{"ymdb_id":"YMDB00204","created_at":"2011-05-29T16:06:39.000Z","updated_at":"2016-09-08T18:35:10.000Z","name":"L-Sorbose","cas":"87-79-6","state":"Solid","melting_point":"165 oC","description":"Sorbose is a six-carbon sugar (ketohexose). L-Sorbose is in fact more common than D-Sorbose in nature.","experimental_water_solubility":"360 mg/mL at 17 oC [YALKOWSKY,SH \u0026 DANNENFELSER,RM (1992)]","experimental_logp_hydrophobicity":"","location":"extracellular;cytoplasm","synthesis_reference":"Banjopnoppakun, Tanaphat; Moonmangmee, Somporn; Moonmangmee, Duangtip.  Production of L-sorbose by thermotolerant acetic acid bacteria.    Proceeding of the Kasetsart University Annual Conference, 44th, Bangkok, Thailand, Jan. 30-Feb. 2, 2006  (2006),    ","chebi_id":"17266","hmdb_id":"HMDB01266","kegg_id":"C00247","pubchem_id":"439192","cs_id":"23936183","foodb_id":null,"wikipedia_link":"Sorbose","biocyc_id":"SORBOSE","iupac":"(2R,3S,4R,5S)-2-(hydroxymethyl)oxane-2,3,4,5-tetrol","traditional_iupac":"α-L-sorbopyranose","logp":"-2.7579993179999995","pka":"12.643871080491373","alogps_solubility":"1.19e+03 g/l","alogps_logp":"-2.51","alogps_logs":"0.82","acceptor_count":"6","donor_count":"5","rotatable_bond_count":"1","polar_surface_area":"110.38000000000001","refractivity":"36.3608","polarizability":"16.051261078337298","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-3.450704169945884","pka_strongest_acidic":"10.291030669254257","bioavailability":"1","number_of_rings":"1","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["alpha-L-Sorbopyranose","hex-2-ulose","L-(-)-Sorbose","L-1,3,4,5,6-Pentahydroxyhexan-2-one","L-Sorbinose","L-Sorbose","L-xylo-2-Hexulose","l-xylo-hexulose","L(-)-Sorbose","Sorbin","Sorbinose","Sorbose","xylo-Hexulose"],"pathways":[{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"}],"growth_conditions":[],"references":[{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"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":"2011-05-26T18:00:48.000Z","updated_at":"2011-07-22T17:54:34.000Z","name":"Sorbitol dehydrogenase 1","uniprot_id":"P35497","uniprot_name":"DHSO1_YEAST","enzyme":true,"transporter":false,"gene_name":"SOR1","num_residues":357,"molecular_weight":"38165.39844","theoretical_pi":"6.94","general_function":"Involved in zinc ion binding","specific_function":"L-iditol + NAD(+) = L-sorbose + NADH","reactions":[{"id":1435,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1705,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2503,"direction":"\u003e","locations":"","altext":"L-iditol + NAD(+) = L-sorbose + NADH.","export":false,"pw_reaction_id":null,"source":null},{"id":3819,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006333","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AY693012","genbank_protein_id":"51013475","gene_card_id":"SOR1","chromosome_location":"chromosome 10","locus":"YJR159W","synonyms":["L-iditol 2-dehydrogenase 1"],"enzyme_classes":["1.1.1.14"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"},{"name":"Fructose Metabolism","kegg_map_id":null}],"gene_sequence":"ATGTCTCAAAATAGTAACCCTGCAGTAGTTCTAGAGAAAGTCGGCGATATTGCCATCGAGCAAAGACCAATCCCTACCATTAAGGACCCCCATTATGTCAAGTTAGCTATTAAAGCCACTGGTATCTGCGGCTCTGATATTCATTATTATAGAAGCGGTGGTATTGGTAAGTACATATTGAAGGCGCCAATGGTTTTAGGTCATGAATCAAGCGGACAGGTTGTGGAAGTTGGTGATGCCGTCACAAGGGTCAAAGTTGGTGACCGTGTTGCTATTGAACCTGGTGTTCCTAGCCGTTACTCTGATGAGACCAAAGAAGGGAGGTATAACCTTTGCCCACATATGGCATTTGCTGCAACTCCTCCAATTGATGGTACTCTTGTGAAGTACTATTTATCTCCAGAAGATTTCCTTGTGAAATTGCCAGAAGGCGTCAGTTATGAAGAGGGCGCTTGTGTCGAACCCTTATCAGTCGGTGTACACTCTAATAAATTGGCTGGGGTCCGCTTTGGTACCAAAGTTGTTGTATTTGGTGCAGGTCCTGTGGGGCTTTTAACTGGCGCAGTCGCCCGCGCTTTTGGTGCCACCGACGTCATTTTCGTCGATGTATTCGACAACAAGCTACAGAGAGCAAAAGATTTCGGAGCCACAAACACTTTCAATTCTTCCCAGTTTTCCACCGATAAAGCCCAAGACTTGGCCGATGGGGTCCAAAAGCTTTTGGGCGGAAATCACGCAGATGTGGTGTTTGAGTGTTCAGGTGCTGATGTTTGCATTGATGCCGCTGTCAAAACAACTAAGGTTGGAGGTACCATGGTGCAAGTCGGTATGGGTAAAAACTACACTAATTTTCCAATTGCTGAAGTTAGTGGAAAGGAAATGAAATTGATTGGATGTTTCCGTTATTCATTCGGTGATTATCGTGACGCTGTGAACTTGGTTGCCACAGGAAAAGTCAATGTCAAGCCATTGATAACCCACAAATTTAAATTTGAAGATGCAGCCAAGGCTTACGACTACAACATTGCCCATGGTGGAGAGGTAGTCAAGACTATTATCTTTGGTCCTGAATGA","protein_sequence":"MSQNSNPAVVLEKVGDIAIEQRPIPTIKDPHYVKLAIKATGICGSDIHYYRSGGIGKYILKAPMVLGHESSGQVVEVGDAVTRVKVGDRVAIEPGVPSRYSDETKEGRYNLCPHMAFAATPPIDGTLVKYYLSPEDFLVKLPEGVSYEEGACVEPLSVGVHSNKLAGVRFGTKVVVFGAGPVGLLTGAVARAFGATDVIFVDVFDNKLQRAKDFGATNTFNSSQFSTDKAQDLADGVQKLLGGNHADVVFECSGADVCIDAAVKTTKVGGTMVQVGMGKNYTNFPIAEVSGKEMKLIGCFRYSFGDYRDAVNLVATGKVNVKPLITHKFKFEDAAKAYDYNIAHGGEVVKTIIFGPE"},{"created_at":"2011-05-26T18:01:23.000Z","updated_at":"2011-05-27T15:01:03.000Z","name":"Sorbitol dehydrogenase 2","uniprot_id":"Q07786","uniprot_name":"DHSO2_YEAST","enzyme":true,"transporter":false,"gene_name":"SOR2","num_residues":357,"molecular_weight":"38096.30078","theoretical_pi":"6.71","general_function":"Involved in zinc ion binding","specific_function":"L-iditol + NAD(+) = L-sorbose + NADH","reactions":[{"id":2503,"direction":"\u003e","locations":"","altext":"L-iditol + NAD(+) = L-sorbose + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"Z74294","genbank_protein_id":"1431420","gene_card_id":"SOR2","chromosome_location":"chromosome 4","locus":"YDL246C","synonyms":["L-iditol 2-dehydrogenase 2"],"enzyme_classes":["1.1.1.14"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" metal ion binding"},{"category":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"}],"gene_sequence":"ATGTCTCAAAATAGTAACCCTGCAGTAGTTCTAGAGAAAGTCGGCGATATTGCCATCGAGCAAAGACCAATCCCTACCATTAAGGACCCCCATTATGTCAAGTTAGCTATTAAAGCCACTGGTATCTGCGGCTCTGATATTCATTATTATAGAAGCGGTGGTATTGGTAAGTACATATTGAAGGCGCCAATGGTTTTAGGTCATGAATCAAGCGGACAGGTTGTGGAAGTTGGTGATGCCGTCACAAGGGTCAAAGTTGGTGACCGTGTTGCTATTGAACCTGGTGTTCCTAGCCGTTACTCTGATGAGACCAAAGAAGGGAGCTATAACCTTTGCCCACATATGGCATTTGCTGCAACTCCTCCAATTGATGGTACTCTTGTGAAGTACTATTTATCTCCAGAAGATTTCCTTGTGAAATTGCCAGAAGGCGTCAGTTATGAAGAGGGCGCTTGTGTCGAACCCTTATCAGTCGGTGTACACTCTAATAAATTGGCTGGGGTCCGCTTTGGTACCAAAGTTGTTGTATTTGGTGCAGGTCCTGTGGGGCTTTTAACTGGCGCAGTCGCCCGCGCTTTTGGTGCCACCGACGTCATTTTCGTCGATGTATTCGACAACAAGCTACAGAGAGCAAAAGATTTCGGAGCCACAAACACTTTCAATTCTTCCCAGTTTTCCACCGATAAAGCCCAAGACTTGGCCGATGGGGTCCAAAAGCTTTTGGGCGGAAATCACGCAGATGTGGTGTTTGAGTGTTCAGGTGCTGATGTTTGCATTGATGCCGCTGTCAAAACAACTAAGGTTGGAGGTACCATGGTGCAAGTCGGTATGGGTAAAAACTACACTAATTTTCCAATTGCTGAAGTTAGTGGAAAGGAAATGAAATTGATTGGATGTTTCCGTTATTCATTCGGTGATTATCGTGACGCTGTGAACTTGGTTGCCACAGGAAAAGTCAATGTCAAGCCATTGATAACCCACAAATTTAAATTTGAAGATGCAGCCAAGGCTTACGACTACAACATTGCCCATGGTGGAGAGGTAGTCAAGACTATTATCTTTGGTCCTGAATGA","protein_sequence":"MSQNSNPAVVLEKVGDIAIEQRPIPTIKDPHYVKLAIKATGICGSDIHYYRSGGIGKYILKAPMVLGHESSGQVVEVGDAVTRVKVGDRVAIEPGVPSRYSDETKEGSYNLCPHMAFAATPPIDGTLVKYYLSPEDFLVKLPEGVSYEEGACVEPLSVGVHSNKLAGVRFGTKVVVFGAGPVGLLTGAVARAFGATDVIFVDVFDNKLQRAKDFGATNTFNSSQFSTDKAQDLADGVQKLLGGNHADVVFECSGADVCIDAAVKTTKVGGTMVQVGMGKNYTNFPIAEVSGKEMKLIGCFRYSFGDYRDAVNLVATGKVNVKPLITHKFKFEDAAKAYDYNIAHGGEVVKTIIFGPE"}]}