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Literature summary for 3.4.22.70 extracted from
- Sortase A-catalyzed transpeptidation of glycosylphosphatidylinositol derivatives for chemoenzymatic synthesis of GPI-anchored proteins (2010), J. Am. Chem. Soc., 132, 1567-1571.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | SrtA recognizes LPXTG near the C-terminus of a target protein. The Cys184 of SrtA performs a nucleophilic attack at the peptide bond between T and G in LPXTG, resulting in a thioester intermediate with the carboxyl group of the C-terminal T linked to Cys184. This reactive intermediate reacts with the cross-bridge N-terminus of a cell-wall proteoglycan to anchor the target protein to the cell-wall peptidoglycan. SrtA accepts various peptide/protein substrates, so long as they bear the sorting signal LPXTG, and a range of amino nucleophiles | Staphylococcus aureus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SrtA | - |
Staphylococcus aureus |
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Release 2023.1 (January 2023)
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