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Identification
YMDB IDYMDB00168
Name(S)-3-methyl-2-oxovaleric acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
Description(S)-3-methyl-2-oxopentanoate, also known as (S)-2-oxo-3-methylpentanoic acid or (S)-OMV, 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 (S)-3-methyl-2-oxopentanoate is a very hydrophobic molecule, practically insoluble (in water), and relatively neutral (S)-3-methyl-2-oxopentanoate exists in both E. coli (prokaryote) and yeast (eukaryote).
Structure
Thumb
Synonyms
  • (3R)-3-Methyl-2-oxopentanoate
  • (3R)-3-Methyl-2-oxopentanoic acid
  • (3S)-3-Methyl-2-oxopentanoate
  • (3S)-3-Methyl-2-oxopentanoic acid
  • (r)-2-oxo-3-methylpentanoate
  • (r)-3-methyl-2-oxopentanoate
  • (r)-3-methyl-2-oxopentanoic acid
  • (s)-2-oxo-3-methylpentanoate
  • (S)-3-methyl-2-oxopentanoate
  • (S)-3-methyl-2-oxopentanoic acid
  • (S)-3-methyl-2-oxovalerate
  • 2-Oxo-3-methyl-n-valerate
  • 2-Oxo-3-methyl-n-valeric acid
  • 2-Oxo-3-methylpentanoate
  • 2-Oxo-3-methylpentanoic acid
  • 2-Oxo-3-methylvalerate
  • 2-Oxo-3-methylvaleric acid
  • 2-Oxoisoleucine
  • 2-oxokolavenate
  • 2-oxokolavenic acid
  • 3-methyl-2-oxo-pentanoate
  • 3-methyl-2-oxo-pentanoic acid
  • 3-methyl-2-oxo-Valerate
  • 3-methyl-2-oxo-Valeric acid
  • 3-Methyl-2-oxopentanoate
  • 3-Methyl-2-oxopentanoic acid
  • 3-Methyl-2-oxovalerate
  • 3-Methyl-2-oxovaleric
  • a-keto-b-Methyl-n-valerate
  • a-keto-b-Methyl-n-valeric acid
  • a-Keto-b-methylvalerate
  • a-Keto-b-methylvaleric acid
  • a-Oxo-b-methyl-n-valerate
  • a-Oxo-b-methyl-n-valeric acid
  • a-Oxo-b-methylvalerate
  • a-Oxo-b-methylvaleric acid
  • alpha-keto-beta-Methyl-n-valerate
  • alpha-keto-beta-Methyl-n-valeric acid
  • alpha-Keto-beta-methylvalerate
  • alpha-keto-beta-methylvaleric acid
  • alpha-Oxo-beta-methyl-n-valerate
  • alpha-Oxo-beta-methyl-n-valeric acid
  • alpha-Oxo-beta-methylvalerate
  • alpha-Oxo-beta-methylvaleric acid
  • ketoisoleucine
  • (3S)-2-oxo-3-Methyl-N-valeric acid
  • (S)-2-oxo-3-Methylpentanoic acid
  • (S)-OMV
  • (3S)-2-oxo-3-Methyl-N-valerate
  • 3S-Methyl-2-oxo-pentanoate
CAS number1460-34-0
WeightAverage: 130.1418
Monoisotopic: 130.062994186
InChI KeyJVQYSWDUAOAHFM-BYPYZUCNSA-N
InChIInChI=1S/C6H10O3/c1-3-4(2)5(7)6(8)9/h4H,3H2,1-2H3,(H,8,9)/t4-/m0/s1
IUPAC Name(3S)-3-methyl-2-oxopentanoic acid
Traditional IUPAC Name(S)-omv
Chemical FormulaC6H10O3
SMILESCC[C@H](C)C(=O)C(O)=O
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
  • Branched fatty acid
  • Methyl-branched fatty acid
  • Short-chain keto acid
  • Alpha-keto acid
  • Fatty acyl
  • Alpha-hydroxy ketone
  • Ketone
  • Carboxylic acid derivative
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Carbonyl group
  • Hydrocarbon derivative
  • Organic oxygen compound
  • Organooxygen compound
  • Organic oxide
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water Solubility915.5 mg/mL [sodium salt, HMP experimental]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility9.86 g/LALOGPS
logP1ALOGPS
logP1.75ChemAxon
logS-1.1ALOGPS
pKa (Strongest Acidic)3.52ChemAxon
pKa (Strongest Basic)-9.7ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area54.37 ŲChemAxon
Rotatable Bond Count3ChemAxon
Refractivity31.79 m³·mol⁻¹ChemAxon
Polarizability12.98 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cell Envelope
  • Cytoplasm
  • Endoplasmic Reticulum
  • Extracellular
  • Lipid Particle
  • Mitochondrion
Organoleptic PropertiesNot Available
SMPDB Pathways
Isoleucine degradationPW002491 ThumbThumb?image type=greyscaleThumb?image type=simple
Leucine BiosynthesisPW002475 ThumbThumb?image type=greyscaleThumb?image type=simple
isoleucine biosynthesisPW002476 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Valine, leucine and isoleucine biosynthesisec00290 Map00290
Valine, leucine and isoleucine degradationec00280 Map00280
SMPDB Reactions
(S)-3-methyl-2-oxovaleric acid + hydron2-Methylbutanal + Carbon dioxide
(R)-2,3-Dihydroxy-3-methylvaleratewater + (S)-3-methyl-2-oxovaleric acid
(S)-3-methyl-2-oxovaleric acid + water + Acetyl-CoACoenzyme A + hydron + 2-Isopropylmalic acid
(S)-3-methyl-2-oxovaleric acid + L-Glutamic acidOxoglutaric acid + L-Isoleucine
L-Isoleucine + Oxoglutaric acidL-Glutamic acid + (S)-3-methyl-2-oxovaleric acid
KEGG Reactions
hydron + (S)-3-methyl-2-oxovaleric acid2-Methylbutanal + Carbon dioxide
(R)-2,3-Dihydroxy-3-methylvaleratewater + (S)-3-methyl-2-oxovaleric acid
Oxoglutaric acid + L-IsoleucineL-Glutamic acid + (S)-3-methyl-2-oxovaleric 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
  • 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
  • Kispal, G., Steiner, H., Court, D. A., Rolinski, B., Lill, R. (1996). "Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein." J Biol Chem 271:24458-24464.8798704
Synthesis Reference:Kondo, Shigeo; Sudo, Tetsuji; Ogiwara, Mitsuo; Takeuchi, Hiroshi. a-Oxo-b-methyl-n-valeric acid and its salts. Jpn. Kokai Tokkyo Koho (1979), 3 pp.
External Links:
ResourceLink
CHEBI ID15614
HMDB IDHMDB00491
Pubchem Compound ID439286
Kegg IDC00671
ChemSpider ID388419
FOODB IDFDB030164
Wikipedia IDNot Available
BioCyc ID2-KETO-3-METHYL-VALERATE

Enzymes

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 catalytic activity
Specific function:
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Involved in cell cycle regulation
Gene Name:
BAT2
Uniprot ID:
P47176
Molecular weight:
41624.39844
Reactions
L-leucine + 2-oxoglutarate → 4-methyl-2-oxopentanoate + L-glutamate.
2-oxoglutaric acid + L-isoleucine → (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.
2-oxoglutaric acid + L-valine → 3-methyl-2-oxobutanoic acid + L-glutamic acid.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1
Gene Name:
BAT1
Uniprot ID:
P38891
Molecular weight:
43595.69922
Reactions
L-leucine + 2-oxoglutarate → 4-methyl-2-oxopentanoate + L-glutamate.
2-oxoglutaric acid + L-isoleucine → (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.
2-oxoglutaric acid + L-valine → 3-methyl-2-oxobutanoic acid + L-glutamic acid.
General function:
Involved in magnesium ion binding
Specific function:
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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, phenylalanine, tryptophan, (and probably tyrosine), but also isoleucine, whereas leucine is a low efficiency and valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins
Gene Name:
ARO10
Uniprot ID:
Q06408
Molecular weight:
71383.79688
Reactions
A 2-oxo acid → an aldehyde + CO(2).
Phenylpyruvate → phenylacetaldehyde + CO(2).
3-(indol-3-yl)pyruvate → 2-(indol-3-yl)acetaldehyde + CO(2).
General function:
Involved in metabolic process
Specific function:
2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- oxobutanoate + H(2)O
Gene Name:
ILV3
Uniprot ID:
P39522
Molecular weight:
62860.60156
Reactions
2,3-dihydroxy-3-methylbutanoate → 3-methyl-2-oxobutanoate + H(2)O.
General function:
Involved in magnesium ion binding
Specific function:
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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 leucine and isoleucine, whereas valine, aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission
Gene Name:
THI3
Uniprot ID:
Q07471
Molecular weight:
68365.79688
Reactions
A 2-oxo acid → an aldehyde + CO(2).