{"ymdb_id":"YMDB00847","created_at":"2011-05-29T18:57:56.000Z","updated_at":"2016-09-08T18:35:58.000Z","name":"D-Cystine","cas":"349-46-2","state":null,"melting_point":null,"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":"0.1 mg/mL at 25 oC [BEILSTEIN]","experimental_logp_hydrophobicity":null,"location":null,"synthesis_reference":null,"chebi_id":"35494","hmdb_id":null,"kegg_id":null,"pubchem_id":"6857538","cs_id":"5256874","foodb_id":null,"wikipedia_link":"Cystine","biocyc_id":null,"iupac":"(2S)-2-amino-3-{[(2S)-2-amino-2-carboxyethyl]disulfanyl}propanoic acid","traditional_iupac":"D-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":"22.42620638472798","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"9.34214059674757","pka_strongest_acidic":"1.55642310919034","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["(2S,2'S)-3,3'-dithiobis(2-aminopropanoic acid)","cystine D-form"],"pathways":[],"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":5847960,"citation":"Zenk, M. H., Schmitt, J. H. (1965). \"[Purification and properties of acetyl-CoA: D-amino acid-alpha-N-acetyltransferase from yeast].\" Biochem Z 342:54-65."}],"proteins":[{"created_at":"2011-05-26T23:37:41.000Z","updated_at":"2011-05-29T14:08:02.000Z","name":"N-acetyltransferase HPA3","uniprot_id":"P39979","uniprot_name":"HPA3_YEAST","enzyme":true,"transporter":false,"gene_name":"HPA3","num_residues":179,"molecular_weight":"20698.5","theoretical_pi":"7.84","general_function":"Involved in N-acetyltransferase activity","specific_function":"N-acetyltransferase whose physiological acetyl acceptor substrate is still unknown. In vitro, histone acetylation is very weak","reactions":[{"id":2617,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U18795","genbank_protein_id":"603252","gene_card_id":"HPA3","chromosome_location":"chromosome 5","locus":"YEL066W","synonyms":[],"enzyme_classes":["2.3.1.-","2.3.1.36"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring acyl groups"},{"category":"Function","description":" transferase activity, transferring acyl groups other than amino-acyl groups"},{"category":"Function","description":" acyltransferase activity"},{"category":"Function","description":" acetyltransferase activity"},{"category":"Function","description":" N-acetyltransferase activity"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"Acetyltransf_1","identifier":"PF00583"}],"pathways":[],"gene_sequence":"ATGAAAAAGACCCCAGACCCATCTCCACCTTTTGCAAGCACGAAGAACGTAGGCATGTCAAACGAAGAACCGGAAAAAATGGTTAACGATCGAATTGTGGTGAAGGCCATCGAGCCAAAAGATGAGGAAGCCTGGAACAAACTGTGGAAGGAGTATCAGGGTTTCCAAAAAACGGTTATGCCTCCGGAAGTAGCCACCACTACCTTCGCAAGGTTTATAGACCCTACGGTCAAACTATGGGGTGCTCTAGCCTTTGACACCGAGACCGGCGATGCAATTGGCTTTGCACACTACCTGAACCATTTGACGTCGTGGCATGTCGAAGAAGTTGTCTACATGAATGACTTATATGTCACTGAACGCGCAAGAGTCAAAGGCGTAGGTAGAAAGCTCATAGAATTTGTATACAGCCGTGCCGATGAGCTCGGTACGCCTGCAGTGTACTGGGTTACAGACCATTACAATCACCGCGCACAGTTGCTGTACACCAAAGTGGCTTACAAGACAGATAAGGTTCTTTACAAGAGAAACGGATACTGA","protein_sequence":"MKKTPDPSPPFASTKNVGMSNEEPEKMVNDRIVVKAIEPKDEEAWNKLWKEYQGFQKTVMPPEVATTTFARFIDPTVKLWGALAFDTETGDAIGFAHYLNHLTSWHVEEVVYMNDLYVTERARVKGVGRKLIEFVYSRADELGTPAVYWVTDHYNHRAQLLYTKVAYKTDKVLYKRNGY"}]}