KEGG   ENZYME: 6.3.1.9Help
Entry
EC 6.3.1.9                  Enzyme                                 

Name
trypanothione synthase;
glutathionylspermidine:glutathione ligase (ADP-forming)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-ammonia (or amine) ligases (amide synthases)
BRITE hierarchy
Sysname
spermidine/glutathionylspermidine:glutathione ligase (ADP-forming)
Reaction(IUBMB)
(1) glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate [RN:R03822];
(2) glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate
Reaction(KEGG)
Substrate
glutathione [CPD:C00051];
spermidine [CPD:C00315];
ATP [CPD:C00002];
glutathionylspermidine [CPD:C05730]
Product
glutathionylspermidine [CPD:C05730];
ADP [CPD:C00008];
phosphate [CPD:C00009];
N1,N8-bis(glutathionyl)spermidine [CPD:C02090]
Comment
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).
History
EC 6.3.1.9 created 1999, modified 2014
Pathway
Glutathione metabolism
Metabolic pathways
Orthology
K01833  
trypanothione synthetase/amidase
Genes
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
Taxonomy
Reference
1  [PMID:1304372]
  Authors
Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH.
  Title
Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata.
  Journal
Protein. Sci. 1 (1992) 874-83.
  Organism
Crithidia fasciculata
  Sequence
[up:O60993]
Reference
2  [PMID:12121990]
  Authors
Oza SL, Tetaud E, Ariyanayagam MR, Warnon SS, Fairlamb AH.
  Title
A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi.
  Journal
J. Biol. Chem. 277 (2002) 35853-61.
Reference
3  [PMID:15537651]
  Authors
Comini M, Menge U, Wissing J, Flohe L.
  Title
Trypanothione synthesis in crithidia revisited.
  Journal
J. Biol. Chem. 280 (2005) 6850-60.
Reference
4  [PMID:15610825]
  Authors
Oza SL, Shaw MP, Wyllie S, Fairlamb AH.
  Title
Trypanothione biosynthesis in Leishmania major.
  Journal
Mol. Biochem. Parasitol. 139 (2005) 107-16.
Reference
5  [PMID:18420578]
  Authors
Fyfe PK, Oza SL, Fairlamb AH, Hunter WN
  Title
Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities.
  Journal
J. Biol. Chem. 283 (2008) 17672-80.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
130246-69-4

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