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Study of the peptidasic site of cholinesterase: preliminary results
Author(s) -
Chatonnet Arnaud,
Masson Patrick
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80361-6
Subject(s) - active site , cholinesterase , serine , chemistry , histidine , biochemistry , proteases , serine protease , enzyme , binding site , acetylcholinesterase , substrate (aquarium) , soman , stereochemistry , protease , biology , pharmacology , ecology
The peptidasic site of highly purified human plasma cholinesterase was investigated using active‐site‐directed inhibitors. Peptidase activity was assayed taking substance P as substrate. Inhibition by organophosphates indicated that the peptidasic site contained an active serine. The presence of essential histidine residues associated with serine was revealed by histidine modifications. Carboxyl group reagents showed that the active centre contained carboxyl groups in a non‐polar environment. The removal of sialic acids did not alter peptidase activity. The peptidasic site of cholinesterase shared many properties with serine proteases sites and esteratic sites of cholinesterases. In addition, with the peptidasic site, as well as the esteratic site, there was always the possibility of ‘aging’ when inhibited by DFP or soman.