Study of the peptidasic site of cholinesterase: preliminary results

FEBS Letters

Chatonnet, Arnaud¹  Masson, Patrick¹ 

[1] Centre de Recherches du Service de Santé des Armées, Division de Chimie Pharmacologie, 108 Boulevard Pinel, 69275 Lyon Cedex 03, France

关键词: Cholinesterase;    Peptidase activity;    Substance P;    Active-site labelling;    Protein-modifying reagents;    Serine peptidase;    BuChE;    butyrylcholinesterase;    AChE;    acetylcholinesterase;    DFP;    diisopropyi fluorophosphonate;    DATD;    diallyltartardiamide;    NANA;    N-acetylneuraminic acid;    SP;    substance P;    2-PAM;    pyridine aldoxime methiodide;    DEPC;    diethylpyrocarbonate;    ω-BAP;    ω-bromoacetophenone;    TLCK;    (tosylamido-1)-lysine chloromethyl ketone;    EDAC;    1-ethyl-3-(3-dimethylaminopropyl)carbodiimide;    EEDQ;    N-ethoxycarbonyl-2-ethoxy-1;    2-dihydroquinoline;    TMO;    trimethyloxonium;    NEM;    N-ethylmaleimide;   

DOI  :  10.1016/0014-5793(85)80361-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown