KEGG   PATHWAY: vlg00480
Entry
vlg00480                    Pathway                                
Name
Glutathione metabolism - Vulpes lagopus (Arctic fox)
Class
Metabolism; Metabolism of other amino acids
Pathway map
vlg00480  Glutathione metabolism
vlg00480

Module
vlg_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:vlg00480]
Other DBs
GO: 0006749
Organism
Vulpes lagopus (Arctic fox) [GN:vlg]
Gene
121478448  GGT7; glutathione hydrolase 7 isoform X1 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
121499714  GGT6; glutathione hydrolase 6 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
121475243  GGT5; glutathione hydrolase 5 proenzyme isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
121475244  GGT1; LOW QUALITY PROTEIN: glutathione hydrolase 1 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
121475140  GGCT; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
121484797  CHAC1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
121490643  CHAC2; glutathione-specific gamma-glutamylcyclotransferase 2 isoform X1 [KO:K07232] [EC:4.3.2.7]
121498675  OPLAH; LOW QUALITY PROTEIN: 5-oxoprolinase [KO:K01469] [EC:3.5.2.9]
121484430  GCLC; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
121487111  GCLM; glutamate--cysteine ligase regulatory subunit isoform X1 [KO:K11205]
121478092  GSS; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
121489378  LAP3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
121489730  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
121488295  glutathione S-transferase Mu 1 [KO:K00799] [EC:2.5.1.18]
121488379  GSTM3; glutathione S-transferase Mu 3 [KO:K00799] [EC:2.5.1.18]
121480721  GSTO1; glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
121475214  glutathione S-transferase theta-1 isoform X1 [KO:K00799] [EC:2.5.1.18]
121475225  GSTT2B; glutathione S-transferase theta-2B [KO:K00799] [EC:2.5.1.18]
121475779  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
121475780  glutathione S-transferase theta-4 [KO:K00799] [EC:2.5.1.18]
121483854  glutathione S-transferase GST-6.0-like [KO:K00799] [EC:2.5.1.18]
121475837  glutathione S-transferase theta-3-like [KO:K00799] [EC:2.5.1.18]
121484199  glutathione S-transferase omega-2 [KO:K00799] [EC:2.5.1.18]
121471963  MGST3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
121479439  glutathione S-transferase A4-like [KO:K00799] [EC:2.5.1.18]
121479992  MGST1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
121493085  glutathione S-transferase-like [KO:K00799] [EC:2.5.1.18]
121493092  glutathione S-transferase A4-like isoform X1 [KO:K00799] [EC:2.5.1.18]
121493106  glutathione S-transferase A3 [KO:K00799] [EC:2.5.1.18]
121500598  glutathione S-transferase A4-like [KO:K00799] [EC:2.5.1.18]
121493889  MGST2; microsomal glutathione S-transferase 2 isoform X1 [KO:K00799] [EC:2.5.1.18]
121495003  GSTA4; glutathione S-transferase A4 isoform X1 [KO:K00799] [EC:2.5.1.18]
121489250  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121474755  glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
121472289  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121497865  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121498757  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121492960  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121493582  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121501330  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
121488918  GSTK1; glutathione S-transferase kappa 1 isoform X1 [KO:K13299] [EC:2.5.1.18]
121482109  glutathione S-transferase kappa 1-like [KO:K13299] [EC:2.5.1.18]
121492802  HPGDS; hematopoietic prostaglandin D synthase [KO:K04097] [EC:5.3.99.2 2.5.1.18]
121480728  LANCL1; glutathione S-transferase LANCL1 [KO:K25210] [EC:2.5.1.18]
121491024  NAT8; N-acetyltransferase 8 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
121489630  GSR; glutathione reductase, mitochondrial [KO:K00383] [EC:1.8.1.7]
121480573  IDH1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
121489943  IDH2; isocitrate dehydrogenase [NADP], mitochondrial isoform X1 [KO:K00031] [EC:1.1.1.42]
121497129  PGD; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
121482778  G6PD; glucose-6-phosphate 1-dehydrogenase isoform X1 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
121480971  TXNDC12; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
121494565  GPX4; phospholipid hydroperoxide glutathione peroxidase isoform X1 [KO:K05361] [EC:1.11.1.12]
121481645  GPX7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
121486663  GPX3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
121496493  GPX8; probable glutathione peroxidase 8 isoform X1 [KO:K00432] [EC:1.11.1.9]
121499318  epididymal secretory glutathione peroxidase [KO:K00432] [EC:1.11.1.9]
121499383  GPX6; glutathione peroxidase 6 [KO:K00432] [EC:1.11.1.9]
121492887  GPX2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
121500851  probable glutathione peroxidase 8 [KO:K00432] [EC:1.11.1.9]
121494184  GPX1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
121500379  PRDX6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
121492053  ODC1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
121496721  SRM; spermidine synthase [KO:K00797] [EC:2.5.1.16]
121488958  LOW QUALITY PROTEIN: spermine synthase-like [KO:K00802] [EC:2.5.1.22]
121483312  SMS; spermine synthase [KO:K00802] [EC:2.5.1.22]
121476512  RRM1; ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
121480811  LOW QUALITY PROTEIN: ribonucleoside-diphosphate reductase subunit M2-like [KO:K10808] [EC:1.17.4.1]
121489614  ribonucleoside-diphosphate reductase subunit M2-like [KO:K10808] [EC:1.17.4.1]
121490769  RRM2; ribonucleoside-diphosphate reductase subunit M2 [KO:K10808] [EC:1.17.4.1]
121499043  RRM2B; ribonucleoside-diphosphate reductase subunit M2 B isoform X1 [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
vlg00220  Arginine biosynthesis
vlg00250  Alanine, aspartate and glutamate metabolism
vlg00270  Cysteine and methionine metabolism
vlg00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

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