{"ymdb_id":"YMDB00388","created_at":"2011-05-29T18:11:55.000Z","updated_at":"2016-09-08T18:35:26.000Z","name":"Ketoleucine","cas":"816-66-0","state":"Liquid","melting_point":"8-10 oC","description":"Ketoleucine is an intermediate in the leucine biosynthesis pathway. [Biocyc LEUSYN-PWY]","experimental_water_solubility":"32 mg/mL [HMP experimental]","experimental_logp_hydrophobicity":"","location":"mitochondrion;cytoplasm","synthesis_reference":"Tabuchi, Takeshi; Abe, Matazo.  Fermentative preparation of a-ketoisocaproic acid.    Jpn. Tokkyo Koho  (1970),     3 pp. ","chebi_id":"48430","hmdb_id":"HMDB00695","kegg_id":"C00233","pubchem_id":"70","cs_id":"69","foodb_id":null,"wikipedia_link":null,"biocyc_id":"2K-4CH3-PENTANOATE","iupac":"4-methyl-2-oxopentanoic acid","traditional_iupac":"ketoisocaproate","logp":"1.4979975616666668","pka":null,"alogps_solubility":"6.76e+00 g/l","alogps_logp":"0.82","alogps_logs":"-1.28","acceptor_count":"3","donor_count":"1","rotatable_bond_count":"3","polar_surface_area":"54.37","refractivity":"31.7662","polarizability":"12.995994785498697","formal_charge":"0","physiological_charge":"-1","pka_strongest_basic":"-9.662090237480372","pka_strongest_acidic":"3.528051095084082","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["2-Keto-4-methylpentanoic acid","2-keto-4-Methylvalerate","2-keto-4-Methylvaleric acid","2-Ketoisocaproate","2-Ketoisocaproic acid","2-Oxo-4-methylpentanoate","2-Oxo-4-methylpentanoic acid","2-Oxo-4-methylvalerate","2-Oxo-4-methylvaleric acid","2-Oxoisocaproate","2-Oxoisocaproic acid","2-Oxoleucine","4-methyl-2-oxo-Valerate","4-methyl-2-oxo-Valeric acid","4-Methyl-2-oxopentanoate","4-Methyl-2-oxopentanoic acid","4-Methyl-2-oxovaleric acid","a-Ketoisocaproate","a-Ketoisocaproic acid","a-Ketoisocapronate","a-Ketoisocapronic acid","a-Oxoisocaproate","a-Oxoisocaproic acid","alpha-keto-isocaproate","alpha-keto-isocaproic acid","alpha-ketoisocaproate","alpha-Ketoisocaproic acid","alpha-Ketoisocapronate","alpha-Ketoisocapronic acid","alpha-Oxoisocaproate","alpha-Oxoisocaproic acid","Isopropylpyruvic acid","ketoisocaproate","ketoisocaproic acid","Methyloxovalerate","Methyloxovaleric acid","oxoisocaproate","oxoisocaproic acid","Pentanoic acid, 4-methyl-2-oxo-"],"pathways":[{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Valine, leucine and isoleucine degradation","kegg_map_id":"00280"},{"name":"Leucine Biosynthesis","kegg_map_id":null},{"name":"Leucine Degradation","kegg_map_id":null}],"growth_conditions":[],"references":[{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"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":9341119,"citation":"Dickinson, J. R., Lanterman, M. M., Danner, D. J., Pearson, B. M., Sanz, P., Harrison, S. J., Hewlins, M. J. (1997). \"A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae.\" J Biol Chem 272:26871-26878."},{"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":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":8798704,"citation":"Kispal, G., Steiner, H., Court, D. A., Rolinski, B., Lill, R. (1996). \"Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein.\" J Biol Chem 271:24458-24464."}],"proteins":[{"created_at":"2011-05-24T21:01:35.000Z","updated_at":"2011-07-22T17:53:43.000Z","name":"Branched-chain-amino-acid aminotransferase, cytosolic","uniprot_id":"P47176","uniprot_name":"BCA2_YEAST","enzyme":true,"transporter":false,"gene_name":"BAT2","num_residues":376,"molecular_weight":"41624.39844","theoretical_pi":"7.36","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Involved in cell cycle regulation","reactions":[{"id":1152,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1678,"direction":"\u003c\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1712,"direction":"\u003c\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2045,"direction":"\u003c\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2358,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.","export":false,"pw_reaction_id":null,"source":null},{"id":2359,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"2-oxoglutaric acid + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.","export":false,"pw_reaction_id":null,"source":null},{"id":2360,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"2-oxoglutaric acid + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamic acid.","export":false,"pw_reaction_id":null,"source":null},{"id":14458,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006970","source":"Smpdb"},{"id":14459,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006974","source":"Smpdb"},{"id":14460,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006978","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"Z49648","genbank_protein_id":"1015897","gene_card_id":"BAT2","chromosome_location":"chromosome 10","locus":"YJR148W","synonyms":["BCAT","Protein TWT2"],"enzyme_classes":["2.6.1.42"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring nitrogenous groups"},{"category":"Function","description":" transaminase activity"},{"category":"Function","description":" branched-chain-amino-acid transaminase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"}],"pfams":[{"name":"Aminotran_4","identifier":"PF01063"}],"pathways":[{"name":"Valine, leucine and isoleucine degradation","kegg_map_id":"00280"},{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Pantothenate and CoA biosynthesis","kegg_map_id":"00770"},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Leucine Degradation","kegg_map_id":null},{"name":"Valine Degradation","kegg_map_id":null}],"gene_sequence":"ATGACCTTGGCACCCCTAGACGCCTCCAAAGTTAAGATAACTACCACACAACATGCATCTAAGCCAAAACCGAACAGTGAGTTAGTGTTTGGCAAGAGCTTCACGGACCACATGTTAACTGCGGAATGGACAGCTGAAAAAGGGTGGGGTACCCCAGAGATTAAACCTTATCAAAATCTGTCTTTAGACCCTTCCGCGGTGGTTTTCCATTATGCTTTTGAGCTATTCGAAGGGATGAAGGCTTACAGAACGGTGGACAACAAAATTACAATGTTTCGTCCAGATATGAATATGAAGCGCATGAATAAGTCTGCTCAGAGAATCTGTTTGCCAACGTTCGACCCAGAAGAGTTGATTACCCTAATTGGGAAACTGATCCAGCAAGATAAGTGCTTAGTTCCTGAAGGAAAAGGTTACTCTTTATATATCAGGCCTACATTAATCGGCACTACGGCCGGTTTAGGGGTTTCCACGCCTGATAGAGCCTTGCTATATGTCATTTGCTGCCCTGTGGGTCCTTATTACAAAACTGGATTTAAGGCGGTCAGACTGGAAGCCACTGATTATGCCACAAGAGCTTGGCCAGGAGGCTGTGGTGACAAGAAACTAGGTGCAAACTACGCCCCCTGCGTCCTGCCACAATTGCAAGCTGCTTCAAGGGGTTACCAACAAAATTTATGGCTATTTGGTCCAAATAACAACATTACTGAAGTCGGCACCATGAATGCTTTTTTCGTGTTTAAAGATAGTAAAACGGGCAAGAAGGAACTAGTTACTGCTCCACTAGACGGTACCATTTTGGAAGGTGTTACTAGGGATTCCATTTTAAATCTTGCTAAAGAAAGACTCGAACCAAGTGAATGGACCATTAGTGAACGCTACTTCACTATAGGCGAAGTTACTGAGAGATCCAAGAACGGTGAACTACTTGAAGCCTTTGGTTCTGGTACTGCTGCGATTGTTTCTCCCATTAAGGAAATCGGCTGGAAAGGCGAACAAATTAATATTCCGTTGTTGCCCGGCGAACAAACCGGTCCATTGGCCAAAGAAGTTGCACAATGGATTAATGGAATCCAATATGGCGAGACTGAGCATGGCAATTGGTCAAGGGTTGTTACTGATTTGAACTGA","protein_sequence":"MTLAPLDASKVKITTTQHASKPKPNSELVFGKSFTDHMLTAEWTAEKGWGTPEIKPYQNLSLDPSAVVFHYAFELFEGMKAYRTVDNKITMFRPDMNMKRMNKSAQRICLPTFDPEELITLIGKLIQQDKCLVPEGKGYSLYIRPTLIGTTAGLGVSTPDRALLYVICCPVGPYYKTGFKAVRLEATDYATRAWPGGCGDKKLGANYAPCVLPQLQAASRGYQQNLWLFGPNNNITEVGTMNAFFVFKDSKTGKKELVTAPLDGTILEGVTRDSILNLAKERLEPSEWTISERYFTIGEVTERSKNGELLEAFGSGTAAIVSPIKEIGWKGEQINIPLLPGEQTGPLAKEVAQWINGIQYGETEHGNWSRVVTDLN"},{"created_at":"2011-05-24T21:06:51.000Z","updated_at":"2011-07-22T17:53:43.000Z","name":"Branched-chain-amino-acid aminotransferase, mitochondrial","uniprot_id":"P38891","uniprot_name":"BCA1_YEAST","enzyme":true,"transporter":false,"gene_name":"BAT1","num_residues":393,"molecular_weight":"43595.69922","theoretical_pi":"9.27","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1","reactions":[{"id":1152,"direction":"\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1678,"direction":"\u003c\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1712,"direction":"\u003c\u003e","locations":"mitochondrion;cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2046,"direction":"\u003e","locations":"mitochondrion","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2358,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.","export":false,"pw_reaction_id":null,"source":null},{"id":2359,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"2-oxoglutaric acid + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.","export":false,"pw_reaction_id":null,"source":null},{"id":2360,"direction":"\u003e","locations":"Mitochondrion matrix;Cytoplasm","altext":"2-oxoglutaric acid + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamic acid.","export":false,"pw_reaction_id":null,"source":null},{"id":14455,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006969","source":"Smpdb"},{"id":14456,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006973","source":"Smpdb"},{"id":14457,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006977","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Mitochondrion matrix","genbank_gene_id":"AY558111","genbank_protein_id":"45270112","gene_card_id":"BAT1","chromosome_location":"chromosome 8","locus":"YHR208W","synonyms":["BCAT","Protein ECA39","Protein TWT1"],"enzyme_classes":["2.6.1.42"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring nitrogenous groups"},{"category":"Function","description":" transaminase activity"},{"category":"Function","description":" branched-chain-amino-acid transaminase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"}],"pfams":[{"name":"Aminotran_4","identifier":"PF01063"}],"pathways":[{"name":"Valine, leucine and isoleucine degradation","kegg_map_id":"00280"},{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"},{"name":"Pantothenate and CoA biosynthesis","kegg_map_id":"00770"},{"name":"Isoleucine degradation","kegg_map_id":null},{"name":"Leucine Degradation","kegg_map_id":null},{"name":"Valine Degradation","kegg_map_id":null}],"gene_sequence":"ATGTTGCAGAGACATTCCTTGAAGTTGGGGAAATTCTCCATCAGAACACTCGCTACTGGTGCCCCATTAGATGCATCCAAACTAAAAATTACTAGAAACCCAAATCCATCCAAGCCAAGACCAAATGAAGAATTAGTGTTCGGCCAGACATTCACCGATCATATGTTGACCATTCCTTGGTCAGCCAAAGAAGGGTGGGGCACTCCACACATCAAGCCTTACGGTAATCTTTCTCTTGACCCATCTGCTTGTGTATTCCATTATGCATTTGAATTATTTGAAGGTTTGAAAGCCTACAGAACTCCTCAAAATACTATCACCATGTTCCGTCCGGATAAGAACATGGCCCGTATGAACAAGTCTGCCGCTAGAATTTGTTTGCCAACTTTCGAATCTGAAGAATTGATCAAACTTACCGGGAAATTGATCGAACAAGATAAACACTTGGTTCCTCAAGGTAATGGTTACTCATTATACATCAGACCAACAATGATTGGTACATCCAAGGGTTTAGGTGTTGGCACTCCCTCCGAGGCTCTTCTTTATGTTATTACTTCTCCAGTCGGTCCTTATTATAAGACTGGTTTCAAAGCCGTACGTCTTGAAGCAACAGACTATGCTACAAGAGCTTGGCCAGGTGGTGTTGGCGACAAAAAATTGGGTGCTAACTATGCCCCATGCATCTTACCTCAACTACAAGCTGCCAAAAGAGGGTACCAACAAAATCTATGGTTGTTCGGCCCAGAAAAGAACATCACTGAGGTTGGTACTATGAACGTGTTCTTCGTTTTCCTCAACAAAGTCACTGGCAAGAAGGAATTGGTTACCGCTCCATTAGATGGTACCATTTTAGAAGGTGTTACCAGAGACTCTGTTTTAACATTGGCTCGTGACAAACTAGATCCTCAAGAATGGGACATCAACGAGCGTTATTACACTATTACTGAAGTCGCCACTAGAGCAAAACAAGGTGAACTATTAGAAGCCTTCGGTTCTGGTACTGCTGCTGTCGTTTCACCTATCAAGGAAATTGGCTGGAACAACGAAGATATTCATGTTCCACTATTGCCTGGTGAACAATGTGGTGCATTGACCAAGCAAGTTGCTCAATGGATTGCTGATATCCAATACGGTAGAGTCAATTATGGTAACTGGTCAAAAACTGTTGCCGACTTGAACTAA","protein_sequence":"MLQRHSLKLGKFSIRTLATGAPLDASKLKITRNPNPSKPRPNEELVFGQTFTDHMLTIPWSAKEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPEKNITEVGTMNVFFVFLNKVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQEWDINERYYTITEVATRAKQGELLEAFGSGTAAVVSPIKEIGWNNEDIHVPLLPGEQCGALTKQVAQWIADIQYGRVNYGNWSKTVADLN"},{"created_at":"2011-05-27T01:57:53.000Z","updated_at":"2011-07-22T17:53:47.000Z","name":"3-isopropylmalate dehydrogenase","uniprot_id":"P04173","uniprot_name":"LEU3_YEAST","enzyme":true,"transporter":false,"gene_name":"LEU2","num_residues":364,"molecular_weight":"38952.5","theoretical_pi":"5.48","general_function":"Involved in magnesium ion binding","specific_function":"Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate","reactions":[{"id":1183,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2649,"direction":"\u003e","locations":"Cytoplasm","altext":"(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"X03840","genbank_protein_id":"4698","gene_card_id":"LEU2","chromosome_location":"chromosome 3","locus":"YCL018W","synonyms":["3-IPM-DH","IMDH","Beta-IPM dehydrogenase"],"enzyme_classes":["1.1.1.85"],"go_classes":[{"category":"Component","description":" cell part"},{"category":"Component","description":" intracellular part"},{"category":"Component","description":" cytoplasm"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" catalytic activity"},{"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":" NAD or NADH binding"},{"category":"Function","description":" binding"},{"category":"Function","description":" 3-isopropylmalate dehydrogenase activity"},{"category":"Function","description":" nucleotide 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":" oxidation reduction"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" branched chain family amino acid metabolic process"},{"category":"Process","description":" cellular amino acid and derivative metabolic process"},{"category":"Process","description":" leucine metabolic process"},{"category":"Process","description":" cellular amino acid metabolic process"},{"category":"Process","description":" leucine biosynthetic process"}],"pfams":[{"name":"Iso_dh","identifier":"PF00180"}],"pathways":[{"name":"Valine, leucine and isoleucine biosynthesis","kegg_map_id":"00290"}],"gene_sequence":"ATGTCTGCCCCTAAGAAGATCGTCGTTTTGCCAGGTGACCACGTTGGTCAAGAAATCACAGCCGAAGCCATTAAGGTTCTTAAAGCTATTTCTGATGTTCGTTCCAATGTCAAGTTCGATTTCGAAAATCATTTAATTGGTGGTGCTGCTATCGATGCTACAGGTGTCCCACTTCCAGATGAGGCGCTGGAAGCCTCCAAGAAGGTTGATGCCGTTTTGTTAGGTGCTGTGGGTGGTCCTAAATGGGGTACCGGTAGTGTTAGACCTGAACAAGGTTTACTAAAAATCCGTAAAGAACTTCAATTGTACGCCAACTTAAGACCATGTAACTTTGCATCCGACTCTCTTTTAGACTTATCTCCAATCAAGCCACAATTTGCTAAAGGTACTGACTTCGTTGTTGTCAGAGAATTAGTGGGAGGTATTTACTTTGGTAAGAGAAAGGAAGACGATGGTGATGGTGTCGCTTGGGATAGTGAACAATACACCGTTCCAGAAGTGCAAAGAATCACAAGAATGGCCGCTTTCATGGCCCTACAACATGAGCCACCATTGCCTATTTGGTCCTTGGATAAAGCTAATGTTTTGGCCTCTTCAAGATTATGGAGAAAAACTGTGGAGGAAACCATCAAGAACGAATTCCCTACATTGAAGGTTCAACATCAATTGATTGATTCTGCCGCCATGATCCTAGTTAAGAACCCAACCCACCTAAATGGTATTATAATCACCAGCAACATGTTTGGTGATATCATCTCCGATGAAGCCTCCGTTATCCCAGGTTCCTTGGGTTTGTTGCCATCTGCGTCCTTGGCCTCTTTGCCAGACAAGAACACCGCATTTGGTTTGTACGAACCATGCCACGGTTCTGCTCCAGATTTGCCAAAGAATAAGGTCAACCCTATCGCCACTATCTTGTCTGCTGCAATGATGTTGAAATTGTCATTGAACTTGCCTGAAGAAGGTAAGGCCATTGAAGATGCAGTTAAAAAGGTTTTGGATGCAGGTATCAGAACTGGTGATTTAGGTGGTTCCAACAGTACCACGGAAGTCGGTGATGCTGTCGCCGAAGAAGTTAAGAAAATCCTTGCTTAA","protein_sequence":"MSAPKKIVVLPGDHVGQEITAEAIKVLKAISDVRSNVKFDFENHLIGGAAIDATGVPLPDEALEASKKADAVLLGAVGGPKWGTGSVRPEQGLLKIRKELQLYANLRPCNFASDSLLDLSPIKPQFAKGTDFVVVRELVGGIYFGKRKEDDGDGVAWDSEQYTVPEVQRITRMAAFMALQHEPPLPIWSLDKANVLASSRLWRKTVEETIKNEFPTLKVQHQLIDSAAMILVKNPTHLNGIIITSNMFGDIISDEASVIPGSLGLLPSASLASLPDKNTAFGLYEPCHGSAPDLPKNKVNPIATILSAAMMLKLSLNLPEEGKAIEDAVKKVLDAGIRTGDLGGSNSTTEVGDAVAEEVKKILA"},{"created_at":"2011-05-27T02:09:02.000Z","updated_at":"2011-07-22T17:53:49.000Z","name":"Transaminated amino acid decarboxylase","uniprot_id":"Q06408","uniprot_name":"ARO10_YEAST","enzyme":true,"transporter":false,"gene_name":"ARO10","num_residues":635,"molecular_weight":"71383.79688","theoretical_pi":"6.51","general_function":"Involved in magnesium ion binding","specific_function":"One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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, phenylalanine, tryptophan, (and probably tyrosine), but also isoleucine, whereas leucine is a low efficiency and valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins","reactions":[{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1197,"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":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":2321,"direction":"\u003e","locations":"Cytoplasm. Nucleus;Cytoplasm","altext":"Phenylpyruvate = phenylacetaldehyde + 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":14461,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006975","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"U28373","genbank_protein_id":"849201","gene_card_id":"ARO10","chromosome_location":"chromosome 4","locus":"YDR380W","synonyms":["Transaminated branched-chain amino acid decarboxylase"],"enzyme_classes":["4.1.1.-","4.1.1.43"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic 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":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate 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":"Leucine Degradation","kegg_map_id":null}],"gene_sequence":"ATGGCACCTGTTACAATTGAAAAGTTCGTAAATCAAGAAGAACGACACCTTGTTTCCAACCGATCAGCAACAATTCCGTTTGGTGAATACATATTTAAAAGATTGTTGTCCATCGATACGAAATCAGTTTTCGGTGTTCCTGGTGACTTCAACTTATCTCTATTAGAATATCTCTATTCACCTAGTGTTGAATCAGCTGGCCTAAGATGGGTCGGCACGTGTAATGAACTGAACGCCGCTTATGCGGCCGACGGATATTCCCGTTACTCTAATAAGATTGGCTGTTTAATAACCACGTATGGCGTTGGTGAATTAAGCGCCTTGAACGGTATAGCCGGTTCGTTCGCTGAAAATGTCAAAGTTTTGCACATTGTTGGTGTGGCCAAGTCCATAGATTCGCGTTCAAGTAACTTTAGTGATCGGAACCTACATCATTTGGTCCCACAGCTACATGATTCAAATTTTAAAGGGCCAAATCATAAAGTATATCATGATATGGTAAAAGATAGAGTCGCTTGCTCGGTAGCCTACTTGGAGGATATTGAAACTGCATGTGACCAAGTCGATAATGTTATCCGCGATATTTACAAGTATTCTAAACCTGGTTATATTTTTGTTCCTGCAGATTTTGCGGATATGTCTGTTACATGTGATAATTTGGTTAATGTTCCACGTATATCTCAACAAGATTGTATAGTATACCCTTCTGAAAACCAATTGTCTGACATAATCAACAAGATTACTAGTTGGATATATTCCAGTAAAACACCTGCGATCCTTGGAGACGTACTGACTGATAGGTATGGTGTGAGTAACTTTTTGAACAAGCTTATCTGCAAAACTGGGATTTGGAATTTTTCCACTGTTATGGGAAAATCTGTAATTGATGAGTCAAACCCAACTTATATGGGTCAATATAATGGTAAAGAAGGTTTAAAACAAGTCTATGAACATTTTGAACTGTGCGACTTGGTCTTGCATTTTGGAGTCGACATCAATGAAATTAATAATGGGCATTATACTTTTACTTATAAACCAAATGCTAAAATCATTCAATTTCATCCGAATTATATTCGCCTTGTGGACACTAGGCAGGGCAATGAGCAAATGTTCAAAGGAATCAATTTTGCCCCTATTTTAAAAGAACTATACAAGCGCATTGACGTTTCTAAACTTTCTTTGCAATATGATTCAAATGTAACTCAATATACGAACGAAACAATGCGGTTAGAAGATCCTACCAATGGACAATCAAGCATTATTACACAAGTTCACTTACAAAAGACGATGCCTAAATTTTTGAACCCTGGTGATGTTGTCGTTTGTGAAACAGGCTCTTTTCAATTCTCTGTTCGTGATTTCGCGTTTCCTTCGCAATTAAAATATATATCGCAAGGATTTTTCCTTTCCATTGGCATGGCCCTTCCTGCCGCCCTAGGTGTTGGAATTGCCATGCAAGACCACTCAAACGCTCACATCAATGGTGGCAACGTAAAAGAGGACTATAAGCCAAGATTAATTTTGTTTGAAGGTGACGGTGCAGCACAGATGACAATCCAAGAACTGAGCACCATTCTGAAGTGCAATATTCCACTAGAAGTTATCATTTGGAACAATAACGGCTACACTATTGAAAGAGCCATCATGGGCCCTACCAGGTCGTATAACGACGTTATGTCTTGGAAATGGACCAAACTATTTGAAGCATTCGGAGACTTCGACGGAAAGTATACTAATAGCACTCTCATTCAATGTCCCTCTAAATTAGCACTGAAATTGGAGGAGCTTAAGAATTCAAACAAAAGAAGCGGGATAGAACTTTTAGAAGTCAAATTAGGCGAATTGGATTTCCCCGAACAGCTAAAGTGCATGGTTGAAGCAGCGGCACTTAAAAGAAATAAAAAATAG","protein_sequence":"MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLEDIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQLSDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSNKRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK"},{"created_at":"2011-05-27T08:04:35.000Z","updated_at":"2011-07-22T17:53:49.000Z","name":"Thiamine metabolism regulatory protein THI3","uniprot_id":"Q07471","uniprot_name":"THI3_YEAST","enzyme":true,"transporter":false,"gene_name":"THI3","num_residues":609,"molecular_weight":"68365.79688","theoretical_pi":"6.33","general_function":"Involved in magnesium ion binding","specific_function":"One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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 leucine and isoleucine, whereas valine, aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission","reactions":[{"id":1186,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1197,"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":14461,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006975","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Nucleus","genbank_gene_id":"Z74128","genbank_protein_id":"1431100","gene_card_id":"THI3","chromosome_location":"chromosome 4","locus":"YDL080C","synonyms":["Keto isocaproate decarboxylase KID1"],"enzyme_classes":["4.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic 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":"Function","description":" vitamin binding"},{"category":"Function","description":" magnesium ion binding"},{"category":"Function","description":" thiamin pyrophosphate 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":"Leucine Degradation","kegg_map_id":null}],"gene_sequence":"ATGAATTCTAGCTATACACAGAGATATGCACTGCCGAAGTGTATAGCAATATCAGATTATCTTTTCCATCGGCTCAACCAGCTGAACATACATACCATATTTGGACTCTCCGGAGAATTTAGCATGCCGTTGCTGGATAAACTATACAACATTCCGAACTTACGATGGGCCGGTAATTCTAATGAGTTAAATGCTGCCTACGCAGCAGATGGATACTCACGACTAAAAGGCTTGGGATGTCTCATAACAACCTTTGGTGTAGGCGAATTATCGGCAATCAATGGCGTGGCCGGATCTTACGCTGAACATGTAGGAATACTTCACATAGTGGGTATGCCGCCAACAAGTGCACAAACGAAACAACTACTACTGCATCATACTCTGGGCAATGGTGATTTCACGGTATTTCATAGAATAGCCAGTGATGTAGCATGCTATACAACATTGATTATTGACTCTGAATTATGTGCCGACGAAGTCGATAAGTGCATCAAAAAGGCTTGGATAGAACAGAGGCCAGTATACATGGGCATGCCTGTCAACCAGGTAAATCTCCCGATTGAATCAGCAAGGCTTAATACACCTCTGGATTTACAATTGCATAAAAACGACCCAGACGTAGAGAAAGAAGTTATTTCTCGAATATTGAGTTTTATATACAAAAGCCAGAATCCGGCAATCATCGTAGATGCATGTACTAGTCGACAGAATTTAATCGAGGAGACTAAAGAGCTTTGTAATAGGCTTAAATTTCCAGTTTTTGTTACACCTATGGGTAAGGGTACAGTAAACGAAACAGACCCGCAATTTGGGGGCGTATTCACGGGCTCGATATCAGCCCCAGAAGTAAGAGAAGTAGTTGATTTTGCCGATTTTATCATCGTCATTGGTTGCATGCTCTCCGAATTCAGCACGTCAACTTTCCACTTCCAATATAAAACTAAGAATTGTGCGCTACTATATTCTACATCTGTGAAATTGAAAAATGCCACATATCCTGACTTGAGCATTAAATTACTACTACAGAAAATATTAGCAAATCTTGATGAATCTAAACTGTCTTACCAACCAAGCGAACAACCCAGTATGATGGTTCCAAGACCTTACCCAGCAGGAAATGTCCTCTTGAGACAAGAATGGGTCTGGAATGAAATATCCCATTGGTTCCAACCAGGTGACATAATCATAACAGAAACTGGTGCTTCTGCATTTGGAGTTAACCAGACCAGATTTCCGGTAAATACACTAGGTATTTCGCAAGCTCTTTGGGGATCTGTCGGATATACAATGGGGGCGTGTCTTGGGGCAGAATTTGCTGTTCAAGAGATAAACAAGGATAAATTCCCCGCAACTAAACATAGAGTTATTCTGTTTATGGGTGACGGTGCTTTCCAATTGACAGTTCAAGAATTATCCACAATTGTTAAGTGGGGATTGACACCTTATATTTTTGTGATGAATAACCAAGGTTACTCTGTGGACAGGTTTTTGCATCACAGGTCAGATGCTAGTTATTACGATATCCAACCTTGGAACTACTTGGGATTATTGCGAGTATTTGGTTGCACGAACTACGAAACGAAAAAAATTATTACTGTTGGAGAATTCAGATCCATGATCAGTGACCCAAACTTTGCGACCAATGACAAAATTCGGATGATAGAGATTATGCTACCACCAAGGGATGTTCCACAGGCTCTGCTTGACAGGTGGGTGGTAGAAAAAGAACAGAGCAAACAAGTGCAAGAGGAGAACGAAAATTCTAGCGCAGTAAATACGCCAACTCCAGAATTCCAACCACTTCTAAAAAAAAATCAAGTTGGATACTGA","protein_sequence":"MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNSNELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTKQLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPVNQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIEETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCMLSEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQPSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLTPYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMISDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQPLLKKNQVGY"}]}