Reaction participants Show >> << Hide
- Name help_outline spermine dialdehyde Identifier CHEBI:180902 Charge 2 Formula C10H22N2O2 InChIKeyhelp_outline WPBJCXUUUSDQJO-UHFFFAOYSA-P SMILEShelp_outline O=CCC[NH2+]CCCC[NH2+]CCC=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(4-aminobutyl)-3-aminopropanal Identifier CHEBI:183796 Charge 2 Formula C7H18N2O InChIKeyhelp_outline MMMHAACFRAVQHI-UHFFFAOYSA-P SMILEShelp_outline O=CCC[NH2+]CCCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acrolein Identifier CHEBI:15368 (CAS: 107-02-8) help_outline Charge 0 Formula C3H4O InChIKeyhelp_outline HGINCPLSRVDWNT-UHFFFAOYSA-N SMILEShelp_outline [H]C(=C)C([H])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:69156 | RHEA:69157 | RHEA:69158 | RHEA:69159 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Human aldehyde dehydrogenase. Activity with aldehyde metabolites of monoamines, diamines, and polyamines.
Ambroziak W., Pietruszko R.
Two isozymes (E1 and E2) of human aldehyde dehydrogenase (EC 1.2.1.3) were purified to homogeneity 13 years ago and a third isozyme (E3) with a low Km for gamma-aminobutyraldehyde only recently. Comparison with a variety of substrates demonstrates that substrate specificity of all three isozymes i ... >> More
Two isozymes (E1 and E2) of human aldehyde dehydrogenase (EC 1.2.1.3) were purified to homogeneity 13 years ago and a third isozyme (E3) with a low Km for gamma-aminobutyraldehyde only recently. Comparison with a variety of substrates demonstrates that substrate specificity of all three isozymes is broad and similar. With straight chain aliphatic aldehydes (C1-C6) the Km values of the E3 isozyme are identical with those of the E1 isozyme. All isozymes dehydrogenate naturally occurring aldehydes, 5-imidazoleacetaldehyde (histamine metabolite) and acrolein (product of beta-elimination of oxidized polyamines) with similar catalytic efficiency. Differences between the isozymes are in the Km values for aminoaldehydes. Although all isozymes can dehydrogenate gamma-aminobutyraldehyde, the Km value of the E3 isozyme is much lower: the same appears to apply to aldehyde metabolites of cadaverine, agmatine, spermidine, and spermine for which Km values range between 2-18 microM and kcat values between 0.8-1.9 mumol/min/mg. Thus, the E3 isozyme has properties which make it suitable for the metabolism of aminoaldehydes. The physiological role of E1 and E2 isozymes could be in dehydrogenation of aldehyde metabolites of monoamines such as 3,4-dihydroxyphenylacetaldehyde or 5-hydroxyindoleacetaldehyde; the catalytic efficiency with these substrates is better with E1 and E2 isozymes than with E3 isozyme. Isoelectric focusing of liver homogenates followed by development with various physiological substrates together with substrate specificity data suggest that aldehyde dehydrogenase (EC 1.2.1.3) is the only enzyme in the human liver capable of catalyzing dehydrogenation of aldehydes arising via monoamine, diamine, and plasma amine oxidases. Although the enzyme is generally considered to function in detoxication, our data suggest an additional function in metabolism of biogenic amines. << Less
J. Biol. Chem. 266:13011-13018(1991) [PubMed] [EuropePMC]
This publication is cited by 19 other entries.