| 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 |
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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 |
| PubMedSearch : Masson_2003_Eur.J.Biochem_270_315 |
| PubMedID: 12605682 |
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