KEGG   PATHWAY: ecb00480
Entry
ecb00480                    Pathway                                
Name
Glutathione metabolism - Equus caballus (horse)
Class
Metabolism; Metabolism of other amino acids
Pathway map
ecb00480  Glutathione metabolism
ecb00480

Module
ecb_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:ecb00480]
Other DBs
GO: 0006749
Organism
Equus caballus (horse) [GN:ecb]
Gene
100054524  GGT7; glutathione hydrolase 7 isoform X4 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
100060762  GGT6; glutathione hydrolase 6 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
100050188  GGT1; glutathione hydrolase 1 proenzyme isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
100050259  GGT5; glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
100069874  GGCT; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
100071253  CHAC1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
100052806  CHAC2; glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
100147456  OPLAH; 5-oxoprolinase isoform X1 [KO:K01469] [EC:3.5.2.9]
100056731  GCLC; glutamate--cysteine ligase catalytic subunit isoform X1 [KO:K11204] [EC:6.3.2.2]
100058894  GCLM; glutamate--cysteine ligase regulatory subunit isoform X1 [KO:K11205]
100069411  GSS; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
100068668  LAP3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
100050397  ANPEP; LOW QUALITY PROTEIN: aminopeptidase N [KO:K11140] [EC:3.4.11.2]
111775193  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
111767504  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
100058329  glutathione S-transferase Mu 1 isoform X3 [KO:K00799] [EC:2.5.1.18]
100058290  glutathione S-transferase Mu 1 [KO:K00799] [EC:2.5.1.18]
100056506  glutathione S-transferase A2 [KO:K00799] [EC:2.5.1.18]
100056597  GSTA4; glutathione S-transferase A4 isoform X1 [KO:K00799] [EC:2.5.1.18]
100056462  glutathione S-transferase A1 isoform X2 [KO:K00799] [EC:2.5.1.18]
100056332  GSTA1; glutathione S-transferase alpha 1 [KO:K00799] [EC:2.5.1.18]
100050322  glutathione S-transferase theta-1 isoform X1 [KO:K00799] [EC:2.5.1.18]
100069318  glutathione S-transferase A4-like [KO:K00799] [EC:2.5.1.18]
100061826  GSTM3; glutathione S-transferase Mu 3 [KO:K00799] [EC:2.5.1.18]
100058514  MGST3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
100069640  GSTO1; glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
100064102  MGST1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
100061761  LOW QUALITY PROTEIN: glutathione S-transferase Mu 4 [KO:K00799] [EC:2.5.1.18]
100069628  GSTO2; glutathione S-transferase omega-2 [KO:K00799] [EC:2.5.1.18]
100271875  glutathione S-transferase A1 isoform X1 [KO:K00799] [EC:2.5.1.18]
100630562  MGST2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
100056418  GSTA3; glutathione S-transferase A3 [KO:K00799] [EC:2.5.1.18]
100064796  glutathione S-transferase A1-like isoform X1 [KO:K00799] [EC:2.5.1.18]
100069298  LOW QUALITY PROTEIN: glutathione S-transferase A1 [KO:K00799] [EC:2.5.1.18]
100146315  glutathione S-transferase A1 isoform X1 [KO:K00799] [EC:2.5.1.18]
100146804  glutathione S-transferase A1-like [KO:K00799] [EC:2.5.1.18]
100629609  microsomal glutathione S-transferase 2-like [KO:K00799] [EC:2.5.1.18]
100050390  glutathione S-transferase theta-4 isoform X1 [KO:K00799] [EC:2.5.1.18]
100053468  glutathione S-transferase theta-3-like [KO:K00799] [EC:2.5.1.18]
100053249  glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
100059533  glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
100056014  GSTK1; glutathione S-transferase kappa 1 isoform X1 [KO:K13299] [EC:2.5.1.18]
100053460  HPGDS; hematopoietic prostaglandin D synthase isoform X2 [KO:K04097] [EC:5.3.99.2 2.5.1.18]
100050050  LANCL1; lanC-like protein 1 isoform X1 [KO:K25210] [EC:2.5.1.18]
100058571  putative N-acetyltransferase 8B [KO:K20838] [EC:2.3.1.80 2.3.1.-]
100058847  putative N-acetyltransferase 8B [KO:K20838] [EC:2.3.1.80 2.3.1.-]
100062365  GSR; glutathione reductase, mitochondrial isoform X1 [KO:K00383] [EC:1.8.1.7]
100066416  IDH1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
100069086  IDH2; isocitrate dehydrogenase [NADP], mitochondrial [KO:K00031] [EC:1.1.1.42]
100146298  PGD; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
100059734  G6PD; glucose-6-phosphate 1-dehydrogenase isoform X2 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
100062254  TXNDC12; thioredoxin domain-containing protein 12 isoform X1 [KO:K05360] [EC:1.8.4.2]
102147383  GPX4; phospholipid hydroperoxide glutathione peroxidase, mitochondrial isoform X1 [KO:K05361] [EC:1.11.1.12]
100033835  GPX3; glutathione peroxidase 3 precursor [KO:K00432] [EC:1.11.1.9]
100034079  GPX5; epididymal secretory glutathione peroxidase isoform X1 [KO:K00432] [EC:1.11.1.9]
100050590  GPX7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
100146145  GPX2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
100053396  GPX1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
100061078  GPX6; glutathione peroxidase 6 precursor [KO:K00432] [EC:1.11.1.9]
100052064  GPX8; probable glutathione peroxidase 8 isoform X1 [KO:K00432] [EC:1.11.1.9]
102150050  glutathione peroxidase 1-like [KO:K00432] [EC:1.11.1.9]
100052382  PRDX6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
100072405  ODC1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
100056730  SRM; spermidine synthase [KO:K00797] [EC:2.5.1.16]
100051857  SMS; spermine synthase [KO:K00802] [EC:2.5.1.22]
100053126  RRM1; ribonucleoside-diphosphate reductase large subunit isoform X1 [KO:K10807] [EC:1.17.4.1]
100072410  RRM2; ribonucleoside-diphosphate reductase subunit M2 isoform X1 [KO:K10808] [EC:1.17.4.1]
100062030  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
ecb00220  Arginine biosynthesis
ecb00250  Alanine, aspartate and glutamate metabolism
ecb00270  Cysteine and methionine metabolism
ecb00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   

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