Aminoacetone (ECMDB02134) (M2MDB000441)

IdentificationTaxonomyPhysical PropertiesBiological PropertiesSpectraConcentrationsLinksReferencesEnzymes (3)XML
Proteins (162)
Record Information
Version2.0
Creation Date2012-05-31 13:55:41 -0600
Update Date2015-06-03 15:54:14 -0600
Secondary Accession Numbers
  • ECMDB02134
Identification
Name:Aminoacetone
DescriptionThreonine dehydrogenase catalyzes the oxidation of threonine by NAD+ to glycine and acetyl-CoA (5), but when the ratio acetyl-CoA/CoA increases in nutritional deprivation (e.g., in diabetes) the enzyme produces AA. (Chem. Res. Toxicol., 14 (9), 1323 -1329, 2001);
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms:
  • 1-Amino-(8CI,9CI)-2-propanone
  • 1-Amino-2-propanone
  • 1-Aminopropan-2-one
  • a-Aminoacetone
  • Alpha-Aminoacetone
  • Amino-(6CI)-2-propanone
  • Amino-2-propanone
  • α-Aminoacetone
Chemical Formula:C3H7NO
Weight:Average: 73.0938
Monoisotopic: 73.052763851
InChI Key:BCDGQXUMWHRQCB-UHFFFAOYSA-N
InChI:InChI=1S/C3H7NO/c1-3(5)2-4/h2,4H2,1H3
CAS number:298-08-8
IUPAC Name:1-aminopropan-2-one
Traditional IUPAC Name:α-aminoacetone
SMILES:CC(=O)CN
Chemical Taxonomy
Description belongs to the class of organic compounds known as alpha-amino ketones. These are ketones containing a carboxylic acid, and an amine group attached to the alpha carbon atom relative to C=O group.
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassCarbonyl compounds
Direct ParentAlpha-amino ketones
Alternative Parents
Substituents
  • Alpha-aminoketone
  • Organic nitrogen compound
  • Organopnictogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Primary amine
  • Organonitrogen compound
  • Primary aliphatic amine
  • Amine
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:1
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility528 g/LALOGPS
logP-1.3ALOGPS
logP-0.82ChemAxon
logS0.86ALOGPS
pKa (Strongest Acidic)17.3ChemAxon
pKa (Strongest Basic)7.84ChemAxon
Physiological Charge1ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area43.09 ŲChemAxon
Rotatable Bond Count1ChemAxon
Refractivity19.55 m³·mol⁻¹ChemAxon
Polarizability7.71 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Aminoacetone + Hydrogen ion + NADH <> 1-Amino-2-propanol + NAD
L-2-Amino-3-oxobutanoic acid + Hydrogen ion > Aminoacetone + Carbon dioxide
Aminoacetone + Water + Oxygen <> Pyruvaldehyde + Ammonia + Hydrogen peroxide
Aminoacetone + Water + Oxygen > Hydrogen ion + Pyruvaldehyde + Ammonia + Hydrogen peroxide
1-Amino-2-propanol + NAD < Hydrogen ion + Aminoacetone + NADH
L-Allothreonine + NADP + L-2-Amino-3-oxobutanoic acid <> Aminoacetone + Carbon dioxide + NADPH + Hydrogen ion
1-Amino-2-propanol + NAD + 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene < NADH + Hydrogen ion + Aminoacetone
Aminoacetone + Oxygen + Water > Hydrogen peroxide + Ammonium + Pyruvaldehyde
SMPDB Pathways:
Collection of Reactions without pathwaysPW001891 ThumbThumb?image type=greyscaleThumb?image type=simple
L-threonine degradation to methylglyoxalPW002106 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyrimidine metabolismPW000942 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-001l-9000000000-8a9ae47335e91a60428fView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9000000000-11399cdd8e4f4b0b0a0aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-05fr-9000000000-a82e70bf32acfda0125fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-b3cd82ec754798e33b8bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-1c501c72ceda6ba07e56View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-d7cb45a11c770b6c8611View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0kml-9000000000-b2494e27f62747d5ed80View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9000000000-8a5d09318bc9c06fc3eeView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-7443b05daf1ed122b62eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4r-9000000000-0dbef78008e03c42333fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-bc974757d0839ce6b57cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-19b1c35a423800bd5eadView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-00dl-9000000000-0c98bd36ab2e0978e815View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Dutra F, Knudsen FS, Curi D, Bechara EJ: Aerobic oxidation of aminoacetone, a threonine catabolite: iron catalysis and coupled iron release from ferritin. Chem Res Toxicol. 2001 Sep;14(9):1323-9. Pubmed: 11559049
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Karge E, Klinger W: [Effect of the pH value on the dissociation of the aminoketones delta-aminolevulinic acid and aminoacetone by extraction with ether and dichlormethane] Z Med Lab Diagn. 1981;22(6):358-9. Pubmed: 7342529
  • Kazachkov M, Yu PH: A novel HPLC procedure for detection and quantification of aminoacetone, a precursor of methylglyoxal, in biological samples. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Sep 25;824(1-2):116-22. Pubmed: 16046286
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Thiele I, Swainston N, Fleming RM, Hoppe A, Sahoo S, Aurich MK, Haraldsdottir H, Mo ML, Rolfsson O, Stobbe MD, Thorleifsson SG, Agren R, Bolling C, Bordel S, Chavali AK, Dobson P, Dunn WB, Endler L, Hala D, Hucka M, Hull D, Jameson D, Jamshidi N, Jonsson JJ, Juty N, Keating S, Nookaew I, Le Novere N, Malys N, Mazein A, Papin JA, Price ND, Selkov E Sr, Sigurdsson MI, Simeonidis E, Sonnenschein N, Smallbone K, Sorokin A, van Beek JH, Weichart D, Goryanin I, Nielsen J, Westerhoff HV, Kell DB, Mendes P, Palsson BO: A community-driven global reconstruction of human metabolism. Nat Biotechnol. 2013 Mar 3. doi: 10.1038/nbt.2488. Pubmed: 23455439
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Turner, J. M. Aminoacetone production by microorganisms. Biochemical Journal (1966), 98(1), 7P.
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID17906
HMDB IDHMDB02134
Pubchem Compound ID215
Kegg IDC01888
ChemSpider ID210
Wikipedia1-Amino-2-propanone
BioCyc IDAMINO-ACETONE
EcoCyc IDAMINO-ACETONE
Ligand ExpoGLM

Enzymes

Protein Details
1. Glycerol dehydrogenase
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of gldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively
Gene Name:
gldA
Uniprot ID:
P0A9S5
Molecular weight:
38712
Reactions
Glycerol + NAD(+) = glycerone + NADH.
Protein Details
2. Primary amine oxidase
General function:
Involved in copper ion binding
Specific function:
The enzyme prefers aromatic over aliphatic amines
Gene Name:
tynA
Uniprot ID:
P46883
Molecular weight:
84378
Reactions
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2).
2-phenylethylamine + H(2)O + O(2) = phenylacetaldehyde + NH(3) + H(2)O(2).
Protein Details
3. NADP-dependent L-serine/L-allo-threonine dehydrogenase ydfG
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NADP-dependent oxidation of L-allo- threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on L-serine, D-serine, D-threonine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D- glycerate and L-glycerate
Gene Name:
ydfG
Uniprot ID:
P39831
Molecular weight:
27249
Reactions
3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + NADPH.