KEGG   PATHWAY: pmax00480
Entry
pmax00480                   Pathway                                
Name
Glutathione metabolism - Pecten maximus (king scallop)
Class
Metabolism; Metabolism of other amino acids
Pathway map
pmax00480  Glutathione metabolism
pmax00480

Module
pmax_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:pmax00480]
Other DBs
GO: 0006749
Organism
Pecten maximus (king scallop) [GN:pmax]
Gene
117327172  glutathione hydrolase-like YwrD proenzyme [KO:K00681] [EC:2.3.2.2 3.4.19.13]
117340873  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117333830  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117333838  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117316222  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117327457  glutathione hydrolase 1 proenzyme-like isoform X1 [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117336358  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117336512  glutathione hydrolase 1 proenzyme-like [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
117337406  gamma-glutamylcyclotransferase-like [KO:K00682] [EC:4.3.2.9]
117323305  putative glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
117324075  putative glutathione-specific gamma-glutamylcyclotransferase 2 [KO:K07232] [EC:4.3.2.7]
117318344  5-oxoprolinase-like [KO:K01469] [EC:3.5.2.9]
117337557  5-oxoprolinase-like [KO:K01469] [EC:3.5.2.9]
117316539  glutamate--cysteine ligase catalytic subunit-like [KO:K11204] [EC:6.3.2.2]
117344457  LOW QUALITY PROTEIN: glutamate--cysteine ligase regulatory subunit-like [KO:K11205]
117337321  glutathione synthetase-like isoform X1 [KO:K21456] [EC:6.3.2.3]
117337323  glutathione synthetase-like [KO:K21456] [EC:6.3.2.3]
117338834  cytosol aminopeptidase-like [KO:K11142] [EC:3.4.11.1 3.4.11.5]
117339445  putative aminopeptidase W07G4.4 [KO:K01255] [EC:3.4.11.1]
117315084  aminopeptidase N-like isoform X1 [KO:K11140] [EC:3.4.11.2]
117315547  aminopeptidase N-like [KO:K11140] [EC:3.4.11.2]
117326744  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
117326747  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
117327046  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
117327880  aminopeptidase Ey-like [KO:K11140] [EC:3.4.11.2]
117321578  microsomal glutathione S-transferase 1-like [KO:K00799] [EC:2.5.1.18]
117321579  microsomal glutathione S-transferase 1-like [KO:K00799] [EC:2.5.1.18]
117331603  glutathione S-transferase Mu 5-like [KO:K00799] [EC:2.5.1.18]
117331627  S-crystallin SL11-like isoform X1 [KO:K00799] [EC:2.5.1.18]
117323763  glutathione S-transferase 3-like [KO:K00799] [EC:2.5.1.18]
117332772  microsomal glutathione S-transferase 3-like [KO:K00799] [EC:2.5.1.18]
117342651  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
117342653  glutathione S-transferase theta-1-like isoform X1 [KO:K00799] [EC:2.5.1.18]
117333569  glutathione S-transferase theta-1-like [KO:K00799] [EC:2.5.1.18]
117334278  LOW QUALITY PROTEIN: glutathione S-transferase-like [KO:K00799] [EC:2.5.1.18]
117343811  glutathione S-transferase omega-1-like [KO:K00799] [EC:2.5.1.18]
117316186  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
117316265  glutathione S-transferase A-like [KO:K00799] [EC:2.5.1.18]
117327639  microsomal glutathione S-transferase 3-like isoform X1 [KO:K00799] [EC:2.5.1.18]
117337260  glutathione S-transferase theta-1-like isoform X1 [KO:K00799] [EC:2.5.1.18]
117328697  microsomal glutathione S-transferase 2-like [KO:K00799] [EC:2.5.1.18]
117337899  glutathione S-transferase omega-1-like [KO:K00799] [EC:2.5.1.18]
117326839  glutathione S-transferase P-like [KO:K23790] [EC:2.5.1.18]
117345230  glutathione S-transferase kappa 1-like [KO:K13299] [EC:2.5.1.18]
117330464  glutathione S-transferase 1-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331625  glutathione S-transferase-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331626  glutathione S-transferase 1-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331629  hematopoietic prostaglandin D synthase-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331630  hematopoietic prostaglandin D synthase-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331631  S-crystallin SL11-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331632  glutathione S-transferase-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117337287  glutathione S-transferase 1-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117337288  S-crystallin SL11-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117338211  S-crystallin SL11-like [KO:K04097] [EC:5.3.99.2 2.5.1.18]
117331608  glutathione S-transferase DHAR1, mitochondrial-like [KO:K21888] [EC:1.8.5.1 2.5.1.18]
117342393  glutathione reductase, mitochondrial-like [KO:K00383] [EC:1.8.1.7]
117316070  isocitrate dehydrogenase [NADP], mitochondrial-like isoform X1 [KO:K00031] [EC:1.1.1.42]
117335833  isocitrate dehydrogenase [NADP] cytoplasmic-like [KO:K00031] [EC:1.1.1.42]
117344556  6-phosphogluconate dehydrogenase, decarboxylating-like isoform X1 [KO:K00033] [EC:1.1.1.44 1.1.1.343]
117330805  glucose-6-phosphate 1-dehydrogenase-like isoform X1 [KO:K00036] [EC:1.1.1.49 1.1.1.363]
117325974  thioredoxin domain-containing protein 12-like [KO:K05360] [EC:1.8.4.2]
117325643  glutathione peroxidase-like isoform X1 [KO:K05361] [EC:1.11.1.12]
117324433  glutathione peroxidase 2-like [KO:K00432] [EC:1.11.1.9]
117334561  glutathione peroxidase-like [KO:K00432] [EC:1.11.1.9]
117326367  glutathione peroxidase 7-like [KO:K00432] [EC:1.11.1.9]
117321821  peroxiredoxin-6-like [KO:K11188] [EC:1.11.1.7 1.11.1.27 3.1.1.-]
117322400  ornithine decarboxylase-like [KO:K01581] [EC:4.1.1.17]
117322401  ornithine decarboxylase-like [KO:K01581] [EC:4.1.1.17]
117343595  ornithine decarboxylase-like [KO:K01581] [EC:4.1.1.17]
117326129  ornithine decarboxylase-like [KO:K01581] [EC:4.1.1.17]
117332497  spermidine synthase-like [KO:K00797] [EC:2.5.1.16]
117344961  spermidine synthase-like [KO:K00797] [EC:2.5.1.16]
117315557  spermine synthase-like isoform X1 [KO:K00802] [EC:2.5.1.22]
117329071  ribonucleoside-diphosphate reductase large subunit-like [KO:K10807] [EC:1.17.4.1]
117325265  ribonucleoside-diphosphate reductase small chain-like [KO:K10808] [EC:1.17.4.1]
117336835  ribonucleoside-diphosphate reductase subunit M2-like [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
pmax00220  Arginine biosynthesis
pmax00250  Alanine, aspartate and glutamate metabolism
pmax00270  Cysteine and methionine metabolism
pmax00430  Taurine and hypotaurine metabolism
KO pathway
ko00480   
LinkDB

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