KEGG   PATHWAY: hgl00480
Entry
hgl00480                    Pathway                                
Name
Glutathione metabolism - Heterocephalus glaber (naked mole-rat)
Class
Metabolism; Metabolism of other amino acids
Pathway map
hgl00480  Glutathione metabolism
hgl00480

Module
hgl_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:hgl00480]
Other DBs
GO: 0006749
Organism
Heterocephalus glaber (naked mole-rat) [GN:hgl]
Gene
101700696  Ggt6; gamma-glutamyltransferase 6 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
101705019  Ggt7; gamma-glutamyltransferase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
101722156  Ggt1; gamma-glutamyltransferase 1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
101723554  Ggt5; gamma-glutamyltransferase 5 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
101723887  Ggct; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
101721673  Chac1; ChaC glutathione specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
101716029  Chac2; ChaC cation transport regulator homolog 2 [KO:K07232] [EC:4.3.2.7]
101702464  Oplah; 5-oxoprolinase (ATP-hydrolysing) [KO:K01469] [EC:3.5.2.9]
101718793  Gclc; glutamate-cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
101703324  Gclm; glutamate-cysteine ligase modifier subunit [KO:K11205]
101704674  Gss; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
101712957  Lap3; leucine aminopeptidase 3 [KO:K11142] [EC:3.4.11.1 3.4.11.5]
101706035  Anpep; alanyl aminopeptidase, membrane [KO:K11140] [EC:3.4.11.2]
101725364  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
101726608  glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
101719471  glutathione S-transferase Mu 1 [KO:K00799] [EC:2.5.1.18]
101713569  Mgst1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
101714128  Gstt2; glutathione S-transferase theta-2 [KO:K00799] [EC:2.5.1.18]
101716174  Mgst2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
101707238  Gstm2; glutathione S-transferase mu 2 [KO:K00799] [EC:2.5.1.18]
101705794  glutathione S-transferase B [KO:K00799] [EC:2.5.1.18]
101708562  Gstm3; glutathione S-transferase mu 3 [KO:K00799] [EC:2.5.1.18]
101703755  glutathione S-transferase Mu 1 [KO:K00799] [EC:2.5.1.18]
101712717  Gsto2; glutathione S-transferase omega 2 [KO:K00799] [EC:2.5.1.18]
101712139  Gsto1; glutathione S-transferase omega 1 [KO:K00799] [EC:2.5.1.18]
101717166  Mgst3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
101714626  Gsta4; glutathione S-transferase alpha 4 [KO:K00799] [EC:2.5.1.18]
101714852  Gsta1; glutathione S-transferase A1 [KO:K00799] [EC:2.5.1.18]
101696396  glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
101712988  Gstp1; glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
101713648  Gstk1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
101706734  Hpgds; hematopoietic prostaglandin D synthase [KO:K04097] [EC:5.3.99.2 2.5.1.18]
101696874  Lancl1; LanC like 1 [KO:K25210] [EC:2.5.1.18]
101720890  probable N-acetyltransferase CML3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
101696661  Gsr; glutathione-disulfide reductase [KO:K00383] [EC:1.8.1.7]
101705662  Idh1; isocitrate dehydrogenase (NADP(+)) 1, cytosolic [KO:K00031] [EC:1.1.1.42]
101708667  Idh2; isocitrate dehydrogenase (NADP(+)) 2, mitochondrial [KO:K00031] [EC:1.1.1.42]
101701691  Pgd; phosphogluconate dehydrogenase [KO:K00033] [EC:1.1.1.44 1.1.1.343]
101712640  G6pd; glucose-6-phosphate dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
101714855  Txndc12; thioredoxin domain containing 12 [KO:K05360] [EC:1.8.4.2]
101708875  Gpx4; glutathione peroxidase 4 [KO:K05361] [EC:1.11.1.12]
101701549  Gpx3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
101710466  Gpx1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
101701418  Gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
101698217  Gpx6; glutathione peroxidase 6 [KO:K00432] [EC:1.11.1.9]
101698603  Gpx5; glutathione peroxidase 5 [KO:K00432] [EC:1.11.1.9]
101726259  Gpx8; glutathione peroxidase 8 (putative) [KO:K00432] [EC:1.11.1.9]
101709505  Gpx7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
101696758  Prdx6; peroxiredoxin 6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
101705036  antizyme inhibitor 2-like [KO:K01581] [EC:4.1.1.17]
101699456  Odc1; ornithine decarboxylase 1 [KO:K01581] [EC:4.1.1.17]
101696345  Srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
101718865  spermine synthase [KO:K00802] [EC:2.5.1.22]
101696715  Sms; spermine synthase [KO:K00802] [EC:2.5.1.22]
101708047  Rrm1; ribonucleotide reductase catalytic subunit M1 [KO:K10807] [EC:1.17.4.1]
101700655  Rrm2; ribonucleotide reductase regulatory subunit M2 [KO:K10808] [EC:1.17.4.1]
101718446  Rrm2b; ribonucleotide reductase regulatory TP53 inducible subunit M2B [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
hgl00220  Arginine biosynthesis
hgl00250  Alanine, aspartate and glutamate metabolism
hgl00270  Cysteine and methionine metabolism
hgl00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
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