KEGG   PATHWAY: ptg00480
Entry
ptg00480                    Pathway                                

Name
Glutathione metabolism - Panthera tigris altaica (Amur tiger)
Class
Metabolism; Metabolism of other amino acids
Pathway map
ptg00480  Glutathione metabolism
ptg00480

Module
ptg_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:ptg00480]
Other DBs
GO: 0006749
Organism
Panthera tigris altaica (Amur tiger) [GN:ptg]
Gene
102964946  GGT7; gamma-glutamyltransferase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
102970266  GGT6; gamma-glutamyltransferase 6 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
102958863  GGT1; gamma-glutamyltransferase 1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102959431  GGT5; gamma-glutamyltransferase 5 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
102972301  GGCT; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
102962052  CHAC1; ChaC glutathione specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
102968625  CHAC2; ChaC cation transport regulator homolog 2 [KO:K07232] [EC:4.3.2.7]
102954864  OPLAH; 5-oxoprolinase (ATP-hydrolysing) [KO:K01469] [EC:3.5.2.9]
102949666  GCLC; glutamate-cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
102961711  GCLM; glutamate-cysteine ligase modifier subunit [KO:K11205]
102969006  GSS; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
102961625  LAP3; leucine aminopeptidase 3 [KO:K11142] [EC:3.4.11.1 3.4.11.5]
102962318  ANPEP; alanyl aminopeptidase, membrane [KO:K11140] [EC:3.4.11.2]
102971089  MGST3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
102966922  GSTO1; glutathione S-transferase omega 1 [KO:K00799] [EC:2.5.1.18]
102967394  GSTO2; glutathione S-transferase omega 2 [KO:K00799] [EC:2.5.1.18]
102955989  MGST1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
102962954  MGST2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
102970472  glutathione S-transferase theta-2B-like [KO:K00799] [EC:2.5.1.18]
102960578  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
102959987  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
102960295  glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
102958890  glutathione S-transferase A4 [KO:K00799] [EC:2.5.1.18]
102958324  GSTA2; glutathione S-transferase A2 [KO:K00799] [EC:2.5.1.18]
102949073  glutathione S-transferase-like [KO:K00799] [EC:2.5.1.18]
102958599  glutathione S-transferase A4-like [KO:K00799] [EC:2.5.1.18]
102949368  glutathione S-transferase alpha M14-like [KO:K00799] [EC:2.5.1.18]
102949663  GSTM3; glutathione S-transferase Mu 3 [KO:K00799] [EC:2.5.1.18]
102949366  GSTM4; glutathione S-transferase Mu 4 [KO:K00799] [EC:2.5.1.18]
102960863  glutathione S-transferase theta-4-like [KO:K00799] [EC:2.5.1.18]
102964863  GSTP1; glutathione S-transferase pi 1 [KO:K23790] [EC:2.5.1.18]
102950403  GSTK1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
102970849  HPGDS; hematopoietic prostaglandin D synthase [KO:K04097] [EC:5.3.99.2 2.5.1.18]
102957307  NAT8B; N-acetyltransferase 8B (putative, gene/pseudogene) [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102956995  GSR; glutathione-disulfide reductase [KO:K00383] [EC:1.8.1.7]
102962124  IDH2; isocitrate dehydrogenase (NADP(+)) 2, mitochondrial [KO:K00031] [EC:1.1.1.42]
102967152  IDH1; isocitrate dehydrogenase (NADP(+)) 1, cytosolic [KO:K00031] [EC:1.1.1.42]
102953665  PGD; phosphogluconate dehydrogenase [KO:K00033] [EC:1.1.1.44 1.1.1.343]
102967382  G6PD; glucose-6-phosphate dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
102956818  TXNDC12; thioredoxin domain containing 12 [KO:K05360] [EC:1.8.4.2]
102949955  GPX4; glutathione peroxidase 4 [KO:K05361] [EC:1.11.1.12]
102953855  GPX7; glutathione peroxidase 7 [KO:K00432] [EC:1.11.1.9]
102972733  GPX8; glutathione peroxidase 8 (putative) [KO:K00432] [EC:1.11.1.9]
102959727  GPX3; glutathione peroxidase 3 [KO:K00432] [EC:1.11.1.9]
102967445  GPX5; epididymal secretory glutathione peroxidase [KO:K00432] [EC:1.11.1.9]
102967167  GPX6; glutathione peroxidase 6 [KO:K00432] [EC:1.11.1.9]
102966993  GPX2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
102959037  GPX1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
102958542  PRDX6; peroxiredoxin 6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
102970178  antizyme inhibitor 2-like [KO:K01581] [EC:4.1.1.17]
102950564  ODC1; ornithine decarboxylase 1 [KO:K01581] [EC:4.1.1.17]
102955964  SRM; spermidine synthase [KO:K00797] [EC:2.5.1.16]
102954471  SMS; spermine synthase [KO:K00802] [EC:2.5.1.22]
102953329  RRM1; ribonucleotide reductase catalytic subunit M1 [KO:K10807] [EC:1.17.4.1]
102950840  RRM2B; ribonucleotide reductase regulatory TP53 inducible subunit M2B [KO:K10808] [EC:1.17.4.1]
102950263  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
Related
pathway
ptg00220  Arginine biosynthesis
ptg00250  Alanine, aspartate and glutamate metabolism
ptg00270  Cysteine and methionine metabolism
ptg00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

DBGET integrated database retrieval system