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Irreversible enzyme inhibitors are compounds that permanently deactivate enzymes by forming stable bonds, typically covalent, at the active site. Unlike reversible inhibitors, they do not dissociate, leading to a lasting loss of enzymatic activity. These inhibitors are crucial in regulating metabolic pathways, serving as pharmaceuticals, and are used in agriculture and sanitation. The text explores their potency, measurement, and examples like DFP and DFMO in medical treatments.
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Irreversible inhibitors form a permanent bond with enzymes, while reversible inhibitors do not
Types of reactive groups
Irreversible inhibitors often contain reactive groups such as nitrogen mustards, aldehydes, or fluorophosphonates
Residues in the enzyme's active site that react with these groups
Reactive groups in irreversible inhibitors can react with nucleophilic residues in the enzyme's active site, such as serine, cysteine, or threonine
Irreversible inhibition is a targeted and specific process, while enzyme inactivation can occur through non-specific mechanisms
The potency of irreversible inhibitors is measured using the rate of enzyme inactivation and the concentration of the inhibitor
The ratio of the rate of enzyme inactivation to the concentration of the inhibitor is used to calculate the inhibitor's potency
When the enzyme is saturated with the inhibitor, the rate of enzyme inactivation reaches a maximum value
Techniques such as mass spectrometry can be used to detect the mass increase of the enzyme upon inhibitor binding
Irreversible inhibition involves the formation of a covalently modified, inactive complex between the enzyme and inhibitor
Some inhibitors bind to enzymes with high affinity, leading to slow dissociation and practically irreversible inhibition
Diisopropylfluorophosphate and α-difluoromethylornithine are examples of irreversible inhibitors that target specific enzymes
Some inhibitors can undergo a chemical reaction to create a reactive intermediate that inactivates the enzyme
Enzyme inhibitors play important roles in regulating metabolic pathways, as well as in medicine, agriculture, and sanitation
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Nature of bond in irreversible enzyme inhibitors
Form stable, often covalent bonds, causing permanent loss of enzymatic activity.
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Common reactive groups in irreversible inhibitors
Include nitrogen mustards, aldehydes, haloalkanes, alkenes, Michael acceptors, phenyl sulfonates, fluorophosphonates.
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Amino acid residues targeted by irreversible inhibitors
React with nucleophilic residues like serine, cysteine, threonine, tyrosine in the enzyme's active site.
