{"ymdb_id":"YMDB00886","created_at":"2011-05-29T19:01:23.000Z","updated_at":"2016-09-08T18:36:01.000Z","name":"L-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":"vacuole;cytoplasm","synthesis_reference":null,"chebi_id":"16283","hmdb_id":"HMDB00192","kegg_id":"C00491","pubchem_id":"67678","cs_id":"60997","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-carboxy-ethyl)disulfanyl-propanoic acid","2-Amino-3-[(2-amino-2-carboxyethyl)dithio]propanoate","2-Amino-3-[(2-amino-2-carboxyethyl)dithio]propanoic acid","3,3'-Dithiobis","3,3'-dithiobis-L-Alanine","3,3'-dithiobis[2-amino-[R-(R*,R*)]-Propanoate","3,3'-dithiobis[2-amino-[R-(R*,R*)]-Propanoic acid","3,3'-Dithiodialanine","b,b'-Diamino-b,b'-dicarboxydiethyl disulfide","b,b'-Dithiodialanine","beta,beta'-Dithiobisalanine","beta,beta'-Dithiodialanine","Bis(b-amino-b-carboxyethyl) disulfide","Bis(b-amino-beta-carboxyethyl) disulfide","Cysteine disulfide","Cystin","Cystine","Cystine acid","D(+)-3,3'-Dithiobis(2-aminopropanoate","D(+)-3,3'-Dithiobis(2-aminopropanoic acid","Dicysteine","Gelucystine","L-(-)-Cystine","L-Cysteine disulfide","L-Cystin","l-Cystine","Oxidized L-cysteine"],"pathways":[{"name":"Cysteine and methionine metabolism","kegg_map_id":"00270"}],"growth_conditions":[],"references":[{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."}],"proteins":[{"created_at":"2011-05-27T08:03:07.000Z","updated_at":"2011-05-27T15:01:29.000Z","name":"Cystine transporter","uniprot_id":"P17261","uniprot_name":"ERS1_YEAST","enzyme":false,"transporter":true,"gene_name":"ERS1","num_residues":260,"molecular_weight":"30116.0","theoretical_pi":"8.87","general_function":"Involved in L-cystine transmembrane transporter activity","specific_function":"Transport cystine out of vacuoles/endodomes","reactions":[],"signal_regions":"None","transmembrane_regions":"7-28;40-62;81-102;118-138;151-175;185-205;227-247","pdb_id":null,"cellular_location":"Endosome membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein","genbank_gene_id":"X52468","genbank_protein_id":"3688","gene_card_id":"ERS1","chromosome_location":"chromosome 3","locus":"YCR075C","synonyms":["ERD suppressor","Transmembrane protein ERS1"],"enzyme_classes":[],"go_classes":[],"pfams":[],"pathways":[],"gene_sequence":"ATGGTGTCGTTAGACGATATACTAGGTATCGTGTATGTTACGTCATGGTCGATATCGATGTATCCACCGATAATCACCAATTGGCGCCATAAGTCAGCGAGCGCGATATCGATGGATTTTGTCATGTTAAATACGGCAGGTTACTCTTACCTGGTCATATCCATATTTTTGCAATTGTACTGCTGGAAAATGACGGGTGATGAGTCTGACTTGGGCAGGCCCAAGTTGACGCAATTTGATTTCTGGTATTGCCTGCATGGGTGCTTGATGAATGTTGTCTTATTGACCCAGGTGGTAGCTGGAGCGAGAATCTGGCGATTTCCAGGTAAAGGTCACCGCAAGATGAATCCATGGTACCTAAGGATTTTACTCGCATCACTGGCCATTTTTTCACTGCTAACCGTACAATTTATGTACTCCAACTACTGGTACGATTGGCATAACTCAAGAACTCTGGCGTATTGCAACAATTTGTTTTTACTCAAAATATCGATGTCACTAATCAAGTACATCCCACAAGTGACGCATAACTCGACAAGAAAATCTATGGATTGTTTCCCCATTCAGGGTGTGTTTCTAGATGTCACTGGCGGTATCGCCTCGCTGCTCCAATTGATTTGGCAGTTGTCTAACGATCAAGGTTTCAGTCTGGATACGTTCGTGACAAATTTTGGAAAAGTGGGACTGTCAATGGTAACTTTAATATTCAACTTCATCTTTATCATGCAGTGGTTTGTATATCGATCTCGAGGCCATGATCTGGCGTCAGAGTACCCGCTGTAG","protein_sequence":"MVSLDDILGIVYVTSWSISMYPPIITNWRHKSASAISMDFVMLNTAGYSYLVISIFLQLYCWKMTGDESDLGRPKLTQFDFWYCLHGCLMNVVLLTQVVAGARIWRFPGKGHRKMNPWYLRILLASLAIFSLLTVQFMYSNYWYDWHNSRTLAYCNNLFLLKISMSLIKYIPQVTHNSTRKSMDCFPIQGVFLDVTGGIASLLQLIWQLSNDQGFSLDTFVTNFGKVGLSMVTLIFNFIFIMQWFVYRSRGHDLASEYPL"}]}