The Enzyme Database

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Accepted name: trypanothione-disulfide reductase
Reaction: trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
For diagram of trypanothione biosynthesis, click here
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
trypanothione = N1,N8-bis(glutathionyl)spermidine
Other name(s): trypanothione reductase; NADPH2:trypanothione oxidoreductase
Systematic name: trypanothione:NADP+ oxidoreductase
Comments: Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC, glutathione-disulfide reductase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102210-35-5
1.  Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 25 (1986) 3519–3526. [PMID: 3718941]
2.  Marsh, I.R. and Bradley, M. Substrate specificity of trypanothione reductase. Eur. J. Biochem. 243 (1977) 690–694. [DOI] [PMID: 9057833]
3.  Cunningham, M.L. and Fairlamb, A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. Eur. J. Biochem. 230 (1995) 460–468. [DOI] [PMID: 7607216]
[EC created 1989 as EC, transferred 2002 to EC]
Accepted name: trypanothione synthase
Reaction: (1) glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
(2) glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate
For diagram of trypanothione biosynthesis, click here and for diagram of trypanothione biosynthesis, click here
Glossary: N1,N8-bis(glutathionyl)spermidine = trypanothione
Other name(s): glutathionylspermidine:glutathione ligase (ADP-forming)
Systematic name: spermidine/glutathionylspermidine:glutathione ligase (ADP-forming)
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, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC, glutathionylspermidine amidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 130246-69-4
1.  Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H. Purification of glutathionylspermidine and trypanothione synthase from Crithidia fasciculata. Protein Sci. 1 (1992) 874–883. [DOI] [PMID: 1304372]
2.  Oza, S.L., Tetaud, E., Ariyanayagam, M.R., Warnon, S.S. and Fairlamb, A.H. A single enzyme catalyses formation of trypanothione from glutathione and spermidine in Trypanosoma cruzi. J. Biol. Chem. 277 (2002) 35853–35861. [DOI] [PMID: 12121990]
3.  Comini, M., Menge, U., Wissing, J. and Flohe, L. Trypanothione synthesis in crithidia revisited. J. Biol. Chem. 280 (2005) 6850–6860. [DOI] [PMID: 15537651]
4.  Oza, S.L., Shaw, M.P., Wyllie, S. and Fairlamb, A.H. Trypanothione biosynthesis in Leishmania major. Mol. Biochem. Parasitol. 139 (2005) 107–116. [DOI] [PMID: 15610825]
5.  Fyfe, P.K., Oza, S.L., Fairlamb, A.H. and Hunter, W.N. Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. J. Biol. Chem. 283 (2008) 17672–17680. [DOI] [PMID: 18420578]
[EC created 1999, modified 2014]

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