KEGG   PATHWAY: hsa00480Help
Entry
hsa00480                    Pathway                                

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

All organismsOrtholog table
Module
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)
D01155  
Gemcitabine hydrochloride (JAN/USAN)
D02368  
Gemcitabine (USAN/INN)
D02755  
Acivicin (USAN/INN)
D08917  
Ezatiostat hydrochloride (USAN)
D10026  
Tosedostat (USAN/INN)
D10222  
Gemcitabine elaidate (USAN/INN)
Other DBs
BSID: 
GO: 
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:2.3.2.4]
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:K01920] [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 (brain) [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 (muscle) [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]
2936  
GSR; glutathione 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  
Pidolic acid
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)
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)
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)
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)
Reference
  Authors
Oza SL, Shaw MP, Wyllie S, Fairlamb AH.
  Title
Trypanothione biosynthesis in Leishmania major.
  Journal
Mol Biochem Parasitol 139:107-16 (2005)
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)
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)
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)
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)
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)
Reference
  Authors
Comini M, Menge U, Wissing J, Flohe L.
  Title
Trypanothione synthesis in crithidia revisited.
  Journal
J Biol Chem 280:6850-60 (2005)
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)
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)
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)
Reference
PMID:8892297
  Authors
Krauth-Siegel RL, Ludemann H.
  Title
Reduction of dehydroascorbate by trypanothione.
  Journal
Mol Biochem Parasitol 80:203-8 (1996)
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)
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)
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)
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)
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)
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)
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)
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)
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)
KO pathway
 

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