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Enzymes as DTs I

Enzymes as drug targets I

QuestionAnswer
Define Enzymes. Proteins that catalyse reactions by reducing activation energy.
Names the types of catalytic mechanisms. Acid-Base catalysis, Covalent catalysis, and Metal ion catalysis.
Explain Acid-Base catalysis. Enzyme donates/accepts H+ from substrates to speed up reaction.
Explain Covalent catalysis. Enzymes form transient covalent bonds to substrate.
Explain Metal ion catalysis. Ion stabilises or shields the charge during reaction.
Define Enzyme Cofactors. Low molecular weight compounds that bind to an enzyme and participate in the reaction.
State the Michaelis-Menten equation. v = ((Vmax[S])/[S]+Km)).
What is Km? The concentration of substrates that gives 50% of the maximum velocity of the enzyme.
Define Enzyme Inhibitors. Potential drugs which interfere with catalysis.
What are the two types of enzyme inhibitors? Reversible and Irreversible.
Name types of reversible inhibitions. Competitive, Uncompetitive, Mixed, and Non-competitive.
What happens in competitive inhibition? The inhibitor competes with the substrate for the active site of the enzyme and so prevents the substrate from binding.
State the effects of competitive inhibition. Km increases, Vmax is unaltered.
How can you overcome the effect of competitive inhibition? By adding more substrates.
What happens in uncompetitive inhibition? The inhibitor binds to the enzyme-substrate complex and affects its catalytic function - presumably through an allosteric mechaniam because substrate binding is unaffected.
State the effects of uncompetitive inhibition. Km and Vmax decrease.
What happens in mixed inhibition? The inhibitor binds to the free enzyme and the enzyme-substrate complex and affects its catalytic function - presumably through an allosteric mechanism .
State the effects of mixed inhibition. Vmax decreases, Km is also altered (increase or decrease).
What happens in non-competitive inhibition (a form of mixed)? A special situation of mixed inhibition when the inhibitor binds to the free enzyme and enzyme-substrate complex with equal affinities.
What happens in irreversible inhibition? A drug binds irreversibly to the enzyme, and it effectively eliminates a fraction of the enzyme.
State the effects of irreversible inhibition. Vmax decreases, Km is unaffected.
Created by: Smileyfeng
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