Chemistry Chapter 23
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1 Chemistry 2100 Chapter 23
2 Protein Functions Binding P + L PL Catalysis Structure
3 Why Enzymes? Higher reaction rates Greater reaction specificity Milder reaction conditions Capacity for regulation C - - C NH 2 H - C NH 2 - C H - C Chorismate mutase - C H - C - C Metabolites have many potential pathways of decomposition Enzymes make the desired one most favorable
4 Specificity: Lock-and-Key Model Proteins typically have high specificity: only certain substrates bind High specificity can be explained by the complementary of the binding site and the ligand. Complementarity in size, shape, charge, or hydrophobic / hydrophilic character Lock and Key model by Emil Fisher (1894) assumes that complementary surfaces are preformed. +
5 Specificity: Induced Fit Conformational changes may occur upon ligand binding (Daniel Koshland in 1958). This adaptation is called the induced fit. Induced fit allows for tighter binding of the ligand Induced fit can increase the affinity of the protein for a second ligand Both the ligand and the protein can change their conformations +
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8 Enzymatic Activity Potential Energy Reactants increase [reactant] increase temperature add catalyst Products Reaction
9 TS Potential Energy Reactants increase [reactant] increase temperature add catalyst Products Reaction
10 TS Potential Energy E a Reactants increase [reactant] increase temperature add catalyst Products Reaction
11 TS Potential Energy E a Reactants increase [reactant] increase temperature add catalyst Products Reaction
12 TS Potential Energy E a Reactants increase [reactant] increase temperature add catalyst Products Reaction
13 TS Potential Energy E a Reactants increase [reactant] increase temperature add catalyst Products Reaction
14 TS E a increase [reactant] Potential Energy Reactants E ' a increase temperature add catalyst Products Reaction
15 How to Lower ΔG? Enzymes organizes reactive groups into proximity
16 How to Lower ΔG? Enzymes bind transition states best
17 H 2 + C 2 HC 2 + H + Potential Energy H 2 + C H C + H + Reaction
18 H 2 + C 2 HC 2 + H + Potential Energy H 2 + C Reaction
19 H 2 + C 2 HC 2 + H + Potential Energy H 2 + C H C + H + Reaction
20 H 2 + C 2 HC 2 + H + Potential Energy H 2 + C H C + H + Reaction
21 H 2 + C 2 HC 2 + H + H H C Potential Energy H 2 + C H C + H + Reaction
22 H 2 + C 2 HC 2 + H + H H C E a Potential Energy H 2 + C H C + H + Reaction
23 H 2 + C 2 HC 2 + H + H H C E a Potential Energy H 2 + C E ' a H C + H + Reaction
24 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
25 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
26 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
27 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
28 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
29 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
30 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
31 sucrose + sucrase [ sucrose-sucrase complex ] H 2 glucose + fructose + sucrase
32 How to Do Kinetic Measurements
33 Enzyme Activity Figure 23.3 The effect of enzyme concentration on the rate of an enzyme-catalyzed reaction. Substrate concentration, temperature, and ph are constant.
34 Enzyme Activity Figure 23.4 The effect of substrate concentration on the rate of an enzyme-catalyzed reaction. Enzyme concentration, temperature, and ph are constant.
35 Enzyme Activity Figure 23.5 The effect of temperature on the rate of an enzyme-catalyzed reaction. Substrate and enzyme concentrations and ph are constant.
36 Enzyme Activity Figure 23.6 The effect of ph on the rate of an enzyme-catalyzed reaction. Substrate and enzyme concentrations and temperature are constant.
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39 What equation models this behavior? Michaelis-Menten Equation
40 (CH 3 ) 3 N CH 2 CH 2 C ac et ylc holine (ACh) CH 3 + H 2 AChE (CH 3 ) 3 N CH 2 CH 2 H + H C CH 3 choline (Ch) ac et ic ac id
41 (CH 3 ) 3 N CH 2 CH 2 C ac et ylc holine (ACh) CH 3 + H 2 AChE (CH 3 ) 3 N CH 2 CH 2 H + H C CH 3 choline (Ch) ac et ic ac id
42 (CH 3 ) 3 N CH 2 CH 2 C ac et ylc holine (ACh) CH 3 + H 2 AChE (CH 3 ) 3 N CH 2 CH 2 H + H C CH 3 choline (Ch) ac et ic ac id
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45 (CH 3 ) 3 N CH 2 CH 2 C ac et ylc holine (ACh) CH 3 + H 2 AChE (CH 3 ) 3 N CH 2 CH 2 H + H C CH 3 choline (Ch) ac et ic ac id
46 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
47 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
48 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
49 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
50 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
51 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
52 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
53 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
54 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
55 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
56 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
57 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
58 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
59 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
60 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
61 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
62 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 H C CH 3
63 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
64 Ser Glu CH 2 C Asp CH H H N His NH (CH 3 ) 3 N CH 2 CH 2 C CH 3
65 (CH 3 ) 3 N CH 2 CH 2 C ac et ylc holine (ACh) CH 3 + H 2 AChE (CH 3 ) 3 N CH 2 CH 2 H + H C CH 3 choline (Ch) ac et ic ac id
66 Inhibitors Reversible inhibitors Temporarily bind enzyme and prevent activity Irreversible inhibitors Permanently bind or degrade enzyme
67 Reversible Inhibition
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72 Mechanism of Action! Enzyme kinetics in the presence and the absence of inhibitors. 72!
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81 Irreversible Inhibition
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84 Acetylcholinesterase Ser Glu CH 2 C Asp CH H N His NH
85 Ser Glu CH 2 C Asp CH F H N His NH CH 3 CH P CH 3 CH 3
86 Ser Glu CH 2 C Asp CH F H N His NH CH 3 CH P CH 3 CH 3
87 Ser Glu CH 2 C Asp CH F H N His NH CH 3 CH P CH 3 CH 3
88 Ser Glu CH 2 C Asp CH F H N His NH CH 3 CH P CH 3 CH 3
89 Ser Glu CH 2 C Asp CH F H N His NH CH 3 CH P CH 3 CH 3
90 I N CH N H CH 3 Pyridine aldoxime me thiodide (PAM) Br Br (CH 3 ) 3 N CH 2 CH 2 CH 2 CH 2 CH 2 CH 2 CH 2 CH 2 CH 2 CH 2 N(CH 3 ) 3 decamethonium bromide (CH 3 ) 3 N CH 2 CH 2 CCH 2 CH 2 CCH 2 CH 2 N(CH 3 ) 3 succ inylcholine
91 Commercial Enzymes lactase rennin papain high-fructose corn syrup pectinase clinical assays
92 lactase rennin papain high-fructose corn syrup pectinase clinical assays
93 lactase rennin papain high-fructose corn syrup pectinase clinical assays
94 lactase rennin papain high-fructose corn syrup pectinase clinical assays
95 starch dextrins glucose fructose α-amylase glucoamylase glucose isomerase
96 starch dextrins glucose fructose α-amylase glucoamylase glucose isomerase
97 starch dextrins glucose fructose α-amylase glucoamylase glucose isomerase
98 lactase rennin papain high-fructose corn syrup pectinase clinical assays
99 lactase rennin papain high-fructose corn syrup pectinase clinical assays
100 lactase rennin papain high-fructose corn syrup pectinase clinical assays
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