KEGG   PATHWAY: xla00480
Entry
xla00480                    Pathway                                
Name
Glutathione metabolism - Xenopus laevis (African clawed frog)
Class
Metabolism; Metabolism of other amino acids
Pathway map
xla00480  Glutathione metabolism
xla00480

Module
xla_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:xla00480]
Other DBs
GO: 0006749
Organism
Xenopus laevis (African clawed frog) [GN:xla]
Gene
100036796  XB5764007.L; uncharacterized protein LOC100036796 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
100036918  [KO:K00799] [EC:2.5.1.18]
100036920  gpx4.L; glutathione peroxidase 4 L homeolog [KO:K05361] [EC:1.11.1.12]
100036921  gsta1.L; glutathione S-transferase alpha 1 L homeolog [KO:K00799] [EC:2.5.1.18]
100037104  gsto2.L; glutathione S-transferase omega 2 L homeolog [KO:K00799] [EC:2.5.1.18]
100037213  XB5796436.L; uncharacterized protein LOC100037213 [KO:K00799] [EC:2.5.1.18]
100049719  gclc.L; glutamate-cysteine ligase, catalytic subunit L homeolog [KO:K11204] [EC:6.3.2.2]
100137615  gclc.S; glutamate-cysteine ligase, catalytic subunit S homeolog [KO:K11204] [EC:6.3.2.2]
108695407  [KO:K10808] [EC:1.17.4.1]
108696140  [KO:K00799] [EC:2.5.1.18]
108696285  nat8.1.L; LOW QUALITY PROTEIN: probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108696290  nat8.2.L; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108697419  nat8.5.L; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108699271  chac1.L; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
108699647  mgst2.L; microsomal glutathione S-transferase 2 isoform X2 [KO:K00799] [EC:2.5.1.18]
108699671  [KO:K00799] [EC:2.5.1.18]
108699725  gpx2.S; glutathione peroxidase 2 S homeolog [KO:K00432] [EC:1.11.1.9]
108699968  g6pd.S; glucose-6-phosphate 1-dehydrogenase isoform X2 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
108701001  [KO:K00682] [EC:4.3.2.9]
108701061  ggt7.L; glutathione hydrolase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
108703071  idh1.S; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
108705015  [KO:K01581] [EC:4.1.1.17]
108705079  [KO:K00681] [EC:2.3.2.2 3.4.19.13]
108705345  ggt7.S; glutathione hydrolase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
108705738  nat8.7.S; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108706060  mgst2.S; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
108707119  ggt5.S; glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
108707513  [KO:K01581] [EC:4.1.1.17]
108708014  sms.L; spermine synthase isoform X1 [KO:K00802] [EC:2.5.1.22]
108709596  XB5796436.S; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
108710085  rrm1.S; ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
108711446  idh2.L; isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
108712860  anpep.S; aminopeptidase Ey [KO:K11140] [EC:3.4.11.2]
108716030  ggt5.L; glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
108716035  [KO:K00799] [EC:2.5.1.18]
108716906  [KO:K00799] [EC:2.5.1.18]
108718243  odc1.S; ornithine decarboxylase 1-like [KO:K01581] [EC:4.1.1.17]
108719400  nat8.3.L; probable N-acetyltransferase CML6 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108719408  nat8.6.L; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
108719484  [KO:K01469] [EC:3.5.2.9]
108719977  [KO:K00682] [EC:4.3.2.9]
121397248  [KO:K23790]
121397544  [KO:K07232] [EC:4.3.2.7]
373623  nat8.6.S; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
379056  rrm2b.S; ribonucleotide reductase M2 B (TP53 inducible) S homeolog [KO:K10808] [EC:1.17.4.1]
379379  azin2.S; antizyme inhibitor 2 [KO:K01581] [EC:4.1.1.17]
379417  hpgds.S; prostaglandin D2 synthase, hematopoietic b [KO:K04097] [EC:5.3.99.2 2.5.1.18]
379711  g6pd.L; glucose-6-phosphate dehydrogenase L homeolog [KO:K00036] [EC:1.1.1.49 1.1.1.363]
379859  odc1.L; ornithine decarboxylase 1 [KO:K01581] [EC:4.1.1.17]
379895  gstk1.L; glutathione S-transferase kappa 1 L homeolog [KO:K13299] [EC:2.5.1.18]
380013  idh2.S; isocitrate dehydrogenase 2 (NADP+), mitochondrial S homeolog [KO:K00031] [EC:1.1.1.42]
380105  gclm.L; glutamate-cysteine ligase, modifier subunit L homeolog [KO:K11205]
380448  txndc12.S; thioredoxin domain containing 12 (endoplasmic reticulum) S homeolog precursor [KO:K05360] [EC:1.8.4.2]
380465  rrm2.2.L; ribonucleotide reductase M2 polypeptide [KO:K10808] [EC:1.17.4.1]
380534  gstm1.S; glutathione S-transferase mu 2 [KO:K00799] [EC:2.5.1.18]
394329  gss.L; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
398321  gstp1.L; glutathione S-transferase P 1 [KO:K23790]
398433  lancl1.L; LanC like 1 L homeolog [KO:K25210]
398641  prdx6.S; peroxiredoxin 6 S homeolog [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
398848  pgd.L; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
398969  hpgds.L; prostaglandin D2 synthase, hematopoietic a [KO:K04097] [EC:5.3.99.2 2.5.1.18]
399431  rrm1.L; ribonucleotide reductase M1 L homeolog [KO:K10807] [EC:1.17.4.1]
399434  prdx6.L; peroxiredoxin 6 L homeolog [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
414583  nat8.1.S; uncharacterized protein LOC414583 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
414652  lap3.L; leucine aminopeptidase 3 L homeolog [KO:K11142] [EC:3.4.11.1 3.4.11.5]
414684  mgst1.L; microsomal glutathione S-transferase 1 L homeolog [KO:K00799] [EC:2.5.1.18]
431924  srm.L; spermidine synthase L homeolog [KO:K00797] [EC:2.5.1.16]
431979  MGC82327; uncharacterized protein LOC431979 [KO:K00799] [EC:2.5.1.18]
432086  gpx8.S; probable glutathione peroxidase 8-A [KO:K00432] [EC:1.11.1.9]
432297  gstt1.L; glutathione S-transferase theta 1 L homeolog [KO:K00799] [EC:2.5.1.18]
443744  gpx3.L; glutathione peroxidase 3 L homeolog precursor [KO:K00432] [EC:1.11.1.9]
443815  rrm2.1.L; ribonucleotide reductase M2, gene 1 L homeolog [KO:K10808] [EC:1.17.4.1]
444291  ggt1.S; gamma-glutamyltransferase 1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
444571  gpx3.S; glutathione peroxidase 3 S homeolog precursor [KO:K00432] [EC:1.11.1.9]
444764  mgst3.S; microsomal glutathione S-transferase 3 S homeolog [KO:K00799] [EC:2.5.1.18]
446920  gsta1.S; glutathione S-transferase 3 isoform X2 [KO:K00799] [EC:2.5.1.18]
494689  gpx7.L; uncharacterized protein LOC494689 precursor [KO:K00432] [EC:1.11.1.9]
494713  idh1.L; isocitrate dehydrogenase 1 [KO:K00031] [EC:1.1.1.42]
495339  gpx8.L; probable glutathione peroxidase 8-B [KO:K00432] [EC:1.11.1.9]
495374  gsto1.S; glutathione S-transferase omega 1 S homeolog [KO:K00799] [EC:2.5.1.18]
495430  txndc12.L; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
495476  anpep.L; alanyl aminopeptidase, membrane L homeolog [KO:K11140] [EC:3.4.11.2]
495981  mgst3.L; uncharacterized protein LOC495981 [KO:K00799] [EC:2.5.1.18]
496068  chac2.S; putative glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
496242  gpx1.S; glutathione peroxidase 1 S homeolog [KO:K00432] [EC:1.11.1.9]
496254  gpx7.S; glutathione peroxidase 7 S homeolog precursor [KO:K00432] [EC:1.11.1.9]
734372  gsr.L; glutathione reductase L homeolog [KO:K00383] [EC:1.8.1.7]
734385  gpx1.L; glutathione peroxidase 1 L homeolog [KO:K00432] [EC:1.11.1.9]
734548  gsta4.S; glutathione S-transferase alpha 4 S homeolog [KO:K00799] [EC:2.5.1.18]
734753  gstk1.S; uncharacterized protein LOC734753 [KO:K13299] [EC:2.5.1.18]
734888  gpx4.S; glutathione peroxidase 4 S homeolog [KO:K05361] [EC:1.11.1.12]
734898  ggt1.L; gamma-glutamyltransferase 1 L homeolog [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
779251  gstt1-like.2.L; uncharacterized protein LOC779251 [KO:K00799] [EC:2.5.1.18]
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
xla00220  Arginine biosynthesis
xla00250  Alanine, aspartate and glutamate metabolism
xla00270  Cysteine and methionine metabolism
xla00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   

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