{"ymdb_id":"YMDB00778","created_at":"2011-05-29T18:52:19.000Z","updated_at":"2016-09-08T18:35:53.000Z","name":"Xylitol","cas":"87-99-0","state":"Solid","melting_point":"93.5 oC","description":"Xylitol is a five-carbon sugar alcohol found in many fruits and vegetables. This achiral species is one of four isomers of 1,2,3,4,5-pentapentanol. Xylitol is roughly as sweet as sucrose with only two-thirds the food energy","experimental_water_solubility":"642 mg/mL [MERCK INDEX (1996)]","experimental_logp_hydrophobicity":null,"location":"Cytoplasm, Extracellular","synthesis_reference":"Hasumi, Fumihiko; Teshima, Chitoku; Okura, Ichiro.  Synthesis of xylitol by reduction of xylulose with the combination of hydrogenase and xylulose reductase.    Chemistry Letters  (1996),   (8),  597-598. ","chebi_id":"17151","hmdb_id":"HMDB02917","kegg_id":"C00379","pubchem_id":"6912","cs_id":null,"foodb_id":null,"wikipedia_link":"Xylitol","biocyc_id":"CPD-496","iupac":"(2R,4S)-pentane-1,2,3,4,5-pentol","traditional_iupac":"(2R,4S)-pentane-1,2,3,4,5-pentol","logp":"-3.099683906666666","pka":"13.742189661908146","alogps_solubility":"6.64e+02 g/l","alogps_logp":"-2.53","alogps_logs":"0.64","acceptor_count":"5","donor_count":"5","rotatable_bond_count":"4","polar_surface_area":"101.15","refractivity":"32.4411","polarizability":"14.478298747170115","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-2.9742034412471314","pka_strongest_acidic":"12.760078510562963","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["(2R,3R,4S)-Pentane-1,2,3,4,5-pentaol","D-Xylitol","Eutrit","Fluorette","Klinit","Kylit","L-xylitol","meso-xylitol","Pentitol","Wood sugar alcohol","XLS","Xylit","Xylite","Xylitol","Xylitol C","Xyliton","xylo-Pentitol"],"pathways":[{"name":"Pentose and glucuronate interconversions","kegg_map_id":"00040"},{"name":"xylitol degradation","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":10486580,"citation":"Richard, P., Toivari, M. H., Penttila, M. (1999). \"Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a xylitol dehydrogenase.\" FEBS Lett 457:135-138."},{"pubmed_id":16348083,"citation":"Senac, T., Hahn-Hagerdal, B. (1990). \"Intermediary Metabolite Concentrations in Xylulose- and Glucose-Fermenting Saccharomyces cerevisiae Cells.\" Appl Environ Microbiol 56:120-126."},{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."}],"proteins":[{"created_at":"2011-05-27T01:37:20.000Z","updated_at":"2011-05-27T15:01:15.000Z","name":"D-xylulose reductase","uniprot_id":"Q07993","uniprot_name":"XYL2_YEAST","enzyme":true,"transporter":false,"gene_name":"XYL2","num_residues":356,"molecular_weight":"38600.10156","theoretical_pi":"6.06","general_function":"Involved in zinc ion binding","specific_function":"Xylitol + NAD(+) = D-xylulose + NADH","reactions":[{"id":2050,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2632,"direction":"\u003e","locations":null,"altext":"Xylitol + NAD(+) = D-xylulose + NADH.","export":false,"pw_reaction_id":null,"source":null},{"id":14077,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006504","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"Z73242","genbank_protein_id":"1360424","gene_card_id":"XYL2","chromosome_location":"chromosome 12","locus":"YLR070C","synonyms":["Xylitol dehydrogenase","XDH"],"enzyme_classes":["1.1.1.9"],"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":"Pentose and glucuronate interconversions","kegg_map_id":"00040"},{"name":"xylitol degradation","kegg_map_id":null}],"gene_sequence":"ATGACTGACTTAACTACACAAGAAGCTATTGTTCTAGAGCGACCTGGTAAAATCACCCTAACTAATGTCAGCATCCCAAAGATTTCAGATCCTAACGAAGTAATCATCCAGATCAAGGCGACAGGAATATGCGGGTCAGATATCCATTACTATACCCATGGAAGAATAGCCAATTACGTGGTAGAATCACCAATGGTGCTGGGACATGAATCATCAGGAATAGTGGCCCTCATAGGTGAGAACGTCAAGACACTTAAAGTAGGAGATAGGGTGGCACTTGAGCCCGGAATACCTGACAGGTTTTCACCGGAGATGAAAGAGGGCAGATACAACCTGGACCCCAATTTAAAATTTGCTGCGACACCTCCCTTTGATGGGACCTTGACAAAGTATTATAAGACCATGAAAGATTTCGTCTATAAACTTCCTGATGATGTGTCATTCGAGGAAGGAGCACTAATAGAGCCATTATCAGTGGCAATCCATGCTAATAAATTAGCAAAGATCAAGTTTGGAGCCCGTTGCGTCGTCTTTGGAGCTGGGCCCATAGGTTTGCTAGCCGGGAAAGTAGCCAGTGTCTTTGGTGCTGCAGATGTTGTTTTTGTAGATCTATTAGAAAACAAGCTGGAAACGGCTAGGCAGTTTGGTGCCACCCACATCGTCAACTCAGGTGATCTCCCACATGGCGTTACTGTAGATAGTGTTATAAAAAAAGCAATCGGCAAGAAAGGTGCTGACGTTGTGTTTGAATGTTCTGGTGCAGAGCCTTGCGTTCGAGCAGGCATCGAAGTCTGTAAGGCAGGTGGAACGATCGTTCAAGTTGGAATGGGACAAGAGGAAATACAATTTCCCATCTCGATCATTCCAACAAAAGAACTGACATTCCAAGGCTGTTTCCGATACTGTCAAGGTGATTATAGTGACTCCATCGAGCTAGTCTCTAGCAGAAAACTCTCGCTTAAACCATTCATTACACATCGCTATAGCTTTAAGGATGCTGTCGAGGCATTCGAAGAAACAAGCCACCACCCGTTAAATAATATCAAGACGATCATTGAGGGCCCGGAATGA","protein_sequence":"MTDLTTQEAIVLERPGKITLTNVSIPKISDPNEVIIQIKATGICGSDIHYYTHGRIANYVVESPMVLGHESSGIVALIGENVKTLKVGDRVALEPGIPDRFSPEMKEGRYNLDPNLKFAATPPFDGTLTKYYKTMKDFVYKLPDDVSFEEGALIEPLSVAIHANKLAKIKFGARCVVFGAGPIGLLAGKVASVFGAADVVFVDLLENKLETARQFGATHIVNSGDLPHGVTVDSVIKKAIGKKGADVVFECSGAEPCVRAGIEVCKAGGTIVQVGMGQEEIQFPISIIPTKELTFQGCFRYCQGDYSDSIELVSSRKLSLKPFITHRYSFKDAVEAFEETSHHPLNNIKTIIEGPE"},{"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"}]}