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Indoleacetaldehyde (YMDB00354)

Identification
YMDB IDYMDB00354
NameIndoleacetaldehyde
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionIndoleacetaldehyde, also known as tryptaldehyde, belongs to the class of organic compounds known as 3-alkylindoles. 3-alkylindoles are compounds containing an indole moiety that carries an alkyl chain at the 3-position. Indoleacetaldehyde is an extremely weak basic (essentially neutral) compound (based on its pKa). Indoleacetaldehyde exists in all living species, ranging from bacteria to humans. Within yeast, indoleacetaldehyde participates in a number of enzymatic reactions. In particular, indoleacetaldehyde can be biosynthesized from indole-3-pyruvate; which is catalyzed by the enzyme pyruvate decarboxylase. In addition, indoleacetaldehyde can be converted into tryptophol through its interaction with the enzyme alcohol dehydrogenase. In yeast, indoleacetaldehyde is involved in the metabolic pathway called the tryptophan metabolism pathway.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • 1H-Indol-3-ylacetaldehyde
  • 1H-indole-3-acetaldehyde
  • 2-(3-Indolyl)acetaldehyde
  • 2-(indol-3-yl)acetaldehyde
  • Indol-3-ylacetaldehyde
  • indole-3-acetaldehyde
  • Indoleacetaldehyde
  • Tryptaldehyde
CAS number2591-98-2
WeightAverage: 159.1846
Monoisotopic: 159.068413915
InChI KeyWHOOUMGHGSPMGR-UHFFFAOYSA-N
InChIInChI=1S/C10H9NO/c12-6-5-8-7-11-10-4-2-1-3-9(8)10/h1-4,6-7,11H,5H2
IUPAC Name2-(1H-indol-3-yl)acetaldehyde
Traditional IUPAC Nameindole-3-acetaldehyde
Chemical FormulaC10H9NO
SMILES[H]N1C([H])=C(C2=C1C([H])=C([H])C([H])=C2[H])C([H])([H])C([H])=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as 3-alkylindoles. 3-alkylindoles are compounds containing an indole moiety that carries an alkyl chain at the 3-position.
KingdomOrganic compounds
Super ClassOrganoheterocyclic compounds
ClassIndoles and derivatives
Sub ClassIndoles
Direct Parent3-alkylindoles
Alternative Parents
Substituents
  • 3-alkylindole
  • Substituted pyrrole
  • Benzenoid
  • Alpha-hydrogen aldehyde
  • Pyrrole
  • Heteroaromatic compound
  • Azacycle
  • Aldehyde
  • Hydrocarbon derivative
  • Organic oxide
  • Organopnictogen compound
  • Organic oxygen compound
  • Organooxygen compound
  • Organonitrogen compound
  • Carbonyl group
  • Organic nitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility1.01 g/LALOGPS
logP2.32ALOGPS
logP1.55ChemAxon
logS-2.2ALOGPS
pKa (Strongest Acidic)14.73ChemAxon
pKa (Strongest Basic)-7.1ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area32.86 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity47.53 m³·mol⁻¹ChemAxon
Polarizability16.87 ųChemAxon
Number of Rings2ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Tryptophan metabolismec00380 Map00380
SMPDB Reactions
Indoleacetaldehyde + NADH + hydron → NAD + tryptophol
3-(indol-3-yl)pyruvate + hydron → Indoleacetaldehyde + Carbon dioxide
KEGG Reactions
Indoleacetaldehyde + NAD + water → NADH + hydron + indole-3-acetate
Indoleacetaldehyde + NADP + water → NADPH + hydron + indole-3-acetate
Indoleacetaldehyde + NADH + hydron → NAD + tryptophol
hydron + 3-(indol-3-yl)pyruvic acid ↔ Indoleacetaldehyde + Carbon dioxide
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-0udi-3790000000-d0624211b87a8c0c6eb0JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (1 MEOX; 1 TMS)splash10-0fb9-1890000000-f47966a3402f39ffb15aJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (1 MEOX; 1 TMS)splash10-0ufr-2890000000-4661feb288e5418df124JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0udi-1659000000-1539f9bfe6f3cc9b5cc2JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0udi-1669000000-87b7c126c24be968871eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-0006-0910000000-f73cd81db2b9712b4661JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0udi-1490000000-614e405de09537fc4b35JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00di-9430000000-c2d7214f3eaf0a20e864JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00di-9430000000-75194e386ef16f3f47b2JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0udi-3790000000-d0624211b87a8c0c6eb0JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0fb9-1890000000-f47966a3402f39ffb15aJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0ufr-2890000000-4661feb288e5418df124JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0udi-1659000000-1539f9bfe6f3cc9b5cc2JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0udi-1669000000-87b7c126c24be968871eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0006-0910000000-f73cd81db2b9712b4661JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0udi-1490000000-614e405de09537fc4b35JSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-053r-0900000000-4528170aed93d1f2f6cfJSpectraViewer
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 - LC-ESI-QTOF , negativesplash10-0a7i-0900000000-3a12e240a01798e6d515JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - , negativesplash10-0a4i-0900000000-0d6b7064551a83893c6eJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , positivesplash10-0159-0900000000-868e767ca141d74ec888JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 20V, Negativesplash10-0059-0900000000-dea5f8a3cd655d34e727JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 10V, Negativesplash10-0a7i-0900000000-03eb4dd9323023a06970JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - 40V, Negativesplash10-004i-0900000000-ec1cff588ddd81294ce1JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-0900000000-a292bcb2abf1d2004296JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-03yl-0900000000-c9491489626575ac821cJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00l6-3900000000-c4a5850dd4b1a7da14e1JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0a4i-0900000000-8354b2e6155a5677c353JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0a4i-0900000000-2bd561638cdcf5535ba5JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-014l-3900000000-bb8a2da37c41a8f5040eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0api-0900000000-ab705375598dd738ce6dJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-0900000000-924d3410f1e3855c2336JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-014i-0900000000-74f0d61a0a5ca7d19925JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03ec-0900000000-f09223778d8ebf23f2f5JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-0900000000-474bb30e410332db437aJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0fc0-3900000000-8e24fed06b1ae0ed20afJSpectraViewer
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
  • 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
  • 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
  • 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
  • Tessier, W. D., Meaden, P. G., Dickinson, F. M., Midgley, M. (1998). "Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae." FEMS Microbiol Lett 164:29-34.9675847
Synthesis Reference:Gray, Reed A. Preparation and properties of 3-indoleacetaldehyde. Archives of Biochemistry and Biophysics (1959), 81 480-8.
External Links:
ResourceLink
CHEBI ID18086
HMDB IDHMDB01190
Pubchem Compound ID800
Kegg IDC00637
ChemSpider ID778
FOODB IDFDB013950
Wikipedia IDNot Available
BioCyc IDINDOLE_ACETALDEHYDE

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. 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
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. 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
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. 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
9. 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
10. 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
11. 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
12. 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
13. 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
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.