KEGG   PATHWAY: pgeo00480
Entry
pgeo00480                   Pathway                                
Name
Glutathione metabolism - Pseudochaenichthys georgianus (South Georgia icefish)
Class
Metabolism; Metabolism of other amino acids
Pathway map
pgeo00480  Glutathione metabolism
pgeo00480

Module
pgeo_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:pgeo00480]
Other DBs
GO: 0006749
Organism
Pseudochaenichthys georgianus (South Georgia icefish) [GN:pgeo]
Gene
117439153  [KO:K00799] [EC:2.5.1.18]
117439818  chac1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
117440226  [KO:K00031] [EC:1.1.1.42]
117440936  gclm; glutamate--cysteine ligase regulatory subunit [KO:K11205]
117441026  gstt2; glutathione S-transferase theta-2 [KO:K00799] [EC:2.5.1.18]
117442779  gstt1b; glutathione S-transferase theta-1b [KO:K00799] [EC:2.5.1.18]
117444211  idh1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
117444230  [KO:K10808] [EC:1.17.4.1]
117444964  prdx6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
117445429  gpx4a; glutathione peroxidase 4a isoform X1 [KO:K05361] [EC:1.11.1.12]
117445525  gpx7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
117445941  [KO:K00681] [EC:2.3.2.2 3.4.19.13]
117446249  [KO:K20838] [EC:2.3.1.80 2.3.1.-]
117446581  gpx1b; glutathione peroxidase 1b [KO:K00432] [EC:1.11.1.9]
117446967  gpx1a; glutathione peroxidase 1a [KO:K00432] [EC:1.11.1.9]
117447095  [KO:K00681] [EC:2.3.2.2 3.4.19.13]
117447849  anpeplb; alanyl (membrane) aminopeptidase-like b isoform X1 [KO:K11140] [EC:3.4.11.2]
117448114  idh2; isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
117448846  gss; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
117449164  pgd; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
117449210  [KO:K20838] [EC:2.3.1.80 2.3.1.-]
117449361  [KO:K00681] [EC:2.3.2.2 3.4.19.13]
117449400  srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
117449401  g6pd; glucose-6-phosphate 1-dehydrogenase isoform X1 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
117449876  anpepb.1; alanyl (membrane) aminopeptidase b, tandem duplicate 1 [KO:K11140] [EC:3.4.11.2]
117449893  [KO:K00036] [EC:1.1.1.49 1.1.1.363]
117450004  gstm.1; glutathione S-transferase mu, tandem duplicate 1 [KO:K00799] [EC:2.5.1.18]
117451113  [KO:K00682] [EC:4.3.2.9]
117451395  [KO:K00682] [EC:4.3.2.9]
117451941  ggt1a; gamma-glutamyltransferase 1a [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117452361  [KO:K01255] [EC:3.4.11.1]
117452705  ggt5a; gamma-glutamyltransferase 5a isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117452715  gstt1a; glutathione S-transferase theta-1a [KO:K00799] [EC:2.5.1.18]
117453094  gpx8; probable glutathione peroxidase 8 isoform X1 [KO:K00432] [EC:1.11.1.9]
117453306  gsr; glutathione reductase, mitochondrial [KO:K00383] [EC:1.8.1.7]
117453796  lap3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
117454112  gpx3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
117455238  [KO:K00682] [EC:4.3.2.9]
117455323  [KO:K00799] [EC:2.5.1.18]
117455385  [KO:K00799] [EC:2.5.1.18]
117455534  rrm2b; ribonucleoside-diphosphate reductase subunit M2 B [KO:K10808] [EC:1.17.4.1]
117456282  ggt1b; glutathione hydrolase 1 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117456393  ggt5b; glutathione hydrolase 5 proenzyme isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117457121  [KO:K10807] [EC:1.17.4.1]
117457353  lancl1; glutathione S-transferase LANCL1 [KO:K25210]
117458621  sms; spermine synthase [KO:K00802] [EC:2.5.1.22]
117458698  [KO:K10807] [EC:1.17.4.1]
117459468  gclc; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
117459491  [KO:K00799] [EC:2.5.1.18]
117460191  [KO:K00799] [EC:2.5.1.18]
117460910  [KO:K13299] [EC:2.5.1.18]
117461037  [KO:K13299] [EC:2.5.1.18]
117462377  [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
117462387  mgst3a; microsomal glutathione S-transferase 3a [KO:K00799] [EC:2.5.1.18]
117462835  txndc12; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
117462837  [KO:K05361] [EC:1.11.1.12]
117464416  gpx9; glutathione peroxidase 9 [KO:K00432] [EC:1.11.1.9]
117465012  chac2; putative glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
117465866  oplah; 5-oxoprolinase [KO:K01469] [EC:3.5.2.9]
117467364  [KO:K07232] [EC:4.3.2.7]
117467512  nat8; probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
117467741  mgst3b; microsomal glutathione S-transferase 3b [KO:K00799] [EC:2.5.1.18]
117467810  odc1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
117467832  gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
117468201  [KO:K20838] [EC:2.3.1.80 2.3.1.-]
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
pgeo00220  Arginine biosynthesis
pgeo00250  Alanine, aspartate and glutamate metabolism
pgeo00270  Cysteine and methionine metabolism
pgeo00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   

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