Enzymes III. Dr. Kevin Ahern
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1 Enzymes III Dr. Kevin Ahern
2 Enzyme Inhibition
3 Enzyme Inhibition Competitive Inhibitor Resembles Natural Substrate and Competes with it for Binding to the Active Site
4 Enzyme Inhibition Normal Substrate for Dihydrofolate Reductase
5 Enzyme Inhibition Normal Substrate for Dihydrofolate Reductase Competitive Inhibitor of Dihydrofolate Reductase
6 Enzyme Inhibition
7 Enzyme Inhibition At Low [S], Competitive Inhibitor Very Effective - Km Increases
8 Enzyme Inhibition At Low [S], Competitive Inhibitor Very Effective - Km Increases Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
9 Enzyme Inhibition At Low [S], Competitive Inhibitor Very Effective - Km Increases Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
![Enzyme Inhibition At Low [S], Competitive Inhibitor Very Effective - Km](/docs-images/80/81392973/images/10-1.jpg "Increases Competitive Inhibitor Less Effective as [S] Increases - Vmax Does")
10 Enzyme Inhibition At Low [S], Competitive Inhibitor Very Effective - Km Increases Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
11 Enzyme Inhibition
12 Enzyme Inhibition 1/Vmax Unchanged
13 Enzyme Inhibition 1/Vmax Unchanged -1/Km Increases (=Km Increases)
14 Enzyme Inhibition
15 Enzyme Inhibition Non-Competitive Inhibitors Do Not Resemble the Substrate and Do Not Compete With it for the Active Site.
16 Enzyme Inhibition Non-Competitive Inhibitors Do Not Resemble the Substrate and Do Not Compete With it for the Active Site. Instead, They Affect Enzymes by Binding a Different Location on the Enzyme
17 Enzyme Inhibition
18 Enzyme Inhibition Noncompetitive Inhibitors Cannot be Out-Competed by Substrate,
19 Enzyme Inhibition Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, Inhibit a Fixed Amount of Enzyme.
20 Enzyme Inhibition Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, Inhibit a Fixed Amount of Enzyme. Vmax Varies With the Amount of Enzyme,
21 Enzyme Inhibition Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, Inhibit a Fixed Amount of Enzyme. Vmax Varies With the Amount of Enzyme, Vmax Decreases for a Non-Competitive Inhibitor
22 Enzyme Inhibition Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, Inhibit a Fixed Amount of Enzyme. Vmax Varies With the Amount of Enzyme, Vmax Decreases for a Non-Competitive Inhibitor
23 Enzyme Inhibition Km is Not Affected by Non-Competitive Inhibition
24 Enzyme Inhibition
25 Enzyme Inhibition Same Values of -1/Km
26 Enzyme Inhibition 1/Vmax Increases (=Vmax Decreases) Same Values of -1/Km
27 Suicide Inhibition
28 Suicide Inhibition
29 Suicide Inhibition Penicillin Covalently Binds to Active Site of Enzyme Needed for Making Bacterial Cell Walls
30 Enzyme Regulation
31 Enzyme Regulation Allosterism - binding of a small molecule to an enzyme affects enzyme activity
32 Enzyme Regulation Allosterism - binding of a small molecule to an enzyme affects enzyme activity Homotropic effector - A substrate for the enzyme
33 Enzyme Regulation Allosterism - binding of a small molecule to an enzyme affects enzyme activity Homotropic effector - A substrate for the enzyme Heterotropic effector - A non-substrate
34 Models of Allosterism
35 Models of Allosterism Sequential Model
36 Models of Allosterism Sequential Model
37 Models of Allosterism Sequential Model Cause/Effect between binding of substrate/effector and enzyme change to T or R state
38 Models of Allosterism Concerted Model of Catalysis
39 Models of Allosterism Subunit in T-State Concerted Model of Catalysis
40 Models of Allosterism Subunit in T-State Subunit in R-State Concerted Model of Catalysis
41 Models of Allosterism Subunit in T-State Subunit in R-State Concerted Model of Catalysis Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same
42 Models of Allosterism Subunit in T-State Sequential Model Subunit in R-State Concerted Model of Catalysis Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same
43 Models of Allosterism Subunit in T-State Sequential Model Subunit in R-State Concerted Model of Catalysis Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same Cause/Effect between binding of substrate/effector and enzyme change to T or R state
44 Models of Allosterism
45 Models of Allosterism Concerted (MWC) Model
46 Models of Allosterism Concerted (MWC) Model
47 Models of Allosterism Concerted (MWC) Model Enzyme flips as a complex independently of binding of effector Effector locks enzyme in T or R state
48 Models of Allosterism
49 Models of Allosterism Morpheein Model
50 Models of Allosterism Morpheein Model
51 Enzymes EC Classification EC 1, Oxidoreductases: oxidation/reduction reaction catalysis EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group) EC 3, Hydrolases: Concerted hydrolysis of bonds Model of Catalysis EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds EC 5, Isomerases: catalyze isomerization changes within a single molecule EC 6, Ligases: join two molecules by making covalent bonds.
52 Enzymes Oxidoreductases + Concerted Model of Catalysis
53 Enzymes Oxidoreductases + Concerted Model of Catalysis EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
54 Enzymes Oxidoreductases Concerted Model of Catalysis + Malate Dehydrogenase EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
55 Enzymes Oxidoreductases + NAD + <=> + NADH + H + Concerted Model of Catalysis Malate Dehydrogenase EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
56 Enzymes Oxidoreductases + NAD + <=> + NADH + H + Concerted Model of Catalysis Malate Dehydrogenase EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
57 Enzymes Transferases
58 Enzymes Transferases EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
59 Enzymes Transferases Hexokinase EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
60 Enzymes Transferases Hexokinase EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
61 Enzymes Transferases Hexokinase EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
62 Enzymes Hydrolases
63 Enzymes Hydrolases EC 3, Hydrolases: hydrolysis of bonds
64 Enzymes Hydrolases Proteases EC 3, Hydrolases: hydrolysis of bonds
65 Enzymes Hydrolases Proteases EC 3, Hydrolases: hydrolysis of bonds
66 Enzymes Hydrolases Proteases EC 3, Hydrolases: hydrolysis of bonds
67 Enzymes Hydrolases Proteases EC 3, Hydrolases: hydrolysis of bonds
68 Enzymes Lyases
69 Enzymes Lyases EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
70 Enzymes Lyases Isocitrate Lyase EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
71 Enzymes Lyases Isocitrate Lyase EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
72 Enzymes Lyases Isocitrate Lyase EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
73 Enzymes Lyases Isocitrate Lyase EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
74 Enzymes Isomerases
75 Enzymes Isomerases EC 5, Isomerases: catalyze isomerization changes within a single molecule
76 Enzymes Isomerases Phosphoglucoisomerase EC 5, Isomerases: catalyze isomerization changes within a single molecule
77 Enzymes Isomerases Phosphoglucoisomerase EC 5, Isomerases: catalyze isomerization changes within a single molecule
78 Enzymes Ligases
79 Enzymes Ligases EC 6, Ligases: join two molecules by making covalent bonds.
80 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi EC 6, Ligases: join two molecules by making covalent bonds.
81 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
82 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
83 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
84 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
85 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
86 Enzymes Ligases Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi Argininosuccinate Synthetase EC 6, Ligases: join two molecules by making covalent bonds.
87 Metabolic Melody
88 Catalyze (To the tune of "Close to You") Copyright Kevin Ahern
89 My enzymes Truly are inclined To convert Things they bind Turn the key Covalently Cat-a-lyze Catalyze (To the tune of "Close to You") Copyright Kevin Ahern How do cells Regulate these roles? Allo-ster -ic controls Two forms, see States R and T Mod-u-late Competing inhibition keeps The substrates from the active site They raise Km, but leave Vmax and shirk While the non-competers bind elsewhere And lift the plot made on Lineweaver-Burk Other ways Enzymes can be blocked When things bind Then get locked Stuck not free Tied to the key Su-i-cide
90 My enzymes Truly are inclined To convert Things they bind Turn the key Covalently Cat-a-lyze How do cells Regulate these roles? Allo-ster -ic controls Two forms, see States R and T Mod-u-late Competing inhibition keeps The substrates from the active site They raise Km, but leave Vmax and shirk While the non-competers bind elsewhere And lift the plot made on Lineweaver-Burk Other ways Enzymes can be blocked When things bind Then get locked Stuck not free Tied to the key Su-i-cide Catalyze (To the tune of "Close to You") Copyright Kevin Ahern Penicillin s action stops Peptidoglycan cross-links in Bacterial cell walls in awesome ways Beta lactam ring s reactive site Starts bonding with D-D-transpeptidase So there are Several enzyme states Counteract -ing substrates Now you see Blocking the key Regulates Cat-a-lysts Have to be controlled Some get slowed Put on hold It's sublime How the enzymes (slow) Cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze
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