2.02012-05-31 13:58:24 -06002015-06-03 15:54:21 -0600ECMDB03288M2MDB000488SelenocysteineSelenocysteine is considered to be the 21st proteinogenic amino acid. It exists naturally in all kingdoms of life as a building block of selenoproteins. Selenocysteine is a cysteine analogue with a selenium-containing selenol group in place of the sulfur-containing thiol group. Selenocysteine is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5' deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases,(2R)-2-amino-3-selanylpropanoate(2R)-2-amino-3-selanylpropanoic acid3-Seleno-alanine3-Selenoalanine3-Selenyl-L-AlanineL-SelenocysteinL-SelenocysteineL-SelenozysteinUC3H7NO2Se168.05168.964200301(2R)-2-amino-3-selanylpropanoic acidL-selenocysteine3614-08-2N[C@@H](C[SeH])C(O)=OInChI=1S/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1ZKZBPNGNEQAJSX-REOHCLBHSA-NSolidCytoplasmPeriplasmlogp-3.20logs0.29solubility3.25e+02 g/llogp-4.1pka_strongest_acidic1.27pka_strongest_basic8.4iupac(2R)-2-amino-3-selanylpropanoic acidaverage_mass168.05mono_mass168.964200301smilesN[C@@H](C[SeH])C(O)=OformulaC3H7NO2SeinchiInChI=1S/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1inchikeyZKZBPNGNEQAJSX-REOHCLBHSA-Npolar_surface_area63.32refractivity33.45polarizability10.67rotatable_bond_count2acceptor_count4donor_count3physiological_charge0formal_charge0Selenoamino acid metabolismec00450Specdb::CMs2681Specdb::CMs38562Specdb::CMs153066Specdb::NmrOneD135550Specdb::NmrOneD135551Specdb::NmrOneD135552Specdb::NmrOneD135553Specdb::NmrOneD135554Specdb::NmrOneD135555Specdb::NmrOneD135556Specdb::NmrOneD135557Specdb::NmrOneD135558Specdb::NmrOneD135559Specdb::NmrOneD135560Specdb::NmrOneD135561Specdb::NmrOneD135562Specdb::NmrOneD135563Specdb::NmrOneD135564Specdb::NmrOneD135565Specdb::NmrOneD135566Specdb::NmrOneD135567Specdb::NmrOneD135568Specdb::NmrOneD135569Specdb::MsMs29324Specdb::MsMs29325Specdb::MsMs29326Specdb::MsMs35882Specdb::MsMs35883Specdb::MsMs35884Specdb::MsMs2717892Specdb::MsMs2717893Specdb::MsMs2717894Specdb::MsMs2963673Specdb::MsMs2963674Specdb::MsMs2963675HMDB03288632698323436C056889093L-SELENOCYSTEINECSESelenocysteineZinoni, F., Birkmann, A., Stadtman, T. C., Bock, A. (1986). "Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli." Proc Natl Acad Sci U S A 83:4650-4654.2941757Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8.1339300Mostert V, Wolff S, Dreher I, Kohrle J, Abel J: Identification of an element within the promoter of human selenoprotein P responsive to transforming growth factor-beta. Eur J Biochem. 2001 Dec;268(23):6176-81.11733012Zimmermann MB, Kohrle J: The impact of iron and selenium deficiencies on iodine and thyroid metabolism: biochemistry and relevance to public health. 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Epub 2004 Aug 4.15294905Rooseboom M, Vermeulen NP, Andreadou I, Commandeur JN: Evaluation of the kinetics of beta-elimination reactions of selenocysteine Se-conjugates in human renal cytosol: possible implications for the use as kidney selective prodrugs. J Pharmacol Exp Ther. 2000 Aug;294(2):762-9.10900258Cystathionine gamma-synthaseP00935METB_ECOLImetBhttp://ecmdb.ca/proteins/P00935.xmlCysteine synthase AP0ABK5CYSK_ECOLIcysKhttp://ecmdb.ca/proteins/P0ABK5.xmlCysteine synthase BP16703CYSM_ECOLIcysMhttp://ecmdb.ca/proteins/P16703.xmlCysteine desulfurase_P77444SUFS_ECOLIsufShttp://ecmdb.ca/proteins/P77444.xmlUncharacterized amino-acid ABC transporter ATP-binding protein yecCP37774YECC_ECOLIyecChttp://ecmdb.ca/proteins/P37774.xmlInner membrane amino-acid ABC transporter permease protein yecSP0AFT2YECS_ECOLIyecShttp://ecmdb.ca/proteins/P0AFT2.xmlSelenocysteine + Reduced acceptor <> Hydrogen selenide + L-Alanine + AcceptorR03599O-Acetylserine + Hydrogen selenide <> Selenocysteine + Acetic acidR03601O-Phosphorylhomoserine + Selenocysteine <> Selenocystathionine + PhosphateR04944o-acetyl-l-homoserine + Selenocysteine <> Selenocystathionine + Acetic acidR04945O-Succinyl-L-homoserine + Selenocysteine <> Selenocystathionine + Succinic acidR04946a reduced electron acceptor + Selenocysteine <> L-Alanine + Selenium + an oxidized electron acceptor + Hydrogen ionSELENOCYSTEINE-LYASE-RXNSelenocysteine + reduced acceptor > Hydrogen selenide + L-Alanine + acceptor