The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

cysteine     (2S)-2-amino-3-sulfanyl- propanoic acid

Synonyms: cisteina, Cisteinum, Cystein, Cysteinum, Thioserine, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Half cystine

  • Pure L-threonine dehydrogenase from Escherichia coli is a tetrameric protein (Mr = 148,000) with 6 half-cystine residues/subunit; its catalytic activity as isolated is stimulated 5-10-fold by added Mn2+ or Cd2+ [1].
  • Twenty-four mutants, each containing a single free cysteine substituted for an amino acid in the COX-2 membrane binding domain were expressed using the baculovirus system and purified, then conjugated with a nitroxide spin label and reconstituted into liposomes [2].
  • Characterization of the disulfide bonds and free cysteine residues of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein [3].
  • Both pertussis toxin and eukaryotic enzymes ADP-ribosylate cysteine residues in proteins and also, it has been suggested, free cysteine [4].
  • In Azotobacter vinelandii and Escherichia coli NifS or NifS-like proteins are involved in FeS protein assembly by mobilizing sulfur from free cysteine [5].
  • The patients treated with the cysteine-rich protein had a mean increase of 2.5% body weight, whereas casein-treated patients lost 2.6% (p = 0.049) [6].

Psychiatry related information on Half cystine

  • Patients with anorexia nervosa exhibited lower circulating concentrations of free cysteine (8.9+/-1.5 vs 12.0+/-1.4 micromol/l) and free and total glutathione (5.0+/-1.3 vs 7.1+/-1.2 and 11.2+/-3.8 vs 16.2+/-5.0 micromol/l, respectively) [7].

High impact information on Half cystine


Chemical compound and disease context of Half cystine


Biological context of Half cystine

  • Sequencing from the acid cleavage site of HLA-7 through the third half-cystine revealed consideralbe homology with amino acid sequences around a half-cystine in immunoglobulin variable regions [18].
  • Homology is especially apparent in the following: 1) the pattern of 14 half-cystine residues, 2) conservation of hydrophobic residues which have been shown to encircle the active site, and 3) conservation of Asp-99 and His-48 which have been implicated in the catalytic reaction itself [19].
  • This membrane protein contains 31 mol per cent hydrophobic amino acid residues, 6 half-cystine residues, and a single tryptophan residue as determined by amino acid analysis after mineral or organic acid hydrolysis [20].
  • In contrast, cells with the plasmid containing C1276A expressed trimers like those with unmutated plasmid, suggesting that half-cystine 1276 is not involved in formation of disulfide-bonded multimers [21].
  • This B2 chain contains 100 half-cystine residues, most of which are located in two cysteine-rich domains, and 11 N-X-S or N-X-T sequences which are potential sites of N-linked glycosylation [22].

Anatomical context of Half cystine

  • Its amino acid composition is similar to parsley carbonic anhydrase; both contain large numbers of half-cystine residues relative to erythrocyte carbonic anhydrases [23].
  • In conclusion, we suggest that in the presence of a free cysteine at the COOH terminus of the rHuAChE polypeptide, secretion of monomers is not effectuated, whereas in its absence, monomers are exported from the endoplasmic reticulum and are capable of traversing the entire secretory pathway [24].
  • COS-7 cells with the plasmid containing C1199A expressed primarily monomers, suggesting that half-cystine 1199 in the D3-domain is involved in forming mucin multimers [21].
  • The cytosol enzyme contains four half-cystine molecules per subunit, which is in contrast with two reported for the enzyme from pea seed [25].
  • The free cysteine-peptide was also able to induce lysis of the B-lymphoma target by the T-lymphocyte clone, but at a molar concentration 500 to 1000 times higher than that of the coupled peptide [26].

Associations of Half cystine with other chemical compounds

  • The fragment (designated Cp F5) contains 159 amino acid residues and has a molecular weight of 18,650; it lacks carbohydrate, is rich in histidine, and contains one free cysteine that may be part of a copper-binding site [27].
  • The binding domain of the low affinity nerve growth factor receptor (p75NGFR) is built from four "cysteine repeats," with almost identical patterns of half-cystine residues [28].
  • Two additional mutant vectors encoding serine instead of half-cystine at residues 13244 and 13246 in submaxillary mucin expressed both monomers and dimers of the disulfide-rich domain but no aggregates [29].
  • Cys111 is the invariable third half-cystine of the second complement control protein module of C2 [30].
  • Specifically, 2-[(5-fluoresceinyl)aminocarbonyl]ethyl methanethiosulfonate was conjugated to a free cysteine on loop C and to five substituted cysteines at strategic locations in the subunit sequence, and the backbone flexibility around each site of conjugation was measured with time-resolved fluorescence anisotropy [31].
  • NAC, best known for its ability to counter acetaminophen toxicity, is a safe, well-tolerated antidote for cysteine/GSH deficiency [32].
  • N-Ethylmaleimide blocked auto-cleavage induced by the addition of myo-inositol hexakisphosphate, suggesting that cysteine residues are essential for the processing of clostridial glucosylating toxins [33].
  • All data obtained from this combination of approaches support the conclusion that the initial site of radical formation is a Tyr, which then abstracts an electron from a cysteine residue to produce a cysteinyl radical [34].
  • The observation of the first reaction suggests that the condensation of cysteine sulfenic acid to give cysteine thiosulfinate ester can be competitive with the reaction of cysteine sulfenic acid with cysteine [35].
  • Using mass spectrometry and limited proteolysis, this upper band was identified as an oxidized subunit of SOD1; the sulfhydryl group (Cys-SH) of Cys(111) was selectively oxidized to cysteine sulfinic acid (Cys-SO(2)H) and to cysteine sulfonic acid (Cys-SO(3)H) [36].

Gene context of Half cystine

  • Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges [37].
  • We have engineered a disulfide-linked dimer of KIR2DL1 by introducing a free cysteine at the C-terminal stem region of the receptor [38].
  • Comparison of the aa and/or nucleotide (nt) sequences of EDN and other proteins possessing ribonucleolytic activity, namely bovine seminal RNase, human and rat pancreatic RNases, eosinophil cationic protein (ECP), and human angiogenin, shows extensive identity at half-cystine residues and at aa of active sites [39].
  • The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported [40].
  • The inhibition of binding IL5 to its receptor by the isothiazolone derivatives is abrogated by free-sulfhydryl-containing compounds such as dithiothreitol, indicating that the isothiazolones react with the sulfhydryl group of free cysteine residues in the hIL5R alpha [41].
  • Overall, the regulation of Cys-Tyr cofactor formation in CDO by ambient cysteine levels represents an unusual form of substrate-mediated feed-forward activation of enzyme activity with important physiological consequences [42].

Analytical, diagnostic and therapeutic context of Half cystine

  • Plasmids encoding the amino-terminal region of porcine submaxillary mucin were modified by site-specific mutagenesis to assess the roles of individual half-cystine residues in the assembly of disulfide-linked multimers of mucin [21].
  • Our sequence analysis of a 110-kDa plasmic vWF peptide also permitted identification of a major plasmin cleavage site 705 residues from the COOH terminus and a half-cystine residue (1360) involved in maintaining the multimeric structure of plasmin-degraded vWF.(ABSTRACT TRUNCATED AT 400 WORDS)[43]
  • Thiol titration revealed no free cysteine residues, implying that there are three disulphide groups, the positions of which remain to be determined [44].
  • Subsequently, a disulfide-linked dimer is observed on SDS-PAGE, and the free cysteine content is decreased by 2 per heterodimer [45].
  • Free cysteine is increased in plasma from hemodialysis patients [46].


  1. L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. Epperly, B.R., Dekker, E.E. J. Biol. Chem. (1991) [Pubmed]
  2. Topography of the prostaglandin endoperoxide h2 synthase-2 in membranes. Mirafzali, Z., Leipprandt, J.R., McCracken, J.L., Dewitt, D.L. J. Biol. Chem. (2006) [Pubmed]
  3. Characterization of the disulfide bonds and free cysteine residues of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Yen, T.Y., Pal, S., de la Maza, L.M. Biochemistry (2005) [Pubmed]
  4. Amino acid-specific ADP-ribosylation: structural characterization and chemical differentiation of ADP-ribose-cysteine adducts formed nonenzymatically and in a pertussis toxin-catalyzed reaction. McDonald, L.J., Wainschel, L.A., Oppenheimer, N.J., Moss, J. Biochemistry (1992) [Pubmed]
  5. Role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins. Jaschkowitz, K., Seidler, A. Biochemistry (2000) [Pubmed]
  6. Cysteine-rich protein reverses weight loss in lung cancer patients receiving chemotherapy or radiotherapy. Tozer, R.G., Tai, P., Falconer, W., Ducruet, T., Karabadjian, A., Bounous, G., Molson, J.H., Dröge, W. Antioxid. Redox Signal. (2008) [Pubmed]
  7. Decreased glutathione in patients with anorexia nervosa. Risk factor for toxic liver injury? Zenger, F., Russmann, S., Junker, E., Wüthrich, C., Bui, M.H., Lauterburg, B.H. European journal of clinical nutrition. (2004) [Pubmed]
  8. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Cabantous, S., Terwilliger, T.C., Waldo, G.S. Nat. Biotechnol. (2005) [Pubmed]
  9. Cytochrome c conformations resolved by the photon counting histogram: watching the alkaline transition with single-molecule sensitivity. Perroud, T.D., Bokoch, M.P., Zare, R.N. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  10. Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: analysis of the sulfhydryl alkylation of free cysteine residues by fast-atom bombardment mass spectrometry. Glocker, M.O., Arbogast, B., Milley, R., Cowgill, C., Deinzer, M.L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  11. Effects of site-directed mutagenesis at residues cysteine-31 and cysteine-184 on lecithin-cholesterol acyltransferase activity. Francone, O.L., Fielding, C.J. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  12. Amino acid sequence of porcine spleen cathepsin D. Shewale, J.G., Tang, J. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  13. Mechanism of irreversible inactivation of phosphomannose isomerases by silver ions and flamazine. Wells, T.N., Scully, P., Paravicini, G., Proudfoot, A.E., Payton, M.A. Biochemistry (1995) [Pubmed]
  14. The use of synthetic tRNAs as probes for examining nascent peptides on Escherichia coli ribosomes. Picking, W., Picking, W.D., Hardesty, B. Biochimie (1991) [Pubmed]
  15. Configuration of thiols dictates their ability to promote iron-induced reactive oxygen species generation. Yang, E.Y., Campbell, A., Bondy, S.C. Redox Rep. (2000) [Pubmed]
  16. Biochemical properties of human urinary megakaryocyte colony-stimulating factor and erythropoietin: the role of sulfhydryl groups and disulfide bonds. Shimizu, T., Miyake, T., Pilch, A.M., Mantel, C., Murphy, M.J. Exp. Cell Biol. (1986) [Pubmed]
  17. Use of biotinylated-cysteinyl-tRNA as a non-RI probe in protein synthesis. Ohtsuka, H., Yokogawa, T., Asahara, H., Nishikawa, K. Nucleic Acids Symp. Ser. (1997) [Pubmed]
  18. Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins. Terhorst, C., Robb, R., Jones, C., Strominger, J.L. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  19. The lysine-49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus. Relation of structure and function to other phospholipases A2. Maraganore, J.M., Heinrikson, R.L. J. Biol. Chem. (1986) [Pubmed]
  20. NADPH-cytochrome P-450 reductase. Circular dichroism and physical studies. Knapp, J.A., Dignam, J.D., Strobel, H.W. J. Biol. Chem. (1977) [Pubmed]
  21. Identification of the half-cystine residues in porcine submaxillary mucin critical for multimerization through the D-domains. Roles of the CGLCG motif in the D1- and D3-domains. Perez-Vilar, J., Hill, R.L. J. Biol. Chem. (1998) [Pubmed]
  22. Primary structure of the Drosophila laminin B2 chain and comparison with human, mouse, and Drosophila laminin B1 and B2 chains. Chi, H.C., Hui, C.F. J. Biol. Chem. (1989) [Pubmed]
  23. Carbonic anhydrase from spinach leaves. Isolation and some chemical properties. Kandel, M., Gornall, A.G., Cybulsky, D.L., Kandel, S.I. J. Biol. Chem. (1978) [Pubmed]
  24. Interrelations between assembly and secretion of recombinant human acetylcholinesterase. Kerem, A., Kronman, C., Bar-Nun, S., Shafferman, A., Velan, B. J. Biol. Chem. (1993) [Pubmed]
  25. The purification and properties of the glutamine synthetase from the cytosol of Soya-bean root nodules. McParland, R.H., Guevara, J.G., Becker, R.R., Evans, H.J. Biochem. J. (1976) [Pubmed]
  26. Peptide-antibody conjugates for tumour therapy: a MHC-class-II-restricted tetanus toxin peptide coupled to an anti-Ig light chain antibody can induce cytotoxic lysis of a human B-cell lymphoma by specific CD4 T cells. Yu, Z., Healy, F., Valmori, D., Escobar, P., Corradin, G., Mach, J.P. Int. J. Cancer (1994) [Pubmed]
  27. Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin. Kingston, I.B., Kingston, B.L., Putnam, F.W. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  28. Disulfide mutants of the binding domain of the rat low affinity nerve growth factor receptor (p75NGFR). Baldwin, A.N., Shooter, E.M. J. Biol. Chem. (1994) [Pubmed]
  29. The carboxyl-terminal 90 residues of porcine submaxillary mucin are sufficient for forming disulfide-bonded dimers. Perez-Vilar, J., Hill, R.L. J. Biol. Chem. (1998) [Pubmed]
  30. A novel type II complement C2 deficiency allele in an African-American family. Zhu, Z.B., Atkinson, T.P., Volanakis, J.E. J. Immunol. (1998) [Pubmed]
  31. Influence of Agonists and Antagonists on the Segmental Motion of Residues near the Agonist Binding Pocket of the Acetylcholine-binding Protein. Hibbs, R.E., Radic, Z., Taylor, P., Johnson, D.A. J. Biol. Chem. (2006) [Pubmed]
  32. N-Acetylcysteine--a safe antidote for cysteine/glutathione deficiency. Atkuri, K.R., Mantovani, J.J., Herzenberg, L.A., Herzenberg, L.A. Curr. Opin. Pharmacol (2007) [Pubmed]
  33. Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. Egerer, M., Giesemann, T., Jank, T., Satchell, K.J., Aktories, K. J. Biol. Chem. (2007) [Pubmed]
  34. Electron transfer between a tyrosyl radical and a cysteine residue in hemoproteins: spin trapping analysis. Bhattacharjee, S., Deterding, L.J., Jiang, J., Bonini, M.G., Tomer, K.B., Ramirez, D.C., Mason, R.P. J. Am. Chem. Soc. (2007) [Pubmed]
  35. Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid. Nagy, P., Ashby, M.T. J. Am. Chem. Soc. (2007) [Pubmed]
  36. Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase. Fujiwara, N., Nakano, M., Kato, S., Yoshihara, D., Ookawara, T., Eguchi, H., Taniguchi, N., Suzuki, K. J. Biol. Chem. (2007) [Pubmed]
  37. Arrangement of the disulphide bridges in human low-Mr kininogen. Kellermann, J., Thelen, C., Lottspeich, F., Henschen, A., Vogel, R., Müller-Esterl, W. Biochem. J. (1987) [Pubmed]
  38. A disulfide-linked natural killer cell receptor dimer has higher affinity for HLA-C than wild-type monomer. Fan, Q.R., Long, E.O., Wiley, D.C. Eur. J. Immunol. (2000) [Pubmed]
  39. Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases. Hamann, K.J., Barker, R.L., Loegering, D.A., Pease, L.R., Gleich, G.J. Gene (1989) [Pubmed]
  40. The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase. Thomsen, A.R., Sottrup-Jensen, L., Gleich, G.J., Oxvig, C. Arch. Biochem. Biophys. (2000) [Pubmed]
  41. Covalent modification of the interleukin-5 receptor by isothiazolones leads to inhibition of the binding of interleukin-5. Devos, R., Guisez, Y., Plaetinck, G., Cornelis, S., Tavernier, J., van der Heyden, J., Foley, L.H., Scheffler, J.E. Eur. J. Biochem. (1994) [Pubmed]
  42. Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity. Dominy, J.E., Hwang, J., Guo, S., Hirschberger, L.L., Zhang, S., Stipanuk, M.H. J. Biol. Chem. (2008) [Pubmed]
  43. Substructure of human von Willebrand factor. Proteolysis by V8 and characterization of two functional domains. Fretto, L.J., Fowler, W.E., McCaslin, D.R., Erickson, H.P., McKee, P.A. J. Biol. Chem. (1986) [Pubmed]
  44. Purification and characterization of recombinant human interleukin 4. Biological activities, receptor binding and the generation of monoclonal antibodies. Solari, R., Quint, D., Obray, H., McNamee, A., Bolton, E., Hissey, P., Champion, B., Zanders, E., Chaplin, A., Coomber, B. Biochem. J. (1989) [Pubmed]
  45. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Ralat, L.A., Manevich, Y., Fisher, A.B., Colman, R.F. Biochemistry (2006) [Pubmed]
  46. Free cysteine is increased in plasma from hemodialysis patients. Nakanishi, T., Hasuike, Y., Otaki, Y., Hama, Y., Nanami, M., Miyagawa, K., Moriguchi, R., Nishikage, H., Izumi, M., Takamitsu, Y. Kidney Int. (2003) [Pubmed]
WikiGenes - Universities