{"ymdb_id":"YMDB00656","created_at":"2011-05-29T18:40:51.000Z","updated_at":"2016-09-08T18:35:44.000Z","name":"D-glucitol","cas":"50-70-4","state":"Liquid","melting_point":"11 oC","description":"Sorbitol (glucitol) is a six-carbon sugar alcohol found in apples, pears, peaches, and prunes. It is synthesized by sorbitol-6-phosphate dehydrogenase, and converted to fructose by succinate dehydrogenase and sorbitol dehydrogenase. Succinate dehydrogenase is an enzyme complex that participates in the citric acid cycle.","experimental_water_solubility":"2750 mg/mL at 30 oC [MULLIN,JW (1972)]","experimental_logp_hydrophobicity":"-2.20 [SANGSTER (1994)]","location":"extracellular;cytoplasm","synthesis_reference":"Liu, Haichao; Luo, Chen.  Method for manufacturing sorbitol and mannitol with cellulose.    Faming Zhuanli Shenqing Gongkai Shuomingshu  (2007),     8pp.","chebi_id":"17924","hmdb_id":"HMDB00247","kegg_id":"C00794","pubchem_id":"5780","cs_id":"24533858","foodb_id":null,"wikipedia_link":"Sorbitol","biocyc_id":"SORBITOL","iupac":"(2R,3R,4R,5S)-hexane-1,2,3,4,5,6-hexol","traditional_iupac":"D-sorbitol","logp":"-3.7300188486666666","pka":"13.37874915684328","alogps_solubility":"2.29e+02 g/l","alogps_logp":"-2.68","alogps_logs":"0.10","acceptor_count":"6","donor_count":"6","rotatable_bond_count":"5","polar_surface_area":"121.38000000000001","refractivity":"38.4036","polarizability":"17.12411136029489","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-2.974211614825128","pka_strongest_acidic":"12.585200956788803","bioavailability":"1","number_of_rings":"0","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["(-)-Sorbitol","(2R,3R,4R,5S)-hexane-1,2,3,4,5,6-hexol","1,2,3,4,5,6-Hexanehexol","Cholaxine","clucitol","Cystosol","D-(-)-Sorbitol","D-1,2,3,4,5,6-hexanehexol","d-Galactitol","D-Glucitol","d-sorbit","d-Sorbite","D-Sorbitol","D-Sorbol","Diakarmon","Esasorb","Glucarine","glucitol","Glucitol, D-","gulitol","Hexahydric alcohol","Hexitol","Karion","l-gulitol","Multitol","Nivitin","Orbit","Probilagol","Resulax","Sionit","Sionit K","Sionite","Sionon","Siosan","Sorban","Sorbelite C","Sorbicolan","Sorbilande","Sorbilax","sorbite","Sorbitol","Sorbitur","Sorbo","Sorbol","Sorbostryl","Sorbostyl","Sorvilande"],"pathways":[{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"},{"name":"Galactose metabolism","kegg_map_id":"00052"},{"name":"Fructose Metabolism","kegg_map_id":null}],"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."},{"pubmed_id":8125328,"citation":"Sarthy, A. V., Schopp, C., Idler, K. B. (1994). \"Cloning and sequence determination of the gene encoding sorbitol dehydrogenase from Saccharomyces cerevisiae.\" Gene 140:121-126."}],"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":" 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":"Function","description":" metal ion 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":"2011-05-27T01:58:22.000Z","updated_at":"2011-07-22T17:54:34.000Z","name":"NADPH-dependent aldose reductase GRE3","uniprot_id":"P38715","uniprot_name":"GRE3_YEAST","enzyme":true,"transporter":false,"gene_name":"GRE3","num_residues":327,"molecular_weight":"37118.5","theoretical_pi":"7.09","general_function":"Involved in oxidoreductase activity","specific_function":"Reduces the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde similar to GRE2. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction","reactions":[{"id":1292,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1325,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1436,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1702,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2051,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2650,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"Alditol + NAD(P)(+) = aldose + NAD(P)H.","export":false,"pw_reaction_id":null,"source":null},{"id":2651,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"(R)-lactaldehyde + NADP(+) = methylglyoxal + NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":14078,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006505","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U00059","genbank_protein_id":"529125","gene_card_id":"GRE3","chromosome_location":"chromosome 8","locus":"YHR104W","synonyms":["Genes de respuesta a estres protein 3","NADPH-dependent aldo-keto reductase GRE3","NADPH-dependent methylglyoxal reductase GRE3","Xylose reductase"],"enzyme_classes":["1.1.1.21","1.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"Aldo_ket_red","identifier":"PF00248"}],"pathways":[{"name":"Pentose and glucuronate interconversions","kegg_map_id":"00040"},{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"},{"name":"Galactose metabolism","kegg_map_id":"00052"},{"name":"Glycerolipid metabolism","kegg_map_id":"00561"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"xylitol degradation","kegg_map_id":null}],"gene_sequence":"ATGTCTTCACTGGTTACTCTTAATAACGGTCTGAAAATGCCCCTAGTCGGCTTAGGGTGCTGGAAAATTGACAAAAAAGTCTGTGCGAATCAAATTTATGAAGCTATCAAATTAGGCTACCGTTTATTCGATGGTGCTTGCGACTACGGCAACGAAAAGGAAGTTGGTGAAGGTATCAGGAAAGCCATCTCCGAAGGTCTTGTTTCTAGAAAGGATATATTTGTTGTTTCAAAGTTATGGAACAATTTTCACCATCCTGATCATGTAAAATTAGCTTTAAAGAAGACCTTAAGCGATATGGGACTTGATTATTTAGACCTGTATTATATTCACTTCCCAATCGCCTTCAAATATGTTCCATTTGAAGAGAAATACCCTCCAGGATTCTATACGGGCGCAGATGACGAGAAGAAAGGTCACATCACCGAAGCACATGTACCAATCATAGATACGTACCGGGCTCTGGAAGAATGTGTTGATGAAGGCTTGATTAAGTCTATTGGTGTTTCCAACTTTCAGGGAAGCTTGATTCAAGATTTATTACGTGGTTGTAGAATCAAGCCCGTGGCTTTGCAAATTGAACACCATCCTTATTTGACTCAAGAACACCTAGTTGAGTTTTGTAAATTACACGATATCCAAGTAGTTGCTTACTCCTCCTTCGGTCCTCAATCATTCATTGAGATGGACTTACAGTTGGCAAAAACCACGCCAACTCTGTTCGAGAATGATGTAATCAAGAAGGTCTCACAAAACCATCCAGGCAGTACCACTTCCCAAGTATTGCTTAGATGGGCAACTCAGAGAGGCATTGCCGTCATTCCAAAATCTTCCAAGAAGGAAAGGTTACTTGGCAACCTAGAAATCGAAAAAAAGTTCACTTTAACGGAGCAAGAATTGAAGGATATTTCTGCACTAAATGCCAACATCAGATTTAATGATCCATGGACCTGGTTGGATGGTAAATTCCCCACTTTTGCCTGA","protein_sequence":"MSSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA"}]}