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Acetaldehyde (YMDB00022)

Identification
YMDB IDYMDB00022
NameAcetaldehyde
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionAcetaldehyde, also known as ethanal, 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. Acetaldehyde is an extremely weak basic (essentially neutral) compound (based on its pKa). Acetaldehyde exists in all living species, ranging from bacteria to humans. Acetaldehyde is formally rated as a possible carcinogen (by IARC 2B) and is also a potentially toxic compound.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • Acetaldehyd
  • acetaldehyde
  • Acetaldehydes
  • acetic aldehyde
  • aldehyde
  • Azetaldehyd
  • ethanal
  • ethyl aldehyde
CAS number75-07-0
WeightAverage: 44.0526
Monoisotopic: 44.02621475
InChI KeyIKHGUXGNUITLKF-UHFFFAOYSA-N
InChIInChI=1S/C2H4O/c1-2-3/h2H,1H3
IUPAC Nameacetaldehyde
Traditional IUPAC Nameacetaldehyde
Chemical FormulaC2H4O
SMILES[H]C(=O)C([H])([H])[H]
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-123 °C
Experimental Properties
PropertyValueReference
Water Solubility1000 mg/mL at 25 oC [RIDDICK,JA et al. (1986)]PhysProp
LogP-0.34 [TSCATS]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility225 g/LALOGPS
logP-0.01ALOGPS
logP-0.38ChemAxon
logS0.71ALOGPS
pKa (Strongest Acidic)16.73ChemAxon
pKa (Strongest Basic)-6.9ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area17.07 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity11.72 m³·mol⁻¹ChemAxon
Polarizability4.48 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
AldehydicFDB008297
EtherFDB008297
EtherealFDB008297
FruityFDB008297
PungentFDB008297
WhiskeyFDB008297
SMPDB Pathways
Ethanol fermentationPW002448 ThumbThumb?image type=greyscaleThumb?image type=simple
Glycerophospholipid metabolismPW002493 ThumbThumb?image type=greyscaleThumb?image type=simple
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
glycine metabolismPW002398 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycerophospholipid metabolismec00564 Map00564
Glycolysis / Gluconeogenesisec00010 Map00010
Phenylalanine metabolismec00360 Map00360
Pyruvate metabolismec00620 Map00620
SMPDB Reactions
L-Threonine → Acetaldehyde + Glycine
Acetaldehyde + NAD + Coenzyme A → NADH + hydron + Acetyl-CoA
Acetaldehyde + Coenzyme A + NAD → NADH + hydron + Acetyl-CoA
Acetaldehyde + hydron + NADH ↔ Ethanol + NAD
Pyruvic acid + hydron → Carbon dioxide + Acetaldehyde
KEGG Reactions
Acetaldehyde → (R)-Acetoin
Ethanol + NAD ↔ NADH + Acetaldehyde + hydron
NADH + Acetaldehyde + hydron → Ethanol + NAD
NADP + Acetaldehyde + water → Acetic acid + NADPH + hydron
NAD + Acetaldehyde + water → NADH + Acetic acid + hydron
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
9080 ± 0 µM glucose~(140 g/L), KHzP04 (5 g/L), and yeast extract (10 g/L).anaerobicBaker's yeastPMID: 18609643
Conversion Details Here
Extracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
50 ± 50 µM Synthetic medium with 1% glucose and 0.1% yeast extractaerobicBaker's yeastPMID: 16623706
Conversion Details Here
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9000000000-69e31ccd415894a68912JSpectraViewer
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)splash10-0002-9000000000-f1274d4b6066776ca898JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-001l-9000000000-c1e37abbf2ad6054dc10JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000t-9000000000-2289ead4f7210282cd87JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0002-9000000000-cf54221d95714f5478c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0002-9000000000-8d8afe7422ae76f7ebb9JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-004j-9000000000-d68dec9f846cfe9acc72JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0006-9000000000-4430d6a790eca4132aa4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0006-9000000000-607a755de038203a6b68JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-63c9f623d8dc4b1e60a2JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0002-9000000000-00ba25458eb6c0cc2940JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0002-9000000000-00ba25458eb6c0cc2940JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0002-9000000000-0d922cdfd7f6947230c0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0006-9000000000-452a5f79625d3401d495JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0006-9000000000-452a5f79625d3401d495JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-2758497e574a09010547JSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-002f-9000000000-65d53ef91644a0bacd6cJSpectraViewer | 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
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • Stanley, G. A., Pamment, N. B. (1993). "Transport and intracellular accumulation of acetaldehyde in saccharomyces cerevisiae." Biotechnol Bioeng 42:24-29.18609643
  • 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
  • Dickinson, F. M., Monger, G. P. (1973). "A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates." Biochem J 131:261-270.4352908
  • Maestre, O., Garcia-Martinez, T., Peinado, R. A., Mauricio, J. C. (2008). "Effects of ADH2 overexpression in Saccharomyces bayanus during alcoholic fermentation." Appl Environ Microbiol 74:702-707.18065623
  • Schwartz, J. M., Kanehisa, M. (2006). "Quantitative elementary mode analysis of metabolic pathways: the example of yeast glycolysis." BMC Bioinformatics 7:186.16584566
  • 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
  • Saint-Prix, F., Bonquist, L., Dequin, S. (2004). "Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation." Microbiology 150:2209-2220.15256563
  • 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
  • Liu, J. Q., Nagata, S., Dairi, T., Misono, H., Shimizu, S., Yamada, H. (1997). "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme." Eur J Biochem 245:289-293.9151955
  • 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
  • Xu, Z., Tsurugi, K. (2006). "A potential mechanism of energy-metabolism oscillation in an aerobic chemostat culture of the yeast Saccharomyces cerevisiae." FEBS J 273:1696-1709.16623706
Synthesis Reference:Wertheim, E. Laboratory preparation of acetaldehyde. Journal of the American Chemical Society (1922), 44 2658-9.
External Links:
ResourceLink
CHEBI ID15343
HMDB IDHMDB00990
Pubchem Compound ID177
Kegg IDC00084
ChemSpider ID172
FOODB IDFDB008297
WikipediaAcetaldehyde
BioCyc IDACETALD

Enzymes

Protein Details
1. Low specificity L-threonine aldolase
General function:
Involved in lyase activity
Specific function:
Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde
Gene Name:
GLY1
Uniprot ID:
P37303
Molecular weight:
42814.60156
Reactions
L-threonine → glycine + acetaldehyde.
L-allo-threonine → glycine + acetaldehyde.
Protein Details
2. 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
3. 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
4. Putative nitronate monooxygenase
General function:
Involved in nitronate monooxygenase activity
Specific function:
Catalyzes the oxidation of alkyl nitronates to produce the corresponding carbonyl compounds and nitrites
Gene Name:
Not Available
Uniprot ID:
P47177
Molecular weight:
45142.60156
Reactions
Ethylnitronate + O(2) + FMNH(2) → acetaldehyde + nitrite + FMN + H(2)O.
Protein Details
5. 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
6. Potassium-activated aldehyde dehydrogenase, mitochondrial
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(+) + H(2)O = an acid + NADH
Gene Name:
ALD4
Uniprot ID:
P46367
Molecular weight:
56723.19922
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
Protein Details
7. 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
8. 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
9. 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
10. Magnesium-activated aldehyde dehydrogenase, cytosolic
General function:
Involved in oxidoreductase activity
Specific function:
An aldehyde + NAD(+) + H(2)O = an acid + NADH
Gene Name:
ALD6
Uniprot ID:
P54115
Molecular weight:
54413.69922
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
Protein Details
11. 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
12. Aldehyde dehydrogenase 5, mitochondrial
General function:
Involved in oxidoreductase activity
Specific function:
Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose
Gene Name:
ALD5
Uniprot ID:
P40047
Molecular weight:
56620.39844
Reactions
An aldehyde + NAD(+) + H(2)O → an acid + NADH.
An aldehyde + NADP(+) + H(2)O → an acid + NADPH.
Protein Details
13. 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
14. 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
15. 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
16. 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
17. NADPH-dependent methylglyoxal reductase GRE2
General function:
Involved in catalytic activity
Specific function:
Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation
Gene Name:
GRE2
Uniprot ID:
Q12068
Molecular weight:
38169.19922
Reactions
Lactaldehyde + NADP(+) → methylglyoxal + NADPH.
3-methylbutanol + NAD(P)+ → 3-methylbutanal + NAD(P)H + H+
Protein Details
18. 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
19. 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.