Masson_2003_Eur.J.Biochem_270_315

Reference

Title : High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine - Masson_2003_Eur.J.Biochem_270_315
Author(s) : Masson P , Nachon F , Bartels CF , Froment MT , Ribes F , Matthews C , Lockridge O
Ref : European Journal of Biochemistry , 270 :315 , 2003
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

PubMedSearch : Masson_2003_Eur.J.Biochem_270_315
PubMedID: 12605682

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Citations formats

Masson P, Nachon F, Bartels CF, Froment MT, Ribes F, Matthews C, Lockridge O (2003)
High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine
European Journal of Biochemistry 270 :315

Masson P, Nachon F, Bartels CF, Froment MT, Ribes F, Matthews C, Lockridge O (2003)
European Journal of Biochemistry 270 :315