2.0 2012-05-31 13:46:43 -0600 2015-09-13 12:56:10 -0600 ECMDB01167 M2MDB000281 Pyruvaldehyde Pyruvaldehyde is an organic compound used often as a reagent in organic synthesis, as a flavoring agent, and in tanning. It has been demonstrated as an intermediate in the metabolism of acetone and its derivatives in isolated cell preparations, in various culture media, and in vivo in certain animals. 1,2-Propanedione 1-Ketopropionaldehyde 2-Keto Propionaldehyde 2-Ketopropionaldehyde 2-Oxo-propanal 2-Oxo-Propionaldehyde 2-Oxopropanal a-Ketopropionaldehyde Acetylformaldehyde Acetylformyl Alpha-Ketopropionaldehyde Ketopropionaldehyde Methyl-glyoxal Methylglyoxal Oxopropanal Propanedione Propanolone Pyroracemic aldehyde Pyruvaldehyde Pyruvic aldehyde α-Ketopropionaldehyde C3H4O2 72.0627 72.021129372 2-oxopropanal methylglyoxal 78-98-8 CC(=O)C=O InChI=1S/C3H4O2/c1-3(5)2-4/h2H,1H3 AIJULSRZWUXGPQ-UHFFFAOYSA-N Liquid Cytosol logp -0.38 ALOGPS logs 0.40 ALOGPS solubility 1.80e+02 g/l ALOGPS melting_point < 25 oC logp 0.2 ChemAxon pka_strongest_acidic 16.38 ChemAxon pka_strongest_basic -8 ChemAxon iupac 2-oxopropanal ChemAxon average_mass 72.0627 ChemAxon mono_mass 72.021129372 ChemAxon smiles CC(=O)C=O ChemAxon formula C3H4O2 ChemAxon inchi InChI=1S/C3H4O2/c1-3(5)2-4/h2H,1H3 ChemAxon inchikey AIJULSRZWUXGPQ-UHFFFAOYSA-N ChemAxon polar_surface_area 34.14 ChemAxon refractivity 17.05 ChemAxon polarizability 6.42 ChemAxon rotatable_bond_count 1 ChemAxon acceptor_count 2 ChemAxon donor_count 0 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Glycine, serine and threonine metabolism ec00260 Pyruvate metabolism ec00620 Propanoate metabolism Starting from L-threonine, this compound is deaminated through a threonine deaminase resulting in a hydrogen ion, a water molecule and a (2z)-2-aminobut-2-enoate. The latter compound then isomerizes to a 2-iminobutanoate, This compound then reacts spontaneously with hydrogen ion and a water molecule resulting in a ammonium and a 2-Ketobutyric acid. The latter compound interacts with CoA through a pyruvate formate-lyase / 2-ketobutyrate formate-lyase resulting in a formic acid and a propionyl-CoA. Propionyl-CoA can then be processed either into a 2-methylcitric acid or into a propanoyl phosphate. Propionyl-CoA interacts with oxalacetic acid and a water molecule through a 2-methylcitrate synthase resulting in a hydrogen ion, a CoA and a 2-Methylcitric acid.The latter compound is dehydrated through a 2-methylcitrate dehydratase resulting in a water molecule and cis-2-methylaconitate. The latter compound is then dehydrated by a bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase resulting in a water molecule and methylisocitric acid. The latter compound is then processed by 2-methylisocitrate lyase resulting in a release of succinic acid and pyruvic acid. Succinic acid can then interact with a propionyl-CoA through a propionyl-CoA:succinate CoA transferase resulting in a propionic acid and a succinyl CoA. Succinyl-CoA is then isomerized through a methylmalonyl-CoA mutase resulting in a methylmalonyl-CoA. This compound is then decarboxylated through a methylmalonyl-CoA decarboxylase resulting in a release of Carbon dioxide and Propionyl-CoA. ropionyl-CoA interacts with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. Propionyl-CoA can react with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. The latter compound is then dephosphorylated through a ADP driven acetate kinase/propionate kinase protein complex resulting in an ATP and Propionic acid. Propionic acid can be processed by a reaction with CoA through a ATP-driven propionyl-CoA synthetase resulting in a pyrophosphate, an AMP and a propionyl-CoA. PW000940 ec00640 Metabolic Microbial metabolism in diverse environments ec01120 L-threonine degradation to methylglyoxal L-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways. PW002106 Metabolic methylglyoxal degradation II The most common pathway for methylglyoxal detoxification is the glyoxalase system, which is composed of two enzymes that together convert methylglyoxal to (R)-lactate in the presence of glutathione. However, in E. coli, a single enzyme, glyoxalase III, catalyzes this conversion in a single step without involvement of glutathione. Activity of glyoxalase III increases at the transition to stationary phase and expression is dependent on RpoS, suggesting that this pathway may be important during stationary phase. (EcoCyc) PW002084 Metabolic methylglyoxal degradation III In E. coli there are several pathways for the removal of methylglyoxal. In this pathway, methylglyoxal is reduced to acetol by the action of various enzymes possessing methylglyoxal reductase activity. Most of the enzymes that have been characterized with this activity belong to the NADPH-dependent aldo-keto reductase subfamily of the aldo-keto reductase (AKR) superfamily. AKRs are found in both prokaryotes and eukaryotes and catalyze the reduction of carbonyl-containing aldehyde and/or ketone containing compounds to their corresponding alcohols. A few dual-specificity AKRs are also able to utilize NADH. An AKR from E. coli has been identified that is NADH-specific (AKR11B2, the product of gene ydjG). AKRs have been of considerable interest in metabolic engineering studies. E. coli K-12 enzymes homologous to mammalian AKRs have been shown to catalyze the methylglyoxal reductase reaction. Overexpression of the aldo-keto reductase AKR14A1, encoded by the yghZ gene, leads to increased resistance to methylglyoxal. In addition, three other genes yeaE (yeaE), dkgA (yqhE), and dkgB (yafB) were shown to encode proteins with similar activities. All four proteins were purified, and shown to catalyze the reaction in vitro, in the presence of NADPH. Prolonged incubation of E. coli cell-free extracts with methylglyoxal resulted in conversion of acetol to (S)-propane-1,2-diol. The enzyme proposed to catalyze (S)-propane-1,2-diol production is L-1,2-propanediol dehydrogenase / glycerol dehydrogenase. In bacteria (S)-propane-1,2-diol is a dead-end metabolite and exits the cell rapidly. Although AKRs can reduce methylglyoxal to acetol, a methylglyoxal reductase (NADPH-dependent) encoded by an unknown gene was purified from E. coli and shown to convert methylglyoxal to lactaldehyde. (EcoCyc) PW002079 Metabolic methylglyoxal degradation IV In this pathway, which has been characterized in Escherichia coli K-12, methylglyoxal is reduced to lactaldehyde by the enzyme methylglyoxal reductase. (S)-lactaldehyde is then reduced to (S)-lactate which is finally converted to pyruvate and joins the pool of central metobolites. Methylglyoxal reductases have been characterized in bacteria and fungi. Some of the enzymes are NADP-linked, while others are NAD-linked. Two variants of this pathway have been entered in MetaCyc to reflect the different biochemistry of the last enzyme, L-lactate dehydrogenase. The Escherichia coli K-12 enzyme encoded by gene lldD uses an unidentified electron acceptor, while the Saccharomyces cerevisiae enzyme uses an an oxidized c-type cytochrome. (EcoCyc) PW002078 Metabolic threonine degradation III (to methylglyoxal) THRDLCTCAT-PWY methylglyoxal degradation I PWY-5386 methylglyoxal degradation IV PWY-5459 methylglyoxal degradation III PWY-5453 methylglyoxal degradation II PWY-901 Specdb::CMs 3344 Specdb::CMs 161686 Specdb::NmrOneD 21362 Specdb::NmrOneD 21363 Specdb::NmrOneD 21364 Specdb::NmrOneD 21365 Specdb::NmrOneD 21366 Specdb::NmrOneD 21367 Specdb::NmrOneD 21368 Specdb::NmrOneD 21369 Specdb::NmrOneD 21370 Specdb::NmrOneD 21371 Specdb::NmrOneD 21372 Specdb::NmrOneD 21373 Specdb::NmrOneD 21374 Specdb::NmrOneD 21375 Specdb::NmrOneD 21376 Specdb::NmrOneD 21377 Specdb::NmrOneD 21378 Specdb::NmrOneD 21379 Specdb::NmrOneD 21380 Specdb::NmrOneD 21381 Specdb::MsMs 1442 Specdb::MsMs 1443 Specdb::MsMs 1444 Specdb::MsMs 20852 Specdb::MsMs 20853 Specdb::MsMs 20854 Specdb::MsMs 22403 Specdb::MsMs 22404 Specdb::MsMs 22405 Specdb::MsMs 2437012 Specdb::MsMs 2437013 Specdb::MsMs 2437014 Specdb::MsMs 2528988 Specdb::MsMs 2528989 Specdb::MsMs 2528990 HMDB01167 880 857 C00546 17158 METHYL-GLYOXAL PVL Pyruvaldehyde Keseler, I. 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Jingxi Huagong (2000), 17(9), 507-510. http://hmdb.ca/system/metabolites/msds/000/001/046/original/HMDB01167.pdf?1358462226 Methylglyoxal synthase P0A731 MGSA_ECOLI mgsA http://ecmdb.ca/proteins/P0A731.xml Glycerol dehydrogenase P0A9S5 GLDA_ECOLI gldA http://ecmdb.ca/proteins/P0A9S5.xml Lactoylglutathione lyase P0AC81 LGUL_ECOLI gloA http://ecmdb.ca/proteins/P0AC81.xml Lactaldehyde dehydrogenase P25553 ALDA_ECOLI aldA http://ecmdb.ca/proteins/P25553.xml 2,5-diketo-D-gluconic acid reductase B P30863 DKGB_ECOLI dkgB http://ecmdb.ca/proteins/P30863.xml Primary amine oxidase P46883 AMO_ECOLI tynA http://ecmdb.ca/proteins/P46883.xml Glyoxylate/hydroxypyruvate reductase A P75913 GHRA_ECOLI ghrA http://ecmdb.ca/proteins/P75913.xml 2,5-diketo-D-gluconic acid reductase A Q46857 DKGA_ECOLI dkgA http://ecmdb.ca/proteins/Q46857.xml Uncharacterized protein yghZ Q46851 YGHZ_ECOLI yghZ http://ecmdb.ca/proteins/Q46851.xml Uncharacterized protein yeaE P76234 YEAE_ECOLI yeaE http://ecmdb.ca/proteins/P76234.xml Molecular chaperone Hsp31 and glyoxalase 3 P31658 hchA http://ecmdb.ca/proteins/P31658.xml Hydrogen ion + Pyruvaldehyde + NADPH > Acetol + NADP Dihydroxyacetone phosphate <> Pyruvaldehyde + Phosphate R01016 METHGLYSYN-RXN Glutathione + Pyruvaldehyde <> S-Lactoylglutathione R02530 GLYOXI-RXN Hydrogen ion + Pyruvaldehyde + NADH > D-Lactaldehyde + NAD R02527 Pyruvaldehyde + NAD + Water <> Pyruvic acid + NADH + Hydrogen ion R00203 D-Lactaldehyde + NAD <> Pyruvaldehyde + NADH + Hydrogen ion R02527 Aminoacetone + Water + Oxygen <> Pyruvaldehyde + Ammonia + Hydrogen peroxide R02529 S-Lactoylglutathione <> Glutathione + Pyruvaldehyde R02530 GLYOXI-RXN Aminoacetone + Water + Oxygen > Hydrogen ion + Pyruvaldehyde + Ammonia + Hydrogen peroxide R02529 AMACETOXID-RXN S-Lactoylglutathione < Pyruvaldehyde + Glutathione GLYOXI-RXN D-Lactic acid + Hydrogen ion < Pyruvaldehyde + Water GLYOXIII-RXN Dihydroxyacetone phosphate > Pyruvaldehyde + Phosphate METHGLYSYN-RXN Lactaldehyde + NADP < Pyruvaldehyde + NADPH + Hydrogen ion RXN-8636 Hydrogen ion + Pyruvaldehyde + NADH acetol + NAD RXN0-5213 D-Lactic acid > Pyruvaldehyde + Water GLYOXIII-RXN S-Lactoylglutathione > Glutathione + Pyruvaldehyde Dihydroxyacetone phosphate > Pyruvaldehyde + Inorganic phosphate D-Lactic acid <> Pyruvaldehyde + Water R09796 Pyruvaldehyde + NADPH + Hydrogen ion <> Hydroxyacetone + NADP PW_R006074 Pyruvaldehyde + Water > D-Lactic acid + Hydrogen ion PW_R006086 Pyruvaldehyde + NADPH + Hydrogen ion > Lactaldehyde + NADP PW_R006073 Aminoacetone + Oxygen + Water > Hydrogen peroxide + Ammonium + Pyruvaldehyde PW_R006139 Pyruvaldehyde + Glutathione > S-Lactoylglutathione PW_R006149 D-Lactic acid <> Pyruvaldehyde + Water Glutathione + Pyruvaldehyde <> S-Lactoylglutathione D-Lactic acid <> Pyruvaldehyde + Water