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Literature summary for 3.4.22.71 extracted from
- Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC (2005), J. Biol. Chem., 280, 16263-16271.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| IsdC + H2O | Staphylococcus aureus | the enzyme anchors the IsdC precursor with a C-terminal NPQTN motif sorting sognal, to the cell wall envelope. The sorting signal of IsdC is cleaved between threonine and asparagine of the NPQTN motif, and the carboxyl group of the thrteonine is amide-linked to the amino group of pentaglycine cross-bridges | ? | - |
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Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
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Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| IsdC + H2O | the enzyme anchors the IsdC precursor with a C-terminal NPQTN motif sorting sognal, to the cell wall envelope. The sorting signal of IsdC is cleaved between threonine and asparagine of the NPQTN motif, and the carboxyl group of the thrteonine is amide-linked to the amino group of pentaglycine cross-bridges | Staphylococcus aureus | ? | - |
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