Any feedback?
Literature summary for 3.1.1.8 extracted from
- Microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon (2009), Anal. Biochem., 389, 97-101.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| paraoxon | paraoxon binds to both the enzyme and acyl-enzyme, but with weak affinities. A slight activation is observed at the lowest paraoxon concentrations and is attributed to the binding of the substrate to the enzyme-inhibitor complex | Equus caballus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Equus caballus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| serum | - |
Equus caballus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| butyrylcholine iodide + H2O | - |
Equus caballus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BChE | - |
Equus caballus |
| butyrylcholinesterase | - |
Equus caballus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Equus caballus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Equus caballus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.123 | - |
paraoxon | - |
Equus caballus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
