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Literature summary for 3.1.1.8 extracted from

  • Fogle, E.J.; Marlier, J.F.; Stillman, A.; Gao, X.; Rao, Y.; Robins, L.I.
    An investigation into the butyrylcholinesterase-catalyzed hydrolysis of formylthiocholine using heavy atom kinetic isotope effects (2016), Bioorg. Chem., 65, 57-60 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information substrate inhibition with formylthiocholine does not occur Equus caballus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic isotope effects for the butrylylcholinesterase catalyzed and non-enzymatic hydrolysis of formylthiocholine, overview Equus caballus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
butyrylcholine + H2O Equus caballus
-
choline + butyrate
-
?

Organism

Organism UniProt Comment Textmining
Equus caballus P81908
-
-

Reaction

Reaction Comment Organism Reaction ID
an acylcholine + H2O = choline + a carboxylate the enzyme follows a mechanism similar to that of a serine protease in which the activated serine attacks the acyl-substrate to form an acyl-enzyme intermediate. The acyl-enzyme intermediate then reacts directly with a water molecule at the active site. Both the acylation and deacylation reactions occur through a tetrahedral intermediate Equus caballus

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Equus caballus
-
serum
-
Equus caballus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylthiocholine + H2O some step (or steps) other than chemical formation of the tetrahedral intermediate are partially rate determining Equus caballus thiocholine + acetate
-
?
butyrylcholine + H2O
-
Equus caballus choline + butyrate
-
?
butyrylthiocholine + H2O
-
Equus caballus thiocholine + butyrate
-
?
formylthiocholine + H2O via formation of the tetrahedral intermediate, measurement of heavy atom kinetic isotope effects Equus caballus thiocholine + formate
-
?
additional information the observed heavy atom kinetic isotope effects of butyrylcholinesterase-catalyzed hydrolysis of formylthiocholine support a mechanism for both acylation and deacylation where the steps up to and including the formation of the tetrahedral intermediate are at least partially rate determining. The first irreversible step is the product release in acylation Equus caballus ?
-
?

Synonyms

Synonyms Comment Organism
BChE
-
Equus caballus
butyrylcholinesterase
-
Equus caballus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Equus caballus

General Information

General Information Comment Organism
physiological function the enzyme is thought to be primarily responsible for detoxification reactions in the serum, liver, lungs, and intestinal mucosa Equus caballus