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Literature summary for 3.1.1.8 extracted from

  • Kim, K.; Yao, J.; Jin, Z.; Zheng, F.; Zhan, C.G.
    Kinetic characterization of cholinesterases and a therapeutically valuable cocaine hydrolase for their catalytic activities against heroin and its metabolite 6-monoacetylmorphine (2018), Chem. Biol. Interact., 293, 107-114 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
C-terminally truncated human enzyme (BChE) is genetically fused to the N-terminal of the Fc portion of wild-type human IgG (Fc(WT)) by overlapping extension PCR, cloned and ligated to the pCMV-MCS expression vector and expressed in CHO-S cells Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0045
-
(-)-cocaine recombinant enzyme, pH 7.4, 37°C Homo sapiens
0.12
-
heroin recombinant enzyme, pH 7.4, 37°C Homo sapiens
8.6
-
6-monoacetylmorphine recombinant enzyme, pH 7.4, 37°C 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
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally truncated enzyme BChE from CHO-S cells by affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(-)-cocaine + H2O
-
Homo sapiens ecgonine methyl ester + benzoate
-
?
6-monoacetylmorphine + H2O
-
Homo sapiens morphine + acetate
-
?
butyrylcholine + H2O
-
Homo sapiens choline + butyrate
-
?
heroin + H2O
-
Homo sapiens 6-monoacetylmorphine + acetate
-
?
additional information substrate specificities compared to acetylcholinesterase (EC 3.1.1.7) and cocaine esterase (EC 3.1.1.84) Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
BChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0042
-
6-monoacetylmorphine recombinant enzyme, pH 7.4, 37°C Homo sapiens
0.068
-
(-)-cocaine recombinant enzyme, pH 7.4, 37°C Homo sapiens
30.67
-
heroin recombinant enzyme, pH 7.4, 37°C Homo sapiens

pH Optimum

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

General Information

General Information Comment Organism
additional information enzyme structure homology modelling, molecular dynamics simulations on the structures of enzyme-substrate complexes using the crystal structures of AChE (PDB ID 1B41), and BChE (PDB IDs 2XQF and 1P0P), molecular docking, overview. The positively charged amino-group of the substrates (heroin and 6-monoacetylmorphine) is placed in the choline-binding site near Trp82 in BChE and CocH1 or Trp86 in AChE. The binding models of heroin and 6-monoacetylmorphine in the corresponding enzyme-substrate complexes are optimized by performing the energy minimization Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0005
-
6-monoacetylmorphine recombinant enzyme, pH 7.4, 37°C Homo sapiens
15.19
-
(-)-cocaine recombinant enzyme, pH 7.4, 37°C Homo sapiens
255.56
-
heroin recombinant enzyme, pH 7.4, 37°C Homo sapiens