Literature summary for 3.1.1.8 extracted from

Alkanaimsh, S.; Corbin, J.; Kailemia, M.; Karuppanan, K.; Rodriguez, R.; Lebrilla, C.; McDonald, K.; Nandi, S.
Purification and site-specific N-glycosylation analysis of human recombinant butyrylcholinesterase from Nicotiana benthamiana (2019), Biochem. Eng. J., 142, 58-67 .

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
gene BCHE, recombinant expression of human butyrylcholinesterase in Nicotiana benthamiana using the Agrobacterium tumefaciens-mediated transfection method, sequence comparison to human native wild-type enzyme	Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P06276	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	site-specific N-glycosylation analysis of human recombinant butyrylcholinesterase expressed in Nicotiana benthamiana, site-specific N-glycosylation profile of the purified BChE, mass spectrometric analysis, overview. The N-glycans are assigned based on the numbers of hexose, N-acetylhexoseamine, fucose, and xylose (Hex, HexNAc, fucose, xylose) in the structure. Several different classes of N-glycans are identified, including oligomannose, paucimannose, and complex structures. A significant percentage of the complex glycans contains plant specific sugars, beta-1,2-xylose and core alpha-1,3-fucose. While hBChE has a homogeneous N-glycan profile predominantly consisting of biantennary, mono- and disialylated structures (over 85%). Seven out of the ten potential N-glycosylation sites are occupied by N-glycans. Five of these sites (Asn57, Asn241, Asn256, Asn341, and Asn455) are represented by individual glycopeptides. Sites Asn17, Asn107, Asn481, and Asn486 are unoccupied	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant human enzyme from Nicotiana benthamiana by tangential flow ultrafiltration, anion exchange chromatography, and tacrine-huperzine A hybrid (Hupresin) affinity chromatography, method optimization and evaluation, comparison to procainamide affinity chromatography purification method. Citrate buffer at pH 4.0 is selected to minimize extraction of host plant proteins and shows a 4.5fold enhancement in rBChE specific activity compared to Tris buffer, pH 8.0. Anion exchange chromatography increases the purity of rBChE by 70% by removing major host plant protein impurities. The rBChE is then adsorbed to Hupresin® and purified to homogeneity and over 95% purity for an overall process yield of 34%. The purification process represents a 3fold higher product yield over the established process	Homo sapiens

Purification (Comment)

Organism

recombinant human enzyme from Nicotiana benthamiana by tangential flow ultrafiltration, anion exchange chromatography, and tacrine-huperzine A hybrid (Hupresin) affinity chromatography, method optimization and evaluation, comparison to procainamide affinity chromatography purification method. Citrate buffer at pH 4.0 is selected to minimize extraction of host plant proteins and shows a 4.5fold enhancement in rBChE specific activity compared to Tris buffer, pH 8.0. Anion exchange chromatography increases the purity of rBChE by 70% by removing major host plant protein impurities. The rBChE is then adsorbed to Hupresin® and purified to homogeneity and over 95% purity for an overall process yield of 34%. The purification process represents a 3fold higher product yield over the established process

Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood plasma	-	Homo sapiens	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
260	-	purified recombinant enzyme, pH 7.4, 25°C	Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
BChE	-	Homo sapiens
butyrylcholinesterase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Homo sapiens