{"ymdb_id":"YMDB00573","created_at":"2011-05-29T18:32:15.000Z","updated_at":"2016-09-08T18:35:38.000Z","name":"isobutanol","cas":"78-83-1","state":"Liquid","melting_point":"-108 oC","description":"Isobutanol is a colorless, flammable liquid with a characteristic smell. Its isomers include n-butanol, 2-butanol, and tert-butanol. Isobutanol is produced naturally during the fermentation of carbohydrates and may also be a byproduct of the decay process of organic matter. This alcohol tends to increase in content during wine aging. It is the final product of the catabolism of valine in S. cerevisiae.","experimental_water_solubility":"85 mg/mL at 25 oC [VALVANI,SC et al. (1981)]","experimental_logp_hydrophobicity":"0.76 [HANSCH,C ET AL. (1995)]","location":"extracellular;mitochondrion;cytoplasm","synthesis_reference":null,"chebi_id":"46645","hmdb_id":"HMDB06006","kegg_id":"C14710","pubchem_id":"6560","cs_id":"6312","foodb_id":null,"wikipedia_link":"Isobutanol","biocyc_id":"ISOBUTANOL","iupac":"2-methylpropan-1-ol","traditional_iupac":"isobutanol","logp":"0.7257261073333335","pka":null,"alogps_solubility":"1.40e+02 g/l","alogps_logp":"0.60","alogps_logs":"0.28","acceptor_count":"1","donor_count":"1","rotatable_bond_count":"1","polar_surface_area":"20.23","refractivity":"22.005499999999998","polarizability":"9.065725629445156","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-1.7809564328612169","pka_strongest_acidic":"17.32703147494006","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["1-Hydroxymethylpropane","1-Propanol, 2-methyl-","2-Methyl propanol","2-Methyl-1-propanol","2-methyl-1-propanyl alcohol","2-Methylpropan-1-ol","2-methylpropanoI","2-Methylpropanol","2-Methylpropanol-1","2-Methylpropyl alcohol","Alcohol","Alcool isobutylique","Butanol-iso","Fermentation butyl alcohol","I-butanol","I-butyl alcohol","IBA","Iso-butyl alcohol","iso-C4H9OH","isobutanol","Isobutanol or isobutyl alcohol","Isobutyl alcohol","Isobutylalkohol","Isopropyl carbitol","Isopropylcarbinol","Methyl-2 propanol-1","Propanol, 2-methyl-"],"pathways":[{"name":"Valine 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":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":17287358,"citation":"Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). \"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.\" Proc Natl Acad Sci U S A 104:2193-2198."},{"pubmed_id":10855721,"citation":"Fukuda, K., Kiyokawa, Y., Yanagiuchi, T., Wakai, Y., Kitamoto, K., Inoue, Y., Kimura, A. (2000). \"Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli.\" Appl Microbiol Biotechnol 53:596-600."},{"pubmed_id":12957907,"citation":"Verstrepen, K. J., Van Laere, S. D., Vanderhaegen, B. M., Derdelinckx, G., Dufour, J. P., Pretorius, I. S., Winderickx, J., Thevelein, J. M., Delvaux, F. R. (2003). \"Expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters.\" Appl Environ Microbiol 69:5228-5237."},{"pubmed_id":12423374,"citation":"Larroy, C., Pares, X., Biosca, J. A. (2002). \"Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family.\" Eur J Biochem 269:5738-5745."},{"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."},{"pubmed_id":11742541,"citation":"Larroy, C., Fernandez, M. R., Gonzalez, E., Pares, X., Biosca, J. A. (2002). \"Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction.\" Biochem J 361:163-172."},{"pubmed_id":9748245,"citation":"Dickinson, J. R., Harrison, S. J., Hewlins, M. J. (1998). \"An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae.\" J Biol Chem 273:25751-25756."},{"pubmed_id":12236692,"citation":"Patel, S., Shibamoto, T. (2002). \"Effect of different strains of Saccharomyces cerevisiae on production of volatiles in Napa Gamay wine and Petite Sirah wine.\" J Agric Food Chem 50:5649-5653."}],"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":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"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":" small molecule metabolic process"},{"category":"Process","description":" alcohol metabolic process"},{"category":"Process","description":" monohydric alcohol metabolic process"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" ethanol metabolic process"},{"category":"Process","description":" ethanol oxidation"},{"category":"Process","description":" oxidation reduction"}],"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":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"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 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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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oxidation reduction"}],"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 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process"}],"pfams":[{"name":"Lipase_GDSL","identifier":"PF00657"}],"pathways":[],"gene_sequence":"ATGGATTACGAGAAGTTTCTGTTATTTGGGGATTCCATTACTGAATTTGCTTTTAATACTAGGCCCATTGAAGATGGCAAAGATCAGTATGCTCTTGGAGCCGCATTAGTCAACGAATATACGAGAAAAATGGATATTCTTCAAAGAGGGTTCAAAGGGTACACTTCTAGATGGGCGTTGAAAATACTTCCTGAGATTTTAAAGCATGAATCCAATATTGTCATGGCCACAATATTTTTGGGTGCCAACGATGCATGCTCAGCAGGTCCCCAAAGTGTCCCCCTCCCCGAATTTATCGATAATATTCGTCAAATGGTATCTTTGATGAAGTCTTACCATATCCGTCCTATTATAATAGGACCGGGGCTAGTAGATAGAGAGAAGTGGGAAAAAGAAAAATCTGAAGAAATAGCTCTCGGATACTTCCGTACCAACGAGAACTTTGCCATTTATTCCGATGCCTTAGCAAAACTAGCCAATGAGGAAAAAGTTCCCTTCGTGGCTTTGAATAAGGCGTTTCAACAGGAAGGTGGTGATGCTTGGCAACAACTGCTAACAGATGGACTGCACTTTTCCGGAAAAGGGTACAAAATTTTTCATGACGAATTATTGAAGGTCATTGAGACATTCTACCCCCAATATCATCCCAAAAACATGCAGTACAAACTGAAAGATTGGAGAGATGTGCTAGATGATGGATCTAACATAATGTCTTGA","protein_sequence":"MDYEKFLLFGDSITEFAFNTRPIEDGKDQYALGAALVNEYTRKMDILQRGFKGYTSRWALKILPEILKHESNIVMATIFLGANDACSAGPQSVPLPEFIDNIRQMVSLMKSYHIRPIIIGPGLVDREKWEKEKSEEIALGYFRTNENFAIYSDALAKLANEEKVPFVALNKAFQQEGGDAWQQLLTDGLHFSGKGYKIFHDELLKVIETFYPQYHPKNMQYKLKDWRDVLDDGSNIMS"}]}