Entry
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:
R01917 ];
(2) glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate [RN:
R03822 ]
Reaction(KEGG)
Substrate
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
Orthology
K01833 trypanothione synthetase/amidase
Genes
Taxonomy
Reference
Authors
Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH
Title
Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata.
Journal
Sequence
Reference
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
Sequence
Reference
Authors
Comini M, Menge U, Wissing J, Flohe L.
Title
Trypanothione synthesis in crithidia revisited.
Journal
Sequence
Reference
Authors
Oza SL, Shaw MP, Wyllie S, Fairlamb AH.
Title
Trypanothione biosynthesis in Leishmania major.
Journal
Sequence
Reference
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
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.3.1.9
ExPASy - ENZYME nomenclature database: 6.3.1.9
BRENDA, the Enzyme Database: 6.3.1.9