KEGG   PATHWAY: adl00480
Entry
adl00480                    Pathway                                
Name
Glutathione metabolism - Auricularia subglabra
Class
Metabolism; Metabolism of other amino acids
Pathway map
adl00480  Glutathione metabolism
adl00480

Other DBs
GO: 0006749
Organism
Auricularia subglabra [GN:adl]
Gene
AURDEDRAFT_109869  gamma-glutamyltranspeptidase [KO:K00681] [EC:2.3.2.2 3.4.19.13]
AURDEDRAFT_158431  gamma-glutamyltranspeptidase [KO:K18592] [EC:2.3.2.2 3.4.19.13 3.4.19.14]
AURDEDRAFT_109505  ChaC-like protein [KO:K07232] [EC:4.3.2.7]
AURDEDRAFT_113393  5-oxoprolinase [KO:K01469] [EC:3.5.2.9]
AURDEDRAFT_111295  glutamate-cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]
AURDEDRAFT_117060  glutathione synthase [KO:K21456] [EC:6.3.2.3]
AURDEDRAFT_158038  hypothetical protein [KO:K11142] [EC:3.4.11.1 3.4.11.5]
AURDEDRAFT_111539  CNDP dipeptidase [KO:K15428] [EC:3.4.13.-]
AURDEDRAFT_115243  microsomal glutathione S-transferase 3 [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_115569  hypothetical protein [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_115924  hypothetical protein [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_115308  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_111080  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_111081  hypothetical protein [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_62077  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_183862  glutathione transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_62042  glutathione transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_123306  putative glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_64199  glutathione S-transferase like protein [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_84076  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_110264  glutathione S-transferase-like protein [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_132852  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_52268  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_184895  glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
AURDEDRAFT_183093  thioredoxin-like protein [KO:K13299] [EC:2.5.1.18]
AURDEDRAFT_113593  thioredoxin-like protein [KO:K13299] [EC:2.5.1.18]
AURDEDRAFT_154150  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_116513  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_114492  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_167047  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_167052  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_114501  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_114504  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_167063  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_111004  hypothetical protein [KO:K04097] [EC:5.3.99.2 2.5.1.18]
AURDEDRAFT_133857  glutathione-disulfide reductase [KO:K00383] [EC:1.8.1.7]
AURDEDRAFT_189035  isocitrate dehydrogenase [KO:K00031] [EC:1.1.1.42]
AURDEDRAFT_111632  decarboxylating 6-phosphogluconate dehydrogenase [KO:K00033] [EC:1.1.1.44 1.1.1.343]
AURDEDRAFT_110495  glucose-6-P dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
AURDEDRAFT_110556  cysteine peroxiredoxin [KO:K24137] [EC:1.11.1.25 1.11.1.27]
AURDEDRAFT_59007  ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
AURDEDRAFT_115750  saccharopine dehydrogenase [KO:K24034] [EC:2.5.1.16 1.5.1.10]
AURDEDRAFT_116331  ribonucleotide reductase alpha subunit [KO:K10807] [EC:1.17.4.1]
AURDEDRAFT_147076  hypothetical protein [KO:K10807] [EC:1.17.4.1]
AURDEDRAFT_77142  ferritin-like protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_177699  ferritin-like protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_77517  ribonucleotide reductase [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_170879  hypothetical protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_170886  hypothetical protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_140589  ribonucleotide reductase [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_43747  ferritin-like protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_161255  hypothetical protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_159367  hypothetical protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_161783  hypothetical protein [KO:K10808] [EC:1.17.4.1]
AURDEDRAFT_110332  ribonucleotide reductase small subunit [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
adl00220  Arginine biosynthesis
adl00250  Alanine, aspartate and glutamate metabolism
adl00270  Cysteine and methionine metabolism
adl00430  Taurine and hypotaurine metabolism
adl00460  Cyanoamino acid metabolism
KO pathway
ko00480   
LinkDB

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