Negatively charged reactants as probes in the study of the essential mercaptide-imidazolium ion-pair of thiolenzymes.
The reactive mercaptide-imidazolium ion-pair at the active site of papain and thiolsubtilisin was alkylated with negatively charged reactants. The reactivities of the two thiolenzymes differ considerably. The iodoacetate reaction is faster by more than 1000 times with papain than with thiolsubtilisin. On the other hand, towards 3-iodopropionate thiolsubtilisin is more reactive than papain by about a factor of 7. These findings, which are interpreted in terms of the different geometries of the two ion-pairs, offer an explanation of the basic difference between the catalytic abilities of papain and thiolsubtilisin.
D000478:Alkylation; D000838:Anions; D001665:Binding Sites; D002384:Catalysis; D003545:Cysteine; D006639:Histidine; D007461:Iodoacetates; D007700:Kinetics; D010206:Papain / Q000378:metabolism; D011422:Propionates; D013381:Subtilisins / Q000378:metabolism
D000838:Anions; D007461:Iodoacetates; D011422:Propionates; D006639:Histidine; D013381:Subtilisins; D010206:Papain; D003545:Cysteine