TAILIEUCHUNG - Báo cáo khoa học: Hydrolysis of acetylthiocoline, o-nitroacetanilide and o-nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase

Besides esterase activity, acetylcholinesterase (AChE) and butyrylcholinest-erase (BuChE) hydrolyze o-nitroacetanilides through aryl acylamidase activity. We have reported that BuChE tetramers and monomers of human blood plasma differ ino-nitroacetanilide (ONA) hydrolysis. The homology in quaternary structure and folding of subunits in the prevalent BuChE species (G H 4) of human plasma and AChE forms of fetal bovine serum prompted us to study the esterase and amidase activities of fetal bovine serum AChE. . | ễFEBS Journal Hydrolysis of acetylthiocoline o-nitroacetanilide and o-nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase Maria F. Montenegro Maria T. Moral-Naranjo Encarnacion Munoz-Delgado Francisco J. Campoy and Cecilio J. Vidal Departamento de Bioquimica y Biologia Molecular-A Universidad de Murcia Spain Keywords aryl acylamidase chemical denaturation cholinesterases kinetic parameters molecular forms Correspondence C. J. Vidal Departamento de Bioquimica y Biologia Molecular-A Edificio de Veterinaria Universidad de Murcia Apdo. 4021 E-30071 Espinardo Murcia Spain Fax 34 968 364147 Tel 34 968 364774 E-mail cevidal@ Received 12 November 2008 revised 27 January 2009 accepted 30 January 2009 doi Besides esterase activity acetylcholinesterase AChE and butyrylcholinesterase BuChE hydrolyze o-nitroacetanilides through aryl acylamidase activity. We have reported that BuChE tetramers and monomers of human blood plasma differ in o-nitroacetanilide ONA hydrolysis. The homology in quaternary structure and folding of subunits in the prevalent BuChE species Gh of human plasma and AChE forms of fetal bovine serum prompted us to study the esterase and amidase activities of fetal bovine serum AChE. The kcat Km values for acetylthiocholine ATCh ONA and its trifluoro derivative N- 2-nitrophenyl -trifluoroacetamide F-ONA were 398 X 106 M-1-min-1 X 106 M-1-min-1 and X 106 M-1-min-1 respectively. The lack of inhibition of amidase activity at high F-ONA concentrations makes it unlikely that there is a role for the peripheral anionic site PAS in F-ONA degradation but the inhibition of ATCh ONA and F-ONA hydrolysis by the PAS ligand fasciculin-2 points to the transit of o-nitroacetalinides near the PAS on their way to the active site. Sedimentation analysis confirmed substrate hydrolysis by tetrameric AChE. As compared with esterase activity amidase activity was less sensitive to guanidine hydrochloride. This reagent

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