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
K00681  gamma-glutamyltranspeptidase / glutathione hydrolase [EC:2.3.2.2 3.4.19.13]
K18592  gamma-glutamyltranspeptidase / glutathione hydrolase / leukotriene-C4 hydrolase [EC:2.3.2.2 3.4.19.13 3.4.19.14]
K00682  gamma-glutamylcyclotransferase [EC:4.3.2.9]
K22596  gamma-glutamylcyclotransferase, plant [EC:4.3.2.9]
K07232  glutathione-specific gamma-glutamylcyclotransferase [EC:4.3.2.7]
K01469  5-oxoprolinase (ATP-hydrolysing) [EC:3.5.2.9]
K07160  5-oxoprolinase (ATP-hydrolysing) subunit A [EC:3.5.2.9]
K23123  5-oxoprolinase (ATP-hydrolysing) subunit B [EC:3.5.2.9]
K23124  5-oxoprolinase (ATP-hydrolysing) subunit C [EC:3.5.2.9]
K11204  glutamate--cysteine ligase catalytic subunit [EC:6.3.2.2]
K11205  glutamate--cysteine ligase regulatory subunit
K06048  glutamate---cysteine ligase / carboxylate-amine ligase [EC:6.3.2.2 6.3.-.-]
K01919  glutamate--cysteine ligase [EC:6.3.2.2]
K01920  glutathione synthase [EC:6.3.2.3]
K21456  glutathione synthase [EC:6.3.2.3]
K03423  bis-gamma-glutamylcystine reductase [EC:1.8.1.13]
K11142  cytosol aminopeptidase [EC:3.4.11.1 3.4.11.5]
K01255  leucyl aminopeptidase [EC:3.4.11.1]
K07751  PepB aminopeptidase [EC:3.4.11.23]
K11140  aminopeptidase N [EC:3.4.11.2]
K01256  aminopeptidase N [EC:3.4.11.2]
K01270  dipeptidase D [EC:3.4.13.-]
K15428  Cys-Gly metallodipeptidase DUG1 [EC:3.4.13.-]
K00799  glutathione S-transferase [EC:2.5.1.18]
K23790  glutathione S-transferase P [EC:2.5.1.18]
K13299  glutathione S-transferase kappa 1 [EC:2.5.1.18]
K04097  prostaglandin-H2 D-isomerase / glutathione transferase [EC:5.3.99.2 2.5.1.18]
K21888  glutathione dehydrogenase/transferase [EC:1.8.5.1 2.5.1.18]
K25210  glutathione transferase [EC:2.5.1.18]
K20838  N-acetyltransferase 8 [EC:2.3.1.80 2.3.1.-]
K00383  glutathione reductase (NADPH) [EC:1.8.1.7]
K00031  isocitrate dehydrogenase [EC:1.1.1.42]
K00032  phosphogluconate 2-dehydrogenase [EC:1.1.1.43]
K00033  6-phosphogluconate dehydrogenase [EC:1.1.1.44 1.1.1.343]
K00036  glucose-6-phosphate 1-dehydrogenase [EC:1.1.1.49 1.1.1.363]
K05360  protein-disulfide reductase (glutathione) [EC:1.8.4.2]
K05361  phospholipid-hydroperoxide glutathione peroxidase [EC:1.11.1.12]
K00432  glutathione peroxidase [EC:1.11.1.9]
K11188  peroxiredoxin 6 [EC:1.11.1.7 1.11.1.27 3.1.1.-]
K24137  glutaredoxin/glutathione-dependent peroxiredoxin [EC:1.11.1.25 1.11.1.27]
K24136  glutathione-dependent peroxiredoxin [EC:1.11.1.27]
K24138  glutaredoxin/glutathione-dependent peroxiredoxin [EC:1.11.1.25 1.11.1.27]
K00310  pyrimidodiazepine synthase [EC:1.5.4.1]
K01581  ornithine decarboxylase [EC:4.1.1.17]
K00797  spermidine synthase [EC:2.5.1.16]
K24034  spermidine synthase / saccharopine dehydrogenase (NADP+, L-glutamate-forming) [EC:2.5.1.16 1.5.1.10]
K01917  glutathionylspermidine synthase [EC:6.3.1.8]
K01460  glutathionylspermidine amidase/synthetase [EC:3.5.1.78 6.3.1.8]
K00802  spermine synthase [EC:2.5.1.22]
K01833  trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-]
K04283  trypanothione-disulfide reductase [EC:1.8.1.12]
K00434  L-ascorbate peroxidase [EC:1.11.1.11]
K11185  cytosolic tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-]
K11186  mitochondrial tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-]
K11207  glutathione peroxidase-type tryparedoxin peroxidase [EC:1.11.1.-]
K10807  ribonucleoside-diphosphate reductase subunit M1 [EC:1.17.4.1]
K10808  ribonucleoside-diphosphate reductase subunit M2 [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
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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