KEGG   PATHWAY: hsa00480Help
Entry
hsa00480                    Pathway                                

Name
Glutathione metabolism - Homo sapiens (human)
Class
Metabolism; Metabolism of other amino acids
BRITE hierarchy
Pathway map
hsa00480  Glutathione metabolism
hsa00480

Ortholog table
Module
hsa_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:hsa00480]
Disease
H00597  Snyder-Robinson syndrome
H00668  Anemia due to disorders of glutathione metabolism
H01118  Progressive external ophthalmoplegia (PEO)
H01225  D-2-hydroxyglutaric aciduria (D-2-HGA)
H01375  Glucose 6-phosphate dehydrogenase deficiency
Drug
D00341  Hydroxyurea (USP)
D00829  Eflornithine hydrochloride (USAN)
D02755  Acivicin (USAN/INN)
D07883  Eflornithine (INN)
D08917  Ezatiostat hydrochloride (USAN)
D10026  Tosedostat (USAN/INN)
Other DBs
BSID: 82973
GO: 0006749
Organism
Homo sapiens (human) [GN:hsa]
Gene
2686  GGT7; gamma-glutamyltransferase 7 [KO:K00681] [EC:3.4.19.13 2.3.2.2]
124975  GGT6; gamma-glutamyltransferase 6 [KO:K00681] [EC:3.4.19.13 2.3.2.2]
2678  GGT1; gamma-glutamyltransferase 1 [KO:K18592] [EC:3.4.19.14 3.4.19.13 2.3.2.2]
2687  GGT5; gamma-glutamyltransferase 5 [KO:K18592] [EC:3.4.19.14 3.4.19.13 2.3.2.2]
79017  GGCT; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
79094  CHAC1; ChaC glutathione specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
494143  CHAC2; ChaC cation transport regulator homolog 2 [KO:K07232] [EC:4.3.2.7]
26873  OPLAH; 5-oxoprolinase, ATP-hydrolysing [KO:K01469] [EC:3.5.2.9]
2729  GCLC; glutamate-cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
2730  GCLM; glutamate-cysteine ligase modifier subunit [KO:K11205]
2937  GSS; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
51056  LAP3; leucine aminopeptidase 3 [KO:K11142] [EC:3.4.11.5 3.4.11.1]
290  ANPEP; alanyl aminopeptidase, membrane [KO:K11140] [EC:3.4.11.2]
221357  GSTA5; glutathione S-transferase alpha 5 [KO:K00799] [EC:2.5.1.18]
2939  GSTA2; glutathione S-transferase alpha 2 [KO:K00799] [EC:2.5.1.18]
2941  GSTA4; glutathione S-transferase alpha 4 [KO:K00799] [EC:2.5.1.18]
119391  GSTO2; glutathione S-transferase omega 2 [KO:K00799] [EC:2.5.1.18]
2948  GSTM4; glutathione S-transferase mu 4 [KO:K00799] [EC:2.5.1.18]
2953  GSTT2; glutathione S-transferase theta 2 (gene/pseudogene) [KO:K00799] [EC:2.5.1.18]
2952  GSTT1; glutathione S-transferase theta 1 [KO:K00799] [EC:2.5.1.18]
2947  GSTM3; glutathione S-transferase mu 3 [KO:K00799] [EC:2.5.1.18]
4257  MGST1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
4259  MGST3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
2950  GSTP1; glutathione S-transferase pi 1 [KO:K00799] [EC:2.5.1.18]
2944  GSTM1; glutathione S-transferase mu 1 [KO:K00799] [EC:2.5.1.18]
2949  GSTM5; glutathione S-transferase mu 5 [KO:K00799] [EC:2.5.1.18]
4258  MGST2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
2938  GSTA1; glutathione S-transferase alpha 1 [KO:K00799] [EC:2.5.1.18]
2946  GSTM2; glutathione S-transferase mu 2 [KO:K00799] [EC:2.5.1.18]
2940  GSTA3; glutathione S-transferase alpha 3 [KO:K00799] [EC:2.5.1.18]
9446  GSTO1; glutathione S-transferase omega 1 [KO:K00799] [EC:2.5.1.18]
653689  GSTT2B; glutathione S-transferase theta 2B (gene/pseudogene) [KO:K00799] [EC:2.5.1.18]
373156  GSTK1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
27306  HPGDS; hematopoietic prostaglandin D synthase [KO:K04097] [EC:2.5.1.18 5.3.99.2]
9027  NAT8; N-acetyltransferase 8 (putative) [KO:K20838] [EC:2.3.1.- 2.3.1.80]
51471  NAT8B; N-acetyltransferase 8B (putative, gene/pseudogene) [KO:K20838] [EC:2.3.1.- 2.3.1.80]
2936  GSR; glutathione-disulfide reductase [KO:K00383] [EC:1.8.1.7]
3417  IDH1; isocitrate dehydrogenase (NADP(+)) 1, cytosolic [KO:K00031] [EC:1.1.1.42]
3418  IDH2; isocitrate dehydrogenase (NADP(+)) 2, mitochondrial [KO:K00031] [EC:1.1.1.42]
5226  PGD; phosphogluconate dehydrogenase [KO:K00033] [EC:1.1.1.343 1.1.1.44]
2539  G6PD; glucose-6-phosphate dehydrogenase [KO:K00036] [EC:1.1.1.363 1.1.1.49]
51060  TXNDC12; thioredoxin domain containing 12 [KO:K05360] [EC:1.8.4.2]
257202  GPX6; glutathione peroxidase 6 [KO:K00432] [EC:1.11.1.9]
2882  GPX7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
2877  GPX2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
2878  GPX3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
2876  GPX1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
2880  GPX5; glutathione peroxidase 5 [KO:K00432] [EC:1.11.1.9]
493869  GPX8; glutathione peroxidase 8 (putative) [KO:K00432] [EC:1.11.1.9]
2879  GPX4; glutathione peroxidase 4 [KO:K05361] [EC:1.11.1.12]
4953  ODC1; ornithine decarboxylase 1 [KO:K01581] [EC:4.1.1.17]
6723  SRM; spermidine synthase [KO:K00797] [EC:2.5.1.16]
6611  SMS; spermine synthase [KO:K00802] [EC:2.5.1.22]
6240  RRM1; ribonucleotide reductase catalytic subunit M1 [KO:K10807] [EC:1.17.4.1]
50484  RRM2B; ribonucleotide reductase regulatory TP53 inducible subunit M2B [KO:K10808] [EC:1.17.4.1]
6241  RRM2; ribonucleotide reductase regulatory 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
KO pathway
ko00480   

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