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Literature summary extracted from

  • Oza, S.L.; Wyllie, S.; Fairlamb, A.H.
    Mapping the functional synthetase domain of trypanothione synthetase from Leishmania major (2006), Mol. Biochem. Parasitol., 149, 117-120.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.9 expressed in Escherichia coli Leishmania major

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.9 DELTAN236 unable to produce trypanothione Leishmania major
6.3.1.9 DELTAN250 unable to produce trypanothione Leishmania major

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.9 Leishmania major Q711P7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.9 glutathione + spermidine + ATP
-
 Leishmania major glutathionylspermidine + ADP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.1.9 Trypanothione synthetase
-
 Leishmania major
6.3.1.9 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