Record Information
Version2.0
Creation Date2012-05-31 13:46:43 -0600
Update Date2015-09-13 12:56:10 -0600
Secondary Accession Numbers
  • ECMDB01167
Identification
Name:Pyruvaldehyde
DescriptionPyruvaldehyde 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.
Structure
Thumb
Synonyms:
  • 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
Chemical Formula:C3H4O2
Weight:Average: 72.0627
Monoisotopic: 72.021129372
InChI Key:AIJULSRZWUXGPQ-UHFFFAOYSA-N
InChI:InChI=1S/C3H4O2/c1-3(5)2-4/h2H,1H3
CAS number:78-98-8
IUPAC Name:2-oxopropanal
Traditional IUPAC Name:methylglyoxal
SMILES:CC(=O)C=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as alpha ketoaldehydes. These are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon.
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassCarbonyl compounds
Direct ParentAlpha ketoaldehydes
Alternative Parents
Substituents
  • Alpha-ketoaldehyde
  • Ketone
  • Organic oxide
  • Hydrocarbon derivative
  • Short-chain aldehyde
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Liquid
Charge:0
Melting point:< 25 °C
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility180 g/LALOGPS
logP-0.38ALOGPS
logP0.2ChemAxon
logS0.4ALOGPS
pKa (Strongest Acidic)16.38ChemAxon
pKa (Strongest Basic)-8ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area34.14 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity17.05 m³·mol⁻¹ChemAxon
Polarizability6.42 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:
L-threonine degradation to methylglyoxalPW002106 ThumbThumb?image type=greyscaleThumb?image type=simple
Propanoate metabolismPW000940 ThumbThumb?image type=greyscaleThumb?image type=simple
methylglyoxal degradation IIPW002084 ThumbThumb?image type=greyscaleThumb?image type=simple
methylglyoxal degradation IIIPW002079 ThumbThumb?image type=greyscaleThumb?image type=simple
methylglyoxal degradation IVPW002078 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
  • Glycine, serine and threonine metabolism ec00260
  • Microbial metabolism in diverse environments ec01120
  • Propanoate metabolism ec00640
  • Pyruvate metabolism ec00620
EcoCyc Pathways:
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9000000000-43f9b3c94058c64733b5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00dj-9000000000-964129275940a60a617dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-006y-9000000000-0ae1e5fd2d50b28f967cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-00dj-9000000000-964129275940a60a617dView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9000000000-110d6fcd891f2c54a2cbView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-05fr-9000000000-bec3651f9ea6825cf4f7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-8db5b1ba128748e220c3View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-f968a2358e6fd85ae268View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-0797bdeaa575b54943c5View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0uk9-9000000000-89ef1c082b2ef672eb67View in MoNA
References
References:
  • Ahmed MU, Brinkmann Frye E, Degenhardt TP, Thorpe SR, Baynes JW: N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem J. 1997 Jun 1;324 ( Pt 2):565-70. Pubmed: 9182719
  • Ahmed N, Dobler D, Dean M, Thornalley PJ: Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J Biol Chem. 2005 Feb 18;280(7):5724-32. Epub 2004 Nov 22. Pubmed: 15557329
  • Ahmed N, Thornalley PJ, Dawczynski J, Franke S, Strobel J, Stein G, Haik GM: Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins. Invest Ophthalmol Vis Sci. 2003 Dec;44(12):5287-92. Pubmed: 14638728
  • Baskaran S, Rajan DP, Balasubramanian KA: Formation of methylglyoxal by bacteria isolated from human faeces. J Med Microbiol. 1989 Mar;28(3):211-5. Pubmed: 2926792
  • Beisswenger PJ, Drummond KS, Nelson RG, Howell SK, Szwergold BS, Mauer M: Susceptibility to diabetic nephropathy is related to dicarbonyl and oxidative stress. Diabetes. 2005 Nov;54(11):3274-81. Pubmed: 16249455
  • Gildersleeve DL, Tobes MC, Natale RB: Rapid analysis for methylglyoxal bis(guanylhydrazone) by reversed-phase ion-pair liquid chromatography. Clin Chem. 1985 Dec;31(12):1979-84. Pubmed: 4064286
  • Haik GM Jr, Lo TW, Thornalley PJ: Methylglyoxal concentration and glyoxalase activities in the human lens. Exp Eye Res. 1994 Oct;59(4):497-500. Pubmed: 7859825
  • Jan CR, Chen CH, Wang SC, Kuo SY: Effect of methylglyoxal on intracellular calcium levels and viability in renal tubular cells. Cell Signal. 2005 Jul;17(7):847-55. Epub 2004 Dec 8. Pubmed: 15763427
  • Kanehisa, 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. Pubmed: 22080510
  • Keseler, 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. Pubmed: 21097882
  • Kuhla B, Luth HJ, Haferburg D, Boeck K, Arendt T, Munch G: Methylglyoxal, glyoxal, and their detoxification in Alzheimer's disease. Ann N Y Acad Sci. 2005 Jun;1043:211-6. Pubmed: 16037241
  • Lo TW, Selwood T, Thornalley PJ: The reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins. Biochem Pharmacol. 1994 Nov 16;48(10):1865-70. Pubmed: 7986197
  • Mottaran E, Stewart SF, Rolla R, Vay D, Cipriani V, Moretti M, Vidali M, Sartori M, Rigamonti C, Day CP, Albano E: Lipid peroxidation contributes to immune reactions associated with alcoholic liver disease. Free Radic Biol Med. 2002 Jan 1;32(1):38-45. Pubmed: 11755315
  • Nemet I, Varga-Defterdarovic L, Turk Z: Preparation and quantification of methylglyoxal in human plasma using reverse-phase high-performance liquid chromatography. Clin Biochem. 2004 Oct;37(10):875-81. Pubmed: 15369718
  • Riley ML, Harding JJ: The reaction of methylglyoxal with human and bovine lens proteins. Biochim Biophys Acta. 1995 Jan 25;1270(1):36-43. Pubmed: 7827133
  • Schupp N, Schinzel R, Heidland A, Stopper H: Genotoxicity of advanced glycation end products: involvement of oxidative stress and of angiotensin II type 1 receptors. Ann N Y Acad Sci. 2005 Jun;1043:685-95. Pubmed: 16037294
  • Seppanen P, Alhonen-Hongisto L, Janne J: Polyamine deprivation-induced enhanced uptake of methylglyoxal bis(guanylhydrazone) by tumor cells. Biochim Biophys Acta. 1981 May 5;674(2):169-77. Pubmed: 6786360
  • Shamsi FA, Lin K, Sady C, Nagaraj RH: Methylglyoxal-derived modifications in lens aging and cataract formation. Invest Ophthalmol Vis Sci. 1998 Nov;39(12):2355-64. Pubmed: 9804144
  • Thornalley PJ, Argirova M, Ahmed N, Mann VM, Argirov O, Dawnay A: Mass spectrometric monitoring of albumin in uremia. Kidney Int. 2000 Nov;58(5):2228-34. Pubmed: 11044246
  • van 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. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
  • Wondrak GT, Cervantes-Laurean D, Roberts MJ, Qasem JG, Kim M, Jacobson EL, Jacobson MK: Identification of alpha-dicarbonyl scavengers for cellular protection against carbonyl stress. Biochem Pharmacol. 2002 Feb 1;63(3):361-73. Pubmed: 11853687
Synthesis Reference:Zhang, Jing-An; Chen, Yu-Ping. Synthesis of pyruvaldehyde. Jingxi Huagong (2000), 17(9), 507-510.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID17158
HMDB IDHMDB01167
Pubchem Compound ID880
Kegg IDC00546
ChemSpider ID857
WikipediaPyruvaldehyde
BioCyc IDMETHYL-GLYOXAL
EcoCyc IDMETHYL-GLYOXAL
Ligand ExpoPVL

Enzymes

General function:
Involved in methylglyoxal synthase activity
Specific function:
Glycerone phosphate = methylglyoxal + phosphate
Gene Name:
mgsA
Uniprot ID:
P0A731
Molecular weight:
16918
Reactions
Glycerone phosphate = methylglyoxal + phosphate.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of gldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively
Gene Name:
gldA
Uniprot ID:
P0A9S5
Molecular weight:
38712
Reactions
Glycerol + NAD(+) = glycerone + NADH.
General function:
Involved in lactoylglutathione lyase activity
Specific function:
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione
Gene Name:
gloA
Uniprot ID:
P0AC81
Molecular weight:
14920
Reactions
(R)-S-lactoylglutathione = glutathione + methylglyoxal.
General function:
Involved in oxidoreductase activity
Specific function:
Acts on lactaldehyde as well as other aldehydes
Gene Name:
aldA
Uniprot ID:
P25553
Molecular weight:
52272
Reactions
(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH.
Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG)
Gene Name:
dkgB
Uniprot ID:
P30863
Molecular weight:
29437
Reactions
2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + NADPH.
General function:
Involved in copper ion binding
Specific function:
The enzyme prefers aromatic over aliphatic amines
Gene Name:
tynA
Uniprot ID:
P46883
Molecular weight:
84378
Reactions
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2).
2-phenylethylamine + H(2)O + O(2) = phenylacetaldehyde + NH(3) + H(2)O(2).
General function:
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific function:
Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low
Gene Name:
ghrA
Uniprot ID:
P75913
Molecular weight:
35343
Reactions
Glycolate + NADP(+) = glyoxylate + NADPH.
D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H.
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives
Gene Name:
dkgA
Uniprot ID:
Q46857
Molecular weight:
31109
Reactions
2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + NADPH.
General function:
Energy production and conversion
Specific function:
Specific function unknown
Gene Name:
yghZ
Uniprot ID:
Q46851
Molecular weight:
38832
General function:
Involved in oxidoreductase activity
Specific function:
Specific function unknown
Gene Name:
yeaE
Uniprot ID:
P76234
Molecular weight:
30986
General function:
Not Available
Specific function:
Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus. Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus.
Gene Name:
hchA
Uniprot ID:
P31658
Molecular weight:
Not Available
Reactions
(R)-lactate = methylglyoxal + H(2)O.
(R)-lactate = methylglyoxal + H(2)O.