KEGG   PATHWAY: ola00480
Entry
ola00480                    Pathway                                
Name
Glutathione metabolism - Oryzias latipes (Japanese medaka)
Class
Metabolism; Metabolism of other amino acids
Pathway map
ola00480  Glutathione metabolism
ola00480

Module
ola_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:ola00480]
Other DBs
GO: 0006749
Organism
Oryzias latipes (Japanese medaka) [GN:ola]
Gene
100820717  ggt7; gamma-glutamyltransferase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
100820718  glutathione hydrolase 7 isoform X1 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
101171819  uncharacterized protein LOC101171819 isoform X1 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
100820715  ggt1b; gamma-glutamyl transferase 1b [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
100820728  ggtl1b; gamma-glutamyl transferase-like 1b [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
105357674  glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
100820716  ggtl1a; gamma-glutamyl transferase-like 1a [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
100820714  ggt1a; gamma-glutamyl transferase 1a [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
101161114  glutathione hydrolase 5 proenzyme isoform X2 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
101170211  gamma-glutamylcyclotransferase-like [KO:K00682] [EC:4.3.2.9]
101162615  gamma-glutamylcyclotransferase isoform X1 [KO:K00682] [EC:4.3.2.9]
101169827  glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
101167586  chac1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
101167244  chac2; glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
101169497  oplah; 5-oxoprolinase isoform X1 [KO:K01469] [EC:3.5.2.9]
101169230  gclc; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
101162516  gclm; glutamate--cysteine ligase regulatory subunit [KO:K11205]
101170676  gss; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
101160217  lap3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
101154783  putative aminopeptidase W07G4.4 isoform X2 [KO:K01255] [EC:3.4.11.1]
101170261  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
101159739  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
101173145  aminopeptidase Ey [KO:K11140] [EC:3.4.11.2]
101171894  aminopeptidase N [KO:K11140] [EC:3.4.11.2]
101163069  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
101157367  glutathione S-transferase Mu 3 [KO:K00799] [EC:2.5.1.18]
101157858  glutathione S-transferase Mu 5 [KO:K00799] [EC:2.5.1.18]
101173040  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
101168100  glutathione S-transferase A-like isoform X1 [KO:K00799] [EC:2.5.1.18]
101169583  glutathione S-transferase A [KO:K00799] [EC:2.5.1.18]
101167553  glutathione S-transferase A [KO:K00799] [EC:2.5.1.18]
101168055  glutathione S-transferase A isoform X1 [KO:K00799] [EC:2.5.1.18]
101168304  glutathione S-transferase A isoform X1 [KO:K00799] [EC:2.5.1.18]
101168556  glutathione S-transferase A isoform X2 [KO:K00799] [EC:2.5.1.18]
101173739  mgst3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
101171103  glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
101171354  glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
101174370  gsta4; glutathione S-transferase A4 [KO:K00799] [EC:2.5.1.18]
101163699  mgst1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
101161354  microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
101170897  glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
101167806  glutathione S-transferase A [KO:K00799] [EC:2.5.1.18]
101171358  gstk1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
101159421  lancl1; lanC-like protein 1 [KO:K25210] [EC:2.5.1.18]
101173383  N-acetyltransferase 8-like [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101173140  N-acetyltransferase 8 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101159785  probable N-acetyltransferase CML1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101160033  probable N-acetyltransferase CML1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101160718  probable N-acetyltransferase CML3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101173914  LOW QUALITY PROTEIN: probable N-acetyltransferase CML1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101174600  gsr; glutathione reductase, mitochondrial isoform X1 [KO:K00383] [EC:1.8.1.7]
101166704  isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
101171328  isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
101173937  pgd; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
100049251  glucose-6-phosphate 1-dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
101158357  glucose-6-phosphate 1-dehydrogenase isoform X1 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
101170372  txndc12; thioredoxin domain-containing protein 12 [KO:K05360] [EC:1.8.4.2]
101160762  phospholipid hydroperoxide glutathione peroxidase, mitochondrial-like [KO:K05361] [EC:1.11.1.12]
111946273  phospholipid hydroperoxide glutathione peroxidase, mitochondrial-like [KO:K05361] [EC:1.11.1.12]
101160642  phospholipid hydroperoxide glutathione peroxidase, mitochondrial isoform X3 [KO:K05361] [EC:1.11.1.12]
101172806  gpx1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
101164048  gpx7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
101165150  gpx8; probable glutathione peroxidase 8 [KO:K00432] [EC:1.11.1.9]
101161096  glutathione peroxidase 1-like [KO:K00432] [EC:1.11.1.9]
101170806  gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
105354929  gpx3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
101174176  peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
101173412  peroxiredoxin-6-like [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
101170722  odc1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
101173057  srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
101166897  sms; spermine synthase isoform X1 [KO:K00802] [EC:2.5.1.22]
101156995  ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
101156188  ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
101164326  ribonucleoside-diphosphate reductase subunit M2 B [KO:K10808] [EC:1.17.4.1]
101166844  ribonucleoside-diphosphate reductase subunit M2-like [KO:K10808] [EC:1.17.4.1]
101158912  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
ola00220  Arginine biosynthesis
ola00250  Alanine, aspartate and glutamate metabolism
ola00270  Cysteine and methionine metabolism
ola00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

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