| First Author | Algar EM | Year | 1985 |
| Journal | Mouse News Lett | Volume | 72 |
| Pages | 101-102 | Mgi Jnum | J:32774 |
| Mgi Id | MGI:80264 | Citation | Algar EM, et al. (1985) Aldehyde Dehydrogenase (Ahd). Mouse News Lett 72:101-102 |
| abstractText | Full text of MNL contribution: Biochemical and genetic studies of aldehyde dehydrogenases from tissues of the mouse have provided evidence for at least six isozymes: Isozyme (Subunit Structure) : AHD-1 (A>2<) . Tissue (Subcellular) Localization: liver, kidney, heart (mitochondrial). Locus (Chromosome) (*provisional): Ahd-1 (4). Isozyme (Subunit Structure): AHD-2. Tissue (Subcellular) Localization: liver (cytoplasmic. Locus (Chromosome) (*provisional): Ahd-2 (19). Isozyme (Subunit Structure): AHD-3. Tissue (Subcellular) Localization: liver (microsomal). Locus (Chromosome) (*provisional): (Ahd-3)*. Isozyme (Subunit Structure): AHD-4 (D>2<). Tissue (Subcellular) Localization: stomach. Locus (Chromosome) (*provisional): Ahd-4. Isozyme (Subunit Structure): AHD-5 (E>2<). Tissue (Subcellular) Localization: wide tissue distribution (mitochondrial). Locus (Chromosome) (*provisional): (Ahd-5)*. Isozyme (Subunit Structure): AHD-6. Tissue (Subcellular) Localization: testis. Locus (Chromosome) (*provisional): Ahd-6. Allelic variants have been described for Ahd-1 (Biochemical Genetics 16 (1978) 1207), Ahd-2 (Genetics 97 (1981) 327) and more recently for Ahd-4 and Ahd-6 (Biochemical Genetics Ð in press). The latter two loci have been proposed for the stomach and testis specific aldehyde dehydrogenases which are linked on the mouse genome (7+2% recombination frequency), but are presently unmapped. No variants have been observed, so far, for the microsomal (AHD-3) and mitochondrial (AHD-5) isozymes among 56 strains of mice. Liver mitochondrial isozymes, AHD-1 and AHD-5, have been purified to homogeneity and characterized biochemically (International Journal of Biochemistry Ð in press). The enzymes are dimers (designated as A>2< and E>2< in accordance with isozymes nomenclature) with distinct subunit sizes: AHD-1, 63,000; and AHD-5, 49,000. Kinetic analyses showed that the purified allelic forms of AHD-1, AHD-1A (C57BL/6J mice) and AHD-1B (CBA/H mice), exhibited low affinity for acetaldehyde as substrate (with Km values of 1.4mM and 0.8mM respectively), whereas AHD-5 showed a high affinity for this substrate (0.2UM Km value). It is proposed that AHD-5 is the primary enzyme for oxidizing mitochondrial acetaldehyde during ethanol oxidation in vivo. |
