Human butyrylcholinesterase components differ in aryl acylamidase activity
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María F. Montenegro
, María T. Moral-Naranjo , María Páez de la Cadena , Francisco J. Campoy , Encarnación Muñoz-Delgado und Cecilio J. Vidal
Abstract
Apart from its esterase activity, butyrylcholinesterase (BuChE) displays aryl acylamidase (AAA) activity able to hydrolyze o-nitroacetanilide (ONA) and its trifluoro-derivative (F-ONA). We report here that, despite amidase and esterase sites residing in the same protein, in human samples depleted of acetylcholinesterase the ratio of amidase to esterase activity varied depending on the source of BuChE. The much faster degradation of ONA and F-ONA by BuChE monomers (G1) of colon and kidney than by the tetramers (G4) suggests aggregation-driven differences in the AAA site between single and polymerized subunits. The similar ratio of F-ONA to butyrylthiocholine hydrolysis by serum G1 and G4 forms support structural differences in the amidase site according to the source of BuChE. The changing ratios of amidase to esterase activities in the human sources probably arise from post-translational modifications in BuChE subunits, the specific proportion of monomers and oligomers and the variable capacity of the tetramers for degrading ONA and F-ONA. The elevated amidase activity of BuChE monomers and the scant activity of the tetramers justify the occurrence of single BuChE subunits in cells as a means to sustain the AAA activity of BuChE which otherwise could be lost by tetramerization.
©2008 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Highlight: 59th Mosbach Kolloquium
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- The histone H1 family: specific members, specific functions?
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- Role of histone modifications in defining chromatin structure and function
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