Any feedback?
Literature summary extracted from
- Recombinant acetylcholinesterase purification and its interaction with silver nanoparticle (2017), Protein Expr. Purif., 136, 58-65 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.7 | recombinant expression of His-tagged enzyme in eukaryote cells using the baculovirus transfection system | Drosophila melanogaster |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.7 | additional information | the interaction between AChE and silver nanoparticles (AgNPs) leads not only to a decrease in AChE activity, but also to a reduction in the crystallinity and stability of AgNPs. The circular dichroism demonstrates that the secondary structure of AChE also declines after 30 min of incubation with AgNPs at 37°C. Smaller AgNPs result in size increments after interaction with enzymes, while the larger ones show size decrements | Drosophila melanogaster |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.7 | Drosophila melanogaster | P07140 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.7 | recombinant His-tagged enzyme by procainamide affinity chromatography and desalting gel filtration | Drosophila melanogaster |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.7 | AChE | - |
Drosophila melanogaster |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.7 | 37 | - |
assay at | Drosophila melanogaster |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.7 | 7.4 | - |
assay at | Drosophila melanogaster |
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
