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Literature summary for 3.1.1.7 extracted from
- Structural characterization of the asymmetric (17+13) S species of acetylcholinesterase from Torpedo. II. Component peptides obtained by selective proteolysis and disulfide bond reduction (1982), J. Biol. Chem., 257, 12292-12301.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Torpedo sp. |
| 68000 | - |
x * 68000, x * 100000, two types of subunits | Torpedo sp. |
| 100000 | - |
x * 68000, x * 100000, two types of subunits | Torpedo sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Torpedo sp. | - |
Torpedo californica | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Torpedo sp. |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| electric organ | basal lamina | Torpedo sp. | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylcholine + H2O | - |
Torpedo sp. | choline + acetate | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| polymer | x * 68000, x * 100000, two types of subunits | Torpedo sp. |
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