{"ymdb_id":"YMDB00577","created_at":"2011-05-29T18:32:32.000Z","updated_at":"2016-09-08T18:35:38.000Z","name":"tryptophol","cas":"526-55-6","state":"Solid","melting_point":"59 oC","description":"Tryptophol is a degradation product of tryptophan. It induces sleep in humans and is also found in wine as a secondary product of alcoholic fermentation. [Biocyc PWY-3162]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"extracellular;mitochondrion;cytoplasm","synthesis_reference":"Snyder, H. R.; Pilgrim, Frederick J. Preparation of 3-indoleacetic acid; new synthesis of tryptophol. Journal of the American Chemical Society (1948), 70 3770-1.","chebi_id":"17890","hmdb_id":"HMDB03447","kegg_id":"C00955","pubchem_id":"10685","cs_id":"10235","foodb_id":null,"wikipedia_link":"Tryptophol","biocyc_id":"CPD-341","iupac":"2-(1H-indol-3-yl)ethan-1-ol","traditional_iupac":"tryptophol","logp":"1.5933192466666666","pka":"17.392512752772014","alogps_solubility":"1.61e+00 g/l","alogps_logp":"1.82","alogps_logs":"-2.00","acceptor_count":"1","donor_count":"2","rotatable_bond_count":"2","polar_surface_area":"36.019999999999996","refractivity":"48.71540000000002","polarizability":"17.87526502062822","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-2.4393148808629768","pka_strongest_acidic":"15.796075232386734","bioavailability":"1","number_of_rings":"2","rule_of_five":"1","ghose_filter":"1","veber_rule":"1","mddr_like_rule":"0","synonyms":["\u0026beta;-(3-Indole)ethanol","1H-Indole-3-ethanol","1H-indolyl-3-ethanol","2-(1H-Indol-3-yl)ethanol","2-(3-Indolyl)ethanol","2-(3-Indolylethanol","2-(indol-3-yl)ethanol","3-(\u0026beta;-Hydroxyethyl)indole","3-(2-Hydroxyethyl)indole","3-(b-Hydroxyethyl)indole","3-(beta-Hydroxyethyl)indole","3-Indoleethanol","3-Indolylethanol","b-(3-Indole)ethanol","beta-(3-Indole)ethanol","beta-Indol-3-ylethanol","dl-Tryptophanol","Ethanol, 2-indol-3-yl-","Ethanol, 3-indolyl-","IEA","Indole ethanol","Indole-3-ethanol","Indoleethanol","Tryptophol"],"pathways":[{"name":"Tryptophan metabolism","kegg_map_id":"00380"}],"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":12902239,"citation":"Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). \"Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae.\" Appl Environ Microbiol 69:4534-4541."},{"pubmed_id":12702265,"citation":"Leskovac, V., Trivic, S., Pericin, D. (2002). \"The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae.\" FEMS Yeast Res 2:481-494."},{"pubmed_id":12499363,"citation":"Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). \"The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae.\" J Biol Chem 278:8028-8034."}],"proteins":[{"created_at":"2011-05-24T20:23:50.000Z","updated_at":"2011-07-22T17:54:09.000Z","name":"Alcohol dehydrogenase 3, mitochondrial","uniprot_id":"P07246","uniprot_name":"ADH3_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH3","num_residues":375,"molecular_weight":"40369.19922","theoretical_pi":"8.62","general_function":"Involved in zinc ion binding","specific_function":"An alcohol + NAD(+) = an aldehyde or ketone + NADH","reactions":[{"id":1293,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion matrix","genbank_gene_id":"AY692988","genbank_protein_id":"51013427","gene_card_id":"ADH3","chromosome_location":"chromosome 13","locus":"YMR083W","synonyms":["Alcohol dehydrogenase III","YADH-3"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"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":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTTGAGAACGTCAACATTGTTCACCAGGCGTGTCCAACCAAGCCTATTTTCTAGAAACATTCTTAGATTGCAATCCACAGCTGCAATCCCTAAGACTCAAAAAGGTGTCATCTTTTATGAGAATAAGGGGAAGCTGCATTACAAAGATATCCCTGTCCCCGAGCCTAAGCCAAATGAAATTTTAATCAACGTTAAATATTCTGGTGTATGTCACACCGATTTACATGCTTGGCACGGCGATTGGCCATTACCTGTTAAACTACCATTAGTAGGTGGTCATGAAGGTGCTGGTGTAGTTGTCAAACTAGGTTCCAATGTCAAGGGCTGGAAAGTCGGTGATTTAGCAGGTATCAAATGGCTGAACGGTTCTTGTATGACATGCGAATTCTGTGAATCAGGTCATGAATCAAATTGTCCAGATGCTGATTTATCTGGTTACACTCATGATGGTTCTTTCCAACAATTTGCGACCGCTGATGCTATTCAAGCCGCCAAAATTCAACAGGGTACCGACTTGGCCGAAGTAGCCCCAATATTATGTGCTGGTGTTACTGTATATAAAGCACTAAAAGAGGCAGACTTGAAAGCTGGTGACTGGGTTGCCATCTCTGGTGCTGCAGGTGGCTTGGGTTCCTTGGCCGTTCAATATGCAACTGCGATGGGTTACAGAGTTCTAGGTATTGATGCAGGTGAGGAAAAGGAAAAACTTTTCAAGAAATTGGGGGGTGAAGTATTCATCGACTTTACTAAAACAAAGAATATGGTTTCTGACATTCAAGAAGCTACCAAAGGTGGCCCTCATGGTGTCATTAACGTTTCCGTTTCTGAAGCCGCTATTTCTCTATCTACGGAATATGTTAGACCATGTGGTACCGTCGTTTTGGTTGGTTTGCCCGCTAACGCCTACGTTAAATCAGAGGTATTCTCTCATGTGGTGAAGTCCATCAATATCAAGGGTTCTTATGTTGGTAACAGAGCTGATACGAGAGAAGCCTTAGACTTCTTTAGCAGAGGTTTGATCAAATCACCAATCAAAATTGTTGGATTATCTGAATTACCAAAGGTTTATGACTTGATGGAAAAGGGCAAGATTTTGGGTAGATACGTCGTCGATACTAGTAAATAA","protein_sequence":"MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLMEKGKILGRYVVDTSK"},{"created_at":"2011-05-24T20:25:28.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"S-(hydroxymethyl)glutathione dehydrogenase","uniprot_id":"P32771","uniprot_name":"FADH_YEAST","enzyme":true,"transporter":false,"gene_name":"SFA1","num_residues":386,"molecular_weight":"41041.69922","theoretical_pi":"6.76","general_function":"Involved in zinc ion binding","specific_function":"Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1545,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2317,"direction":"\u003e","locations":null,"altext":"S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.","export":false,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"X68020","genbank_protein_id":"288591","gene_card_id":"SFA1","chromosome_location":"chromosome 4","locus":"YDL168W","synonyms":["Alcohol dehydrogenase SFA","Glutathione-dependent formaldehyde dehydrogenase","FALDH","FDH","FLD","GSH-FDH"],"enzyme_classes":["1.1.1.284","1.1.1.1","1.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" zinc ion binding"},{"category":"Function","description":" oxidoreductase activity, acting on CH-OH group of donors"},{"category":"Function","description":" oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor"},{"category":"Function","description":" S-(hydroxymethyl)glutathione dehydrogenase activity"},{"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":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" small molecule metabolic process"},{"category":"Process","description":" alcohol metabolic process"},{"category":"Process","description":" monohydric alcohol metabolic process"},{"category":"Process","description":" ethanol metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" ethanol oxidation"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Methane metabolism","kegg_map_id":"00680"}],"gene_sequence":"ATGTCCGCCGCTACTGTTGGTAAACCTATTAAGTGCATTGCTGCTGTTGCGTATGATGCGAAGAAACCATTAAGTGTTGAAGAAATCACGGTAGACGCCCCAAAAGCGCACGAAGTACGTATCAAAATTGAATATACTGCTGTATGCCACACTGATGCGTACACTTTATCAGGCTCTGATCCAGAAGGACTTTTCCCTTGCGTTCTGGGCCACGAAGGAGCCGGTATCGTAGAATCTGTAGGCGATGATGTCATAACAGTTAAGCCTGGTGATCATGTTATTGCTTTGTACACTGCTGAGTGTGGCAAATGTAAGTTCTGTACTTCCGGTAAAACCAACTTATGTGGTGCTGTTAGAGCTACTCAAGGGAAAGGTGTAATGCCTGATGGGACCACAAGATTTCATAATGCGAAAGGTGAAGATATATACCATTTCATGGGTTGCTCTACTTTTTCCGAATATACTGTGGTGGCAGATGTCTCTGTGGTTGCCATCGATCCAAAAGCTCCCTTGGATGCTGCCTGTTTACTGGGTTGTGGTGTTACTACTGGTTTTGGGGCGGCTCTTAAGACAGCTAATGTGCAAAAAGGCGATACCGTTGCAGTATTTGGCTGCGGGACTGTAGGACTCTCCGTTATCCAAGGTGCAAAGTTAAGGGGCGCTTCCAAGATCATTGCCATTGACATTAACAATAAGAAAAAACAATATTGTTCTCAATTTGGTGCCACGGATTTTGTTAATCCCAAGGAAGATTTGGCCAAAGATCAAACTATCGTTGAAAAGTTAATTGAAATGACTGATGGGGGTCTGGATTTTACTTTTGACTGTACTGGTAATACCAAAATTATGAGAGATGCTTTGGAAGCCTGTCATAAAGGTTGGGGTCAATCTATTATCATTGGTGTGGCTGCCGCTGGTGAAGAAATTTCTACAAGGCCGTTCCAGCTGGTCACTGGTAGAGTGTGGAAAGGCTCTGCTTTTGGTGGCATCAAAGGTAGATCTGAAATGGGCGGTTTAATTAAAGACTATCAAAAAGGTGCCTTAAAAGTCGAAGAATTTATCACTCACAGGAGACCATTCAAAGAAATCAATCAAGCCTTTGAAGATTTGCATAACGGTGATTGCTTAAGAACCGTCTTGAAGTCTGATGAAATAAAATAG","protein_sequence":"MSAATVGKPIKCIAAVAYDAKKPLSVEEITVDAPKAHEVRIKIEYTAVCHTDAYTLSGSDPEGLFPCVLGHEGAGIVESVGDDVITVKPGDHVIALYTAECGKCKFCTSGKTNLCGAVRATQGKGVMPDGTTRFHNAKGEDIYHFMGCSTFSEYTVVADVSVVAIDPKAPLDAACLLGCGVTTGFGAALKTANVQKGDTVAVFGCGTVGLSVIQGAKLRGASKIIAIDINNKKKQYCSQFGATDFVNPKEDLAKDQTIVEKLIEMTDGGLDFTFDCTGNTKIMRDALEACHKGWGQSIIIGVAAAGEEISTRPFQLVTGRVWKGSAFGGIKGRSEMGGLIKDYQKGALKVEEFITHRRPFKEINQAFEDLHNGDCLRTVLKSDEIK"},{"created_at":"2011-05-24T20:29:06.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"Alcohol dehydrogenase 1","uniprot_id":"P00330","uniprot_name":"ADH1_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH1","num_residues":348,"molecular_weight":"36849.0","theoretical_pi":"6.67","general_function":"Involved in zinc ion binding","specific_function":"This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"M38456","genbank_protein_id":"171025","gene_card_id":"ADH1","chromosome_location":"chromosome 15","locus":"YOL086C","synonyms":["Alcohol dehydrogenase I","YADH-1"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"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":"Function","description":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" metabolic process"}],"pfams":[{"name":"ADH_N","identifier":"PF08240"},{"name":"ADH_zinc_N","identifier":"PF00107"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTCTATCCCAGAAACTCAAAAAGGTGTTATCTTCTACGAATCCCACGGTAAATTGGAACACAAGGATATTCCAGTTCCAAAGCCAAAGGCCAACGAATTGTTGATCAACGTTAAGTACTCTGGTGTCTGTCACACCGACTTGCACGCTTGGCACGGTGACTGGCCATTGCCAGTTAAGCTACCATTAGTCGGTGGTCACGAAGGTGCCGGTGTCGTTGTCGGCATGGGTGAAAACGTTAAGGGCTGGAAGATCGGTGACTACGCCGGTATCAAATGGTTGAACGGTTCTTGTATGGCCTGTGAATACTGTGAATTGGGTAACGAATCCAACTGTCCTCACGCTGACTTGTCTGGTTACACCCACGACGGTTCTTTCCAACAATACGCTACCGCTGACGCTGTTCAAGCCGCTCACATTCCTCAAGGTACCGACTTGGCCCAAGTCGCCCCCATCTTGTGTGCTGGTATCACCGTCTACAAGGCTTTGAAGTCTGCTAACTTGATGGCCGGTCATTGGGTTGCCATTTCCGGTGCTGCCGGTGGTCTAGGTTCTTTGGCTGTTCAATACGCCAAGGCTATGGGTTACAGAGTCTTGGGTATTGACGGTGGTGAAGGTAAGGAAGAATTATTCAGATCCATCGGTGGTGAAGTCTTCATTGACTTCACTAAGGAAAAGGACATTGTCGGTGCTGTTCTAAAGGCCACTGACGGTGGTGCTCACGGTGTCATCAACGTTTCCGTTTCCGAAGCCGCTATTGAAGCTTCTACCAGATACGTTAGAGCTAACGGTACCACCGTTTTGGTCGGTATGCCAGCTGGTGCCAAGTGTTGTTCTGATGTCTTCAACCAAGTCGTCAAGTCCATCTCTATTGTTGGTTCTTACGTCGGTAACAGAGCCGACACCAGAGAAGCTTTGGACTTCTTCGCCAGAGGTTTGGTCAAGTCTCCAATCAAGGTTGTCGGCTTGTCTACCTTGCCAGAAATTTACGAAAAGATGGAAAAGGGTCAAATCGTTGGTAGATACGTTGTTGACACTTCTAAATAA","protein_sequence":"MSIPETQKGVIFYESHGKLEYKDIPVPKPKANELLINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQQYATADAVQAAHIPQGTDLAQVAPILCAGITVYKALKSANLMAGHWVAISGAAGGLGSLAVQYAKAMGYRVLGIDGGEGKEELFRSIGGEVFIDFTKEKDIVGAVLKATDGGAHGVINVSVSEAAIEASTRYVRANGTTVLVGMPAGAKCCSDVFNQVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSTLPEIYEKMEKGQIVGRYVVDTSK"},{"created_at":"2011-05-24T20:30:23.000Z","updated_at":"2011-07-22T17:54:08.000Z","name":"Alcohol dehydrogenase 4","uniprot_id":"P10127","uniprot_name":"ADH4_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH4","num_residues":382,"molecular_weight":"41141.69922","theoretical_pi":"6.09","general_function":"Involved in oxidoreductase activity","specific_function":"Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all","reactions":[{"id":1291,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1294,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1296,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1303,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1305,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1308,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2314,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm;Mitochondrion","altext":"An alcohol + NAD(+) = an aldehyde or ketone + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion","genbank_gene_id":"X05992","genbank_protein_id":"3337","gene_card_id":"ADH4","chromosome_location":"chromosome 7","locus":"YGL256W","synonyms":["Alcohol dehydrogenase IV","ADHIV"],"enzyme_classes":["1.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"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":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"Fe-ADH","identifier":"PF00465"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Fatty acid metabolism","kegg_map_id":"00071"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Tyrosine 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dehydrogenase 5","uniprot_id":"P38113","uniprot_name":"ADH5_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH5","num_residues":351,"molecular_weight":"37647.89844","theoretical_pi":"6.34","general_function":"Involved in zinc ion binding","specific_function":"An alcohol + NAD(+) = an aldehyde or ketone + 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