Any feedback?
Literature summary for 3.5.1.78 extracted from
- Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities (2008), J. Biol. Chem., 283, 17672-17680.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging gamma-drop vapor diffusion method, structure of Leishmania major trypanothione synthetase-amidase, determined in three crystal forms, reveals two catalytic domains | Leishmania major |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leishmania major | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| trypanothione + H2O | - |
Leishmania major | glutathione + glutathionylspermidine | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| trypanothione synthetase-amidase | bifunctional | Leishmania major |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
