You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
Identification
YMDB IDYMDB00175
NamePyruvic acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionPyruvic acid is an organic acid, a ketone, as well as the simplest of the alpha-keto acids. The carboxylate (COOH) ion (anion) of pyruvic acid is known as pyruvate, and is a key intersection in several metabolic pathways. It can be made from glucose through glycolysis, converted back to carbohydrates (such as glucose) via gluconeogenesis, or to fatty acids through acetyl-CoA. It can also be used to construct the amino acid alanine and be converted into ethanol. It supplies energy to living cells through the citric acid cycle when oxygen is present (aerobic respiration), and alternatively ferments to produce lactate when oxygen is lacking (fermentation). [Wikipedia]
Structure
Thumb
Synonyms
  • 2-ketopropionic acid
  • 2-Oxopropanoate
  • 2-Oxopropanoic acid
  • 2-Oxopropionate
  • 2-Oxopropionic acid
  • a-Ketopropionate
  • a-Ketopropionic acid
  • Acetylformate
  • Acetylformic acid
  • alpha-Ketopropionate
  • alpha-Ketopropionic acid
  • BTS
  • Propanoic acid, 2-oxo-
  • Pyroracemate
  • Pyroracemic acid
  • Pyruvate
  • pyruvic acid
  • 2-Oxopropansaeure
  • 2-Oxopropionsaeure
  • Acide pyruvique
  • alpha-Oxopropionsaeure
  • Brenztraubensaeure
  • CH3COCOOH
  • 2-Ketopropionate
  • Α-ketopropionate
  • Α-ketopropionic acid
  • a-Oxopropionsaeure
  • Α-oxopropionsaeure
  • Acid, pyruvic
  • alpha-Ketopropanoic acid
  • α-Ketopropanoic acid
CAS number127-17-3
WeightAverage: 88.0621
Monoisotopic: 88.016043994
InChI KeyLCTONWCANYUPML-UHFFFAOYSA-N
InChIInChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
IUPAC Name2-oxopropanoic acid
Traditional IUPAC Namepyruvic acid
Chemical FormulaC3H4O3
SMILES[H]OC(=O)C(=O)C([H])([H])[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as alpha-keto acids and derivatives. These are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassKeto acids and derivatives
Sub ClassAlpha-keto acids and derivatives
Direct ParentAlpha-keto acids and derivatives
Alternative Parents
Substituents
  • Alpha-keto acid
  • Alpha-hydroxy ketone
  • Ketone
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Carboxylic acid derivative
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateLiquid
Charge0
Melting point13.8 °C
Experimental Properties
PropertyValueReference
Water Solubility1000 mg/mL at 20 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility134 g/LALOGPS
logP-0.38ALOGPS
logP0.066ChemAxon
logS0.18ALOGPS
pKa (Strongest Acidic)2.93ChemAxon
pKa (Strongest Basic)-9.6ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area54.37 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity17.99 m³·mol⁻¹ChemAxon
Polarizability7.31 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondrion
  • Peroxisome
Organoleptic Properties
Flavour/OdourSource
AceticFDB031141
CaramellicFDB031141
SharpFDB031141
SourFDB031141
SMPDB Pathways
Citric Acid CyclePW000952 ThumbThumb?image type=greyscaleThumb?image type=simple
Citric Acid Cycle 1434561204PW000970 ThumbThumb?image type=greyscaleThumb?image type=simple
Cysteine MetabolismPW002383 ThumbThumb?image type=greyscaleThumb?image type=simple
Ethanol fermentationPW002448 ThumbThumb?image type=greyscaleThumb?image type=simple
Glycolysis IPW002386 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Alanine, aspartate and glutamate metabolismec00250 Map00250
Arginine and proline metabolismec00330 Map00330
Butanoate metabolismec00650 Map00650
Citrate cycle (TCA cycle)ec00020 Map00020
Cysteine and methionine metabolismec00270 Map00270
SMPDB Reactions
Pyruvic acid + Coenzyme A + NADAcetyl-CoA + Carbon dioxide + NADH
Pyruvic acid + Thiamine pyrophosphateCarbon dioxide + 2-(a-Hydroxyethyl)thiamine diphosphate
Adenosine triphosphate + Pyruvic acid + Hydrogen carbonateADP + phosphate + Oxalacetic acid
Pyruvic acid + L-Glutamic acidOxoglutaric acid + L-Alanine
L-Valine + Pyruvic acidL-Alanine + Alpha-Ketoisovaleric acid
KEGG Reactions
ferricytochrome c + D-Lactic acid → ferrocytochrome c + Pyruvic acid
L-Lactic acid + ferricytochrome c → ferrocytochrome c + Pyruvic acid
Pyruvic acid + hydron + 2-Ketobutyric acidCarbon dioxide + (S)-2-acetyl-2-hydroxybutanoate
4-amino-4-deoxychorismic acidPyruvic acid + hydron + 4-Aminobenzoic acid
Pyruvic acid + hydronCarbon dioxide + 2-Acetolactate
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
3390 ± 540 µM 20 ml 2% (wt/vol) glucose, 0.5% (wt/vol) ammonium sulfate, 0.17% (wt/vol) yeast nitrogen base without amino acids (Difco, Detroit, MI) and 100 mM potassium phthalate at pH 5.0, supplemented with required nutrients (40 mg/L uracil, 40 mg/L Ltryptophan, 60 aerobicBaker's yeastPMID: 11135551
3380 ± 169 µM YEB media with 0.5 mM glucoseaerobicBaker's yeastExperimentally Determined
Not Available
130 ± 0 µM Minimal medium supplemented with ammonia saltsaerobic;resting cellsBaker's yeastPMID: 4578278
140 ± 80 µM Minimal medium supplemented with ammonia salts and glucoseaerobic and anaerobic;resting cellsBaker's yeastPMID: 4578278
5250 ± 4750 µM Minimal medium supplemented with ammonia salts and (glucose or galactose)aerobic;growing cellsBaker's yeastPMID: 4578278
1600 ± 10 µM Synthetic medium with 2% glucoseaerobic;growing cellsBaker's yeastPMID: 6229402
440 ± 40 µM Synthetic medium with 2% glucoseaerobic;resting cellsBaker's yeastPMID: 6229402
340 ± 110 µM Synthetic medium with 2% glucoseanaerobic;resting cellsBaker's yeastPMID: 6229402
1300 ± 300 µM Synthetic medium with 2% galactoseaerobic;resting cellsBaker's yeastPMID: 6229402
Conversion Details Here
Extracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
1771 ± 273 µM hops, malted barleyanaerobicBaker's yeastPMID: 16448171
118 ± 20 µM Synthetic medium with 20 g/L glucoseaerobicBaker's yeastPMID: 12584756
Conversion Details Here
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-00dr-4900000000-f26ef76666e40ab9fe61JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (1 MEOX; 1 TMS)splash10-00di-5900000000-b8e81f82572d4796e944JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-014i-5970000000-154bf9ad168a12593fccJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-9000000000-a2cf85a5e1d2379d26dfJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00dr-4900000000-f26ef76666e40ab9fe61JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00di-5900000000-b8e81f82572d4796e944JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-014i-5970000000-154bf9ad168a12593fccJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00dr-5900000000-5b1f470d4ff91420618cJSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9000000000-5417b44aa241a7ba27e8JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-00dm-9400000000-6db65a709bdc47e3adf7JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_2) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TBDMS_1_1) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TBDMS_1_2) - 70eV, PositiveNot AvailableJSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - EI-B (HITACHI M-80B) , Positivesplash10-0006-9000000000-a2cf85a5e1d2379d26dfJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-000i-9000000000-dd49835da8355fb6e625JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-000i-9000000000-f09d8e3d7a774b255d89JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-0006-9000000000-7d91f6f626cab1a366fdJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Negativesplash10-0006-9000000000-8ae98cdb3e142034e52aJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Negativesplash10-0006-9000000000-e04e6c68013983e1b6dcJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-000i-9000000000-dd49835da8355fb6e625JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-000i-9000000000-f09d8e3d7a774b255d89JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-0006-9000000000-7d91f6f626cab1a366fdJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-0006-9000000000-8ae98cdb3e142034e52aJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , negativesplash10-0006-9000000000-e04e6c68013983e1b6dcJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 10V, Negativesplash10-000f-9000000000-f24c93ecfd3928827154JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 40V, Negativesplash10-0udj-9000000000-fc3b9ad0c57f44261fbaJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 20V, Negativesplash10-014i-9000000000-f3444f8b94ee5a0a9f74JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 33V, Negativesplash10-0avr-9000000000-dc40a6a1b9b166d6e68aJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 33V, Negativesplash10-016r-9000000000-efac7b176bb77118ecb8JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-9000000000-d0defa72b09503c6d6d1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000f-9000000000-c25fa150e9c490319a2aJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-ccb42b4c05ddd001990fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-000i-9000000000-faf36ff70d6205370270JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-000i-9000000000-60c1a02aabf80f51050fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-000f-9000000000-ca5f4a2f06787d8b62a0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0006-9000000000-0eb1fb2cdd24bdc78601JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0006-9000000000-87bbaed151efac084591JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-87bbaed151efac084591JSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-0006-9000000000-f315d0752893e7d0c657JSpectraViewer | MoNA
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • 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-D676.21062828
  • Raamsdonk, L. M., Teusink, B., Broadhurst, D., Zhang, N., Hayes, A., Walsh, M. C., Berden, J. A., Brindle, K. M., Kell, D. B., Rowland, J. J., Westerhoff, H. V., van Dam, K., Oliver, S. G. (2001). "A functional genomics strategy that uses metabolome data to reveal the phenotype of silent mutations." Nat Biotechnol 19:45-50.11135551
  • 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 26:1155-1160.18846089
  • Ryan, E. D., Kohlhaw, G. B. (1974). "Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast." J Bacteriol 120:631-637.4616942
  • Goncalves, P., Planta, R. J. (1998). "Starting up yeast glycolysis." Trends Microbiol 6:314-319.9746941
  • Luttik, M. A., Kotter, P., Salomons, F. A., van der Klei, I. J., van Dijken, J. P., Pronk, J. T. (2000). "The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism." J Bacteriol 182:7007-7013.11092862
  • Thevelein, J. M., Hohmann, S. (1995). "Trehalose synthase: guard to the gate of glycolysis in yeast?" Trends Biochem Sci 20:3-10.7878741
  • Schwartz, J. M., Kanehisa, M. (2006). "Quantitative elementary mode analysis of metabolic pathways: the example of yeast glycolysis." BMC Bioinformatics 7:186.16584566
  • Takada, Y., Noguchi, T. (1985). "Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates." Biochem J 231:157-163.3933486
  • Almeida, C., Duarte, I. F., Barros, A., Rodrigues, J., Spraul, M., Gil, A. M. (2006). "Composition of beer by 1H NMR spectroscopy: effects of brewing site and date of production." J Agric Food Chem 54:700-706.16448171
  • Hans, M. A., Heinzle, E., Wittmann, C. (2003). "Free intracellular amino acid pools during autonomous oscillations in Saccharomyces cerevisiae." Biotechnol Bioeng 82:143-151.12584756
  • Senac, T., Hahn-Hagerdal, B. (1990). "Intermediary Metabolite Concentrations in Xylulose- and Glucose-Fermenting Saccharomyces cerevisiae Cells." Appl Environ Microbiol 56:120-126.16348083
  • Crombie, T., Boyle, J. P., Coggins, J. R., Brown, A. J. (1994). "The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase." Eur J Biochem 226:657-664.8001582
  • Singh, J., Kumar, D., Ramakrishnan, N., Singhal, V., Jervis, J., Garst, J. F., Slaughter, S. M., DeSantis, A. M., Potts, M., Helm, R. F. (2005). "Transcriptional response of Saccharomyces cerevisiae to desiccation and rehydration." Appl Environ Microbiol 71:8752-8763.16332871
  • Burke, R. L., Tekamp-Olson, P., Najarian, R. (1983). "The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae." J Biol Chem 258:2193-2201.6185493
  • 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 69:4534-4541.12902239
  • Cullin, C., Baudin-Baillieu, A., Guillemet, E., Ozier-Kalogeropoulos, O. (1996). "Functional analysis of YCL09C: evidence for a role as the regulatory subunit of acetolactate synthase." Yeast 12:1511-1518.8972574
  • Gancedo, J. M., Gancedo, C. (1973). "Concentrations of intermediary metabolites in yeast." Biochimie 55:205-211.4578278
  • Lagunas, R., Gancedo, C. (1983). "Role of phosphate in the regulation of the Pasteur effect in Saccharomyces cerevisiae." Eur J Biochem 137:479-483.6229402
Synthesis Reference:Xiang, Wei; Okita, Motomu. Preparation of pyruvic acid. Jpn. Kokai Tokkyo Koho (2003), 5 pp.
External Links:
ResourceLink
CHEBI ID32816
HMDB IDHMDB00243
Pubchem Compound ID1060
Kegg IDC00022
ChemSpider ID1031
FOODB IDFDB031141
WikipediaPyruvic_acid
BioCyc IDPYRUVATE

Enzymes

General function:
Involved in catalytic activity
Specific function:
Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
Gene Name:
TRP3
Uniprot ID:
P00937
Molecular weight:
53488.89844
Reactions
Chorismate + L-glutamine → anthranilate + pyruvate + L-glutamate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate → 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
General function:
Involved in biosynthetic process
Specific function:
Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
Gene Name:
TRP2
Uniprot ID:
P00899
Molecular weight:
56767.0
Reactions
Chorismate + L-glutamine → anthranilate + pyruvate + L-glutamate.
General function:
Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Specific function:
Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA)
Gene Name:
BNA3
Uniprot ID:
P47039
Molecular weight:
50081.89844
Reactions
L-kynurenine + 2-oxoglutarate → 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
General function:
Involved in metabolic process
Specific function:
Has alanine:glyoxylate aminotransferase activity
Gene Name:
AGX1
Uniprot ID:
P43567
Molecular weight:
41906.80078
Reactions
L-alanine + glyoxylate → pyruvate + glycine.
General function:
Involved in oxidoreductase activity
Specific function:
Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine
Gene Name:
LPD1
Uniprot ID:
P09624
Molecular weight:
54009.69922
Reactions
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) → protein N(6)-(lipoyl)lysine + NADH.
General function:
Involved in magnesium ion binding
Specific function:
Second most abundant of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo 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 valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins
Gene Name:
PDC5
Uniprot ID:
P16467
Molecular weight:
61911.60156
Reactions
A 2-oxo acid → an aldehyde + CO(2).
3-(indol-3-yl)pyruvate → 2-(indol-3-yl)acetaldehyde + CO(2).
Phenylpyruvate → phenylacetaldehyde + CO(2).
Pyruvate → Acetaldehyde + CO(2).
A 2-oxo acid + an aldehyde → A 2-hydroxy ketone + CO(2).
An aldehyde + an aldehyde → A 2-hydroxy ketone.
General function:
Involved in magnesium ion binding
Specific function:
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo 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 valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it can not compensate for the other two pyruvate decarboxylases to sustain fermentation
Gene Name:
PDC6
Uniprot ID:
P26263
Molecular weight:
61579.89844
Reactions
A 2-oxo acid → an aldehyde + CO(2).
3-(indol-3-yl)pyruvate → 2-(indol-3-yl)acetaldehyde + CO(2).
Phenylpyruvate → phenylacetaldehyde + CO(2).
Pyruvate → Acetaldehyde + CO(2).
A 2-oxo acid + an aldehyde → A 2-hydroxy ketone + CO(2).
An aldehyde + an aldehyde → A 2-hydroxy ketone.
General function:
Involved in magnesium ion binding
Specific function:
Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo 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 valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins
Gene Name:
PDC1
Uniprot ID:
P06169
Molecular weight:
61494.89844
Reactions
A 2-oxo acid → an aldehyde + CO(2).
3-(indol-3-yl)pyruvate → 2-(indol-3-yl)acetaldehyde + CO(2).
Phenylpyruvate → phenylacetaldehyde + CO(2).
Pyruvate → Acetaldehyde + CO(2).
A 2-oxo acid + an aldehyde → A 2-hydroxy ketone + CO(2).
An aldehyde + an aldehyde → A 2-hydroxy ketone.
General function:
Involved in pyridoxal phosphate binding
Specific function:
L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate
Gene Name:
CYS3
Uniprot ID:
P31373
Molecular weight:
42541.69922
Reactions
L-cystathionine + H(2)O → L-cysteine + NH(3) + 2-oxobutanoate.
General function:
Involved in oxidoreductase activity
Specific function:
Maintains high levels of reduced glutathione in the cytosol
Gene Name:
GLR1
Uniprot ID:
P41921
Molecular weight:
53440.60156
Reactions
2 glutathione + NADP(+) → glutathione disulfide + NADPH.
General function:
Involved in catalytic activity
Specific function:
L-serine = pyruvate + NH(3)
Gene Name:
CHA1
Uniprot ID:
P25379
Molecular weight:
39301.0
Reactions
L-serine → pyruvate + NH(3).
L-threonine → 2-oxobutanoate + NH(3).
General function:
Involved in catalytic activity
Specific function:
L-serine = pyruvate + NH(3)
Gene Name:
SDL1
Uniprot ID:
P0CF21
Molecular weight:
13942.90039
Reactions
L-serine → pyruvate + NH(3).
General function:
Involved in pyridoxal phosphate binding
Specific function:
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate
Gene Name:
STR3
Uniprot ID:
P53101
Molecular weight:
51828.0
Reactions
L-cystathionine + H(2)O → L-homocysteine + NH(3) + pyruvate.
General function:
Involved in pyridoxal phosphate binding
Specific function:
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate
Gene Name:
IRC7
Uniprot ID:
P43623
Molecular weight:
36971.10156
Reactions
L-cystathionine + H(2)O → L-homocysteine + NH(3) + pyruvate.
General function:
Involved in isocitrate lyase activity
Specific function:
Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl- CoA. Does not act on isocitrate
Gene Name:
ICL2
Uniprot ID:
Q12031
Molecular weight:
64975.39844
Reactions
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate → pyruvate + succinate.
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second
Gene Name:
PYC1
Uniprot ID:
P11154
Molecular weight:
130098.0
Reactions
ATP + pyruvate + HCO(3)(-) → ADP + phosphate + oxaloacetate.
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Gene Name:
FAS3
Uniprot ID:
Q00955
Molecular weight:
250351.0
Reactions
ATP + acetyl-CoA + HCO(3)(-) → ADP + phosphate + malonyl-CoA.
ATP + biotin-[carboxyl-carrier-protein] + CO(2) → ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
General function:
Involved in magnesium ion binding
Specific function:
ATP + pyruvate = ADP + phosphoenolpyruvate
Gene Name:
PYK1
Uniprot ID:
P00549
Molecular weight:
54544.10156
Reactions
ATP + pyruvate → ADP + phosphoenolpyruvate.
General function:
Involved in magnesium ion binding
Specific function:
May be used by cells under conditions in which the level of glycolytic flux is very low
Gene Name:
PYK2
Uniprot ID:
P52489
Molecular weight:
55194.69922
Reactions
ATP + pyruvate → ADP + phosphoenolpyruvate.
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second
Gene Name:
PYC2
Uniprot ID:
P32327
Molecular weight:
130166.0
Reactions
ATP + pyruvate + HCO(3)(-) → ADP + phosphate + oxaloacetate.
General function:
Involved in oxidoreductase activity
Specific function:
(S)-malate + NAD(+) = pyruvate + CO(2) + NADH
Gene Name:
MAE1
Uniprot ID:
P36013
Molecular weight:
74375.29688
Reactions
(S)-malate + NAD(+) → pyruvate + CO(2) + NADH.
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity and kynurenine aminotransferase activity
Gene Name:
ARO9
Uniprot ID:
P38840
Molecular weight:
58527.0
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
General function:
Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Specific function:
L-alanine + 2-oxoglutarate = pyruvate + L- glutamate
Gene Name:
ALT2
Uniprot ID:
P52892
Molecular weight:
56769.30078
Reactions
L-alanine + 2-oxoglutarate → pyruvate + L-glutamate.
General function:
Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Specific function:
L-alanine + 2-oxoglutarate = pyruvate + L- glutamate
Gene Name:
ALT1
Uniprot ID:
P52893
Molecular weight:
66421.10156
Reactions
L-alanine + 2-oxoglutarate → pyruvate + L-glutamate.
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)
Gene Name:
PDA1
Uniprot ID:
P16387
Molecular weight:
46342.69922
Reactions
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine → [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
General function:
Involved in catalytic activity
Specific function:
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
Gene Name:
CYB2
Uniprot ID:
P00175
Molecular weight:
65538.79688
Reactions
(S)-lactate + 2 ferricytochrome c → pyruvate + 2 ferrocytochrome c + 2 H(+).
General function:
Involved in catalytic activity
Specific function:
Catalyzes the stereospecific oxidation of D-lactate to pyruvate
Gene Name:
DLD1
Uniprot ID:
P32891
Molecular weight:
65291.89844
Reactions
(R)-lactate + 2 ferricytochrome c → pyruvate + 2 ferrocytochrome c.
General function:
Involved in catalytic activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)
Gene Name:
PDB1
Uniprot ID:
P32473
Molecular weight:
40053.19922
Reactions
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine → [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
General function:
Involved in catalytic activity
Specific function:
(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c
Gene Name:
DLD3
Uniprot ID:
P39976
Molecular weight:
55224.5
Reactions
(R)-lactate + 2 ferricytochrome c → pyruvate + 2 ferrocytochrome c.
General function:
Involved in magnesium ion binding
Specific function:
2 pyruvate = 2-acetolactate + CO(2)
Gene Name:
ILV2
Uniprot ID:
P07342
Molecular weight:
74936.29688
Reactions
2 pyruvate → 2-acetolactate + CO(2).
General function:
Involved in catalytic activity
Specific function:
In addition to its enzymatic role it could play an important role in the yeast cell morphology
Gene Name:
DLD2
Uniprot ID:
P46681
Molecular weight:
59268.0
Reactions
(R)-lactate + 2 ferricytochrome c → pyruvate + 2 ferrocytochrome c.
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC1
Uniprot ID:
P00044
Molecular weight:
12181.90039
Reactions
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC7
Uniprot ID:
P00045
Molecular weight:
12532.2998
Reactions
General function:
Involved in D-serine ammonia-lyase activity
Specific function:
Converts specifically D-serine to pyruvate and ammonia. May play a role in D-serine detoxification
Gene Name:
DSD1
Uniprot ID:
P53095
Molecular weight:
47827.39844
Reactions
D-serine → pyruvate + NH(3).
General function:
Involved in catalytic activity
Specific function:
Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate
Gene Name:
ABZ2
Uniprot ID:
Q03266
Molecular weight:
42639.39844
Reactions
4-amino-4-deoxychorismate → 4-aminobenzoate + pyruvate.

Transporters

General function:
Involved in carbohydrate transmembrane transporter activity
Specific function:
Essential to lactate transport
Gene Name:
JEN1
Uniprot ID:
P36035
Molecular weight:
69375.60156