TLS Online TPP Program

#Id: 8546

#XL - Q Biochemistry

The extent of irreversible inhibition of the enzyme is dependent upon the reaction rate constant (and hence time) for covalent bond formation and upon the amount of inhibitor present.

TLS Online TPP Program

#Id: 8547

#XL - Q Biochemistry

The irreversible inhibitors cannot be removed by simple physical techniques such as dialysis, is to reduce the amount of enzyme available for reaction.

TLS Online TPP Program

#Id: 8548

#XL - Q Biochemistry

TLS Online TPP Program

#Id: 8549

#XL - Q Biochemistry

The irreversible inhibition involves reactions with a functional group, such as hydroxyl or sulphydryl, or with a metal atom in the active site or a distinct allosteric site.

TLS Online TPP Program

#Id: 8550

#XL - Q Biochemistry

diisopropylphosphofluoridate, reacts with a serine OH group in the active site of esterases such as acetylcholinesterase/chymotrypsin, whilst the organomercury compound p-hydroxymercuribenzoate reacts with a cysteine group, in both cases resulting in covalent bond formation and enzyme inhibition.

TLS Online TPP Program

#Id: 8551

#XL - Q Biochemistry

di-isopropylphosphofluoridate (DFP), phenylmethyl sulphonylfluoride

(PMSF) and tosylphenylalanyl-chloromethylketone (TPCK) (all serine protease inhibitors); 

iodoacetate and cystatin (thiol protease inhibitors); 

pepstatin (aspartic protease inhibitor); 

EDTA and 1,10-phenanthroline (metalloprotease inhibitors); and amastatin and bestatin (exopeptidase inhibitors).