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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
butyrylcholine + H2O | Homo sapiens | - |
choline + butyrate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P06276 | - |
- |
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 (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 | Comment | Organism | Textmining |
---|---|---|---|
blood plasma | - |
Homo sapiens | - |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
butyrylcholine + H2O | - |
Homo sapiens | choline + butyrate | - |
? | |
butyrylthiocholine + H2O | - |
Homo sapiens | thiocholine + butyrate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BChE | - |
Homo sapiens |
butyrylcholinesterase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |