{"ymdb_id":"YMDB00482","created_at":"2011-05-29T18:22:24.000Z","updated_at":"2016-09-08T18:35:31.000Z","name":"isobutyraldehyde","cas":"78-84-2","state":"Liquid","melting_point":"-65.9 oC","description":"Isobutyraldehyde (2-methylpropanal) is an intermediate in valine degradation (Ehrlich pathway), and sphingolipid metabolism pathways. It is responsible for blue cheese aromas. [Biocyc PWY-5057 and SPHINGOLIPID-SYN-PWY]","experimental_water_solubility":"89 mg/mL at 25 oC [YALKOWSKY,SH \u0026 DANNENFELSER,RM (1992)]","experimental_logp_hydrophobicity":null,"location":"extracellular;mitochondrion;cytoplasm","synthesis_reference":null,"chebi_id":"48943","hmdb_id":null,"kegg_id":"C03219","pubchem_id":"6561","cs_id":"6313","foodb_id":null,"wikipedia_link":"Isobutyraldehyde","biocyc_id":null,"iupac":"2-methylpropanal","traditional_iupac":"isobutyraldehyde","logp":"0.8615601586666667","pka":null,"alogps_solubility":"5.37e+01 g/l","alogps_logp":"0.60","alogps_logs":"-0.13","acceptor_count":"1","donor_count":"0","rotatable_bond_count":"1","polar_surface_area":"17.07","refractivity":"20.919700000000002","polarizability":"8.241472886046427","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-7.008050141091526","pka_strongest_acidic":"17.84796973452829","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["\u0026alpha;-Methylpropionaldehyde","2-Methyl-1-propanal","2-Methylpropanal","2-Methylpropanal oxime","2-Methylpropionaldehyde","alpha-Methylpropionaldehyde","iso-C3H7CHO","Isobutaldehyde","Isobutanal","Isobutanal oxime","Isobutylaldehyde","Isobutyraldehyd","Isobutyraldehyde oxime","Isobutyric aldehyde","Isobutyryl aldehyde","Isopropylaldehyde","Isopropylformaldehyde","Methyl propanal","Propanal, 2-methyl-","Propionaldehyde, 2-methyl-","so-Butyl aldehyde","Valine aldehyde"],"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":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":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."}],"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":" 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":"Function","description":" zinc ion binding"},{"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":" 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"},{"category":"Process","description":" small molecule metabolic process"}],"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":"2011-05-24T20:26:42.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 2","uniprot_id":"P16467","uniprot_name":"PDC5_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC5","num_residues":563,"molecular_weight":"61911.60156","theoretical_pi":"6.4","general_function":"Involved in magnesium ion binding","specific_function":"Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm;Nucleus","altext":"A 2-oxo acid = an aldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2320,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2322,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Pyruvate = Acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2323,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2324,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"An aldehyde + an aldehyde = A 2-hydroxy ketone.","export":false,"pw_reaction_id":null,"source":null},{"id":14096,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006520","source":"Smpdb"},{"id":14097,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006525","source":"Smpdb"},{"id":14098,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006537","source":"Smpdb"},{"id":14099,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006557","source":"Smpdb"},{"id":14100,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006971","source":"Smpdb"},{"id":14101,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006979","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U53881","genbank_protein_id":"1256902","gene_card_id":"PDC5","chromosome_location":"chromosome 12","locus":"YLR134W","synonyms":[],"enzyme_classes":["4.1.1.-","4.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine Degradation","kegg_map_id":null}],"gene_sequence":"ATGTCTGAAATAACCTTAGGTAAATATTTATTTGAAAGATTGAGCCAAGTCAACTGTAACACCGTCTTCGGTTTGCCAGGTGACTTTAACTTGTCTCTTTTGGATAAGCTTTATGAAGTCAAAGGTATGAGATGGGCTGGTAACGCTAACGAATTGAACGCTGCCTATGCTGCTGATGGTTACGCTCGTATCAAGGGTATGTCCTGTATTATTACCACCTTCGGTGTTGGTGAATTGTCTGCTTTGAATGGTATTGCCGGTTCTTACGCTGAACATGTCGGTGTTTTGCACGTTGTTGGTGTTCCATCCATCTCTTCTCAAGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGTGACTTCACTGTTTTCCACAGAATGTCTGCCAACATTTCTGAAACCACTGCCATGATCACTGATATTGCTAACGCTCCAGCTGAAATTGACAGATGTATCAGAACCACCTACACTACCCAAAGACCAGTCTACTTGGGTTTGCCAGCTAACTTGGTTGACTTGAACGTCCCAGCCAAGTTATTGGAAACTCCAATTGACTTGTCTTTGAAGCCAAACGACGCTGAAGCTGAAGCTGAAGTTGTTAGAACTGTTGTTGAATTGATCAAGGATGCTAAGAACCCAGTTATCTTGGCTGATGCTTGTGCTTCTAGACATGATGTCAAGGCTGAAACTAAGAAGTTGATGGACTTGACTCAATTCCCAGTTTACGTCACCCCAATGGGTAAGGGTGCTATTGACGAACAACACCCAAGATACGGTGGTGTTTACGTTGGTACCTTGTCTAGACCAGAAGTTAAGAAGGCTGTAGAATCTGCTGATTTGATATTGTCTATCGGTGCTTTGTTGTCTGATTTCAATACCGGTTCTTTCTCTTACTCCTACAAGACCAAAAATATCGTTGAATTCCACTCTGACCACATCAAGATCAGAAACGCCACCTTCCCAGGTGTTCAAATGAAATTTGCCTTGCAAAAATTGTTGGATGCTATTCCAGAAGTCGTCAAGGACTACAAACCTGTTGCTGTCCCAGCTAGAGTTCCAATTACCAAGTCTACTCCAGCTAACACTCCAATGAAGCAAGAATGGATGTGGAACCATTTGGGTAACTTCTTGAGAGAAGGTGATATTGTTATTGCTGAAACCGGTACTTCCGCCTTCGGTATTAACCAAACTACTTTCCCAACAGATGTATACGCTATCGTCCAAGTCTTGTGGGGTTCCATTGGTTTCACAGTCGGCGCTCTATTGGGTGCTACTATGGCCGCTGAAGAACTTGATCCAAAGAAGAGAGTTATTTTATTCATTGGTGACGGTTCTCTACAATTGACTGTTCAAGAAATCTCTACCATGATTAGATGGGGTTTGAAGCCATACATTTTTGTCTTGAATAACAACGGTTACACCATTGAAAAATTGATTCACGGTCCTCATGCCGAATATAATGAAATTCAAGGTTGGGACCACTTGGCCTTATTGCCAACTTTTGGTGCTAGAAACTACGAAACCCACAGAGTTGCTACCACTGGTGAATGGGAAAAGTTGACTCAAGACAAGGACTTCCAAGACAACTCTAAGATTAGAATGATTGAAGTTATGTTGCCAGTCTTTGATGCTCCACAAAACTTGGTTAAACAAGCTCAATTGACTGCCGCTACTAACGCTAAACAATAA","protein_sequence":"MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKLLETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQFPVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYSYKTKNIVEFHSDHIKIRNATFPGVQMKFALQKLLDAIPEVVKDYKPVAVPARVPITKSTPANTPMKQEWMWNHLGNFLREGDIVIAETGTSAFGINQTTFPTDVYAIVQVLWGSIGFTVGALLGATMAAEELDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYIFVLNNNGYTIEKLIHGPHAEYNEIQGWDHLALLPTFGARNYETHRVATTGEWEKLTQDKDFQDNSKIRMIEVMLPVFDAPQNLVKQAQLTAATNAKQ"},{"created_at":"2011-05-24T20:27:16.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 3","uniprot_id":"P26263","uniprot_name":"PDC6_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC6","num_residues":563,"molecular_weight":"61579.89844","theoretical_pi":"6.11","general_function":"Involved in magnesium ion binding","specific_function":"Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it can not compensate for the other two pyruvate decarboxylases to sustain fermentation","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm;Nucleus","altext":"A 2-oxo acid = an aldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2320,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2322,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Pyruvate = Acetaldehyde + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2323,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO(2).","export":false,"pw_reaction_id":null,"source":null},{"id":2324,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"An aldehyde + an aldehyde = A 2-hydroxy ketone.","export":false,"pw_reaction_id":null,"source":null},{"id":14096,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006520","source":"Smpdb"},{"id":14097,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006525","source":"Smpdb"},{"id":14098,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006537","source":"Smpdb"},{"id":14099,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006557","source":"Smpdb"},{"id":14100,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006971","source":"Smpdb"},{"id":14101,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006979","source":"Smpdb"},{"id":14283,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006759","source":"Smpdb"},{"id":14285,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006770","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"X55905","genbank_protein_id":"4116","gene_card_id":"PDC6","chromosome_location":"chromosome 7","locus":"YGR087C","synonyms":[],"enzyme_classes":["4.1.1.-","4.1.1.1"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate binding"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" lyase activity"},{"category":"Function","description":" carbon-carbon lyase activity"},{"category":"Function","description":" carboxy-lyase activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" ion binding"},{"category":"Function","description":" cation binding"},{"category":"Function","description":" metal ion binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine Biosynthesis","kegg_map_id":null},{"name":"Valine Degradation","kegg_map_id":null},{"name":"isoleucine biosynthesis","kegg_map_id":null}],"gene_sequence":"ATGTCTGAAATTACTCTTGGAAAATACTTATTTGAAAGATTGAAGCAAGTTAATGTTAACACCATTTTTGGGCTACCAGGCGACTTCAACTTGTCCCTATTGGACAAGATTTACGAGGTAGATGGATTGAGATGGGCTGGTAATGCAAATGAGCTGAACGCCGCCTATGCCGCCGATGGTTACGCACGCATCAAGGGTTTATCTGTGCTGGTAACTACTTTTGGCGTAGGTGAATTATCCGCCTTGAATGGTATTGCAGGATCGTATGCAGAACACGTCGGTGTACTGCATGTTGTTGGTGTCCCCTCTATCTCCGCTCAGGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGTGATTTTACCGTTTTTCACAGAATGTCCGCCAATATCTCAGAAACTACATCAATGATTACAGACATTGCTACAGCCCCTTCAGAAATCGATAGGTTGATCAGGACAACATTTATAACACAAAGGCCTAGCTACTTGGGGTTGCCAGCGAATTTGGTAGATCTAAAGGTTCCTGGTTCTCTTTTGGAAAAACCGATTGATCTATCATTAAAACCTAACGATCCCGAAGCTGAAAAGGAAGTTATTGATACCGTACTAGAATTGATCCAGAATTCGAAAAACCCTGTTATACTATCGGATGCCTGTGCTTCTAGGCACAACGTTAAAAAAGAAACCCAGAAGTTAATTGATTTGACGCAATTCCCAGCTTTTGTGACACCTCTAGGTAAAGGGTCAATAGATGAACAGCATCCCAGATATGGCGGTGTTTATGTGGGAACGCTGTCCAAACAAGACGTGAAACAGGCCGTTGAGTCGGCTGATTTGATCCTTTCGGTCGGTGCTTTGCTCTCTGATTTTAACACAGGTTCGTTTTCCTACTCCTACAAGACTAAAAATGTAGTGGAGTTTCATTCCGATTACGTAAAGGTGAAGAACGCTACGTTCCTCGGTGTACAAATGAAATTTGCACTACAAAACTTACTGAAGGTTATTCCCGATGTTGTTAAGGGCTACAAGAGCGTTCCCGTACCAACCAAAACTCCCGCAAACAAAGGTGTACCTGCTAGCACGCCCTTGAAACAAGAGTGGTTGTGGAACGAATTGTCCAAATTCTTGCAAGAAGGTGATGTTATCATTTCCGAGACCGGCACGTCTGCCTTCGGTATCAATCAAACTATCTTTCCTAAGGACGCCTACGGTATCTCGCAGGTGTTGTGGGGGTCCATCGGTTTTACAACAGGAGCAACTTTAGGTGCTGCCTTTGCCGCTGAGGAGATTGACCCCAACAAGAGAGTCATCTTATTCATAGGTGACGGGTCTTTGCAGTTAACCGTCCAAGAAATCTCCACCATGATCAGATGGGGGTTAAAGCCGTATCTTTTTGTCCTTAACAACGACGGCTACACTATCGAAAAGCTGATTCATGGGCCTCACGCAGAGTACAACGAAATCCAGACCTGGGATCACCTCGCCCTGTTGCCCGCATTTGGTGCGAAAAAGTACGAAAATCACAAGATCGCCACTACGGGTGAGTGGGATGCCTTAACCACTGATTCAGAGTTCCAGAAAAACTCGGTGATCAGACTAATTGAACTGAAACTGCCCGTCTTTGATGCTCCGGAAAGTTTGATCAAACAAGCGCAATTGACTGCCGCTACAAATGCCAAACAATAA","protein_sequence":"MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIRLIELKLPVFDAPESLIKQAQLTAATNAKQ"},{"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":" 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":"Function","description":" zinc ion binding"},{"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 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 metabolism","kegg_map_id":"00350"}],"gene_sequence":"ATGTCTTCCGTTACTGGGTTTTACATTCCACCAATCTCTTTCTTTGGTGAAGGTGCTTTAGAAGAAACCGCTGATTACATCAAAAACAAGGATTACAAAAAGGCTTTGATCGTTACTGATCCTGGTATTGCAGCTATTGGTCTCTCCGGTAGAGTCCAAAAGATGTTGGAAGAACGTGGCTTAAACGTTGCTATCTATGACAAAACTCAACCAAACCCAAATATTGCCAATGTCACAGCTGGTTTGAAGGTTTTGAAGGAAGAAAACTCTGAAATTGTCGTTTCCATTGGTGGTGGTTCTGCTCACGACAATGCTAAGGCCATTGCTTTATTGGCTACTAACGGTGGGGAAATTGGAGATTATGAAGGTGTCAACCAATCTAAGAAGGCTGCTTTACCGCTATTTGCCATCAACACTACTGCTGGTACTGCTTCCGAGATGACCAGATTCACTATTATCTCTAATGAAGAAAAGAAAATCAAGATGGCCATCATTGACAACAACGTCACTCCAGCTGTTGCTGTCAACGACCCATCTACCATGTTTGGTTTGCCACCTGCTTTGACTGCTGCTACTGGTCTAGATGCTTTGACTCACTGTATCGAAGCTTACGTTTCCACCGCCTCTAACCCAATCACCGATGCTTGTGCTTTGAAGGGTATTGATTTGATCAATGAAAGCTTGGTCGCCGCATACAAAGACGGTAAAGACAAGAAGGCCAGAACTGATATGTGTTACGCAGAATACTTGGCAGGTATGGCTTTCAACAATGCTTCTCTAGGTTATGTTCATGCCCTTGCTCATCAACTTGGTGGTTTCTACCACTTGCCTCATGGTGTTTGTAACGCTGTCTTGTTGCCTCATGTTCAAGAGGCCAACATGCAATGTCCAAAGGCCAAGAAGAGATTAGGTGAAATTGCCTTGCATTGCGGTGCTTCTCAAGAAGATCCAGAAGAAACCATCAAGGCTTTGCACGTTTTAAACAGAACCATGAACATTCCAAGAAACTTGAAAGACTTAGGTGTTAAAACCGAAGATTTTGACATTTTGGCTGAACACGCCATGCATGATGCCTGCCATTTGACTAACCCAGTTCAATTCACCAAAGAACAAGTGGTTGCCATTATCAAGAAAGCCTATGAATATTAA","protein_sequence":"MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQEDPEETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAYEY"},{"created_at":"2011-05-24T20:31:18.000Z","updated_at":"2011-07-22T17:53:52.000Z","name":"Pyruvate decarboxylase isozyme 1","uniprot_id":"P06169","uniprot_name":"PDC1_YEAST","enzyme":true,"transporter":false,"gene_name":"PDC1","num_residues":563,"molecular_weight":"61494.89844","theoretical_pi":"6.11","general_function":"Involved in magnesium ion binding","specific_function":"Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1184,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1228,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1658,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1841,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1933,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1934,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2319,"direction":"\u003e","locations":"Cytoplasm. 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binding"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"TPP_enzyme_C","identifier":"PF02775"},{"name":"TPP_enzyme_M","identifier":"PF00205"},{"name":"TPP_enzyme_N","identifier":"PF02776"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Ethanol fermentation","kegg_map_id":null},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Phenylalanine metabolism","kegg_map_id":"00360"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Tryptophan metabolism","kegg_map_id":"00380"},{"name":"Tyrosine metabolism","kegg_map_id":"00350"},{"name":"Valine 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NADH","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":null,"genbank_gene_id":"Z36014","genbank_protein_id":"536448","gene_card_id":"ADH5","chromosome_location":"chromosome 2","locus":"YBR145W","synonyms":["Alcohol dehydrogenase V"],"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":" transition metal ion binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" zinc ion binding"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" 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dehydrogenase 2","uniprot_id":"P00331","uniprot_name":"ADH2_YEAST","enzyme":true,"transporter":false,"gene_name":"ADH2","num_residues":348,"molecular_weight":"36731.60156","theoretical_pi":"6.73","general_function":"Involved in zinc ion binding","specific_function":"This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. 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