Topic
Aldehyde dehydrogenase
About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.
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TL;DR: Chromosomal assignment of the genes for two major human aldehyde dehydrogenase isozymes, ALDH1 and ALDH2, were determined and AL DH1 was assigned to the long arm of human chromosome 9 andALDH2 to chromosome 12.
Abstract: Chromosomal assignment of the genes for two major human aldehyde dehydrogenase isozymes, that is, cytosolic aldehyde dehydrogenase-1 (ALDH1) and mitochondrial aldehyde dehydrogenase-2 (ALDH2) were determined. Genomic DNA, isolated from a panel of mouse-human and Chinese hamster-human hybrid cell lines, was digested by restriction endonucleases and subjected to Southern blot hybridization using cDNA probes for ALDH1 and for ALDH2. Based on the distribution pattern of ALDH1 and ALDH2 in cell hybrids, ALDH1 was assigned to the long arm of human chromosome 9 and ALDH2 to chromosome 12.
62 citations
TL;DR: Results indicated that this ALDH gene was the only gene of the NAD(+)-preferring alphaKGSA dehydrogenase in A. brasilense, and this is the first evidence of unique "convergent evolution" in the ALDH family.
62 citations
TL;DR: The values are used to show that the metabolic fates of the various aldehydes—and hence of the parent amines—may be explained in terms of the simple kinetics of these enzymes.
Abstract: The Michaelis constants of purified aldehyde dehydrogenase (aldehyde: NAD oxidoreductase, EC 1.2.1.3) and aldehyde reductases (alcohol: NADP oxidoreductase, EC 1.1.1.2) from pig brain have been obtained for a number of biologically important aldehydes. The aldehydes include 3,4-dihydroxyphenylacetaldehyde, D-3,4-dihydroxyphenylglycolaldehyde, and 5-hydroxyindoleacetaldehyde. The relative activities of the aldehyde-catabolizing enzymes in the soluble fractions of the cerebral cortex and caudate nucleus of pig brain have also been obtained. The values are used to show that the metabolic fates of the various aldehydes—and hence of the parent amines—may be explained in terms of the simple kinetics of these enzymes. It is also shown that the metabolic fates of the aldehydes may be influenced by their rates of synthesis. As the rate of aldehyde production increases the proportion of aldehyde reduced may be expected to increase at the expense of the proportion of aldehyde oxidized.
It is further concluded from the kinetic constants that selective inhibition of aldehyde dehydrogenase may greatly affect the catabolism of dopamine and 5-hydroxytryptamine by altering the relevant aldehyde concentrations, while the catabolism of norepinephrine is little affected under these circumstances. Conversely, it is concluded that selective inhibition of the aldehyde reductases should scarcely affect the catabolism of dopamine and 5-hydroxytryptamine, but that the catabolism of norepinephrine should be markedly affected.
The results also indicate that the concentrations of the various deaminated metabolites of the biogenic amines could be selectively controlled by modulation of the activity of the enzymes of aldehyde catabolism in brain.
62 citations
TL;DR: The aim of this review is to briefly describe the multiple post-translational modifications of mitochondrial ALDH2, as an example, after exposure to toxic chemicals or under different disease states and their pathophysiological roles in promoting alcohol/drug-mediated tissue damage.
62 citations
TL;DR: Genetic variants for ADH-C2 established its identity with a second form of sorbitol dehydrogenase observed in stomach and other tissues, which was found in high activity in liver, kidney, pancreas and male reproductive tissues.
Abstract: 1. 1. Cellulose acetate zymograms of alcohol dehydrogenase (ADH), aldehyde dehydrogenase, sorbitol dehydrogenase, aldehyde oxidase, “phenazine” oxidase and xanthine oxidase extracted from tissues of inbred mice were examined. 2. 2. ADH isozymes were differentially distributed in mouse tissues: A 2 —liver, kidney, adrenals and intestine; B 2 —all tissues examined; C 2 —stomach, adrenals, epididymis, ovary, uterus, lung. 3. 3. Two NAD + -specific aldehyde dehydrogenase isozymes were observed in liver and kidney and differentially distributed in other tissues. Alcohol dehydrogenase, aldehyde oxidase, “phenazine” oxidase and xanthine oxidase were also stained when aldehyde dehydrogenase was being examined. 4. 4. Two aldehyde oxidase isozymes exhibited highest activities in liver. 5. 5. “Phenazine oxidase” was widely distributed in mouse tissues whereas xanthine oxidase exhibited highest activity in intestine and liver extracts. 6. 6. Genetic variants for ADH-C 2 established its identity with a second form of sorbitol dehydrogenase observed in stomach and other tissues. The major sorbitol dehydrogenase was found in high activity in liver, kidney, pancreas and male reproductive tissues.
62 citations