Literature summary for 3.1.1.8 extracted from

Ngamelue, M.N.; Homma, K.; Lockridge, O.; Asojo, O.A.
Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase (2007), Acta Crystallogr. Sect. F, 63, 723-727.

Application

Application	Comment	Organism
medicine	therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning, in order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers, full-length recombinant BChE produced for therapeutical use	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression of full-length enzyme in CHO or HEK-293 cells, overview	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, 8 mg/ml protein in 50 mM Tris-HCl and 10 mM MES, pH 8.0, sitting drop vapour diffusion method, 20°C, 0.005 ml protein solution are mixed with 0.001 ml of reservoir solution containing at least 1.6 M ammonium sulfate and other additives, e.g. 0.2 M diammonium phosphate, 0.2 M ammonium iodide, and 0.5 M lithium chloride, two different crystal forms are obtained, X-ray diffraction structure determination and analysis at 2.8-4.6 A resolution, molecular replacement	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant enzyme, 8 mg/ml protein in 50 mM Tris-HCl and 10 mM MES, pH 8.0, sitting drop vapour diffusion method, 20°C, 0.005 ml protein solution are mixed with 0.001 ml of reservoir solution containing at least 1.6 M ammonium sulfate and other additives, e.g. 0.2 M diammonium phosphate, 0.2 M ammonium iodide, and 0.5 M lithium chloride, two different crystal forms are obtained, X-ray diffraction structure determination and analysis at 2.8-4.6 A resolution, molecular replacement

Homo sapiens

Localization

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

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85000	-	4 * 85000, determination of structural basis for tetramer formation, overview	Homo sapiens
340000	-	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetylthiocholine + H2O	Homo sapiens	-	thiocholine + acetate	-	?
butyrylthiocholine + H2O	Homo sapiens	-	thiocholine + butyrate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P06276	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	six Asn-linked glycans on Asn57, Asn106, Asn241, Asn256, Asn341 and Asn485, Asn485 is not glycosylated in wild-type BChE, but is glycosylated in the 4-sugars-off mutant lacking the four glycosylation sites at Asn17, Asn455, Asn481 and Asn486 through deletion	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant full-length enzyme from CHO cells	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
serum	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetylthiocholine + H2O	-	Homo sapiens	thiocholine + acetate	-	?
butyrylthiocholine + H2O	-	Homo sapiens	thiocholine + butyrate	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 85000, determination of structural basis for tetramer formation, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
BChE	-	Homo sapiens
butyrylcholinesterase	-	Homo sapiens