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isobutyraldehyde (YMDB00482)

Identification
YMDB IDYMDB00482
Nameisobutyraldehyde
SpeciesSaccharomyces cerevisiae
StrainBrewer's yeast
Description2-Methylpropanal, also known as isobutanal or isobutylaldehyde, belongs to the class of organic compounds known as short-chain aldehydes. These are an aldehyde with a chain length containing between 2 and 5 carbon atoms. 2-Methylpropanal exists in all eukaryotes, ranging from yeast to plants to humans. In yeast, 2-methylpropanal is involved in the metabolic pathway called the valine degradation pathway. Based on a literature review a significant number of articles have been published on 2-Methylpropanal.
Structure
Thumb
MOLSDF3D-SDFPDBSMILESInChI View 3D Structure
Synonyms
  • α-Methylpropionaldehyde
  • 2-Methyl-1-propanal
  • 2-Methylpropanal
  • 2-Methylpropanal oxime
  • 2-Methylpropionaldehyde
  • alpha-Methylpropionaldehyde
  • iso-C3H7CHO
  • Isobutaldehyde
  • Isobutanal
  • Isobutanal oxime
  • Isobutylaldehyde
  • Isobutyraldehyd
  • Isobutyraldehyde oxime
  • Isobutyric aldehyde
  • Isobutyryl aldehyde
  • Isopropylaldehyde
  • Isopropylformaldehyde
  • Methyl propanal
  • Propanal, 2-methyl-
  • Propionaldehyde, 2-methyl-
  • so-Butyl aldehyde
  • Valine aldehyde
  • a-Methylpropionaldehyde
  • Α-methylpropionaldehyde
  • 2-METHYL-propanal
  • 2-Methyl-propionaldehyde
  • alpha -Methylpropionaldehyde
  • Butyric iso aldehyde
  • FEMA 2220
  • iso-Butyraldehyde
  • Isobutyl aldehy de
  • Isobutyl aldehyde
  • Isobutyral
  • Isobutyraldehyde
  • Isopropyl aldehyde
  • Isopropyl formaldehyde
  • Methylpropanal
CAS number78-84-2
WeightAverage: 72.1057
Monoisotopic: 72.057514878
InChI KeyAMIMRNSIRUDHCM-UHFFFAOYSA-N
InChIInChI=1S/C4H8O/c1-4(2)3-5/h3-4H,1-2H3
IUPAC Name2-methylpropanal
Traditional IUPAC Nameisobutyraldehyde
Chemical FormulaC4H8O
SMILES[H]C(=O)C(C)C
Chemical Taxonomy
Description belongs to the class of organic compounds known as short-chain aldehydes. These are an aldehyde with a chain length containing between 2 and 5 carbon atoms.
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassCarbonyl compounds
Direct ParentShort-chain aldehydes
Alternative Parents
Substituents
  • Organic oxide
  • Hydrocarbon derivative
  • Short-chain aldehyde
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateLiquid
Charge0
Melting point-65.9 °C
Experimental Properties
PropertyValueReference
Water Solubility89 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility53.7 g/LALOGPS
logP0.6ALOGPS
logP0.86ChemAxon
logS-0.13ALOGPS
pKa (Strongest Acidic)17.85ChemAxon
pKa (Strongest Basic)-7ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area17.07 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity20.92 m³·mol⁻¹ChemAxon
Polarizability8.24 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
AldehydicFDB003271
FloralFDB003271
FreshFDB003271
GreenFDB003271
MaltFDB003271
PungentFDB003271
SMPDB Pathways
Valine DegradationPW002489 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
isobutyraldehyde + NADH + hydron → isobutanol + NAD
Alpha-Ketoisovaleric acid + hydron → Carbon dioxide + isobutyraldehyde
KEGG Reactions
Alpha-Ketoisovaleric acid + hydron → Carbon dioxide + isobutyraldehyde
NADH + isobutyraldehyde + hydron → NAD + isobutanol
isobutyraldehyde + NADPH + hydron → NADP + isobutanol
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-002f-9000000000-987cd15323d99af9f551JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-9000000000-1fed4d315b146112b21eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-002f-9000000000-987cd15323d99af9f551JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-9000000000-1fed4d315b146112b21eJSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9000000000-dc3ff3769744ad1ee9d0JSpectraViewer
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 LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9000000000-58d96802e35b00bb3438JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00di-9000000000-935757dca5822bf99c59JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-052f-9000000000-70f55b8222bfdf58adb0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-def551c4e49daf8d790bJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-db936d35c1e102f7ca97JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0ab9-9000000000-342576c8a51a5b054f42JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0a4i-9000000000-63d5fc7a9f901fbe55c2JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-a74f47a36c87271fae62JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-1473b269db466f1a2bf2JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-77e5dcf17bd83eca2c67JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-53cc0c445db79b43e5ffJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4i-9000000000-e6db48dafcc5dffdf942JSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-0006-9000000000-cb6baf74480a5a4ab1edJSpectraViewer | MoNA
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
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • 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
  • Leskovac, V., Trivic, S., Pericin, D. (2002). "The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae." FEMS Yeast Res 2:481-494.12702265
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • 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
  • Larroy, C., Pares, X., Biosca, J. A. (2002). "Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family." Eur J Biochem 269:5738-5745.12423374
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Larroy, C., Fernandez, M. R., Gonzalez, E., Pares, X., Biosca, J. A. (2002). "Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction." Biochem J 361:163-172.11742541
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID48943
HMDB IDHMDB0031243
Pubchem Compound ID6561
Kegg IDC03219
ChemSpider ID6313
FOODB IDFDB003271
WikipediaIsobutyraldehyde
BioCyc IDNot Available

Enzymes

Protein Details
1. Alcohol dehydrogenase 3, mitochondrial
General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH3
Uniprot ID:
P07246
Molecular weight:
40369.19922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
2. S-(hydroxymethyl)glutathione dehydrogenase
General function:
Involved in zinc ion binding
Specific function:
Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde
Gene Name:
SFA1
Uniprot ID:
P32771
Molecular weight:
41041.69922
Reactions
S-(hydroxymethyl)glutathione + NAD(P)(+) → S-formylglutathione + NAD(P)H.
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
3. Pyruvate decarboxylase isozyme 2
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.
Protein Details
4. Pyruvate decarboxylase isozyme 3
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.
Protein Details
5. Alcohol dehydrogenase 1
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols
Gene Name:
ADH1
Uniprot ID:
P00330
Molecular weight:
36849.0
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
6. Alcohol dehydrogenase 4
General function:
Involved in oxidoreductase activity
Specific function:
Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all
Gene Name:
ADH4
Uniprot ID:
P10127
Molecular weight:
41141.69922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
7. Pyruvate decarboxylase isozyme 1
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.
Protein Details
8. Alcohol dehydrogenase 5
General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH5
Uniprot ID:
P38113
Molecular weight:
37647.89844
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
9. Alcohol dehydrogenase 2
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols
Gene Name:
ADH2
Uniprot ID:
P00331
Molecular weight:
36731.60156
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
Protein Details
10. NADP-dependent alcohol dehydrogenase 7
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH7
Uniprot ID:
P25377
Molecular weight:
39348.19922
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.
Protein Details
11. Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2
General function:
Involved in enzyme regulator activity
Specific function:
Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis
Gene Name:
CSG2
Uniprot ID:
P35206
Molecular weight:
45441.60156
Reactions
Protein Details
12. NADP-dependent alcohol dehydrogenase 6
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH6
Uniprot ID:
Q04894
Molecular weight:
39617.30078
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.