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 K00031 IDH1, IDH2, icd, IDP; isocitrate dehydrogenase [EC:1.1.1.42] K00032 E1.1.1.43; phosphogluconate 2-dehydrogenase [EC:1.1.1.43] K00033 PGD, gnd, gntZ; 6-phosphogluconate dehydrogenase [EC:1.1.1.44 1.1.1.343] K00036 G6PD, zwf; glucose-6-phosphate 1-dehydrogenase [EC:1.1.1.49 1.1.1.363] K00310 SE; pyrimidodiazepine synthase [EC:1.5.4.1] K00383 GSR, gor; glutathione reductase (NADPH) [EC:1.8.1.7] K00432 gpx, btuE, bsaA; glutathione peroxidase [EC:1.11.1.9] K00434 E1.11.1.11; L-ascorbate peroxidase [EC:1.11.1.11] K00681 ggt; gamma-glutamyltranspeptidase / glutathione hydrolase [EC:2.3.2.2 3.4.19.13] K00682 GGCT; gamma-glutamylcyclotransferase [EC:4.3.2.9] K00797 speE, SRM, SPE3; spermidine synthase [EC:2.5.1.16] K00799 GST; glutathione S-transferase [EC:2.5.1.18] K00802 SMS; spermine synthase [EC:2.5.1.22] K01255 CARP, pepA; leucyl aminopeptidase [EC:3.4.11.1] K01256 pepN; aminopeptidase N [EC:3.4.11.2] K01270 pepD; dipeptidase D [EC:3.4.13.-] K01460 gsp; glutathionylspermidine amidase/synthetase [EC:3.5.1.78 6.3.1.8] K01469 OPLAH, OXP1, oplAH; 5-oxoprolinase (ATP-hydrolysing) [EC:3.5.2.9] K01581 E4.1.1.17, ODC1, speC, speF; ornithine decarboxylase [EC:4.1.1.17] K01833 TRYS; trypanothione synthetase/amidase [EC:6.3.1.9 3.5.1.-] K01917 GSP; glutathionylspermidine synthase [EC:6.3.1.8] K01919 gshA, egtA; glutamate---cysteine ligase [EC:6.3.2.2] K01920 gshB; glutathione synthase [EC:6.3.2.3] K03423 E1.8.1.13; bis-gamma-glutamylcystine reductase K04097 HPGDS; prostaglandin-H2 D-isomerase / glutathione transferase [EC:5.3.99.2 2.5.1.18] K04283 TRYR; trypanothione-disulfide reductase [EC:1.8.1.12] K05360 TXNDC12; protein-disulfide reductase (glutathione) [EC:1.8.4.2] K05361 GPX4; phospholipid-hydroperoxide glutathione peroxidase [EC:1.11.1.12] K06048 gshA, ybdK; glutamate---cysteine ligase / carboxylate-amine ligase [EC:6.3.2.2 6.3.-.-] K07160 pxpA; 5-oxoprolinase (ATP-hydrolysing) subunit A [EC:3.5.2.9] K07232 CHAC; glutathione-specific gamma-glutamylcyclotransferase [EC:4.3.2.7] K07751 pepB; PepB aminopeptidase [EC:3.4.11.23] K10807 RRM1; ribonucleoside-diphosphate reductase subunit M1 [EC:1.17.4.1] K10808 RRM2; ribonucleoside-diphosphate reductase subunit M2 [EC:1.17.4.1] K11140 ANPEP, CD13; aminopeptidase N [EC:3.4.11.2] K11142 LAP3; cytosol aminopeptidase [EC:3.4.11.1 3.4.11.5] K11185 TRYP; cytosolic tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-] K11186 MTRYP; mitochondrial tryparedoxin peroxidase, trypanosomatid typical 2-Cys peroxiredoxin [EC:1.11.1.-] K11188 PRDX6; peroxiredoxin 6 [EC:1.11.1.7 1.11.1.27 3.1.1.-] K11204 GCLC; glutamate---cysteine ligase catalytic subunit [EC:6.3.2.2] K11205 GCLM; glutamate---cysteine ligase regulatory subunit K11207 TDPX; glutathione peroxidase-type tryparedoxin peroxidase [EC:1.11.1.-] K13299 GSTK1; glutathione S-transferase kappa 1 [EC:2.5.1.18] K15428 DUG1; Cys-Gly metallodipeptidase DUG1 [EC:3.4.13.-] K18592 GGT1_5, CD224; gamma-glutamyltranspeptidase / glutathione hydrolase / leukotriene-C4 hydrolase [EC:2.3.2.2 3.4.19.13 3.4.19.14] K20838 NAT8; N-acetyltransferase 8 [EC:2.3.1.80 2.3.1.-] K21456 GSS; glutathione synthase [EC:6.3.2.3] K21888 DHAR; glutathione dehydrogenase/transferase [EC:1.8.5.1 2.5.1.18] K22596 GGCT; gamma-glutamylcyclotransferase, plant [EC:4.3.2.9] K23123 pxpB; 5-oxoprolinase (ATP-hydrolysing) subunit B K23124 pxpC; 5-oxoprolinase (ATP-hydrolysing) subunit C K23790 GSTP; glutathione S-transferase P K24034 SPE3-LYS9; spermidine synthase / saccharopine dehydrogenase (NADP+, L-glutamate-forming) K24136 pgdX; glutathione-dependent peroxiredoxin K24137 PRX1; glutaredoxin/glutathione-dependent peroxiredoxin K24138 prx3; glutaredoxin/glutathione-dependent peroxiredoxin K25210 LANCL1; glutathione transferase K28983 gshAB; glutamate---cysteine ligase / glutathione synthase K29001 GTO; glutathione dehydrogenase/transferase 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 ///