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Literature summary for 3.1.1.8 extracted from
- Characterization of butyrylcholinesterase in bovine serum (2017), Chem. Biol. Interact., 266, 17-27 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of wild-type enzyme BChE containing the 28-residue signal peptide and mutant enzymes in CHO cells | Bos taurus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F398I | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| G117H/P285L/F398I | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| G117S | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| G117S/F398I | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| G117S/P285L | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| G117S/P285L/F398I | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| P285L | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
| P285L/F398I | site-directed mutagenesis, altered structure compared to wild-type enzyme | Bos taurus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| chlorpyrifos oxon | 90% inhibition at 50 nM, recombinant bovine BChE (rBoBChE) expressed in serum-free culture medium spontaneously reactivates from inhibition by chlorpyrifos oxon at a rate of 0.0023/min and ages at a rate of 0.0138/min, reactivation by dilution, overview | Bos taurus |  |
| ethopropazine | - |
Bos taurus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| butyrylcholine + H2O | Bos taurus | - |
choline + butyrate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | P32749 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme BChE from serum by ultrafiltration and immunoaffinity chromatography, recombinant wild-type and mutant enzymes by anion exchange chromatography from CHO cells | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| blood serum | the low concentration of BoBChE in serum is explained by limited quantities of an unidentified polyproline-rich protein | Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylthiocholine + H2O | lower activity | Bos taurus | thiocholine + acetate | - |
? | |
| butyrylcholine + H2O | - |
Bos taurus | choline + butyrate | - |
? | |
| butyrylthiocholine + H2O | - |
Bos taurus | thiocholine + butyrate | - |
? | |
| additional information | BoBChE has 3fold higher activity with butyrylthiocholine than with acetylthiocholine | Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | no polyproline peptides are included in BoBChE tetramers, unlike the human enzyme. BoBChE tetramers use a large polyproline-rich protein to organize subunits into a tetramer and the low concentration of BoBChE in serum is explained by limited quantities of an unidentified polyproline-rich protein | Bos taurus |
| More | BChE trypsin peptide mapping | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BChE | - |
Bos taurus |
| BoBChE | - |
Bos taurus |
| butyrylcholinesterase | - |
Bos taurus |
| plasma esterase | - |
Bos taurus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Bos taurus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bos taurus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0022 | - |
ethopropazine | pH 7.0, 25°C, recombinant enzyme | Bos taurus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | molecular dynamics modeling, homology structure modelling using diethylphosphorylated wild-type human BChE structure, PDB ID 1XLW, structure comparisons, overview. BChE protein has the catalytic triad residues Ser198, Glu325, His438, the choline binding site Trp82, the peripheral site residues Asp70, Tyr332, and the acyl binding pocket Leu286, Val288, Trp231. The oxyanion hole residue is Ser117 in BoBChE | Bos taurus |
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Release 2023.1 (January 2023)
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