Selenoamino acid metabolism (Homo sapiens)

From WikiPathways

Revision as of 09:16, 11 July 2016 by ReactomeTeam (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search
1713282858, 2093114, 18, 22313723, 26, 3456, 1013319, 243204, 7, 1621, 294, 7, 1611, 323325, 303336312, 3512, 27121, 2521, 29cytosol5S rRNA RPL18A Me3Se+RPS15A L-SerGSHRPS2 H2SeRPL35 RPL21 RPS27A(77-156) RPL26L1 RPS28 18S rRNA RPSA 2OBUTARPL35 CTH tetramer:PXLPH3PO4RPL7A RPL19 Sec RPL36A RPL24 H2SeO4MeSeHMTaminoacyl-tRNAsynthetasemultienzyme complexRPL27A GDP CTH tetramer:PXLPRPS6 SECISBP2NADP+L-AlaMAT1A multimersRPL31 RPL23 RPL37 tRNA(Sec)RPLP1 PXLP Hist PAPSS2 FAD RPL34 RPL34 RPL35 TXNRD1 RPL18 ATPRPL38 RPL35A RPS16 TXNRD1 RPL14 RPS3 RPS9 RPL10 ATPRPL29 RPS14 MeOHK+ RPS6 RPL29 RPS27 RPL10A 18S rRNA RARS NADPH5S rRNA RPS26 RPL12 RPL17 RPL27A ADPRPS2 Sep-tRNA(Sec)RPL12 RPL18 PPiRPL26 RPL10 RPS28 RPS25 RPS23 RPL38 PPiAIMP1(1-312) GTP RPL15 RPL23A H2ORPL40 RPL37A FAU NADP+RPL14 RPL4 RPL22 PXLP H2ORPL23 MARS RPL13 RPL3 H2ORPS21 RPS21 KARS RPL37 RPL27 RPL35A RPS5 RPL7A RPS29 RPL26L1 Sec-tRNA(Sec) RPL27 RPL21 GSSGRPL13A acceptorRPS12 RPL39 H2ODARS RPL7A NADP+RPL23 RPS27 FAU Gly RPL32 CTH RPS18 IARS TNXRD1:FAD dimerRPL32 GTP ADPPXLP RPS8 HNMT RPS3A H+RPL15 H2OH+RPL30 ATPRPL22 RPLP0 RPL11 RPLP2 SeCystaRPLP0 RPS19 PiNADP+AMPMNA PAPSeRRPS17 MeHist,N1MNA,MeGlyNADPHFAU RPL39 RPS3A AdoSeMetRPS18 RPL19 ATPAdoHcyRPL36 INMTRPL28 RPL13 SECISBP2 RPL37A MetTrans(1)EEFSEC 80S:Met-tRNAi:mRNA:SECISBP2:SecSARS L-SerRPS16 PAPSS1,2NNMT RPS9 RPL31 AdoHcyRPS3 Mg2+ RPS20 RPL3L FAD RPL24 RPS12 RPS27A(77-156) RPS4X RPS11 reduced acceptorGSSeHRPL37 H2OSCLY RPS24 ATPMet-tRNAi 5.8S rRNA 80S:Met-tRNAi:mRNARPL13A AdoHcyH+RPS13 RPS23 EEFSEC TNXRD1:FAD dimerRPS23 RPS21 PiRPL18A MAT1A SeHCysSeO3(2-)GSR-2:FAD dimerSecGSHRPS7 18S rRNA 80S:Met-tRNAi:mRNA:SECISBP2:Sec-tRNA(Sec):EEFSEC:GTP5.8S rRNA RPL24 RPL41 RPS8 RPL4 RPL9 pyruvic acidRPS3 Me2SeQARS RPLP1 RPS13 RPS29 GSSGRPL5 MeHist RPL9 PXLP PAPSS2 MeSebGalNacRPS4Y1 RPL41 RPS24 RPS25 RPL10 RPS24 RPL38 RPSA RPS4X AdoMetRPL41 RPS6 AIMP2 RPL11 Ser-tRNA(Sec)RPL10A RPL3 PXLP-CBS RPLP2 PAPSS1,2SeMetRPS27 RPL26 RPS15A RPL26 RPL36 SARS dimerRPS4X RPS27A(77-156) SCLY dimer:PXLPH3SePO3SARC FAD MSDMTXNRD1 PAPSS1 RPL13A 5.8S rRNA RPL30 RPS16 APSeRPS13 GSSeSGtRNA(Met)RPS14 RPL37A H2OEEFSEC:GTPRPS15 Ceruloplasmin mRNA RPL6 Sec-tRNA(Sec) H2ORPL36 RPL23A RPL7 RPL13 AHCY28S rRNA RPS2 RPS25 RPL32 RPL34 RPS19 Sec-tRNA(Sec):EEFSEC:GTPH2Oheme RPS17 RPL4 SEPSECStetramer:PXLPRPL6 RPS8 PAPSS1 NH3GSR-2 Ade-RibPSTK RPL8 AMPCTH GSHRPS9 NAM H2OEPRS RPS15A Sec-tRNA(Sec)RPS10 EEFSEC RPL14 RPS19 RPL29 RPL17 28S rRNA RPS26 TNXRD1:FAD dimerEEFSEC:GDPbGalNAc2OBUTARPS7 Met-tRNAi GNMT RPL18A RPS4Y1 RPS5 5S rRNA RPL39 RPS14 Met-tRNAi MeSecRPS12 AdoMetSEPSECS LARS H+RPS11 PAPSeRPL5 RPS15 Ceruloplasmin mRNA RPS20 RPL36A RPL27A RPS18 RPL7 AdoMetSeMet-tRNA(Met)RPS15 H+RPS5 RPL26L1 RPL12 RPL17 RPL40 RPL35A PPiRPL21 ATPRPL11 RPS10 RPL9 PAPMg2+ RPL8 RPS26 H2OH2ONADPHMeSeO2HRPS17 FAD RPL31 HSeMT28S rRNA RPL23A RPL10A GSHRPLP2 RPL36A RPL40 GSSebGalNacRPL28 CBS tetramerRPLP1 2-acetamidoglucalMeSeHRPS3A Hist,NAM,GlyRPL3 AdoHcyPPiNADPHRPL6 RPS29 H+RPL5 RPS10 RPL22 SECISBP2 RPSA RPL30 EEF1E1 RPS20 H2ONADPHRPL8 RPS7 RPL3L RPL28 Ceruloplasmin mRNA EEFSEC RPL15 RPL27 NADP+RPS11 RPS4Y1 AdeSeHCysbGalNAc derivativeMeSeOHRPLP0 RPL7 PSTK:Mg2+RPS28 RPL18 GTP NH3RPL19 RPL3L 15


Description

Selenium (Se) is a trace element essential for the normal function of the body. Selenoamino acids are defined as those amino acids where selenium has been substituted for sulphur. Selenium and sulphur share many chemical properties and so the substitution of normal amino acids with selenoamino acids has little effect on protein structure and function. Both inorganic (selenite, SeO3(2-); and selenate, SeO4(2-)) and organic (selenocysteine, Sec; and selenomethionine, SeMet) forms of selenium can be introduced in the diet where they are transformed into the intermediate selenide (Se(2-)) and then utilized for the de novo synthesis of Sec through a phosphorylated intermediate in a tRNA-dependent fashion. The final step of Sec formation is catalyzed by O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase (SEPSECS) that converts phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec).

All nutritional selenium is metabolised into selenide directly or through methylselenol (MeSeH). Sec liberated from selenoproteins is transformed to Se(2-) by selenocysteine lyase (SCLY). SeMet liberated from general proteins and from free SeMet sources is transformed into Se(2-) either through MeSeH by cystathionine gamma-lyase (CTH) followed by demethylation (SeMet to CH3SeH to H2Se), or through Sec by SCLY after the trans-selenation pathway (SeMet to Sec to H2Se). MeSec is hydrolysed into MeSeH by CTH. Methylseleninic acid (MeSeO2H) is reduced to methylselenol. MeSeH is demethylated to Se(2-) for further utilization for selenoprotein synthesis or oxidised to selenite (SeO3(2-)) for excretion in the form of selenosugar. Additionally, MeSeH is further methylated to dimethylselenide (Me2Se) and trimethylselenonium (Me3Se+) for excretion. View original pathway at:Reactome.

Comments

Reactome Converter 
Pathway is converted from Reactome id:

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Okuno T, Kubota T, Kuroda T, Ueno H, Nakamuro K.; ''Contribution of enzymic alpha, gamma-elimination reaction in detoxification pathway of selenomethionine in mouse liver.''; PubMed Europe PMC
  2. Bánszky L, Simonics T, Maráz A.; ''Sulphate metabolism of selenate-resistant Schizosaccharomyces pombe mutants.''; PubMed Europe PMC
  3. Kajander EO, Harvima RJ, Eloranta TO, Martikainen H, Kantola M, Kärenlampi SO, Akerman K.; ''Metabolism, cellular actions, and cytotoxicity of selenomethionine in cultured cells.''; PubMed Europe PMC
  4. Eustice DC, Kull FJ, Shrift A.; ''Selenium toxicity: aminoacylation and Peptide bond formation with selenomethionine.''; PubMed Europe PMC
  5. Chavatte L, Brown BA, Driscoll DM.; ''Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes.''; PubMed Europe PMC
  6. Fagegaltier D, Hubert N, Yamada K, Mizutani T, Carbon P, Krol A.; ''Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation.''; PubMed Europe PMC
  7. Daher R, Van Lente F.; ''Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations.''; PubMed Europe PMC
  8. Kobayashi Y, Ogra Y, Ishiwata K, Takayama H, Aimi N, Suzuki KT.; ''Selenosugars are key and urinary metabolites for selenium excretion within the required to low-toxic range.''; PubMed Europe PMC
  9. Venkatachalam KV, Akita H, Strott CA.; ''Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains.''; PubMed Europe PMC
  10. Heckl M, Busch K, Gross HJ.; ''Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure.''; PubMed Europe PMC
  11. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM.; ''Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization.''; PubMed Europe PMC
  12. Amberg R, Mizutani T, Wu XQ, Gross HJ.; ''Selenocysteine synthesis in mammalia: an identity switch from tRNA(Ser) to tRNA(Sec).''; PubMed Europe PMC
  13. Björnstedt M, Kumar S, Holmgren A.; ''Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase.''; PubMed Europe PMC
  14. Wolfe CL, Warrington JA, Davis S, Green S, Norcum MT.; ''Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII.''; PubMed Europe PMC
  15. Carlson BA, Xu XM, Kryukov GV, Rao M, Berry MJ, Gladyshev VN, Hatfield DL.; ''Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase.''; PubMed Europe PMC
  16. Okuno T, Motobayashi S, Ueno H, Nakamuro K.; ''Purification and characterization of mouse hepatic enzyme that converts selenomethionine to methylselenol by its alpha,gamma-elimination.''; PubMed Europe PMC
  17. Gromer S, Gross JH.; ''Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium.''; PubMed Europe PMC
  18. Yu M, Martin RL, Jain S, Chen LJ, Segel IH.; ''Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions.''; PubMed Europe PMC
  19. Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Söll D.; ''RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea.''; PubMed Europe PMC
  20. Suzuki KT, Somekawa L, Suzuki N.; ''Distribution and reuse of 76Se-selenosugar in selenium-deficient rats.''; PubMed Europe PMC
  21. Suzuki KT, Kurasaki K, Suzuki N.; ''Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide.''; PubMed Europe PMC
  22. Vincent C, Tarbouriech N, Härtlein M.; ''Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase.''; PubMed Europe PMC
  23. Hsieh HS, Ganther HE.; ''Biosynthesis of dimethyl selenide from sodium selenite in rat liver and kidney cell-free systems.''; PubMed Europe PMC
  24. Palioura S, Sherrer RL, Steitz TA, Söll D, Simonovic M.; ''The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation.''; PubMed Europe PMC
  25. Kajander EO, Harvima RJ, Kauppinen L, Akerman KK, Martikainen H, Pajula RL, Kärenlampi SO.; ''Effects of selenomethionine on cell growth and on S-adenosylmethionine metabolism in cultured malignant cells.''; PubMed Europe PMC
  26. Tamura T, Yamamoto S, Takahata M, Sakaguchi H, Tanaka H, Stadtman TC, Inagaki K.; ''Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation.''; PubMed Europe PMC
  27. Sun QA, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, Gladyshev VN.; ''Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases.''; PubMed Europe PMC
  28. Kajander EO, Raina AM.; ''Affinity-chromatographic purification of S-adenosyl-L-homocysteine hydrolase. Some properties of the enzyme from rat liver.''; PubMed Europe PMC
  29. Esaki N, Nakamura T, Tanaka H, Suzuki T, Morino Y, Soda K.; ''Enzymatic synthesis of selenocysteine in rat liver.''; PubMed Europe PMC
  30. Pinto JT, Lee JI, Sinha R, MacEwan ME, Cooper AJ.; ''Chemopreventive mechanisms of α-keto acid metabolites of naturally occurring organoselenium compounds.''; PubMed Europe PMC
  31. Kumar S, Björnstedt M, Holmgren A.; ''Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen.''; PubMed Europe PMC
  32. Mozier NM, McConnell KP, Hoffman JL.; ''S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism.''; PubMed Europe PMC
  33. Burnell JN.; ''Methionyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties.''; PubMed Europe PMC
  34. Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N.; ''Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.''; PubMed Europe PMC
  35. Tujebajeva RM, Copeland PR, Xu XM, Carlson BA, Harney JW, Driscoll DM, Hatfield DL, Berry MJ.; ''Decoding apparatus for eukaryotic selenocysteine insertion.''; PubMed Europe PMC
  36. Fairweather-Tait SJ, Bao Y, Broadley MR, Collings R, Ford D, Hesketh JE, Hurst R.; ''Selenium in human health and disease.''; PubMed Europe PMC
  37. Ohta Y, Suzuki KT.; ''Methylation and demethylation of intermediates selenide and methylselenol in the metabolism of selenium.''; PubMed Europe PMC
  38. Okuno T, Ueno H, Nakamuro K.; ''Cystathionine gamma-lyase contributes to selenomethionine detoxification and cytosolic glutathione peroxidase biosynthesis in mouse liver.''; PubMed Europe PMC

History

View all...
CompareRevisionActionTimeUserComment
101347view11:23, 1 November 2018ReactomeTeamreactome version 66
100885view20:57, 31 October 2018ReactomeTeamreactome version 65
100426view19:31, 31 October 2018ReactomeTeamreactome version 64
99976view16:15, 31 October 2018ReactomeTeamreactome version 63
99530view14:51, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99168view12:42, 31 October 2018ReactomeTeamreactome version 62
93759view13:34, 16 August 2017ReactomeTeamreactome version 61
93281view11:19, 9 August 2017ReactomeTeamreactome version 61
87653view08:55, 25 July 2016LindarieswijkOntology Term : 'selenoamino acid metabolic pathway' added !
86360view09:16, 11 July 2016ReactomeTeamNew pathway

External references

DataNodes

View all...