Record Information
Version2.0
Creation Date2012-05-31 13:58:24 -0600
Update Date2015-06-03 15:54:21 -0600
Secondary Accession Numbers
  • ECMDB03288
Identification
Name:Selenocysteine
Description:Selenocysteine 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,
Structure
Thumb
Synonyms:
  • (2R)-2-amino-3-selanylpropanoate
  • (2R)-2-amino-3-selanylpropanoic acid
  • 3-Seleno-alanine
  • 3-Selenoalanine
  • 3-Selenyl-L-Alanine
  • L-Selenocystein
  • L-Selenocysteine
  • L-Selenozystein
  • U
Chemical Formula:C3H7NO2Se
Weight:Average: 168.05
Monoisotopic: 168.964200301
InChI Key:ZKZBPNGNEQAJSX-REOHCLBHSA-N
InChI:InChI=1S/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
CAS number:3614-08-2
IUPAC Name:(2R)-2-amino-3-selanylpropanoic acid
Traditional IUPAC Name:L-selenocysteine
SMILES:N[C@@H](C[SeH])C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentL-alpha-amino acids
Alternative Parents
Substituents
  • L-alpha-amino acid
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Amine
  • Organic oxide
  • Hydrocarbon derivative
  • Organopnictogen compound
  • Selenol
  • Primary amine
  • Organoselenium compound
  • Organooxygen compound
  • Organonitrogen compound
  • Organic oxygen compound
  • Primary aliphatic amine
  • Organic nitrogen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility325 g/LALOGPS
logP-3.2ALOGPS
logP-4.1ChemAxon
logS0.29ALOGPS
pKa (Strongest Acidic)1.27ChemAxon
pKa (Strongest Basic)8.42ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity33.45 m³·mol⁻¹ChemAxon
Polarizability10.67 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:Not Available
KEGG Pathways:
EcoCyc Pathways:Not Available
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-00di-5900000000-827b47dc191649f521acView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-00di-5900000000-32e999fe6e3d67e322cbView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-01b9-0900000000-fadd5a69b2b225d034acView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-01b9-0900000000-8fe6412cebc1ca99fe59View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00dl-5900000000-2408222e037ff9db752aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014i-0900000000-91ba91d891f89ff1fc23View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00kk-6900000000-67c579b8ba30e155bcb3View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-00di-9200000000-0b58b77f13cec3df121dView in MoNA
References
References:
  • Blotcky AJ, Ebrahim A, Rack EP: Determination of selenium metabolites in biological fluids using instrumental and molecular neutron activation analysis. Anal Chem. 1988 Dec 15;60(24):2734-7. Pubmed: 3245598
  • Chu 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. Pubmed: 1339300
  • Kanehisa, 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. Pubmed: 22080510
  • Keseler, 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. Pubmed: 21097882
  • Mostert 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. Pubmed: 11733012
  • Rooseboom 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. Pubmed: 10900258
  • Sun QA, Su D, Novoselov SV, Carlson BA, Hatfield DL, Gladyshev VN: Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase. Biochemistry. 2005 Nov 8;44(44):14528-37. Pubmed: 16262253
  • Utomo A, Jiang X, Furuta S, Yun J, Levin DS, Wang YC, Desai KV, Green JE, Chen PL, Lee WH: Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells. J Biol Chem. 2004 Oct 15;279(42):43522-9. Epub 2004 Aug 4. Pubmed: 15294905
  • van 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. Pubmed: 17765195
  • Winder, 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. Pubmed: 18331064
  • Zimmermann MB, Kohrle J: The impact of iron and selenium deficiencies on iodine and thyroid metabolism: biochemistry and relevance to public health. Thyroid. 2002 Oct;12(10):867-78. Pubmed: 12487769
  • Zinoni, 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. Pubmed: 2941757
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID9093
HMDB IDHMDB03288
Pubchem Compound ID6326983
Kegg IDC05688
ChemSpider ID23436
WikipediaSelenocysteine
BioCyc IDL-SELENOCYSTEINE
EcoCyc IDL-SELENOCYSTEINE
Ligand ExpoCSE

Enzymes

General function:
Involved in pyridoxal phosphate binding
Specific function:
O(4)-succinyl-L-homoserine + L-cysteine = L- cystathionine + succinate
Gene Name:
metB
Uniprot ID:
P00935
Molecular weight:
41550
Reactions
O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.
General function:
Involved in cysteine biosynthetic process from serine
Specific function:
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate
Gene Name:
cysK
Uniprot ID:
P0ABK5
Molecular weight:
34489
Reactions
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate.
3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride.
General function:
Involved in cysteine biosynthetic process from serine
Specific function:
Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product
Gene Name:
cysM
Uniprot ID:
P16703
Molecular weight:
32664
Reactions
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate.
General function:
Involved in metabolic process
Specific function:
Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo
Gene Name:
sufS
Uniprot ID:
P77444
Molecular weight:
44433
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.

Transporters

General function:
Involved in nucleotide binding
Specific function:
Probably part of a binding-protein-dependent transport system yecCS for an amino acid. Probably responsible for energy coupling to the transport system
Gene Name:
yecC
Uniprot ID:
P37774
Molecular weight:
27677
General function:
Involved in transporter activity
Specific function:
Probably part of the binding-protein-dependent transport system yecCS for an amino acid; probably responsible for the translocation of the substrate across the membrane
Gene Name:
yecS
Uniprot ID:
P0AFT2
Molecular weight:
24801