{"ymdb_id":"YMDB00861","created_at":"2011-05-29T18:59:05.000Z","updated_at":"2016-09-08T18:35:59.000Z","name":"Cystine","cas":"56-89-3","state":"Solid","melting_point":"260.5 oC","description":"Cystine is an oxidized dimeric form of the amino acid cysteine. It is formed by linking two cysteine residues via a disulfide bond (cys-S-S-cys) between the -SH groups. Through formation of disulfide bonds within and between protein molecules, cystine is a significant determinant of the tertiary structure of most proteins. Disulfide bonding, along with hydrogen bonding and hydrophobic interactions is partially responsible for the formation of the gluten matrix in bread.","experimental_water_solubility":"0.19 mg/mL at 20 oC [YALKOWSKY,SH \u0026 DANNENFELSER,RM (1992)]","experimental_logp_hydrophobicity":"-5.08 [CHMELIK,J ET AL. (1991)]","location":null,"synthesis_reference":"Grossi, Loris; Montevecchi, Pier Carlo. S-Nitrosocysteine and Cystine from Reaction of Cysteine with Nitrous Acid. A Kinetic Investigation. Journal of Organic Chemistry  (2002),  67(24),  8625-8630.","chebi_id":"17376","hmdb_id":"HMDB00192","kegg_id":"C00491","pubchem_id":"67678","cs_id":"575","foodb_id":null,"wikipedia_link":"Cystine","biocyc_id":"CYSTINE","iupac":"(2R)-2-amino-3-{[(2R)-2-amino-2-carboxyethyl]disulfanyl}propanoic acid","traditional_iupac":"L-cystine","logp":"-5.897687960059564","pka":"2.267408279723485","alogps_solubility":"1.68e+01 g/l","alogps_logp":"-3.16","alogps_logs":"-1.16","acceptor_count":"6","donor_count":"4","rotatable_bond_count":"7","polar_surface_area":"126.64000000000001","refractivity":"54.87179999999999","polarizability":"22.772305661239265","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"9.342140596747571","pka_strongest_acidic":"1.5564231091903382","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["(-)-Cystine","(R-(R*,R*))-3,3'-Dithiobis","[R-(R*,R*)]-3,3'-Dithiobis","2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoate","2-Amino-3-[(2-amino-2-carboxyethyl)dithio]propanoate","2-Amino-3-[(2-amino-2-carboxyethyl)dithio]propanoic acid","3, 3'-Dithiobis(2-aminopropanoic acid)","3,3'-Dithiobis","3,3'-dithiobis-L-Alanine","3,3'-Dithiobis(2-aminopropanoic acid)","3,3'-Dithiobis(2-aminopropionic acid)","3,3'-dithiobis[2-amino-[R-(R*,R*)]-Propanoate","3,3'-dithiobis[2-amino-[R-(R*,R*)]-Propanoic acid","3,3'-Dithiodialanine","Alanine, 3, 3'-dithiobis-","Alanine, 3,3'-dithiobis-","Alanine, 3,3'-dithiodi-","alpha-Diamino-beta-dithiolactic acid","b,b'-Diamino-b,b'-dicarboxydiethyl disulfide","b,b'-Dithiodialanine","beta,beta'-Diamino-beta,beta'-dicarboxydiethyl disulfide","beta,beta'-Dithiobisalanine","beta,beta'-Dithiodialanine","Bis(b-amino-b-carboxyethyl) disulfide","Bis(b-amino-beta-carboxyethyl) disulfide","Bis(beta-amino-beta-carboxyethyl) disulfide","cistina","Cysteine disulfide","Cystin","Cystine","Cystine acid","Cystine, L-","D(+)-3,3'-Dithiobis(2-aminopropanoate","D(+)-3,3'-Dithiobis(2-aminopropanoic acid","Dicysteine","Gelucystine","Gelucystine (L form)","L-(-)-Cystine","L-3,3'-dithiodialanine","l-alpha-diamino-beta-dithiolactic acid","L-Cysteine disulfide","L-Cystin","L-Cystine","l-dicysteine","Nephrin","Oxidized L-cysteine","Propanoic acid, 3, {3'-dithiobis[2-amino-,} {[R-(R*,R*)]-}","Propanoic acid, 3,3'-dithiobis(2-amino-, (R-(R*,R*))-","Zystin"],"pathways":[{"name":"Cysteine and methionine metabolism","kegg_map_id":"00270"}],"growth_conditions":[],"references":[{"pubmed_id":21062828,"citation":"Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). \"BRENDA, the enzyme information system in 2011.\" Nucleic Acids Res 39:D670-D676."},{"pubmed_id":13174550,"citation":"ROMANO, A. H., NICKERSON, W. J. (1954). \"Cystine reductase of pea seeds and yeasts.\" J Biol Chem 208:409-416."},{"pubmed_id":5646485,"citation":"Nagai, S., Black, S. (1968). \"A thiol-disulfide transhydrogenase from yeast.\" J Biol Chem 243:1942-1947."}],"proteins":[]}