EC 6.3.1.9 - Trypanothione synthase

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IntEnz Enzyme Nomenclature
EC 6.3.1.9

Names

Accepted name:
trypanothione synthase
Other names:
TSR synthetase
glutathionylspermidine:glutathione ligase (ADP-forming)
Systematic name:
spermidine/glutathionylspermidine:glutathione ligase (ADP-forming)

Reactions

Cofactor

Comments:

The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78, glutathionylspermidine amidase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50975
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047479
UniProtKB/Swiss-Prot:

References

  1. Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H.
    Purification of glutathionyl spermidine and trypanothione synthase from Crithidia fasciculata.
    Protein Sci. 1: 874-883 (1992). [PMID: 1304372]
  2. Oza, S. L., Tetaud, E., Ariyanayagam, M. R., Warnon, S. S., Fairlamb, A. H.
    A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi.
    J. Biol. Chem. 277: 35853-35861 (2002). [PMID: 12121990]
  3. Comini, M., Menge, U., Wissing, J., Flohe, L.
    Trypanothione synthesis in crithidia revisited.
    J. Biol. Chem. 280: 6850-6860 (2005). [PMID: 15537651]
  4. Oza, S. L., Shaw, M. P., Wyllie, S., Fairlamb, A. H.
    Trypanothione biosynthesis in Leishmania major.
    Mol. Biochem. Parasitol. 139: 107-116 (2005). [PMID: 15610825]
  5. Fyfe, P. K., Oza, S. L., Fairlamb, A. H., Hunter, W. N.
    Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities.
    J. Biol. Chem. 283: 17672-17680 (2008). [PMID: 18420578]

[EC 6.3.1.9 created 1999, modified 2014]