2.02012-05-31 13:46:43 -06002015-09-13 12:56:10 -0600ECMDB01167M2MDB000281PyruvaldehydePyruvaldehyde 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-Propanedione1-Ketopropionaldehyde2-Keto Propionaldehyde2-Ketopropionaldehyde2-Oxo-propanal2-Oxo-Propionaldehyde2-Oxopropanala-KetopropionaldehydeAcetylformaldehydeAcetylformylAlpha-KetopropionaldehydeKetopropionaldehydeMethyl-glyoxalMethylglyoxalOxopropanalPropanedionePropanolonePyroracemic aldehydePyruvaldehydePyruvic aldehydeα-KetopropionaldehydeC3H4O272.062772.0211293722-oxopropanalmethylglyoxal78-98-8CC(=O)C=OInChI=1S/C3H4O2/c1-3(5)2-4/h2H,1H3AIJULSRZWUXGPQ-UHFFFAOYSA-NLiquidCytosollogp-0.38logs0.40solubility1.80e+02 g/lmelting_point< 25 oClogp0.2pka_strongest_acidic16.38pka_strongest_basic-8iupac2-oxopropanalaverage_mass72.0627mono_mass72.021129372smilesCC(=O)C=OformulaC3H4O2inchiInChI=1S/C3H4O2/c1-3(5)2-4/h2H,1H3inchikeyAIJULSRZWUXGPQ-UHFFFAOYSA-Npolar_surface_area34.14refractivity17.05polarizability6.42rotatable_bond_count1acceptor_count2donor_count0physiological_charge0formal_charge0Glycine, serine and threonine metabolismec00260Pyruvate metabolismec00620Propanoate 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.PW000940ec00640MetabolicMicrobial metabolism in diverse environmentsec01120L-threonine degradation to methylglyoxalL-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.PW002106Metabolicmethylglyoxal degradation IIThe 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)PW002084Metabolicmethylglyoxal degradation IIIIn 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)PW002079Metabolicmethylglyoxal degradation IVIn 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)PW002078Metabolicthreonine degradation III (to methylglyoxal)THRDLCTCAT-PWYmethylglyoxal degradation IPWY-5386methylglyoxal degradation IVPWY-5459methylglyoxal degradation IIIPWY-5453methylglyoxal degradation IIPWY-901Specdb::CMs3344Specdb::CMs161686Specdb::NmrOneD21362Specdb::NmrOneD21363Specdb::NmrOneD21364Specdb::NmrOneD21365Specdb::NmrOneD21366Specdb::NmrOneD21367Specdb::NmrOneD21368Specdb::NmrOneD21369Specdb::NmrOneD21370Specdb::NmrOneD21371Specdb::NmrOneD21372Specdb::NmrOneD21373Specdb::NmrOneD21374Specdb::NmrOneD21375Specdb::NmrOneD21376Specdb::NmrOneD21377Specdb::NmrOneD21378Specdb::NmrOneD21379Specdb::NmrOneD21380Specdb::NmrOneD21381Specdb::MsMs1442Specdb::MsMs1443Specdb::MsMs1444Specdb::MsMs20852Specdb::MsMs20853Specdb::MsMs20854Specdb::MsMs22403Specdb::MsMs22404Specdb::MsMs22405Specdb::MsMs2437012Specdb::MsMs2437013Specdb::MsMs2437014Specdb::MsMs2528988Specdb::MsMs2528989Specdb::MsMs2528990HMDB01167880857C0054617158METHYL-GLYOXALPVLPyruvaldehydeKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). 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Jingxi Huagong (2000), 17(9), 507-510. http://hmdb.ca/system/metabolites/msds/000/001/046/original/HMDB01167.pdf?1358462226Methylglyoxal synthaseP0A731MGSA_ECOLImgsAhttp://ecmdb.ca/proteins/P0A731.xmlGlycerol dehydrogenaseP0A9S5GLDA_ECOLIgldAhttp://ecmdb.ca/proteins/P0A9S5.xmlLactoylglutathione lyaseP0AC81LGUL_ECOLIgloAhttp://ecmdb.ca/proteins/P0AC81.xmlLactaldehyde dehydrogenaseP25553ALDA_ECOLIaldAhttp://ecmdb.ca/proteins/P25553.xml2,5-diketo-D-gluconic acid reductase BP30863DKGB_ECOLIdkgBhttp://ecmdb.ca/proteins/P30863.xmlPrimary amine oxidaseP46883AMO_ECOLItynAhttp://ecmdb.ca/proteins/P46883.xmlGlyoxylate/hydroxypyruvate reductase AP75913GHRA_ECOLIghrAhttp://ecmdb.ca/proteins/P75913.xml2,5-diketo-D-gluconic acid reductase AQ46857DKGA_ECOLIdkgAhttp://ecmdb.ca/proteins/Q46857.xmlUncharacterized protein yghZQ46851YGHZ_ECOLIyghZhttp://ecmdb.ca/proteins/Q46851.xmlUncharacterized protein yeaEP76234YEAE_ECOLIyeaEhttp://ecmdb.ca/proteins/P76234.xmlMolecular chaperone Hsp31 and glyoxalase 3P31658hchAhttp://ecmdb.ca/proteins/P31658.xmlHydrogen ion + Pyruvaldehyde + NADPH > Acetol + NADPDihydroxyacetone phosphate <> Pyruvaldehyde + PhosphateR01016METHGLYSYN-RXNGlutathione + Pyruvaldehyde <> S-LactoylglutathioneR02530GLYOXI-RXNHydrogen ion + Pyruvaldehyde + NADH > D-Lactaldehyde + NADR02527Pyruvaldehyde + NAD + Water <> Pyruvic acid + NADH + Hydrogen ionR00203D-Lactaldehyde + NAD <> Pyruvaldehyde + NADH + Hydrogen ionR02527Aminoacetone + Water + Oxygen <> Pyruvaldehyde + Ammonia + Hydrogen peroxideR02529S-Lactoylglutathione <> Glutathione + PyruvaldehydeR02530GLYOXI-RXNAminoacetone + Water + Oxygen > Hydrogen ion + Pyruvaldehyde + Ammonia + Hydrogen peroxideR02529AMACETOXID-RXNS-Lactoylglutathione < Pyruvaldehyde + GlutathioneGLYOXI-RXND-Lactic acid + Hydrogen ion < Pyruvaldehyde + WaterGLYOXIII-RXNDihydroxyacetone phosphate > Pyruvaldehyde + PhosphateMETHGLYSYN-RXNLactaldehyde + NADP < Pyruvaldehyde + NADPH + Hydrogen ionRXN-8636Hydrogen ion + Pyruvaldehyde + NADH acetol + NADRXN0-5213D-Lactic acid > Pyruvaldehyde + WaterGLYOXIII-RXNS-Lactoylglutathione > Glutathione + PyruvaldehydeDihydroxyacetone phosphate > Pyruvaldehyde + Inorganic phosphateD-Lactic acid <> Pyruvaldehyde + WaterR09796 Pyruvaldehyde + NADPH + Hydrogen ion <> Hydroxyacetone + NADPPW_R006074Pyruvaldehyde + Water > D-Lactic acid + Hydrogen ionPW_R006086Pyruvaldehyde + NADPH + Hydrogen ion > Lactaldehyde + NADPPW_R006073Aminoacetone + Oxygen + Water > Hydrogen peroxide + Ammonium + PyruvaldehydePW_R006139Pyruvaldehyde + Glutathione > S-LactoylglutathionePW_R006149D-Lactic acid <> Pyruvaldehyde + WaterGlutathione + Pyruvaldehyde <> S-LactoylglutathioneD-Lactic acid <> Pyruvaldehyde + Water