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Literature summary for 3.4.22.70 extracted from
- Sortase A as a tool for high-yield histatin cyclization (2011), FASEB J., 25, 2650-2658.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Staphylococcus aureus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni2+-HisTrap column chromatography | Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Dabcyl-LPETG-EDANS + H2O | - |
Staphylococcus aureus | Dabcyl-LPET + Gly-EDANS | - |
? |  |
| additional information | sortase A optimal cleavage site is LPETGG | Staphylococcus aureus | ? | - |
? | |
| additional information | sortase-mediated cyclization of histatin-1 (GG-histatin 1-LPETGG) provides a yield of more than 90% | Staphylococcus aureus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SrtA | - |
Staphylococcus aureus |
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Release 2023.1 (January 2023)
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