KEGG   PATHWAY: pcq00480
Entry
pcq00480                    Pathway                                
Name
Glutathione metabolism - Pseudomonas citronellolis
Class
Metabolism; Metabolism of other amino acids
Pathway map
pcq00480  Glutathione metabolism
pcq00480

Module
pcq_M00118  Glutathione biosynthesis, glutamate => glutathione [PATH:pcq00480]
Other DBs
GO: 0006749
Organism
Pseudomonas citronellolis [GN:pcq]
Gene
PcP3B5_25380  ywrD_1; Putative gamma-glutamyltransferase YwrD [KO:K00681] [EC:2.3.2.2 3.4.19.13]
PcP3B5_61650  ywrD_2; Putative gamma-glutamyltransferase YwrD [KO:K00681] [EC:2.3.2.2 3.4.19.13]
PcP3B5_04990  ggt; Gamma-glutamyltranspeptidase precursor [KO:K00681] [EC:2.3.2.2 3.4.19.13]
PcP3B5_01880  ChaC-like protein [KO:K07232] [EC:4.3.2.7]
PcP3B5_18470  LamB/YcsF family protein [KO:K07160] [EC:3.5.2.9]
PcP3B5_11100  hypothetical protein [KO:K07160] [EC:3.5.2.9]
PcP3B5_18460  kipI_2; Kinase A inhibitor [KO:K23123] [EC:3.5.2.9]
PcP3B5_11110  kipI_1; Kinase A inhibitor [KO:K23123] [EC:3.5.2.9]
PcP3B5_18450  kipA_2; KipI antagonist [KO:K23124] [EC:3.5.2.9]
PcP3B5_11120  kipA_1; KipI antagonist [KO:K23124] [EC:3.5.2.9]
PcP3B5_27150  ybdK; Carboxylate-amine ligase YbdK [KO:K06048] [EC:6.3.2.2 6.3.-.-]
PcP3B5_02870  gshA; Glutamate--cysteine ligase [KO:K01919] [EC:6.3.2.2]
PcP3B5_05480  gshB; Glutathione synthetase [KO:K01920] [EC:6.3.2.3]
PcP3B5_50160  pepA_2; Cytosol aminopeptidase [KO:K01255] [EC:3.4.11.1]
PcP3B5_18030  pepN; Aminopeptidase N [KO:K01256] [EC:3.4.11.2]
PcP3B5_18910  yfcG_2; Disulfide-bond oxidoreductase YfcG [KO:K00799] [EC:2.5.1.18]
PcP3B5_20940  gstB_2; Glutathione S-transferase GstB [KO:K00799] [EC:2.5.1.18]
PcP3B5_12320  yfcF; Glutathione S-transferase YfcF [KO:K00799] [EC:2.5.1.18]
PcP3B5_21340  Glutathione S-transferase [KO:K00799] [EC:2.5.1.18]
PcP3B5_21820  yfcG_3; Disulfide-bond oxidoreductase YfcG [KO:K00799] [EC:2.5.1.18]
PcP3B5_39880  yfcG_5; Disulfide-bond oxidoreductase YfcG [KO:K00799] [EC:2.5.1.18]
PcP3B5_08240  gstB_1; Glutathione S-transferase GstB [KO:K00799] [EC:2.5.1.18]
PcP3B5_20740  hypothetical protein [KO:K00799] [EC:2.5.1.18]
PcP3B5_27870  garB; Glutathione amide reductase [KO:K00383] [EC:1.8.1.7]
PcP3B5_38030  icd_1; Isocitrate dehydrogenase [NADP] [KO:K00031] [EC:1.1.1.42]
PcP3B5_38040  icd_2; Isocitrate dehydrogenase [NADP] [KO:K00031] [EC:1.1.1.42]
PcP3B5_34720  ghrB_4; Glyoxylate/hydroxypyruvate reductase B [KO:K00032] [EC:1.1.1.43]
PcP3B5_02710  zwf_1; Glucose-6-phosphate 1-dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
PcP3B5_16690  zwf_2; Glucose-6-phosphate 1-dehydrogenase [KO:K00036] [EC:1.1.1.49 1.1.1.363]
PcP3B5_44760  hypothetical protein [KO:K00432] [EC:1.11.1.9]
PcP3B5_20690  gpx1_1; Hydroperoxy fatty acid reductase gpx1 [KO:K00432] [EC:1.11.1.9]
PcP3B5_42740  gpx1_2; Hydroperoxy fatty acid reductase gpx1 [KO:K00432] [EC:1.11.1.9]
PcP3B5_51300  gpx2; Hydroperoxy fatty acid reductase gpx2 [KO:K00432] [EC:1.11.1.9]
PcP3B5_11020  ldc; Lysine/ornithine decarboxylase [KO:K01581] [EC:4.1.1.17]
PcP3B5_39700  speE_2; Spermidine synthase [KO:K00797] [EC:2.5.1.16]
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
pcq00220  Arginine biosynthesis
pcq00250  Alanine, aspartate and glutamate metabolism
pcq00270  Cysteine and methionine metabolism
pcq00430  Taurine and hypotaurine metabolism
pcq00460  Cyanoamino acid metabolism
KO pathway
ko00480   
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