KEGG   PATHWAY: ko00450
Entry
ko00450                     Pathway                                
Name
Selenocompound metabolism
Class
Metabolism; Metabolism of other amino acids
Pathway map
ko00450  Selenocompound metabolism
ko00450

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
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
  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
  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
  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
  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
  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
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