KEGG   ENZYME: 6.3.1.9
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)
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)
R01917 R03822;
(other) R08352 R08353 R08354 R08355
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
ec00480  Glutathione metabolism
ec01100  Metabolic pathways
Orthology
K01833  trypanothione synthetase/amidase
Genes
TBR: Tb927.2.4370
TBG: TbgDal_II2440
TCR: 509099.50 509319.90
LMA: LMJF_27_1870(TRYS)
LIF: LINJ_27_1770(TRYS)
LDO: LDBPK_271770
LMI: LMXM_27_1870
LMAT: 92513588(LSCM1_03537)
LBZ: LBRM_27_2010
LPAN: LPMP_271850(TRYS)
LOI: 92360186(LSCM4_04265)
LEIS: 94180091(GH5_04666)
LENR: 94170906(CUR178_03666)
LEIN: 94187816(JIQ42_04153)
PHET: 94289445(JKF63_03364)
 » show all
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 1:874-83 (1992)
DOI:10.1002/pro.5560010705
  Sequence
[ag:AAC39132]
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 277:35853-61 (2002)
DOI:10.1074/jbc.M204403200
  Sequence
[tcr:509099.50 509319.90]
Reference
3  [PMID:15537651]
  Authors
Comini M, Menge U, Wissing J, Flohe L.
  Title
Trypanothione synthesis in crithidia revisited.
  Journal
J Biol Chem 280:6850-60 (2005)
DOI:10.1074/jbc.M404486200
  Sequence
[ag:AAC39132]
Reference
4  [PMID:15610825]
  Authors
Oza SL, Shaw MP, Wyllie S, Fairlamb AH.
  Title
Trypanothione biosynthesis in Leishmania major.
  Journal
Mol Biochem Parasitol 139:107-16 (2005)
DOI:10.1016/j.molbiopara.2004.10.004
  Sequence
[lma:LMJF_27_1870]
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 283:17672-80 (2008)
DOI:10.1074/jbc.M801850200
  Sequence
[lma:LMJF_27_1870]
Other DBs
ExplorEnz - The Enzyme Database: 6.3.1.9
IUBMB Enzyme Nomenclature: 6.3.1.9
ExPASy - ENZYME nomenclature database: 6.3.1.9
BRENDA, the Enzyme Database: 6.3.1.9
CAS: 130246-69-4

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Protein sequence (68)   
   UniProt (43)   
   SWISS-PROT (2)   
   RefSeq(pep) (18)   
   PDBSTR (5)   
DNA sequence (115)   
   RefSeq(nuc) (36)   
   GenBank (38)   
   EMBL (41)   
3D Structure (3)   
   PDB (3)   
Protein domain (5)   
   InterPro (5)   
All databases (191)   

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