KEGG   PATHWAY: amex00480
Entry
amex00480                   Pathway                                
Name
Glutathione metabolism - Astyanax mexicanus (Mexican tetra)
Class
Metabolism; Metabolism of other amino acids
Pathway map
amex00480  Glutathione metabolism
amex00480

Module
amex_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:amex00480]
Other DBs
GO: 0006749
Organism
Astyanax mexicanus (Mexican tetra) [GN:amex]
Gene
103022494  glutathione hydrolase 7 isoform X1 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
103026045  si:ch73-337l15.2; glutathione hydrolase 6 isoform X1 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
103032290  glutathione hydrolase-like YwrD proenzyme isoform X2 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
103046599  ggt5b; glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
103031291  ggt5a; gamma-glutamyltransferase 5a [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
103031919  ggt1a; gamma-glutamyltransferase 1a [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
103029848  ggt1b; glutathione hydrolase 1 proenzyme isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
103033278  ggctb; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
103036016  ggcta; gamma-glutamylcyclotransferase a [KO:K00682] [EC:4.3.2.9]
125797559  gamma-glutamylcyclotransferase-like [KO:K00682] [EC:4.3.2.9]
103029103  chac1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
103027661  chac2; putative glutathione-specific gamma-glutamylcyclotransferase 2 isoform X1 [KO:K07232] [EC:4.3.2.7]
103042964  oplah; 5-oxoprolinase [KO:K01469] [EC:3.5.2.9]
103047245  gclc; glutamate--cysteine ligase catalytic subunit isoform X1 [KO:K11204] [EC:6.3.2.2]
103026947  gclm; glutamate--cysteine ligase regulatory subunit [KO:K11205]
103038781  gss; glutathione synthetase isoform X1 [KO:K21456] [EC:6.3.2.3]
103025918  lap3; cytosol aminopeptidase isoform X1 [KO:K11142] [EC:3.4.11.1 3.4.11.5]
103036797  zgc:152830; putative aminopeptidase W07G4.4 [KO:K01255] [EC:3.4.11.1]
103045941  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
103040424  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
103040113  anpepa; aminopeptidase Ey [KO:K11140] [EC:3.4.11.2]
103035985  anpeplb; alanyl (membrane) aminopeptidase-like b [KO:K11140] [EC:3.4.11.2]
103037903  anpepb.1; alanyl (membrane) aminopeptidase b, tandem duplicate 1 [KO:K11140] [EC:3.4.11.2]
125782284  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
111188250  gstr; glutathione S-transferase rho isoform X1 [KO:K00799] [EC:2.5.1.18]
111192043  gstt2; glutathione S-transferase theta-2 [KO:K00799] [EC:2.5.1.18]
103032768  glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
103033890  gsta.1; glutathione S-transferase, alpha tandem duplicate 1 [KO:K00799] [EC:2.5.1.18]
103038409  gstt1a; glutathione S-transferase theta-1a [KO:K00799] [EC:2.5.1.18]
103043280  mgst3b; microsomal glutathione S-transferase 3b [KO:K00799] [EC:2.5.1.18]
103033581  mgst1.1; microsomal glutathione S-transferase 1.1 [KO:K00799] [EC:2.5.1.18]
103025109  glutathione S-transferase Mu 3 isoform X1 [KO:K00799] [EC:2.5.1.18]
103021311  mgst2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
103036743  microsomal glutathione S-transferase 1-like [KO:K00799] [EC:2.5.1.18]
103025412  glutathione S-transferase Mu 4 [KO:K00799] [EC:2.5.1.18]
103023854  glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
103042111  glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
103042430  glutathione S-transferase theta-3 [KO:K00799] [EC:2.5.1.18]
103038276  glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
103043665  gstk1; glutathione S-transferase kappa 1 isoform X3 [KO:K13299] [EC:2.5.1.18]
103021348  lancl1; glutathione S-transferase LANCL1 [KO:K25210] [EC:2.5.1.18]
125785895  glutathione S-transferase LANCL1-like [KO:K25210] [EC:2.5.1.18]
111193668  N-acetyltransferase family 8 member 3-like isoform X1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103041541  probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103027576  N-acetyltransferase family 8 member 3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103037014  probable N-acetyltransferase camello [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103037654  probable N-acetyltransferase CML1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103035650  nat8l2; N-acetyltransferase family 8 member 3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
125780474  N-acetyltransferase family 8 member 3-like isoform X1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
103035485  gsr; glutathione reductase, mitochondrial isoform X1 [KO:K00383] [EC:1.8.1.7]
103035389  idh1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
103037962  idh2; isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
103026797  pgd; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
103035433  g6pd; glucose-6-phosphate 1-dehydrogenase isoform X3 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
103036206  glucose-6-phosphate 1-dehydrogenase isoform X1 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
103026714  txndc12; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
103026361  gpx4b; phospholipid hydroperoxide glutathione peroxidase [KO:K05361] [EC:1.11.1.12]
103047294  gpx4a; glutathione peroxidase 4a isoform X1 [KO:K05361] [EC:1.11.1.12]
111193044  gpx3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
111193167  gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
103044349  gpx9; glutathione peroxidase 9 [KO:K00432] [EC:1.11.1.9]
103032783  gpx7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
103035764  gpx1b; glutathione peroxidase 1b [KO:K00432] [EC:1.11.1.9]
103031640  gpx1a; glutathione peroxidase 1a [KO:K00432] [EC:1.11.1.9]
103033499  gpx8; probable glutathione peroxidase 8 [KO:K00432] [EC:1.11.1.9]
111188290  peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
103026271  prdx6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
103026254  odc1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
103022244  srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
103023143  sms; LOW QUALITY PROTEIN: spermine synthase [KO:K00802] [EC:2.5.1.22]
103038586  rrm1; ribonucleoside-diphosphate reductase large subunit isoform X1 [KO:K10807] [EC:1.17.4.1]
103028967  rrm2b; ribonucleoside-diphosphate reductase subunit M2 B [KO:K10808] [EC:1.17.4.1]
103024314  ribonucleoside-diphosphate reductase subunit M2 [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
amex00220  Arginine biosynthesis
amex00250  Alanine, aspartate and glutamate metabolism
amex00270  Cysteine and methionine metabolism
amex00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

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