Escherichia coli K-12 substr. MG1655 Compound: 2-oxobutanoate

Systematic Name: 2-oxobutanoic acid

Synonyms: 2-oxobutyrate, 2-ketobutyrate, 2-oxobutyric acid, α-oxobutyric acid, α-ketobutyrate, α-ketobutyric acid, 2-oxo-butyrate, 2-keto-butyrate, 2-ketobutyric acid, a-ketobutyric acid

Superclasses: an acidall carboxy acidsa carboxylatea 2-oxo acida 2-oxo carboxylate
an acidall carboxy acidsa carboxylatea 2-oxo carboxylate

Chemical Formula: C4H5O3

Molecular Weight: 101.08 Daltons

Monoisotopic Molecular Weight: 102.0316940589 Daltons

2-oxobutanoate compound structure


InChI: InChI=1S/C4H6O3/c1-2-3(5)4(6)7/h2H2,1H3,(H,6,7)/p-1


Unification Links: CAS:600-18-0, ChEBI:16763, ChemSpider:2829426, HMDB:HMDB00005, IAF1260:33889, KEGG:C00109, MetaboLights:MTBLC16763, PubChem:3593277

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -111.07

Reactions known to consume the compound:

L-isoleucine biosynthesis I (from threonine) :
pyruvate + 2-oxobutanoate + H+ → (S)-2-aceto-2-hydroxybutanoate + CO2

L-threonine degradation I :
2-oxobutanoate + coenzyme A → propanoyl-CoA + formate

Reactions known to produce the compound:

L-isoleucine biosynthesis I (from threonine) , L-threonine degradation I :
2-iminobutanoate + H+ + H2O → 2-oxobutanoate + ammonium

Not in pathways:
L-threonine → 2-oxobutanoate + ammonium
O-succinyl-L-homoserine + H2O → 2-oxobutanoate + succinate + ammonium + H+

Not in pathways:
a D-amino acid + an electron-transfer quinone[inner membrane] + H2O → ammonium + a 2-oxo carboxylate + an electron-transfer quinol[inner membrane]

Not in pathways:
a carboxylic ester + H2O → an alcohol + a carboxylate + H+
an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+
an acyl phosphate + H2O → a carboxylate + phosphate + H+
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 1-acyl 2-lyso-phosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+

In Reactions of unknown directionality:

Not in pathways:
an aminated amino group donor + 2-oxobutanoate = 2-aminobutanoate + a deaminated amino group donor

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:

In Redox half-reactions:
a 2-oxo carboxylate[in] + ammonium[in] + 2 H+[in] + 2 e-[membrane] → a D-amino acid[in] + H2O[in]

Enzymes activated by 2-oxobutanoate, sorted by the type of activation, are:

Activator (Mechanism unknown) of: D-lactate dehydrogenase [Tarmy68]

Enzymes inhibited by 2-oxobutanoate, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: threonine dehydratase [Shizuta73], pyruvate dehydrogenase [Saumweber81, Bisswanger81] Inhibitor (Mechanism unknown) of: acetolactate synthase [deFelice78]

This compound has been characterized as an alternative substrate of the following enzymes: pyruvate oxidase, acetohydroxybutanoate synthase, putrescine aminotransferase, diamine transaminase

In Growth Media: PMA carbon source test + 2-oxobutanoate


Bisswanger81: Bisswanger H (1981). "Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli." J Biol Chem 256(2);815-22. PMID: 7005225

deFelice78: de Felice M, Squires C, Levinthal M "A comparative study of the acetohydroxy acid synthase isoenzymes of Escherichia coli K-12." BBA 1978;541:9-17.

Saumweber81: Saumweber H, Binder R, Bisswanger H (1981). "Pyruvate dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Purification and characterization." Eur J Biochem 1981;114(2);407-11. PMID: 7011811

Shizuta73: Shizuta Y, Kurosawa A, Inoue K, Tanabe T, Hayaishi O (1973). "Regulation of biodegradative threonine deaminase. I. Allosteric inhibition of the enzyme by a reaction product and its reversal by adenosin 5'-monophosphate." J Biol Chem 248(2);512-20. PMID: 4346334

Tarmy68: Tarmy EM, Kaplan NO (1968). "Kinetics of Escherichia coli B D-lactate dehydrogenase and evidence for pyruvate-controlled change in conformation." J Biol Chem 1968;243(10);2587-96. PMID: 4297266

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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