High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine. |
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| Authors: | Patrick Masson Florian Nachon Cynthia F Bartels Marie-Therese Froment Fabien Ribes Cedric Matthews Oksana Lockridge |
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| Institution: | Centre de Recherches du Service de Santé des Armées, Unité d'Enzymologie, La Tronche, France. pymasson@compuserve.com |
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| Abstract: | Butyrylcholinesterase is a serine esterase, closely related to acetylcholinesterase. Both enzymes employ a catalytic triad mechanism for catalysis, similar to that used by serine proteases such as alpha-chymotrypsin. Enzymes of this type are generally considered to be inactive at pH values below 5, because the histidine member of the catalytic triad becomes protonated. We have found that butyrylcholinesterase retains activity at pH
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