KEGG   PATHWAY: ko00480
Entry
ko00480                     Pathway                                
Name
Glutathione metabolism
Class
Metabolism; Metabolism of other amino acids
Pathway map
ko00480  Glutathione metabolism
ko00480

Module
M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:ko00480]
Other DBs
GO: 0006749
Orthology
K00031  IDH1, IDH2, icd; isocitrate dehydrogenase [EC:1.1.1.42]
K00032  E1.1.1.43; phosphogluconate 2-dehydrogenase [EC:1.1.1.43]
K00033  PGD, gnd, gntZ; 6-phosphogluconate dehydrogenase [EC:1.1.1.44 1.1.1.343]
K00036  G6PD, zwf; glucose-6-phosphate 1-dehydrogenase [EC:1.1.1.49 1.1.1.363]
K00310  SE; pyrimidodiazepine synthase [EC:1.5.4.1]
K00383  GSR, gor; glutathione reductase (NADPH) [EC:1.8.1.7]
K00432  gpx, btuE, bsaA; glutathione peroxidase [EC:1.11.1.9]
K00434  E1.11.1.11; L-ascorbate peroxidase [EC:1.11.1.11]
K00681  ggt; gamma-glutamyltranspeptidase / glutathione hydrolase [EC:2.3.2.2 3.4.19.13]
K00682  GGCT; gamma-glutamylcyclotransferase [EC:4.3.2.9]
K00797  speE, SRM, SPE3; spermidine synthase [EC:2.5.1.16]
K00799  GST; glutathione S-transferase [EC:2.5.1.18]
K00802  SMS; spermine synthase [EC:2.5.1.22]
K01255  CARP, pepA; leucyl aminopeptidase [EC:3.4.11.1]
K01256  pepN; aminopeptidase N [EC:3.4.11.2]
K01270  pepD; dipeptidase D [EC:3.4.13.-]
K01460  gsp; glutathionylspermidine amidase/synthetase [EC:3.5.1.78 6.3.1.8]
K01469  OPLAH, OXP1, oplAH; 5-oxoprolinase (ATP-hydrolysing) [EC:3.5.2.9]
K01581  E4.1.1.17, ODC1, speC, speF; ornithine decarboxylase [EC:4.1.1.17]
K01833  TRYS; trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-]
K01917  E6.3.1.8; glutathionylspermidine synthase [EC:6.3.1.8]
K01919  gshA; glutamate--cysteine ligase [EC:6.3.2.2]
K01920  gshB; glutathione synthase [EC:6.3.2.3]
K03423  E1.8.1.13; bis-gamma-glutamylcystine reductase
K04097  HPGDS; prostaglandin-H2 D-isomerase / glutathione transferase [EC:5.3.99.2 2.5.1.18]
K04283  TRYR; trypanothione-disulfide reductase [EC:1.8.1.12]
K05360  TXNDC12; protein-disulfide reductase (glutathione) [EC:1.8.4.2]
K05361  GPX4; phospholipid-hydroperoxide glutathione peroxidase [EC:1.11.1.12]
K06048  gshA, ybdK; glutamate---cysteine ligase / carboxylate-amine ligase [EC:6.3.2.2 6.3.-.-]
K07160  pxpA; 5-oxoprolinase (ATP-hydrolysing) subunit A [EC:3.5.2.9]
K07232  CHAC; glutathione-specific gamma-glutamylcyclotransferase [EC:4.3.2.7]
K07751  pepB; PepB aminopeptidase [EC:3.4.11.23]
K10807  RRM1; ribonucleoside-diphosphate reductase subunit M1 [EC:1.17.4.1]
K10808  RRM2; ribonucleoside-diphosphate reductase subunit M2 [EC:1.17.4.1]
K11140  ANPEP, CD13; aminopeptidase N [EC:3.4.11.2]
K11142  LAP3; cytosol aminopeptidase [EC:3.4.11.1 3.4.11.5]
K11185  TRYP; cytosolic tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-]
K11186  MTRYP; mitochondrial tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-]
K11188  PRDX6; peroxiredoxin 6 [EC:1.11.1.7 1.11.1.27 3.1.1.-]
K11204  GCLC; glutamate--cysteine ligase catalytic subunit [EC:6.3.2.2]
K11205  GCLM; glutamate--cysteine ligase regulatory subunit
K11207  TDPX; glutathione peroxidase-type tryparedoxin peroxidase [EC:1.11.1.-]
K13299  GSTK1; glutathione S-transferase kappa 1 [EC:2.5.1.18]
K15428  DUG1; Cys-Gly metallodipeptidase DUG1 [EC:3.4.13.-]
K18592  GGT1_5, CD224; gamma-glutamyltranspeptidase / glutathione hydrolase / leukotriene-C4 hydrolase [EC:2.3.2.2 3.4.19.13 3.4.19.14]
K20838  NAT8; N-acetyltransferase 8 [EC:2.3.1.80 2.3.1.-]
K21456  GSS; glutathione synthase [EC:6.3.2.3]
K21888  DHAR; glutathione dehydrogenase/transferase [EC:1.8.5.1 2.5.1.18]
K22596  GGCT; gamma-glutamylcyclotransferase, plant [EC:4.3.2.9]
K23123  pxpB; 5-oxoprolinase (ATP-hydrolysing) subunit B
K23124  pxpC; 5-oxoprolinase (ATP-hydrolysing) subunit C
K23790  GSTP; glutathione S-transferase P
K24034  SPE3-LYS9; spermidine synthase / saccharopine dehydrogenase (NADP+, L-glutamate-forming)
K24136  pgdX; glutathione-dependent peroxiredoxin
K24137  PRX1; glutaredoxin/glutathione-dependent peroxiredoxin
K24138  prx3; glutaredoxin/glutathione-dependent peroxiredoxin
K25210  LANCL1; glutathione transferase
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
ko00220  Arginine biosynthesis
ko00250  Alanine, aspartate and glutamate metabolism
ko00270  Cysteine and methionine metabolism
ko00430  Taurine and hypotaurine metabolism
ko00460  Cyanoamino acid metabolism

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