{"ymdb_id":"YMDB00170","created_at":"2011-05-29T16:03:30.000Z","updated_at":"2016-09-08T18:35:08.000Z","name":"Pyruvaldehyde","cas":"78-98-8","state":"Liquid","melting_point":"\u003c 25 oC","description":"Methylglyoxal, also called pyruvaldehyde or 2-oxopropanal is the aldehyde form of pyruvic acid. It has two carbonyl groups, so it is a dicarbonyl compound. Methylglyoxal is both an aldehyde and a ketone. Methylglyoxal is formed as a side-product of several metabolic pathways. It may form from 3-amino acetone, which is an intermediate of threonine catabolism, as well as through lipid peroxidation. However, the most important source is glycolysis. Here, methylglyoxal arises from nonenzymatic phosphate elimination from glyceraldehyde phosphate and dihydroxyacetone phosphate, two intermediates of glycolysis. Methylglyoxal is toxic due to its high reactivity. [Wikipedia]\n","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"cytoplasm","synthesis_reference":"Zhang, Jing-An; Chen, Yu-Ping.  Synthesis of pyruvaldehyde.    Jingxi Huagong  (2000),  17(9),  507-510. ","chebi_id":"17158","hmdb_id":"HMDB01167","kegg_id":"C00546","pubchem_id":"880","cs_id":"857","foodb_id":null,"wikipedia_link":"Methylglyoxal","biocyc_id":"METHYL-GLYOXAL","iupac":"2-oxopropanal","traditional_iupac":"methylglyoxal","logp":"0.19595048433333334","pka":null,"alogps_solubility":"1.80e+02 g/l","alogps_logp":"-0.38","alogps_logs":"0.40","acceptor_count":"2","donor_count":"0","rotatable_bond_count":"1","polar_surface_area":"34.14","refractivity":"17.0511","polarizability":"6.421644584802687","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"-8.021418549550578","pka_strongest_acidic":"16.38193786809808","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"0","veber_rule":"1","mddr_like_rule":"0","synonyms":["1-Ketopropionaldehyde","1,2-Propanedione","2-keto Propionaldehyde","2-Ketopropionaldehyde","2-oxo-Propionaldehyde","2-Oxopropanal","Acetylformaldehyde","Acetylformyl","alpha-Ketopropionaldehyde","Ketopropionaldehyde","Methylglyoxal","Propanedione","Propanolone","Pyroracemic aldehyde","Pyruvaldehyde","Pyruvic aldehyde"],"pathways":[{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"}],"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":21062828,"citation":"Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). \"BRENDA, the enzyme information system in 2011.\" Nucleic Acids Res 39:D670-D676."},{"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":12722185,"citation":"Chen, C. N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L. G., Dover, J. L., Johnston, M., Chitnis, P. R., Kohl, D. H. (2003). \"Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae.\" Yeast 20:545-554."},{"pubmed_id":3908097,"citation":"Inoue, Y., Watanabe, K., Shimosaka, M., Saikusa, T., Fukuda, Y., Murata, K., Kimura, A. (1985). \"Metabolism of 2-oxoaldehydes in yeasts. Purification and characterization of lactaldehyde dehydrogenase from Saccharomyces cerevisiae.\" Eur J Biochem 153:243-247."}],"proteins":[{"created_at":"2011-05-26T23:22:53.000Z","updated_at":"2011-05-29T14:08:01.000Z","name":"NADPH-dependent methylglyoxal reductase GRE2","uniprot_id":"Q12068","uniprot_name":"GRE2_YEAST","enzyme":true,"transporter":false,"gene_name":"GRE2","num_residues":342,"molecular_weight":"38169.19922","theoretical_pi":"6.06","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation","reactions":[{"id":1702,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2615,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"Lactaldehyde + NADP(+) = methylglyoxal + NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":2616,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+","export":false,"pw_reaction_id":null,"source":null},{"id":14116,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006547","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"AY558040","genbank_protein_id":"45269970","gene_card_id":"GRE2","chromosome_location":"chromosome 15","locus":"YOL151W","synonyms":["Genes de respuesta a estres protein 2"],"enzyme_classes":["1.1.1.283","1.1.1.265"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" cofactor binding"},{"category":"Function","description":" coenzyme binding"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"}],"pfams":[{"name":"Epimerase","identifier":"PF01370"}],"pathways":[{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Stress-activated signalling pathways: high osmolarity test 1","kegg_map_id":null}],"gene_sequence":"ATGTCAGTTTTCGTTTCAGGTGCTAACGGGTTCATTGCCCAACACATTGTCGATCTCCTGTTGAAGGAAGACTATAAGGTCATCGGTTCTGCCAGAAGTCAAGAAAAGGCCGAGAATTTAACGGAGGCCTTTGGTAACAACCCAAAATTCTCCATGGAAGTTGTCCCAGACATATCTAAGCTGGACGCATTTGACCATGTTTTCCAAAAGCACGGCAAGGATATCAAGATAGTTCTACATACGGCCTCTCCATTCTGCTTTGATATCACTGACAGTGAACGCGATTTATTAATTCCTGCTGTGAACGGTGTTAAGGGAATTCTCCACTCAATTAAAAAATACGCCGCTGATTCTGTAGAACGTGTAGTTCTCACCTCTTCTTATGCAGCTGTGTTCGATATGGCAAAAGAAAACGATAAGTCTTTAACATTTAACGAAGAATCCTGGAACCCAGCTACCTGGGAGAGTTGCCAAAGTGACCCAGTTAACGCCTACTGTGGTTCTAAGAAGTTTGCTGAAAAAGCAGCTTGGGAATTTCTAGAGGAGAATAGAGACTCTGTAAAATTCGAATTAACTGCCGTTAACCCAGTTTACGTTTTTGGTCCGCAAATGTTTGACAAAGATGTGAAAAAACACTTGAACACATCTTGCGAACTCGTCAACAGCTTGATGCATTTATCACCAGAGGACAAGATACCGGAACTATTTGGTGGATACATTGATGTTCGTGATGTTGCAAAGGCTCATTTAGTTGCCTTCCAAAAGAGGGAAACAATTGGTCAAAGACTAATCGTATCGGAGGCCAGATTTACTATGCAGGATGTTCTCGATATCCTTAACGAAGACTTCCCTGTTCTAAAAGGCAATATTCCAGTGGGGAAACCAGGTTCTGGTGCTACCCATAACACCCTTGGTGCTACTCTTGATAATAAAAAGAGTAAGAAATTGTTAGGTTTCAAGTTCAGGAACTTGAAAGAGACCATTGACGACACTGCCTCCCAAATTTTAAAATTTGAGGGCAGAATATAA","protein_sequence":"MSVFVSGANGFIAQHIVDLLLKEDYKVIGSARSQEKAENLTEAFGNNPKFSMEVVPDISKLDAFDHVFQKHGKDIKIVLHTASPFCFDITDSERDLLIPAVNGVKGILHSIKKYAADSVERVVLTSSYAAVFDMAKENDKSLTFNEESWNPATWESCQSDPVNAYCGSKKFAEKAAWEFLEENRDSVKFELTAVNPVYVFGPQMFDKDVKKHLNTSCELVNSLMHLSPEDKIPELFGGYIDVRDVAKAHLVAFQKRETIGQRLIVSEARFTMQDVLDILNEDFPVLKGNIPVGKPGSGATHNTLGATLDNKKSKKLLGFKFRNLKETIDDTASQILKFEGRI"},{"created_at":"2011-05-27T01:58:22.000Z","updated_at":"2011-07-22T17:54:34.000Z","name":"NADPH-dependent aldose reductase GRE3","uniprot_id":"P38715","uniprot_name":"GRE3_YEAST","enzyme":true,"transporter":false,"gene_name":"GRE3","num_residues":327,"molecular_weight":"37118.5","theoretical_pi":"7.09","general_function":"Involved in oxidoreductase activity","specific_function":"Reduces the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde similar to GRE2. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction","reactions":[{"id":1292,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1325,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1436,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":1702,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2051,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2650,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"Alditol + NAD(P)(+) = aldose + NAD(P)H.","export":false,"pw_reaction_id":null,"source":null},{"id":2651,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"(R)-lactaldehyde + NADP(+) = methylglyoxal + NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":14078,"direction":"\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006505","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"U00059","genbank_protein_id":"529125","gene_card_id":"GRE3","chromosome_location":"chromosome 8","locus":"YHR104W","synonyms":["Genes de respuesta a estres protein 3","NADPH-dependent aldo-keto reductase GRE3","NADPH-dependent methylglyoxal reductase GRE3","Xylose reductase"],"enzyme_classes":["1.1.1.21","1.1.1.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" oxidation reduction"}],"pfams":[{"name":"Aldo_ket_red","identifier":"PF00248"}],"pathways":[{"name":"Pentose and glucuronate interconversions","kegg_map_id":"00040"},{"name":"Fructose and mannose metabolism","kegg_map_id":"00051"},{"name":"Galactose metabolism","kegg_map_id":"00052"},{"name":"Glycerolipid metabolism","kegg_map_id":"00561"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"xylitol degradation","kegg_map_id":null}],"gene_sequence":"ATGTCTTCACTGGTTACTCTTAATAACGGTCTGAAAATGCCCCTAGTCGGCTTAGGGTGCTGGAAAATTGACAAAAAAGTCTGTGCGAATCAAATTTATGAAGCTATCAAATTAGGCTACCGTTTATTCGATGGTGCTTGCGACTACGGCAACGAAAAGGAAGTTGGTGAAGGTATCAGGAAAGCCATCTCCGAAGGTCTTGTTTCTAGAAAGGATATATTTGTTGTTTCAAAGTTATGGAACAATTTTCACCATCCTGATCATGTAAAATTAGCTTTAAAGAAGACCTTAAGCGATATGGGACTTGATTATTTAGACCTGTATTATATTCACTTCCCAATCGCCTTCAAATATGTTCCATTTGAAGAGAAATACCCTCCAGGATTCTATACGGGCGCAGATGACGAGAAGAAAGGTCACATCACCGAAGCACATGTACCAATCATAGATACGTACCGGGCTCTGGAAGAATGTGTTGATGAAGGCTTGATTAAGTCTATTGGTGTTTCCAACTTTCAGGGAAGCTTGATTCAAGATTTATTACGTGGTTGTAGAATCAAGCCCGTGGCTTTGCAAATTGAACACCATCCTTATTTGACTCAAGAACACCTAGTTGAGTTTTGTAAATTACACGATATCCAAGTAGTTGCTTACTCCTCCTTCGGTCCTCAATCATTCATTGAGATGGACTTACAGTTGGCAAAAACCACGCCAACTCTGTTCGAGAATGATGTAATCAAGAAGGTCTCACAAAACCATCCAGGCAGTACCACTTCCCAAGTATTGCTTAGATGGGCAACTCAGAGAGGCATTGCCGTCATTCCAAAATCTTCCAAGAAGGAAAGGTTACTTGGCAACCTAGAAATCGAAAAAAAGTTCACTTTAACGGAGCAAGAATTGAAGGATATTTCTGCACTAAATGCCAACATCAGATTTAATGATCCATGGACCTGGTTGGATGGTAAATTCCCCACTTTTGCCTGA","protein_sequence":"MSSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA"},{"created_at":"2011-05-27T03:01:53.000Z","updated_at":"2011-05-29T05:06:37.000Z","name":"Lactoylglutathione lyase","uniprot_id":"P50107","uniprot_name":"LGUL_YEAST","enzyme":true,"transporter":false,"gene_name":"GLO1","num_residues":326,"molecular_weight":"37208.69922","theoretical_pi":"6.84","general_function":"Involved in lactoylglutathione lyase activity","specific_function":"Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione","reactions":[{"id":1710,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2704,"direction":"\u003e","locations":null,"altext":"(R)-S-lactoylglutathione = glutathione + methylglyoxal.","export":false,"pw_reaction_id":null,"source":null},{"id":14117,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006548","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":null,"genbank_gene_id":"AJ297938","genbank_protein_id":"11182130","gene_card_id":"GLO1","chromosome_location":"chromosome 13","locus":"YML004C","synonyms":["Aldoketomutase","Glyoxalase I","Glx I","Ketone-aldehyde mutase","Methylglyoxalase","S-D-lactoylglutathione methylglyoxal lyase"],"enzyme_classes":["4.4.1.5"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" 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":" carbon-sulfur lyase activity"},{"category":"Function","description":" lactoylglutathione lyase activity"},{"category":"Process","description":" Not Available"}],"pfams":[{"name":"Glyoxalase","identifier":"PF00903"}],"pathways":[{"name":"Pyruvate metabolism","kegg_map_id":"00620"}],"gene_sequence":"ATGTCCACTGATAGTACACGCTATCCAATTCAGATTGAGAAAGCCTCGAATGATCCAACCCTTCTGCTTAATCACACATGTTTAAGAGTCAAGGATCCAGCAAGGGCTGTTAAGTTCTACACCGAACACTTCGGTATGAAGCTATTAAGCAGAAAGGATTTTGAAGAAGCAAAATTTAGCTTGTACTTTTTAAGCTTTCCAAAAGACGACATACCCAAAAATAAGAATGGAGAGCCTGATGTTTTTAGCGCACACGGTGTCTTAGAACTAACTCACAATTGGGGTACTGAAAAAAACCCAGACTACAAGATCAACAACGGGAATGAGGAACCTCATCGTGGATTTGGGCACATCTGTTTTTCTGTATCCGATATCAATAAAACCTGCGAAGAGCTAGAATCTCAGGGTGTCAAATTCAAGAAGAGACTCTCTGAAGGAAGACAGAAGGACATTGCGTTTGCTTTAGACCCTGATGGATACTGGATTGAGTTGATCACATATTCTAGAGAGGGTCAGGAATACCCAAAGGGCTCAGTAGGTAACAAGTTCAATCATACCATGATTCGTATTAAAAACCCAACCCGGTCTTTAGAATTCTACCAGAATGTGTTGGGCATGAAATTATTAAGAACTAGTGAGCACGAAAGTGCAAAATTTACGTTATACTTTCTTGGTTATGGCGTTCCAAAGACCGACAGCGTTTTTTCATGTGAAAGTGTGTTGGAGTTAACTCATAATTGGGGAACTGAGAATGATCCAAACTTCCACTATCATAACGGTAACTCAGAGCCCCAGGGTTATGGTCACATCTGCATAAGTTGCGATGACGCTGGCGCCCTTTGTAAAGAAATTGAAGTGAAATACGGCGATAAGATCCAATGGTCTCCTAAATTTAACCAAGGCAGAATGAAGAATATTGCCTTTTTGAAGGATCCTGATGGTTATTCCATTGAAGTCGTTCCTTATGGTTTGATTGCCTAA","protein_sequence":"MSTDSTRYPIQIEKASNDPTLLLNHTCLRVKDPARTVKFYTEHFGMKLLSRKDFEEAKFSLYFLSFPKDDIPKNKNGEPDVFSAHGVLELTHNWGTEKNPDYKINNGNEEPHRGFGHICFSVSDINKTCEELESQGVKFKKRLSEGRQKDIAFALGPDGYWIELITYSREGQEYPKGSVGNKFNHTMIRIKNPTRSLEFYQNVLGMKLLRTSEHESAKFTLYFLGYGVPKTDSVFSCESVLELTHNWGTENDPNFHYHNGNSEPQGYGHICISCDDAGALCKEIEVKYGDKIQWSPKFNQGRMKNIAFLKDPDGYSIEVVPHGLIA"}]}