ENTRY ko00450 Pathway NAME Selenocompound metabolism CLASS Metabolism; Metabolism of other amino acids PATHWAY_MAP ko00450 Selenocompound metabolism ORTHOLOGY K01739 cystathionine gamma-synthase [EC:2.5.1.48] K00816 kynurenine---oxoglutarate transaminase / cysteine-S-conjugate beta-lyase / glutamine---phenylpyruvate transaminase [EC:2.6.1.7 4.4.1.13 2.6.1.64] K01760 cysteine-S-conjugate beta-lyase [EC:4.4.1.13] K14155 cysteine-S-conjugate beta-lyase [EC:4.4.1.13] K00548 5-methyltetrahydrofolate--homocysteine methyltransferase [EC:2.1.1.13] K24042 methionine synthase / methylenetetrahydrofolate reductase (NADH) [EC:2.1.1.13 1.5.1.54] K00549 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase [EC:2.1.1.14] K01758 cystathionine gamma-lyase [EC:4.4.1.1] K01761 methionine-gamma-lyase [EC:4.4.1.11] K01763 selenocysteine lyase [EC:4.4.1.16] K11717 cysteine desulfurase / selenocysteine lyase [EC:2.8.1.7 4.4.1.16] K08247 methionine S-methyltransferase [EC:2.1.1.12] K00384 thioredoxin reductase (NADPH) [EC:1.8.1.9] K22182 thioredoxin reductase (NADPH) [EC:1.8.1.9] K00562 methyltransferase [EC:2.1.1.49 2.1.1.96] K17050 selenate/chlorate reductase subunit alpha [EC:1.97.1.9 1.97.1.1] K17051 selenate/chlorate reductase subunit beta [EC:1.97.1.9 1.97.1.1] K17052 selenate/chlorate reductase subunit gamma [EC:1.97.1.9 1.97.1.1] K07309 Tat-targeted selenate reductase subunit YnfE [EC:1.97.1.9] K07310 Tat-targeted selenate reductase subunit YnfF [EC:1.97.1.9] K12527 putative selenate reductase [EC:1.97.1.9] K12528 putative selenate reductase molybdopterin-binding subunit K12529 putative selenate reductase FAD-binding subunit K27874 selenate reductase (quinol) subunit A [EC:1.97.1.14] K27875 selenate reductase (quinol) subunit B [EC:1.97.1.14] K27876 selenate reductase (quinol) subunit C [EC:1.97.1.14] K13811 3'-phosphoadenosine 5'-phosphosulfate synthase [EC:2.7.7.4 2.7.1.25] K00955 bifunctional enzyme CysN/CysC [EC:2.7.7.4 2.7.1.25] K00956 sulfate adenylyltransferase subunit 1 [EC:2.7.7.4] K00957 sulfate adenylyltransferase subunit 2 [EC:2.7.7.4] K00958 sulfate adenylyltransferase [EC:2.7.7.4] K01008 selenide, water dikinase [EC:2.7.9.3] K10837 O-phosphoseryl-tRNA(Sec) kinase [EC:2.7.1.164] K01042 L-seryl-tRNA(Ser) seleniumtransferase [EC:2.9.1.1] K03341 O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase [EC:2.9.1.2] K01874 methionyl-tRNA synthetase [EC:6.1.1.10] COMPOUND C00017 Protein C00041 L-Alanine C01528 Hydrogen selenide C02535 Dimethyl selenide C05172 Selenophosphoric acid C05335 L-Selenomethionine C05336 Selenomethionyl-tRNA(Met) C05684 Selenite C05686 Adenylylselenate C05688 L-Selenocysteine C05689 Se-Methyl-L-selenocysteine C05690 Se-Methylselenomethionine C05695 gamma-Glutamyl-Se-methylselenocysteine C05697 Selenate C05698 Selenohomocysteine C05699 L-Selenocystathionine C05703 Methaneselenol C06481 L-Seryl-tRNA(Sec) C06482 L-Selenocysteinyl-tRNA(Sec) C16638 O-Phosphoseryl-tRNA(Sec) C18870 Selenodiglutathione C18871 Glutathioselenol C18872 Trimethylselenonium C18893 1-Methylseleno-N-acetyl-D-galactosamine C18902 Methylselenic acid C18904 Methylselenopyruvate C18905 Methylselenocysteine Se-oxide REFERENCE PMID:21190829 AUTHORS Hoefig CS, Renko K, Kohrle J, Birringer M, Schomburg L TITLE Comparison of different selenocompounds with respect to nutritional value vs. toxicity using liver cells in culture. JOURNAL J Nutr Biochem 22:945-55 (2011) DOI:10.1016/j.jnutbio.2010.08.006 REFERENCE PMID:19051051 AUTHORS McKenzie MJ, Hunter DA, Pathirana R, Watson LM, Joyce NI, Matich AJ, Rowan DD, Brummell DA TITLE Accumulation of an organic anticancer selenium compound in a transgenic Solanaceous species shows wider applicability of the selenocysteine methyltransferase transgene from selenium hyperaccumulators. JOURNAL Transgenic Res 18:407-24 (2009) DOI:10.1007/s11248-008-9233-0 REFERENCE PMID:20383543 AUTHORS Pinto JT, Lee JI, Sinha R, MacEwan ME, Cooper AJ TITLE Chemopreventive mechanisms of alpha-keto acid metabolites of naturally occurring organoselenium compounds. JOURNAL Amino Acids 41:29-41 (2011) DOI:10.1007/s00726-010-0578-3 REFERENCE PMID:17451884 AUTHORS Suzuki KT, Kurasaki K, Suzuki N TITLE Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide. JOURNAL Biochim Biophys Acta 1770:1053-61 (2007) DOI:10.1016/j.bbagen.2007.03.007 REFERENCE PMID:11782468 AUTHORS Gromer S, Gross JH TITLE Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium. JOURNAL J Biol Chem 277:9701-6 (2002) DOI:10.1074/jbc.M109234200 ///