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Literature summary extracted from

  • Dafferner, A.J.; Lushchekina, S.; Masson, P.; Xiao, G.; Schopfer, L.M.; Lockridge, O.
    Characterization of butyrylcholinesterase in bovine serum (2017), Chem. Biol. Interact., 266, 17-27 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.8 recombinant expression of wild-type enzyme BChE containing the 28-residue signal peptide and mutant enzymes in CHO cells Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.8 F398I site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 G117H/P285L/F398I site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 G117S site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 G117S/F398I site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 G117S/P285L site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 G117S/P285L/F398I site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 P285L site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus
3.1.1.8 P285L/F398I site-directed mutagenesis, altered structure compared to wild-type enzyme Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.8 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
3.1.1.8 ethopropazine
-
 Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.8 butyrylcholine + H2O Bos taurus
-
 choline + butyrate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.8 Bos taurus P32749
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.8 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

EC Number Source Tissue Comment Organism Textmining
3.1.1.8 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.8 acetylthiocholine + H2O lower activity Bos taurus thiocholine + acetate
-
 ?
3.1.1.8 butyrylcholine + H2O
-
 Bos taurus choline + butyrate
-
 ?
3.1.1.8 butyrylthiocholine + H2O
-
 Bos taurus thiocholine + butyrate
-
 ?
3.1.1.8 additional information BoBChE has 3fold higher activity with butyrylthiocholine than with acetylthiocholine Bos taurus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.8 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
3.1.1.8 More BChE trypsin peptide mapping Bos taurus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.8 BChE
-
 Bos taurus
3.1.1.8 BoBChE
-
 Bos taurus
3.1.1.8 butyrylcholinesterase
-
 Bos taurus
3.1.1.8 plasma esterase
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.8 25
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.8 7
-
 assay at Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.1.8 0.0022
-
 ethopropazine pH 7.0, 25°C, recombinant enzyme Bos taurus

General Information

EC Number General Information Comment Organism
3.1.1.8 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