KEGG   PATHWAY: xma00480
Entry
xma00480                    Pathway                                
Name
Glutathione metabolism - Xiphophorus maculatus (southern platyfish)
Class
Metabolism; Metabolism of other amino acids
Pathway map
xma00480  Glutathione metabolism
xma00480

Module
xma_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:xma00480]
Other DBs
GO: 0006749
Organism
Xiphophorus maculatus (southern platyfish) [GN:xma]
Gene
102230276  ggt7; glutathione hydrolase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
102228901  uncharacterized protein LOC102228901 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
102231385  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102220560  glutathione hydrolase 5 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102218226  glutathione hydrolase 5 proenzyme-like isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102231814  glutathione hydrolase 5 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102231548  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102224050  gamma-glutamylcyclotransferase-like [KO:K00682] [EC:4.3.2.9]
102218941  LOW QUALITY PROTEIN: gamma-glutamylcyclotransferase-like [KO:K00682] [EC:4.3.2.9]
102237748  chac1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
102216390  glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
102217066  chac2; glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
102226682  oplah; 5-oxoprolinase isoform X1 [KO:K01469] [EC:3.5.2.9]
102219526  gclc; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
102231185  gclm; glutamate--cysteine ligase regulatory subunit [KO:K11205]
102219408  gss; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
102235423  lap3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
102229821  putative aminopeptidase W07G4.4 [KO:K01255] [EC:3.4.11.1]
102236040  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
102235788  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
102236043  aminopeptidase Ey-like isoform X1 [KO:K11140] [EC:3.4.11.2]
102235785  anpep; aminopeptidase N [KO:K11140] [EC:3.4.11.2]
102225423  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
102234342  mgst1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
102235650  glutathione S-transferase Mu 1-like [KO:K00799] [EC:2.5.1.18]
102225310  mgst3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
102217223  microsomal glutathione S-transferase 3-like [KO:K00799] [EC:2.5.1.18]
102232758  glutathione S-transferase theta-3-like [KO:K00799] [EC:2.5.1.18]
102220455  glutathione S-transferase-like [KO:K00799] [EC:2.5.1.18]
102235400  glutathione S-transferase Mu 3-like [KO:K00799] [EC:2.5.1.18]
102225805  glutathione S-transferase omega-1-like [KO:K00799] [EC:2.5.1.18]
102225544  glutathione S-transferase omega-1-like [KO:K00799] [EC:2.5.1.18]
102219186  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102221360  mgst2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
102234727  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102234989  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102235253  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102217716  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102219952  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
102237314  glutathione S-transferase theta-1-like isoform X1 [KO:K00799] [EC:2.5.1.18]
102217916  gstk1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
102222265  lancl1; lanC-like protein 1 [KO:K25210] [EC:2.5.1.18]
102228442  probable N-acetyltransferase CML3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102216856  probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102222280  probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102225553  putative N-acetyltransferase 8B isoform X2 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102232290  gsr; glutathione reductase, mitochondrial isoform X2 [KO:K00383] [EC:1.8.1.7]
102226896  isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
102224071  idh1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
102221860  isocitrate dehydrogenase [NADP], mitochondrial-like [KO:K00031] [EC:1.1.1.42]
102227359  pgd; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
102232098  glucose-6-phosphate 1-dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
102235304  glucose-6-phosphate 1-dehydrogenase-like isoform X2 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
102228365  txndc12; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
102218769  phospholipid hydroperoxide glutathione peroxidase, mitochondrial-like [KO:K05361] [EC:1.11.1.12]
102219707  gpx4; phospholipid hydroperoxide glutathione peroxidase, mitochondrial isoform X1 [KO:K05361] [EC:1.11.1.12]
102237238  glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
102237674  gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
102226821  gpx8; probable glutathione peroxidase 8 [KO:K00432] [EC:1.11.1.9]
102217659  glutathione peroxidase 1-like [KO:K00432] [EC:1.11.1.9]
102224382  glutathione peroxidase 1-like [KO:K00432] [EC:1.11.1.9]
106699799  gpx7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
102234407  prdx6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
102229529  peroxiredoxin-6-like [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
102219476  odc1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
102226005  srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
102233412  sms; spermine synthase [KO:K00802] [EC:2.5.1.22]
102224167  ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
102229193  ribonucleoside-diphosphate reductase large subunit-like [KO:K10807] [EC:1.17.4.1]
102221232  rrm2; ribonucleoside-diphosphate reductase subunit M2 [KO:K10808] [EC:1.17.4.1]
102232339  rrm2b; ribonucleoside-diphosphate reductase subunit M2 B [KO:K10808] [EC:1.17.4.1]
Compound
C00005  NADPH
C00006  NADP+
C00024  Acetyl-CoA
C00025  L-Glutamate
C00037  Glycine
C00051  Glutathione
C00072  Ascorbate
C00077  L-Ornithine
C00097  L-Cysteine
C00127  Glutathione disulfide
C00134  Putrescine
C00151  L-Amino acid
C00315  Spermidine
C00669  gamma-L-Glutamyl-L-cysteine
C00750  Spermine
C01322  RX
C01419  Cys-Gly
C01672  Cadaverine
C01879  5-Oxoproline
C02090  Trypanothione
C02320  R-S-Glutathione
C03170  Trypanothione disulfide
C03646  Bis-gamma-glutamylcystine
C03740  (5-L-Glutamyl)-L-amino acid
C05422  Dehydroascorbate
C05726  S-Substituted L-cysteine
C05727  S-Substituted N-acetyl-L-cysteine
C05729  R-S-Cysteinylglycine
C05730  Glutathionylspermidine
C16562  Glutathionylspermine
C16563  Bis(glutathionyl)spermine
C16564  Bis(glutathionyl)spermine disulfide
C16565  Aminopropylcadaverine
C16566  Glutathionylaminopropylcadaverine
C16567  Homotrypanothione
C16568  Homotrypanothione disulfide
C16663  Tryparedoxin
C16664  Tryparedoxin disulfide
Reference
  Authors
Josch C, Klotz LO, Sies H.
  Title
Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver.
  Journal
Biol Chem 384:213-8 (2003)
DOI:10.1515/BC.2003.023
Reference
  Authors
Chu L, Lai Y, Xu X, Eddy S, Yang S, Song L, Kolodrubetz D.
  Title
A 52-kDa leucyl aminopeptidase from treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism.
  Journal
J Biol Chem 283:19351-8 (2008)
DOI:10.1074/jbc.M801034200
Reference
  Authors
Cappiello M, Lazzarotti A, Buono F, Scaloni A, D'Ambrosio C, Amodeo P, Mendez BL, Pelosi P, Del Corso A, Mura U.
  Title
New role for leucyl aminopeptidase in glutathione turnover.
  Journal
Biochem J 378:35-44 (2004)
DOI:10.1042/BJ20031336
Reference
  Authors
Suzuki H, Kamatani S, Kim ES, Kumagai H.
  Title
Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12.
  Journal
J Bacteriol 183:1489-90 (2001)
DOI:10.1128/JB.183.4.1489-1490.2001
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
Reference
  Authors
Oza SL, Ariyanayagam MR, Fairlamb AH.
  Title
Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata.
  Journal
Biochem J 364:679-86 (2002)
DOI:10.1042/BJ20011370
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
Reference
  Authors
Ariyanayagam MR, Oza SL, Mehlert A, Fairlamb AH.
  Title
Bis(glutathionyl)spermine and other novel trypanothione analogues in Trypanosoma cruzi.
  Journal
J Biol Chem 278:27612-9 (2003)
DOI:10.1074/jbc.M302750200
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
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
Reference
  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
Reference
PMID:7813456
  Authors
Hunter KJ, Le Quesne SA, Fairlamb AH.
  Title
Identification and biosynthesis of N1,N9-bis(glutathionyl)aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi.
  Journal
Eur J Biochem 226:1019-27 (1994)
DOI:10.1111/j.1432-1033.1994.t01-1-01019.x
Reference
  Authors
Krauth-Siegel RL, Meiering SK, Schmidt H.
  Title
The parasite-specific trypanothione metabolism of trypanosoma and leishmania.
  Journal
Biol Chem 384:539-49 (2003)
DOI:10.1515/BC.2003.062
Reference
  Authors
Krauth-Siegel RL, Comini MA.
  Title
Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism.
  Journal
Biochim Biophys Acta 1780:1236-48 (2008)
DOI:10.1016/j.bbagen.2008.03.006
Reference
PMID:8892297
  Authors
Krauth-Siegel RL, Ludemann H.
  Title
Reduction of dehydroascorbate by trypanothione.
  Journal
Mol Biochem Parasitol 80:203-8 (1996)
DOI:10.1016/0166-6851(96)02689-8
Reference
  Authors
Dormeyer M, Reckenfelderbaumer N, Ludemann H, Krauth-Siegel RL.
  Title
Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase.
  Journal
J Biol Chem 276:10602-6 (2001)
DOI:10.1074/jbc.M010352200
Reference
  Authors
Schmidt H, Krauth-Siegel RL.
  Title
Functional and physicochemical characterization of the thioredoxin system in Trypanosoma brucei.
  Journal
J Biol Chem 278:46329-36 (2003)
DOI:10.1074/jbc.M305338200
Reference
PMID:9851611
  Authors
Tetaud E, Fairlamb AH.
  Title
Cloning, expression and reconstitution of the trypanothione-dependent peroxidase system of Crithidia fasciculata.
  Journal
Mol Biochem Parasitol 96:111-23 (1998)
DOI:10.1016/S0166-6851(98)00120-0
Reference
  Authors
Castro H, Sousa C, Santos M, Cordeiro-da-Silva A, Flohe L, Tomas AM.
  Title
Complementary antioxidant defense by cytoplasmic and mitochondrial peroxiredoxins in Leishmania infantum.
  Journal
Free Radic Biol Med 33:1552-62 (2002)
DOI:10.1016/S0891-5849(02)01089-4
Reference
  Authors
Wilkinson SR, Temperton NJ, Mondragon A, Kelly JM.
  Title
Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi.
  Journal
J Biol Chem 275:8220-5 (2000)
DOI:10.1074/jbc.275.11.8220
Reference
  Authors
Konig J, Fairlamb AH.
  Title
A comparative study of type I and type II tryparedoxin peroxidases in Leishmania major.
  Journal
FEBS J 274:5643-58 (2007)
DOI:10.1111/j.1742-4658.2007.06087.x
Reference
  Authors
Hillebrand H, Schmidt A, Krauth-Siegel RL.
  Title
A second class of peroxidases linked to the trypanothione metabolism.
  Journal
J Biol Chem 278:6809-15 (2003)
DOI:10.1074/jbc.M210392200
Reference
  Authors
Soksawatmaekhin W, Kuraishi A, Sakata K, Kashiwagi K, Igarashi K.
  Title
Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli.
  Journal
Mol Microbiol 51:1401-12 (2004)
DOI:10.1046/j.1365-2958.2003.03913.x
Reference
PMID:6798961
  Authors
Pegg AE, Shuttleworth K, Hibasami H.
  Title
Specificity of mammalian spermidine synthase and spermine synthase.
  Journal
Biochem J 197:315-20 (1981)
DOI:10.1042/bj1970315
Related
pathway
xma00220  Arginine biosynthesis
xma00250  Alanine, aspartate and glutamate metabolism
xma00270  Cysteine and methionine metabolism
xma00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

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