KEGG   PATHWAY: rno00480
Entry
rno00480                    Pathway                                

Name
Glutathione metabolism - Rattus norvegicus (rat)
Class
Metabolism; Metabolism of other amino acids
Pathway map
rno00480  Glutathione metabolism
rno00480

Module
rno_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:rno00480]
Other DBs
GO: 0006749
Organism
Rattus norvegicus (rat) [GN:rno]
Gene
156275  Ggt7; glutathione hydrolase 7 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
408206  Ggt6; glutathione hydrolase 6 [KO:K00681] [EC:2.3.2.2 3.4.19.13]
116568  Ggt1; glutathione hydrolase 1 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
29566  Ggt5; glutathione hydrolase 5 proenzyme [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
362368  Ggct; gamma-glutamylcyclotransferase [KO:K00682] [EC:4.3.2.9]
362196  Chac1; glutathione-specific gamma-glutamylcyclotransferase 1 [KO:K07232] [EC:4.3.2.7]
360994  Chac2; putative glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
116684  Oplah; 5-oxoprolinase [KO:K01469] [EC:3.5.2.9]
25283  Gclc; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
29739  Gclm; glutamate--cysteine ligase regulatory subunit [KO:K11205]
25458  Gss; glutathione synthetase [KO:K21456] [EC:6.3.2.3]
289668  Lap3; cytosol aminopeptidase [KO:K11142] [EC:3.4.11.1 3.4.11.5]
81641  Anpep; aminopeptidase N precursor [KO:K11140] [EC:3.4.11.2]
81869  Gstm7; glutathione S-transferase Mu 7 [KO:K00799] [EC:2.5.1.18]
24421  Gsta1; glutathione S-transferase alpha-3 [KO:K00799] [EC:2.5.1.18]
24422  Gsta2; glutathione S-transferase alpha-1 [KO:K00799] [EC:2.5.1.18]
24424  Gstm2; glutathione S-transferase Mu 2 [KO:K00799] [EC:2.5.1.18]
25260  Gstt1; glutathione S-transferase theta-1 [KO:K00799] [EC:2.5.1.18]
29487  Gstt2; glutathione S-transferase theta-2 [KO:K00799] [EC:2.5.1.18]
57298  Gstm3l; glutathione S-transferase Mu 3 [KO:K00799] [EC:2.5.1.18]
295037  Mgst2; microsomal glutathione S-transferase 2 [KO:K00799] [EC:2.5.1.18]
171341  Mgst1; microsomal glutathione S-transferase 1 [KO:K00799] [EC:2.5.1.18]
64352  Gstm5; glutathione S-transferase Mu 5 [KO:K00799] [EC:2.5.1.18]
289197  Mgst3; microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
114846  Gsto1; glutathione S-transferase omega-1 [KO:K00799] [EC:2.5.1.18]
300850  Gsta4; glutathione S-transferase alpha-4 [KO:K00799] [EC:2.5.1.18]
309465  Gsto2; glutathione S-transferase omega-2 [KO:K00799] [EC:2.5.1.18]
363205  RGD1562107; glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
499689  Gstm4; glutathione S-transferase Mu 4 [KO:K00799] [EC:2.5.1.18]
24423  Gstm1; glutathione S-transferase Mu 1 [KO:K00799] [EC:2.5.1.18]
494499  Gsta5; glutathione S-transferase alpha-2 [KO:K00799] [EC:2.5.1.18]
494500  Gsta3; glutathione S-transferase alpha-5 isoform 1 [KO:K00799] [EC:2.5.1.18]
499688  Gstm6; glutathione S-transferase Mu 6 [KO:K00799] [EC:2.5.1.18]
501110  Gsta6; glutathione S-transferase A6 [KO:K00799] [EC:2.5.1.18]
499422  Gstt3; glutathione S-transferase, theta 3 [KO:K00799] [EC:2.5.1.18]
686922  Gstt4; glutathione S-transferase theta-4 [KO:K00799] [EC:2.5.1.18]
295362  Gstm6l; glutathione S-transferase, mu 6-like [KO:K00799] [EC:2.5.1.18]
24426  Gstp1; glutathione S-transferase P [KO:K23790] [EC:2.5.1.18]
100911464  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
293656  RGD1307603; uncharacterized protein LOC293656 [KO:K23790] [EC:2.5.1.18]
297029  Gstk1; glutathione S-transferase kappa 1 [KO:K13299] [EC:2.5.1.18]
58962  Hpgds; hematopoietic prostaglandin D synthase [KO:K04097] [EC:5.3.99.2 2.5.1.18]
64570  Nat8; N-acetyltransferase 8 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
102549803  Nat8f4; N-acetyltransferase family 8 member 2-like [KO:K20838] [EC:2.3.1.80 2.3.1.-]
113892  Nat8f3; N-acetyltransferase family 8 member 3 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
500237  Nat8f2; N-acetyltransferase family 8 member 2 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
59300  Nat8f1; probable N-acetyltransferase CML1 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
114020  Nat8f5; probable N-acetyltransferase CML5 [KO:K20838] [EC:2.3.1.80 2.3.1.-]
116686  Gsr; glutathione reductase [KO:K00383] [EC:1.8.1.7]
24479  Idh1; isocitrate dehydrogenase [NADP] cytoplasmic [KO:K00031] [EC:1.1.1.42]
361596  Idh2; isocitrate dehydrogenase [NADP], mitochondrial precursor [KO:K00031] [EC:1.1.1.42]
100360180  Pgd; 6-phosphogluconate dehydrogenase, decarboxylating [KO:K00033] [EC:1.1.1.44 1.1.1.343]
24377  G6pd; glucose-6-phosphate 1-dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
298370  Txndc12; thioredoxin domain-containing protein 12 precursor [KO:K05360] [EC:1.8.4.2]
29328  Gpx4; phospholipid hydroperoxide glutathione peroxidase isoform A precursor [KO:K05361] [EC:1.11.1.12]
24404  Gpx1; glutathione peroxidase 1 [KO:K00432] [EC:1.11.1.9]
64317  Gpx3; glutathione peroxidase 3 precursor [KO:K00432] [EC:1.11.1.9]
259233  Gpx6; glutathione peroxidase 6 precursor [KO:K00432] [EC:1.11.1.9]
29326  Gpx2; glutathione peroxidase 2 [KO:K00432] [EC:1.11.1.9]
113919  Gpx5; epididymal secretory glutathione peroxidase precursor [KO:K00432] [EC:1.11.1.9]
298376  Gpx7; glutathione peroxidase 7 precursor [KO:K00432] [EC:1.11.1.9]
294744  Gpx8; probable glutathione peroxidase 8 [KO:K00432] [EC:1.11.1.9]
94167  Prdx6; peroxiredoxin-6 [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
24609  Odc1; ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
297899  RGD1562036; antizyme inhibitor 2 [KO:K01581] [EC:4.1.1.17]
84596  Srm; spermidine synthase [KO:K00797] [EC:2.5.1.16]
363469  Sms; spermine synthase [KO:K00802] [EC:2.5.1.22]
685579  Rrm1; ribonucleoside-diphosphate reductase large subunit [KO:K10807] [EC:1.17.4.1]
299976  Rrm2b; ribonucleoside-diphosphate reductase subunit M2 B [KO:K10808] [EC:1.17.4.1]
362720  Rrm2; ribonucleoside-diphosphate reductase 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
rno00220  Arginine biosynthesis
rno00250  Alanine, aspartate and glutamate metabolism
rno00270  Cysteine and methionine metabolism
rno00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   

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