
There are six major classifications of enzymes.
13.
What is the enzyme classification for pyruvate decarboxylase?
14.
Slide 11
15.
The height of the activation energy barrier determines the rate of a reaction.
16.
The sign of ΔG indicates the spontaneity of a reaction.
17.
Enzymes work by lowering the activation energy for a reaction.
18.
Enzymes often use cofactors to aid in catalysis.
19.
Enzymes work by lowering the activation energy for a reaction.
20.
Enzymes often use cofactors to aid in catalysis.
21.
There are three fundamental mechanisms for enzyme catalysis.
22.
Essential BiochemistryPratt (Third Edition)
23.
Rates of Chemical Reactions
24.
Consider the reaction catalyzed by triose phosphate isomerase.
25.
Reaction velocity can be thought of as concentration vs. time.
26.
Slide 21
27.
Many enzymes react with substrates in a nonlinear fashion.
28.
Slide 21
29.
Many enzymes react with substrates in a nonlinear fashion.
30.
Slide 21
31.
Many enzymes react with substrates in a nonlinear fashion.
32.
Rate equations describe chemical processes.
33.
Rate equations describe chemical processes.
34.
Many enzymes obey Michaelis-Menten kinetics.
35.
Rate equations describe chemical processes.
36.
Rate equations describe chemical processes.
37.
Many enzymes react with substrates in a nonlinear fashion.
38.
Slide 21
39.
Many enzymes react with substrates in a nonlinear fashion.
40.
Rate equations describe chemical processes.
41.
Rate equations describe chemical processes.
42.
Many enzymes obey Michaelis-Menten kinetics.
43.
Try to re-express the rate.
44.
Slide 27
45.
Try to re-express the rate.
46.
Slide 27
47.
Try to re-express the rate.
48.
Slide 27
49.
Slide 28
50.
index 3
51.
Slide 29
52.
The Michaelis-Menten equation is hyperbolic.
53.
KM is the substrate concentration at which velocity is half-maximal
54.
The Michaelis-Menten equation is hyperbolic.
55.
KM is the substrate concentration at which velocity is half-maximal
56.
為何要用此公式?
57.
KM is the substrate concentration at which velocity is half-maximal
58.
為何要用此公式?
59.
KM is the substrate concentration at which velocity is half-maximal
60.
The Michaelis-Menten equation is hyperbolic.
61.
KM is the substrate concentration at which velocity is half-maximal
62.
The Michaelis-Menten equation is hyperbolic.
63.
KM is the substrate concentration at which velocity is half-maximal
64.
為何要用此公式?
65.
The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data.
66.
The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data.
67.
KEY CONCEPTS: Section 7-3
68.
The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data.
69.
KEY CONCEPTS: Section 7-3
70.
Competitive inhibitors bind to the same site as the substrate.
71.
Competitive inhibitors increase KM, but do not affect Vmax.
72.
Competitive inhibitors bind to the same site as the substrate.
73.
Competitive inhibitors increase KM, but do not affect Vmax.
74.
A Lineweaver-Burk plot for competitive inhibition
75.
Noncompetitive inhibitors appear to decrease Vmax.
76.
A Lineweaver-Burk plot for competitive inhibition
77.
Competitive inhibitors increase KM, but do not affect Vmax.
78.
A Lineweaver-Burk plot for competitive inhibition
79.
Noncompetitive inhibitors appear to decrease Vmax.
80.
Noncompetitive inhibitors appear to decrease Vmax.
81.
Noncompetitive inhibitors appear to decrease Vmax.
82.
A Lineweaver-Burk plot for competitive inhibition
83.
Competitive inhibitors increase KM, but do not affect Vmax.
84.
A Lineweaver-Burk plot for competitive inhibition
85.
Noncompetitive inhibitors appear to decrease Vmax.
86.
Noncompetitive inhibitors appear to decrease Vmax.
87.
Uncompetitive inhibitors reduce Vmax and KM by roughly the same amount.
88.
Uncompetitive inhibitors reduce Vmax and KM
89.
Uncompetitive inhibitors reduce Vmax and KM
90.
** after ch06 How enzymes work & ch07 Enzyme kinetics and inhibition (108-3-7).ppt
... [more]
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