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Irreversible inhibition of enzymes
An irreversible enzyme inhibition is usually the result of a covalent linkage of the inhibitor with the active center of the enzyme. Virtually all irreversible enzyme inhibitors are toxic, regardless of whether they are natural or synthetic substances.
- Tab. 1
- Typical inhibitors with irreversible effects
|Cyanide||forms complexes with metal ions in the active site of an enzyme|
|DFP (diisopropyl-fluoro-phosphate), parathion (O, O-Diethyl-O-(p-nitrophenyl) thione phosphoric acid ester, E-605), sarin (methyl fluorophosphonic acid isopropyl ester)||block the serine residue in the active center of acetylcholine esterase (AChE)|
|TPCK (N-Tosyl-L-phenylalanine-chloromethyl ketone)||reacts with the histidine residue in the active site of chymotrypsin|
|penicillin||inhibits bacterial glycopeptide transpeptidase and thus the biosynthesis of the cell wall|
|Acetylsalicylic acid||inhibits the cyclooxygenase responsible for the formation of prostaglandins|
In addition to intermediary products of metabolism, therapeutic or toxic substances such as AChE inhibitors, acetazolamide and α-methyldopa as well as so-called mechanism-supported inhibitors or suicide inhibitors or suicide substrates act as enzyme inhibitors (enzyme poisons).
Irreversible inhibitors that attack amino acids in the active center of enzymes are also known as affinity labels.