Literature summary for 3.1.1.8 extracted from

Grigoryan, H.; Halebyan, G.; Lefebvre, B.; Brasme, B.; Masson, P.
Mechanism of hydrolysis of dicholine esters with long polymethylene chain by human butyrylcholinesterase (2008), Biochim. Biophys. Acta, 1784, 1818-1824.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	determination of kinetics by mass spectrometry, activity with long-chain substrates, overview	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P06276	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood serum	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
adipyldicholine + H2O	lower activity, monitoring the dicholine substrates, the monocholine intermediates, the dicarboxylic acid and choline products by mass spectrometry,	Homo sapiens	adipic acid + choline	-	?
additional information	butyrylcholinesterase hydrolyzes long chain dicholine esters more rapidly than short chain dicholine esters. The active site of butyrylcholinesterase contains the catalytic residue Ser198 and is deeply buried within the enzyme molecule and there is limited space for binding of large compounds, three-step binding model for hydrolysis of positively charged substrates by BuChE, overview	Homo sapiens	?	-	?
sebacyldicholine + H2O	high activity, monitoring the dicholine substrates, the monocholine intermediates, the dicarboxylic acid and choline products by mass spectrometry, sebacyldicholine is hydrolyzed at both choline ester sites, though hydrolysis of dicholine is faster than hydrolysis of monocholine, overview	Homo sapiens	sebacic acid + choline	-	?

Synonyms

Synonyms	Comment	Organism
butyrylcholinesterase	-	Homo sapiens

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Release 2023.1 (January 2023)