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Phenylacetaldehyde (YMDB00116)

Identification
YMDB IDYMDB00116
NamePhenylacetaldehyde
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionPhenylacetaldehyde, also known as alpha-tolualdehyde or 2-phenylethanal, belongs to the class of organic compounds known as phenylacetaldehydes. Phenylacetaldehydes are compounds containing a phenylacetaldehyde moiety, which consists of a phenyl group substituted at the second position by an acetalydehyde. Phenylacetaldehyde is an extremely weak basic (essentially neutral) compound (based on its pKa). Phenylacetaldehyde exists in all living species, ranging from bacteria to humans. Within yeast, phenylacetaldehyde participates in a number of enzymatic reactions. In particular, phenylacetaldehyde can be biosynthesized from 2-oxo-3-phenylpropanoic acid (mixture oxo and keto); which is mediated by the enzyme pyruvate decarboxylase. In addition, phenylacetaldehyde can be converted into 2-phenylethanol; which is mediated by the enzyme alcohol dehydrogenase. In yeast, phenylacetaldehyde is involved in the metabolic pathway called the phenylalanine metabolism pathway. Phenylacetaldehyde is a potentially toxic compound.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • .alpha.-toluic aldehyde
  • 1-Oxo-2-phenylethane
  • 2-phenylacetaldehyde
  • 2-Phenylethanal
  • a-Phenylacetaldehyde
  • a-Tolualdehyde
  • a-toluic aldehyde
  • alpha-Phenylacetaldehyde
  • Alpha-tolualdehyde
  • Alpha-toluic aldehyde
  • Benzenacetaldehyde
  • Benzeneacetaldehyde
  • Benzylcarboxaldehyde
  • Hyacinthin
  • Oxophenylethane
  • Phenacetaldehyde
  • phenyl-Acetaldehyde
  • phenylacetaldehyde
  • Phenylacetic aldehyde
  • Phenylethanal
  • Benzacetaldehyde
  • Α-phenylacetaldehyde
  • Α-tolualdehyde
  • Α-toluic aldehyde
  • FEMA no. 2974
CAS number122-78-1
WeightAverage: 120.1485
Monoisotopic: 120.057514878
InChI KeyDTUQWGWMVIHBKE-UHFFFAOYSA-N
InChIInChI=1S/C8H8O/c9-7-6-8-4-2-1-3-5-8/h1-5,7H,6H2
IUPAC Name2-phenylacetaldehyde
Traditional IUPAC Namephenylacetaldehyde
Chemical FormulaC8H8O
SMILES[H]C(=O)C([H])([H])C1=C([H])C([H])=C([H])C([H])=C1[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as phenylacetaldehydes. Phenylacetaldehydes are compounds containing a phenylacetaldehyde moiety, which consists of a phenyl group substituted at the second position by an acetalydehyde.
KingdomOrganic compounds
Super ClassBenzenoids
ClassBenzene and substituted derivatives
Sub ClassPhenylacetaldehydes
Direct ParentPhenylacetaldehydes
Alternative Parents
Substituents
  • Phenylacetaldehyde
  • Alpha-hydrogen aldehyde
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Aldehyde
  • Aromatic homomonocyclic compound
Molecular FrameworkAromatic homomonocyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point120.5-121.5 °C
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogP1.78 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility2.08 g/LALOGPS
logP1.75ALOGPS
logP1.45ChemAxon
logS-1.8ALOGPS
pKa (Strongest Acidic)14.98ChemAxon
pKa (Strongest Basic)-7ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area17.07 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity36.44 m³·mol⁻¹ChemAxon
Polarizability12.91 ųChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
BitterFDB012238
CloverFDB012238
CocoaFDB012238
FloralFDB012238
GrapefruitFDB012238
GreenFDB012238
HawthorneFDB012238
HoneyFDB012238
HyacinthFDB012238
PeanutFDB012238
SweetFDB012238
SMPDB Pathways
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Phenylalanine metabolismec00360 Map00360
SMPDB Reactions
Phenylacetaldehyde + hydron + NADH → 2-phenylethanol + NAD
keto-phenylpyruvic acid + hydron → Carbon dioxide + Phenylacetaldehyde
KEGG Reactions
NADH + Phenylacetaldehyde + hydron → NAD + 2-phenylethanol
Phenylacetaldehyde + NADPH + hydron → NADP + 2-phenylethanol
Phenylacetaldehyde + NAD + water → NADH + hydron + Phenylacetic acid
hydron + keto-phenylpyruvic acid → Phenylacetaldehyde + Carbon dioxide
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00kf-9400000000-bec6e42b47ad1306960fJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-014l-9700000000-152bdd5b77d6af9657ecJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-0006-9000000000-d37cbef4100302e951deJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-00kf-9400000000-bec6e42b47ad1306960fJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-014l-9700000000-152bdd5b77d6af9657ecJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kf-9400000000-e75d2f0bf82f16a80388JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kf-9400000000-32573b7f6ab690a27e3eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-5900000000-21e85148d15d190553c4JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-5900000000-4471e0916a32cf4df7acJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-5900000000-650012e69d0a89a2fd4aJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0006-5900000000-c80b65e383f833509e0fJSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9200000000-b3923f5fae42c664ac4aJSpectraViewer
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
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-0udi-4900000000-5001b07cef2fed3caa2cJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-004i-9100000000-048e2f1b42f7bd5104beJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-0fb9-9000000000-fc1fbd4e7c49f44ba764JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - EI-B (HITACHI M-80A) , Positivesplash10-0006-9000000000-bc0fa2967da6872f3a47JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 35V, Positivesplash10-0ufr-9700000000-507b63b585578b670628JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-0900000000-8c96fee71b311d751181JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0fk9-2900000000-4b405668c302f69a4bc7JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0ufr-9300000000-fe46a418a2f0124566c3JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014i-0900000000-4e064e0123dc18b6136aJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-1900000000-02fff0bd874e6e8616bbJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004l-9200000000-340c7a60a7708fa801f1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-002f-9000000000-e37fda57674e1a53ea10JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0006-9000000000-2071e5b3f45157a1da9cJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-002f-9100000000-219bfc0a518871479977JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00kf-9300000000-3fb47a0274f5792b4bd1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0006-9000000000-5671d4c535a6553aaf0dJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-cc66f13f72898a397be6JSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-0006-9100000000-e7ef9a5c5a6cc5674cd1JSpectraViewer | 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
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
  • 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
  • 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
  • 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:Sun Zhirong; Hu Xiang; Zhou Ding Wastewater minimization in indirect electrochemical synthesis of phenylacetaldehyde. TheScientificWorldJournal (2002), 2 48-52.
External Links:
ResourceLink
CHEBI ID16424
HMDB IDHMDB06236
Pubchem Compound ID998
Kegg IDC00601
ChemSpider ID13876539
FOODB IDFDB012238
WikipediaPhenylacetaldehyde
BioCyc IDHYDRPHENYLAC-CPD

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. Aldehyde dehydrogenase [NAD(P)+] 1
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Gene Name:
ALD2
Uniprot ID:
P47771
Molecular weight:
55187.39844
Reactions
An aldehyde + NAD(P)(+) + H(2)O → an acid + NAD(P)H.
Protein Details
3. 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
4. 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
5. 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
6. Aldehyde dehydrogenase [NAD(P)+] 2
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H
Gene Name:
ALD3
Uniprot ID:
P54114
Molecular weight:
55384.80078
Reactions
An aldehyde + NAD(P)(+) + H(2)O → an acid + NAD(P)H.
Protein Details
7. 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
8. 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
9. 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
10. 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
11. 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
12. 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
13. 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
14. Transaminated amino acid decarboxylase
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).
Protein Details
15. 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.