Enzymes Objective 2.01 Functions of Enzymes How Enzymes Work.
Enzymes III - Oregon State...
Transcript of Enzymes III - Oregon State...
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Enzymes IIIDr. Kevin Ahern
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EnzymeInhibition
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EnzymeInhibition
Competitive Inhibitor Resembles Natural Substrate and Competes with it for Binding to the Active Site
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Normal Substrate for Dihydrofolate Reductase
EnzymeInhibition
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Normal Substrate for Dihydrofolate Reductase
Competitive Inhibitor of Dihydrofolate Reductase
EnzymeInhibition
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EnzymeInhibition
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At Low [S], Competitive Inhibitor Very Effective - Km Increases
EnzymeInhibition
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At Low [S], Competitive Inhibitor Very Effective - Km Increases
Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
EnzymeInhibition
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At Low [S], Competitive Inhibitor Very Effective - Km Increases
Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
EnzymeInhibition
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At Low [S], Competitive Inhibitor Very Effective - Km Increases
Competitive Inhibitor Less Effective as [S] Increases - Vmax Does Not Change
EnzymeInhibition
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EnzymeInhibition
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1/Vmax Unchanged
EnzymeInhibition
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1/Vmax Unchanged
-1/Km Increases (=Km Increases)
EnzymeInhibition
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EnzymeInhibition
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Non-Competitive Inhibitors Do Not Resemble the Substrate and Do Not Compete With it for the Active Site.
EnzymeInhibition
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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
EnzymeInhibition
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EnzymeInhibition
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• Noncompetitive Inhibitors Cannot be Out-Competed by Substrate,
EnzymeInhibition
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• Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, • Inhibit a Fixed Amount of Enzyme.
EnzymeInhibition
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• Noncompetitive Inhibitors Cannot be Out-Competed by Substrate, • Inhibit a Fixed Amount of Enzyme. • Vmax Varies With the Amount of Enzyme,
EnzymeInhibition
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• 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
EnzymeInhibition
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• 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
EnzymeInhibition
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Km is Not Affected by Non-Competitive Inhibition
EnzymeInhibition
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EnzymeInhibition
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EnzymeInhibition
Same Values of -1/Km
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EnzymeInhibition
1/Vmax Increases (=Vmax Decreases)
Same Values of -1/Km
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SuicideInhibition
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SuicideInhibition
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Penicillin Covalently Binds to Active Site of Enzyme
Needed for Making Bacterial Cell Walls
SuicideInhibition
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EnzymeRegulation
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Allosterism-bindingofasmallmoleculetoanenzymeaffectsenzymeactivity
EnzymeRegulation
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Allosterism-bindingofasmallmoleculetoanenzymeaffectsenzymeactivityHomotropiceffector-Asubstratefortheenzyme
EnzymeRegulation
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Allosterism-bindingofasmallmoleculetoanenzymeaffectsenzymeactivityHomotropiceffector-AsubstratefortheenzymeHeterotropiceffector-Anon-substrate
EnzymeRegulation
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ModelsofAllosterism
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ModelsofAllosterism
Sequential Model
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ModelsofAllosterism
Sequential Model
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ModelsofAllosterism
Sequential Model
Cause/Effect between binding of substrate/effector and enzyme change to T or R state
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Concerted Model of Catalysis
ModelsofAllosterism
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Concerted Model of Catalysis
Subunit in T-State
ModelsofAllosterism
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Concerted Model of Catalysis
Subunit in T-State Subunit in R-State
ModelsofAllosterism
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Concerted Model of Catalysis
Subunit in T-State Subunit in R-State
Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same
ModelsofAllosterism
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Concerted Model of Catalysis
Subunit in T-State Subunit in R-State
Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same
Sequential Model
ModelsofAllosterism
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Concerted Model of Catalysis
Subunit in T-State Subunit in R-State
Binding of Ligand Converts Subunit Into R-State and Induces Neighbors to do Same
Sequential Model
ModelsofAllosterism
Cause/Effect between binding of substrate/effector and enzyme change to T or R state
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ModelsofAllosterism
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ModelsofAllosterism
Concerted (MWC) Model
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ModelsofAllosterism
Concerted (MWC) Model
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ModelsofAllosterism
Concerted (MWC) Model
Enzyme flips as a complex independently of binding of effector
Effector “locks” enzyme in T or R state
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ModelsofAllosterism
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ModelsofAllosterism
Morpheein Model
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ModelsofAllosterism
Morpheein Model
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Enzymes• EC Classification
Concerted Model of Catalysis
• EC 1, Oxidoreductases: oxidation/reduction reaction catalysis• EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)• EC 3, Hydrolases: hydrolysis of bonds• 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.
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Enzymes• Oxidoreductases
Concerted Model of Catalysis+
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Enzymes• Oxidoreductases
Concerted Model of Catalysis
• EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
+
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Enzymes• Oxidoreductases
Concerted Model of Catalysis
• EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
+
Malate Dehydrogenase
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Enzymes• Oxidoreductases
Concerted Model of Catalysis
• EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
++ NAD+ <=> NADH + H+
Malate Dehydrogenase
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Enzymes• Oxidoreductases
Concerted Model of Catalysis
• EC 1, Oxidoreductases: oxidation/reduction reaction catalysis
++ NAD+ <=> NADH + H+
Malate Dehydrogenase
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Enzymes• Transferases
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Enzymes• Transferases
• EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
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Enzymes• Transferases
• EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
Hexokinase
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Enzymes• Transferases
• EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
Hexokinase
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Enzymes• Transferases
• EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)
Hexokinase
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Enzymes• Hydrolases
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Enzymes• Hydrolases
• EC 3, Hydrolases: hydrolysis of bonds
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Enzymes• Hydrolases
• EC 3, Hydrolases: hydrolysis of bonds
Proteases
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Enzymes• Hydrolases
• EC 3, Hydrolases: hydrolysis of bonds
Proteases
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Enzymes• Hydrolases
• EC 3, Hydrolases: hydrolysis of bonds
Proteases
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Enzymes• Hydrolases
• EC 3, Hydrolases: hydrolysis of bonds
Proteases
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Enzymes• Lyases
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Enzymes• Lyases
• EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
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Enzymes• Lyases
• EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
Isocitrate Lyase
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Enzymes• Lyases
• EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
Isocitrate Lyase
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Enzymes• Lyases
• EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
Isocitrate Lyase
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Enzymes• Lyases
• EC 4, Lyases: non-hydrolytic non-oxidative breaking of bonds
Isocitrate Lyase
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Enzymes• Isomerases
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Enzymes• Isomerases
• EC 5, Isomerases: catalyze isomerization changes within a single molecule
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Enzymes• Isomerases
• EC 5, Isomerases: catalyze isomerization changes within a single molecule
Phosphoglucoisomerase
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Enzymes• Isomerases
• EC 5, Isomerases: catalyze isomerization changes within a single molecule
Phosphoglucoisomerase
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Enzymes• Ligases
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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Enzymes• Ligases
• EC 6, Ligases: join two molecules by making covalent bonds.
Citrulline + Aspartate + ATP <=> Argininosuccinate + AMP + 2Pi
Argininosuccinate Synthetase
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MetabolicMelody
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Catalyze (To the tune of "Close to You")
Copyright Kevin Ahern
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Catalyze (To the tune of "Close to You")
Copyright Kevin AhernMy enzymes Truly are inclined
To convertThings they bind
Turn the key Covalently Cat-a-lyze
How do cellsRegulate these roles?
Allo-ster-ic controls
Two forms, seeStates 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 freeTied to the key
Su-i-cide
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Catalyze (To the tune of "Close to You")
Copyright Kevin AhernMy enzymes Truly are inclined
To convertThings they bind
Turn the key Covalently Cat-a-lyze
How do cellsRegulate these roles?
Allo-ster-ic controls
Two forms, seeStates 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 freeTied to the key
Su-i-cide
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 areSeveral 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