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Identification
YMDB IDYMDB00365
NameAlpha-Ketoisovaleric acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
Descriptionalpha-Ketoisovaleric acid (3-methyl-2-oxobutanoate) is a branched chain organic acid and a precursor to leucine and valine synthesis. It is also a degradation product from valine and the starting compound for R-pantothenate (vitamin B5) biosynthesis pathway. The enzyme dihydroxy-acid dehydratase catalyzes the fourth step in the biosynthesis of isoleucine and valine, through the dehydration of 2,3-dihydroxy-isovaleic acid into alpha-ketoisovaleric acid.
Structure
Thumb
Synonyms
  • 2-keto-3-Methylbutyrate
  • 2-keto-3-Methylbutyric acid
  • 2-keto-isovalerate
  • 2-Ketoisovalerate
  • 2-Ketoisovaleric acid
  • 2-ketovaline
  • 2-Oxo-3-methylbutanoate
  • 2-Oxo-3-methylbutanoic acid
  • 2-Oxo-3-methylbutyrate
  • 2-Oxo-3-methylbutyric acid
  • 2-oxoisopentanoate
  • 2-Oxoisovalerate
  • 2-Oxoisovaleric acid
  • 3-methyl-2-oxo-Butanoate
  • 3-methyl-2-oxo-Butanoic acid
  • 3-methyl-2-oxo-Butyrate
  • 3-methyl-2-oxo-Butyric acid
  • 3-Methyl-2-oxobutanoate
  • 3-Methyl-2-oxobutanoic acid
  • 3-Methyl-2-oxobutinoate
  • 3-Methyl-2-oxobutinoic acid
  • 3-Methyl-2-oxobutyrate
  • 3-Methyl-2-oxobutyric acid
  • a-keto-b-Methylbutyrate
  • a-keto-b-Methylbutyric acid
  • a-keto-Isovalerate
  • a-keto-Isovaleric acid
  • a-Ketoisovalerate
  • a-ketoisovaleric acid
  • a-Oxo-b-methylbutyrate
  • a-Oxo-b-methylbutyric acid
  • a-Oxoisovalerate
  • a-Oxoisovaleric acid
  • alpha-keto-beta-Methylbutyrate
  • alpha-keto-beta-Methylbutyric acid
  • alpha-keto-Isovalerate
  • alpha-keto-Isovaleric acid
  • alpha-keto-valine
  • alpha-ketoisopentanoic acid
  • alpha-Ketoisovalerate
  • alpha-Ketoisovaleric acid
  • alpha-ketovaline
  • alpha-Oxo-beta-methylbutyrate
  • alpha-Oxo-beta-methylbutyric acid
  • alpha-Oxoisovalerate
  • alpha-Oxoisovaleric acid
  • Dimethylpyruvate
  • Dimethylpyruvic acid
  • Isopropylglyoxylate
  • Isopropylglyoxylic acid
  • Ketovaline
  • alpha-oxo-beta-Methylbutyricacid
  • Α-keto-isovalerate
  • Α-keto-isovaleric acid
  • a-Ketovaline
  • Α-ketovaline
  • a-oxo-b-Methylbutyricacid
  • Α-oxo-β-methylbutyricacid
  • Α-oxoisovalerate
  • Α-oxoisovaleric acid
  • 2-Oxoisopentanoic acid
  • Α-ketoisovalerate
  • Α-ketoisovaleric acid
  • 2-Ketoisvaleric acid
  • 2-oxo-3-Methyl-butyrate
CAS number759-05-7
WeightAverage: 116.1152
Monoisotopic: 116.047344122
InChI KeyQHKABHOOEWYVLI-UHFFFAOYSA-N
InChIInChI=1S/C5H8O3/c1-3(2)4(6)5(7)8/h3H,1-2H3,(H,7,8)
IUPAC Name3-methyl-2-oxobutanoic acid
Traditional IUPAC Nameα-ketoisovalerate
Chemical FormulaC5H8O3
SMILES[H]OC(=O)C(=O)C([H])(C([H])([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
  • 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 point31.5 °C
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility30.2 g/LALOGPS
logP0.49ALOGPS
logP1.31ChemAxon
logS-0.59ALOGPS
pKa (Strongest Acidic)3.37ChemAxon
pKa (Strongest Basic)-9.7ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area54.37 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity27.19 m³·mol⁻¹ChemAxon
Polarizability11.04 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
FruityFDB030441
SMPDB Pathways
Pantothenate and CoA biosynthesisPW002463 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
Valine DegradationPW002489 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Pantothenate and CoA biosynthesisec00770 Map00770
Pyruvate metabolismec00620 Map00620
Valine, leucine and isoleucine biosynthesisec00290 Map00290
Valine, leucine and isoleucine degradationec00280 Map00280
SMPDB Reactions
L-Valine + Pyruvic acidL-Alanine + Alpha-Ketoisovaleric acid
Alpha-Ketoisovaleric acid + L-Glutamic acidOxoglutaric acid + L-Valine
Alpha-Ketoisovaleric acid + hydronCarbon dioxide + isobutyraldehyde
2-Isopropylmalic acid + Coenzyme AAcetyl-CoA + water + Alpha-Ketoisovaleric acid
Alpha-Ketoisovaleric acid + 5,10-Methylene-THF + waterTetrahydrofolic acid + 2-Dehydropantoate
KEGG Reactions
Acetyl-CoA + Alpha-Ketoisovaleric acid + water2-Isopropylmalic acid + hydron + Coenzyme A
Alpha-Ketoisovaleric acid + hydronCarbon dioxide + isobutyraldehyde
Alpha-Ketoisovaleric acid + water + 5,10-Methylene-THF2-Dehydropantoic acid + 5,6,7,8-Tetrahydrofolic acid
(R)-2,3-Dihydroxy-isovalerateAlpha-Ketoisovaleric acid + water
Oxoglutaric acid + L-ValineL-Glutamic acid + Alpha-Ketoisovaleric 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
  • 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
  • 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
  • Chang, L. F., Cunningham, T. S., Gatzek, P. R., Chen, W. J., Kohlhaw, G. B. (1984). "Cloning and characterization of yeast Leu4, one of two genes responsible for alpha-isopropylmalate synthesis." Genetics 108:91-106.6090272
  • Dickinson, J. R., Harrison, S. J., Hewlins, M. J. (1998). "An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae." J Biol Chem 273:25751-25756.9748245
  • 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
Synthesis Reference:Pirrung, Michael C.; Ha, Hyun Joon; Holmes, Christopher P. Purification and inhibition of spinach a,b-dihydroxyacid dehydratase . Journal of Organic Chemistry (1989), 54(7), 1543-8.
External Links:
ResourceLink
CHEBI ID16530
HMDB IDHMDB00019
Pubchem Compound ID49
Kegg IDC00141
ChemSpider ID48
FOODB IDFDB030441
WikipediaAlpha-Ketoisovaleric_acid
BioCyc ID2-KETO-ISOVALERATE

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 2-isopropylmalate synthase activity
Specific function:
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible of about 20% of alpha-IPMS activity. Involved in leucine synthesis
Gene Name:
LEU9
Uniprot ID:
Q12166
Molecular weight:
67199.60156
Reactions
Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O → (2S)-2-isopropylmalate + CoA.
General function:
Involved in 2-isopropylmalate synthase activity
Specific function:
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate)
Gene Name:
LEU4
Uniprot ID:
P06208
Molecular weight:
68408.29688
Reactions
Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O → (2S)-2-isopropylmalate + CoA.
General function:
Involved in 3-methyl-2-oxobutanoate hydroxymethyltransferase activity
Specific function:
5,10-methylenetetrahydrofolate + 3-methyl-2- oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate
Gene Name:
ECM31
Uniprot ID:
P38122
Molecular weight:
34464.69922
Reactions
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O → tetrahydrofolate + 2-dehydropantoate.
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.