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 IDYMDB00071
Name2-Ketobutyric acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionAlpha-Ketoglutaric acid (2-oxobutanoate, 2-keto-butyrate) is a key intermediate in the Krebs cycle. It is involved in the metabolism of many amino acids (glycine, methionine, valine, leucine, serine, threonine, isoleucine) as well as propanoate metabolism and C-5 branched dibasic acid metabolism. It can be converted to propionyl-CoA and thus enter the citric acid cycle.
Structure
Thumb
Synonyms
  • 2-Ketobutanoate
  • 2-Ketobutanoic acid
  • 2-ketobutyrate
  • 2-ketobutyric acid
  • 2-Oxo-Butanoate
  • 2-Oxo-Butanoic acid
  • 2-oxo-Butyrate
  • 2-oxo-Butyric acid
  • 2-Oxo-n-butyrate
  • 2-Oxo-n-butyric acid
  • 2-Oxobutanoate
  • 2-Oxobutanoic acid
  • 2-Oxobutyrate
  • 2-Oxobutyric acid
  • 3-Methylpyruvate
  • 3-Methylpyruvic acid
  • a-keto-n-Butyrate
  • a-keto-n-Butyric acid
  • a-Ketobutyrate
  • a-Ketobutyric acid
  • a-Oxo-n-butyrate
  • a-Oxo-n-butyric acid
  • a-Oxobutyrate
  • a-Oxobutyric acid
  • alpha-Keto-n-butyrate
  • alpha-Keto-n-butyric acid
  • alpha-Ketobutric acid
  • alpha-Ketobutyrate
  • alpha-Ketobutyric acid
  • alpha-Oxo-n-butyrate
  • alpha-Oxo-n-butyric acid
  • alpha-Oxobutyrate
  • alpha-Oxobutyric acid
  • Butanoic acid, 2-oxo-
  • Butyric acid, 2-oxo-
  • Formic acid, propionyl-
  • Ketobutyrate
  • methyl-Pyruvate
  • methyl-Pyruvic acid
  • Oxobutyrate
  • propionyl-formate
  • propionyl-formic acid
  • Pyruvic acid, methyl-
  • Α-ketobutyrate
  • Α-ketobutyric acid
  • Α-oxo-N-butyrate
  • Α-oxo-N-butyric acid
  • 3-Methyl pyruvate
  • alpha-Ketobutyric acid, sodium salt
  • 3-Methyl pyruvic acid
CAS number600-18-0
WeightAverage: 102.0886
Monoisotopic: 102.031694058
InChI KeyTYEYBOSBBBHJIV-UHFFFAOYSA-N
InChIInChI=1S/C4H6O3/c1-2-3(5)4(6)7/h2H2,1H3,(H,6,7)
IUPAC Name2-oxobutanoic acid
Traditional IUPAC Name2-oxobutanoic acid
Chemical FormulaC4H6O3
SMILES[H]OC(=O)C(=O)C([H])([H])C([H])([H])[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as short-chain keto acids and derivatives. These are keto acids with an alkyl chain the contains less than 6 carbon atoms.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassKeto acids and derivatives
Sub ClassShort-chain keto acids and derivatives
Direct ParentShort-chain keto acids and derivatives
Alternative Parents
Substituents
  • Short-chain keto acid
  • 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
StateSolid
Charge0
Melting point33°C
Experimental Properties
PropertyValueReference
Water Solubility119 mg/mL [HMP experimental]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility79.2 g/LALOGPS
logP0.07ALOGPS
logP0.77ChemAxon
logS-0.11ALOGPS
pKa (Strongest Acidic)3.19ChemAxon
pKa (Strongest Basic)-9.7ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area54.37 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity22.62 m³·mol⁻¹ChemAxon
Polarizability9.2 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
BrownFDB030356
CaramelFDB030356
CreamyFDB030356
LactonicFDB030356
SweetFDB030356
SMPDB Pathways
Cysteine MetabolismPW002383 ThumbThumb?image type=greyscaleThumb?image type=simple
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
Selenocompound metabolismPW002472 ThumbThumb?image type=greyscaleThumb?image type=simple
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
isoleucine biosynthesisPW002476 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Glycine, serine and threonine metabolismec00260 Map00260
Propanoate metabolismec00640 Map00640
Selenocompound metabolismec00450 Map00450
Sulfur metabolismec00920 Map00920
SMPDB Reactions
water + L-CystathionineAmmonium + L-Cysteine + 2-Ketobutyric acid
4-Methylthio-2-oxobutanoate + L-PhenylalanineL-Methionine + 2-Ketobutyric acid
2-Ketobutyric acid + hydron + Pyruvic acidCarbon dioxide + (S)-2-Aceto-2-hydroxybutanoic acid
Selenomethionine + watermethylselenol + Ammonia + 2-Ketobutyric acid
KEGG Reactions
Pyruvic acid + hydron + 2-Ketobutyric acidCarbon dioxide + (S)-2-acetyl-2-hydroxybutanoate
NAD + 2-hydroxybutyric acidNADH + hydron + 2-Ketobutyric acid
NAD + Coenzyme A + 2-Ketobutyric acidNADH + propionyl-CoA + Carbon dioxide
L-Cystathionine + waterL-Cysteine + Ammonium + 2-Ketobutyric acid
L-ThreonineAmmonium + 2-Ketobutyric acid
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • 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
  • Yamagata, S., Yasugahira, T., Okuda, Y., Iwama, T. (2003). "Conversion of the aminocrotonate intermediate limits the rate of gamma-elimination reaction catalyzed by L-cystathionine gamma-lyase of the yeast Saccharomyces cerevisiae." J Biochem 134:607-613.14607989
  • 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
Synthesis Reference:Figge, Rainer; Lux, Fabien; Raynaud, Celine; Soucaille, Philippe. Production of a-ketobutyrate by engineered Escherichia coli.PCT Int. Appl. (2006), 31pp.
External Links:
ResourceLink
CHEBI ID30831
HMDB IDHMDB00005
Pubchem Compound ID58
Kegg IDC00109
ChemSpider ID57
FOODB IDFDB030356
WikipediaAlpha-ketobutyric_acid
BioCyc ID2-OXOBUTANOATE

Enzymes

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 pyridoxal phosphate binding
Specific function:
O(4)-succinyl-L-homoserine + L-cysteine = L- cystathionine + succinate
Gene Name:
Not Available
Uniprot ID:
Q04533
Molecular weight:
74312.70313
Reactions
O(4)-succinyl-L-homoserine + L-cysteine → L-cystathionine + succinate.
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 catalytic activity
Specific function:
L-threonine = 2-oxobutanoate + NH(3)
Gene Name:
ILV1
Uniprot ID:
P00927
Molecular weight:
63830.69922
Reactions
L-threonine → 2-oxobutanoate + NH(3).
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 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 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).