ENTRY ko00480 Pathway NAME Glutathione metabolism CLASS Metabolism; Metabolism of other amino acids PATHWAY_MAP ko00480 Glutathione metabolism MODULE M00118 Glutathione biosynthesis, glutamate => glutathione [PATH:ko00480] DBLINKS GO: 0006749 ORTHOLOGY K00681 gamma-glutamyltranspeptidase / glutathione hydrolase [EC:2.3.2.2 3.4.19.13] K18592 gamma-glutamyltranspeptidase / glutathione hydrolase / leukotriene-C4 hydrolase [EC:2.3.2.2 3.4.19.13 3.4.19.14] K00682 gamma-glutamylcyclotransferase [EC:4.3.2.9] K22596 gamma-glutamylcyclotransferase, plant [EC:4.3.2.9] K07232 glutathione-specific gamma-glutamylcyclotransferase [EC:4.3.2.7] K01469 5-oxoprolinase (ATP-hydrolysing) [EC:3.5.2.9] K07160 5-oxoprolinase (ATP-hydrolysing) subunit A [EC:3.5.2.9] K23123 5-oxoprolinase (ATP-hydrolysing) subunit B [EC:3.5.2.9] K23124 5-oxoprolinase (ATP-hydrolysing) subunit C [EC:3.5.2.9] K11204 glutamate--cysteine ligase catalytic subunit [EC:6.3.2.2] K11205 glutamate--cysteine ligase regulatory subunit K06048 glutamate---cysteine ligase / carboxylate-amine ligase [EC:6.3.2.2 6.3.-.-] K01919 glutamate--cysteine ligase [EC:6.3.2.2] K01920 glutathione synthase [EC:6.3.2.3] K21456 glutathione synthase [EC:6.3.2.3] K03423 bis-gamma-glutamylcystine reductase [EC:1.8.1.13] K11142 cytosol aminopeptidase [EC:3.4.11.1 3.4.11.5] K01255 leucyl aminopeptidase [EC:3.4.11.1] K07751 PepB aminopeptidase [EC:3.4.11.23] K11140 aminopeptidase N [EC:3.4.11.2] K01256 aminopeptidase N [EC:3.4.11.2] K01270 dipeptidase D [EC:3.4.13.-] K15428 Cys-Gly metallodipeptidase DUG1 [EC:3.4.13.-] K00799 glutathione S-transferase [EC:2.5.1.18] K23790 glutathione S-transferase P [EC:2.5.1.18] K13299 glutathione S-transferase kappa 1 [EC:2.5.1.18] K04097 prostaglandin-H2 D-isomerase / glutathione transferase [EC:5.3.99.2 2.5.1.18] K21888 glutathione dehydrogenase/transferase [EC:1.8.5.1 2.5.1.18] K25210 glutathione transferase [EC:2.5.1.18] K20838 N-acetyltransferase 8 [EC:2.3.1.80 2.3.1.-] K00383 glutathione reductase (NADPH) [EC:1.8.1.7] K00031 isocitrate dehydrogenase [EC:1.1.1.42] K00032 phosphogluconate 2-dehydrogenase [EC:1.1.1.43] K00033 6-phosphogluconate dehydrogenase [EC:1.1.1.44 1.1.1.343] K00036 glucose-6-phosphate 1-dehydrogenase [EC:1.1.1.49 1.1.1.363] K05360 protein-disulfide reductase (glutathione) [EC:1.8.4.2] K05361 phospholipid-hydroperoxide glutathione peroxidase [EC:1.11.1.12] K00432 glutathione peroxidase [EC:1.11.1.9] K11188 peroxiredoxin 6 [EC:1.11.1.7 1.11.1.27 3.1.1.-] K24137 glutaredoxin/glutathione-dependent peroxiredoxin [EC:1.11.1.25 1.11.1.27] K24136 glutathione-dependent peroxiredoxin [EC:1.11.1.27] K24138 glutaredoxin/glutathione-dependent peroxiredoxin [EC:1.11.1.25 1.11.1.27] K00310 pyrimidodiazepine synthase [EC:1.5.4.1] K01581 ornithine decarboxylase [EC:4.1.1.17] K00797 spermidine synthase [EC:2.5.1.16] K24034 spermidine synthase / saccharopine dehydrogenase (NADP+, L-glutamate-forming) [EC:2.5.1.16 1.5.1.10] K01917 glutathionylspermidine synthase [EC:6.3.1.8] K01460 glutathionylspermidine amidase/synthetase [EC:3.5.1.78 6.3.1.8] K00802 spermine synthase [EC:2.5.1.22] K01833 trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-] K04283 trypanothione-disulfide reductase [EC:1.8.1.12] K00434 L-ascorbate peroxidase [EC:1.11.1.11] K11185 cytosolic tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-] K11186 mitochondrial tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-] K11207 glutathione peroxidase-type tryparedoxin peroxidase [EC:1.11.1.-] K10807 ribonucleoside-diphosphate reductase subunit M1 [EC:1.17.4.1] K10808 ribonucleoside-diphosphate reductase subunit M2 [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 PMID:12675513 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 PMID:18482986 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 PMID:14583094 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 PMID:11157967 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 PMID:15610825 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 PMID:12049631 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 PMID:12750367 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 PMID:12967709 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 PMID:12121990 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 PMID:15537651 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 PMID:12751784 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 PMID:18395526 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 PMID:11150302 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 PMID:12949079 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 PMID:12446213 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 PMID:10713147 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 PMID:17922848 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 PMID:12466271 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 PMID:14982633 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 REL_PATHWAY ko00220 Arginine biosynthesis ko00250 Alanine, aspartate and glutamate metabolism ko00270 Cysteine and methionine metabolism ko00430 Taurine and hypotaurine metabolism ko00460 Cyanoamino acid metabolism ///