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Literature summary for 6.3.1.9 extracted from
- Mapping the functional synthetase domain of trypanothione synthetase from Leishmania major (2006), Mol. Biochem. Parasitol., 149, 117-120.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Leishmania major |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTAN236 | unable to produce trypanothione | Leishmania major |
| DELTAN250 | unable to produce trypanothione | Leishmania major |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leishmania major | Q711P7 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathione + spermidine + ATP | - |
Leishmania major | glutathionylspermidine + ADP + phosphate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trypanothione synthetase | - |
Leishmania major |
| TryS | the enzyme has two domains: an ATP-dependent synthetase domain that generates the intermediate glutathionylspermidine and the final product trypanothione from glutathione and spermidine, and an amidase domain which can hydrolyse glutathionylspermidine and trypanothione to the original substrates | Leishmania major |
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Release 2023.1 (January 2023)
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