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Literature summary for 3.4.24.83 extracted from
- Lethal factor of anthrax toxin binds monomeric form of protective antigen (2007), Biochem. Biophys. Res. Commun., 360, 690-695.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 DE3 Star cells | Bacillus anthracis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 90000 | - |
SDS-PAGE | Bacillus anthracis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | Q52NH3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| His-Trap HP nickel column chromatography, ammonium sulfate precipitation, and phenyl-Sepharose column chromatography | Bacillus anthracis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 83 kDa full-length protective antigen + H2O | - |
Bacillus anthracis | 20 kDa N-terminal fragment of protective antigen + 63 kDa N-terminal fragment of protective antigen | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lethal factor of anthrax toxin | the C-terminal region carries out the metalloprotease activity, while the N-terminal domain (residues 1-288) is responsible for protective antigen binding | Bacillus anthracis |
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