KEGG   ORTHOLOGY: K01833
Entry
K01833                      KO                                     

Name
TRYS
Definition
trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-]
Pathway
ko00480  Glutathione metabolism
ko01100  Metabolic pathways
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09106 Metabolism of other amino acids
   00480 Glutathione metabolism
    K01833  TRYS; trypanothione synthetase/amidase
Enzymes [BR:ko01000]
 3. Hydrolases
  3.5  Acting on carbon-nitrogen bonds, other than peptide bonds
   3.5.1  In linear amides
    3.5.1.-  
     K01833  TRYS; trypanothione synthetase/amidase
 6. Ligases
  6.3  Forming carbon-nitrogen bonds
   6.3.1  Acid-D-ammonia (or amine) ligases (amide synthases)
    6.3.1.9  trypanothione synthase
     K01833  TRYS; trypanothione synthetase/amidase
Other DBs
RN: R01917 R01918 R03822 R08350 R08351 R08352 R08353 R08354 R08355
GO: 0047479
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
LBZ: LBRM_27_2010
LPAN: LPMP_271850(TRYS)
AG: AAC39132(TRS)
Reference
PMID:9677355
  Authors
Tetaud E, Manai F, Barrett MP, Nadeau K, Walsh CT, Fairlamb AH.
  Title
Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata.
  Journal
J Biol Chem 273:19383-90 (1998)
DOI:10.1074/jbc.273.31.19383
  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
J Biol Chem 277:35853-61 (2002)
DOI:10.1074/jbc.M204403200
  Sequence
[tcr:509099.50]
Reference
  Authors
Oza SL, Ariyanayagam MR, Aitcheson N, Fairlamb AH.
  Title
Properties of trypanothione synthetase from Trypanosoma brucei.
  Journal
Mol Biochem Parasitol 131:25-33 (2003)
DOI:10.1016/S0166-6851(03)00176-2
  Sequence
Reference
  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
LinkDB

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)
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
LBZ: LBRM_27_2010
LPAN: LPMP_271850(TRYS)
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
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
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
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
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
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
LinkDB

KEGG   REACTION: R08353
Entry
R08353                      Reaction                               

Name
glutathione:glutathionylspermine ligase (ADP-forming)
Definition
ATP + Glutathione + Glutathionylspermine <=> ADP + Orthophosphate + Bis(glutathionyl)spermine
Equation
Reaction class
RC00002  C00002_C00008
RC00090  C00051_C16563
RC00096  C16562_C16563
Enzyme
Pathway
rn00480  Glutathione metabolism
Orthology
K01833  trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-]
LinkDB

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