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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: Sheep liver cytoplasmic aldehyde dehydrogenase was purified to homogeneity to give a sample with a specific activity of 380 nmol NADH min(-1) mg(-1); an amino acid analysis of the enzyme gave results similar to those reported for alde Hyde dehydrogenases from other sources.
Abstract: Sheep liver cytoplasmic aldehyde dehydrogenase was purified to homogeneity to give a sample with a specific activity of 380 nmol NADH min(-1) mg(-1). An amino acid analysis of the enzyme gave results similar to those reported for aldehyde dehydrogenases from other sources. The isoelectric point was at pH 5.25 and the enzyme contained no significant amounts of metal ions. On the binding of NADH to the enzyme there is a shift in absorption maximum of NADH to 344 nm, and a 5.6-fold enhancement of nucleotide fluorescence. The protein fluorescence (lambdaexcit = 290 nm, lambdaemisson = 340 nm) is quenched on the binding of NAD+ and NADH. The enhancement of nucleotide fluorescence on the binding of NADH has been utilised to determine the dissociation constant for the enzyme . NADH complex (Kd = 1.2 +/- 0.2 muM). A Hill plot of the data gave a straight line with a slope of 1.0 +/- 0.3 indicating the absence of co-operative effects. Ellman's reagent reacted only slowly with the enzyme but in the presence of sodium dodecylsulphate complete reaction occurred within a few minutes to an extent corresponding to 36 thiol groups/enzyme. Molecular weights were determined for both cytoplasmic and mitochondrial aldehyde dehydrogenases and were 212 000 +/- 8 000 and 205 000 respectively. Each enzyme consisted of four subunits with molecular weight of 53 000 +/- 2 000. Properties of the cytoplasmic and mitochondrial aldehyde dehydrogenases from sheep liver were compared with other mammalian liver aldehyde dehydrogenases.

48 citations

Journal ArticleDOI
TL;DR: It is found that the nitrate ester antianginal drugs, isosorbide dinitrate and nitroglycerin, are potent inhibitors of human erythrocyte aldehyde dehydrogenase, and these therapies have well-documented disulfiram-like side effects.
Abstract: Disulfiram-like responses to various drug therapies are caused by elevated ethnol-derived blood acetaldehyde concentrations resulting from drug-induced inhibition of aldehyde dehydrogenase enzymes. We have found that the nitrate ester antianginal drugs, isosorbide dinitrate and nitroglycerin, are potent inhibitors of human erythrocyte aldehyde dehydrogenase. To further characterize this drug-induced enzyme inhibition, erythrocyte aldehyde dehydrogenase activities were measured in patients undergoing therapy with nitrate ester antianginals (isosorbide dinitrate and nitroglycerin) and sulfonylurea hypoglycemics (chlorpropamide and tolazamide). The erythrocyte enzyme was decreased by approximately 25% in sulfonylurea-treated patients, whereas in the nitrate ester-treated patients, an 88% inhibition was observed. The minimal enzyme inhibition in the sulfonylurea-treated group was unexpected because these therapies have well-documented disulfiram-like side effects. This weak inhibition contrasted with the severe inhibition observed in the nitrate ester-treated group where the disulfiram-like side effects are not considered a serious clinical problem. This apparent anomaly was attributed to differences in inhibition of the erythrocyte and liver aldehyde dehydrogenase by the parent drugs and their hepatic metabolites.

48 citations

Journal ArticleDOI
TL;DR: An investigation of the sulfhydryl character of the DPN-linked aldehyde dehydrogenase of bovine liver is described, finding that arsenite-thiol combinations are inhibitory but also that arsenosophenylbutyrate is more effective as an inhibitor and does not require any added thiol as an adjunct to its action.

48 citations

01 Jan 1983
TL;DR: It is demonstrated that the isozymes of ALDH may play an important role in the pathogenesis of alcohol-related organ damage and in the biological sensitivity to alcohol in certain ethnic groups.
Abstract: Isozymes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were studied in human organs and tissues using sensitive analytical techniques. Both ADH and ALDH showed an extensive polymorphism among different racial groups. In liver extracts and other tissues of Japanese an isozyme of ALDH (ALDH I) with a low Km for acetaldehyde was found to be deficient. The ALDH isozyme deficiency might account for the marked initial sensitivity to alcohol in Orientals owing to their impaired acetaldehyde oxidizing capacity. Significantly low erythrocyte ALDH activity was noted more frequently in chronic alcoholics than in healthy controls. After subcellular fractionation of livers from alcoholics a preferential damage of mitochondrial ALDH isozyme was observed. The metabolism of acetaldehyde has received considerable attention in the past few years, owing to the toxic effects of this substance. Rapid progress has been made in the understanding of the multiple molecular forms of ADH and ALDH in human tissues. Our recent studies have demonstrated that the isozymes of ALDH may play an important role in the pathogenesis of alcohol-related organ damage and in the biological sensitivity to alcohol in certain ethnic groups. A possible protection of ALDH I deficiency against alcoholism in Japanese has been discussed. More recent reports [Imprain et al, 1982; Jones, 1982] indicate that, in addition to the enzymatically active ALDH II, tissues from Orientals deficient in ALDH I isozyme contain enzymatically inactive, immunologically cross-reactive material homologous with ALDH I. Thus, the absence of ALDH I isozyme is not due to a regulatory mutation, a gene deletion, or a nonsense mutation, but probably results from a structural mutation.(ABSTRACT TRUNCATED AT 250 WORDS)

48 citations

Journal ArticleDOI
TL;DR: The expression of selected Arabidopsis ALDH genes is induced in response to heat and stress combination, and ALDH mutant lines are more sensitive to heat stress and stress combinations.
Abstract: Aldehyde dehydrogenases (ALDH) are a family of enzymes that are involved in plant metabolism and contribute to aldehyde homeostasis to eliminate toxic aldehydes. The ALDH enzymes produce NADPH and NADH in their enzymatic reactions and thus contribute to balancing redox equivalents. Previous studies showed that Arabidopsis ALDH genes are expressed in response to high salinity, dehydration, oxidative stress, or heavy metals, suggesting important roles in environmental adaptation. However, the role of ALDH genes in high temperature and stress combinations (heat stress combined with dehydration, wounding, or salt stress) is unclear. Here, we analysed expression patterns of selected ALDH genes on the transcript and protein level at different time points of heat stress, basal and acquired thermotolerance, and stress combination treatments. Our results indicate that ALDH3I1 and ALDH7B4 are strongly induced by heat stress. Higher levels of ALDH7B4 accumulated in response to dehydration-heat, heat-salt and wounding-heat combination stress than in response to single stressors. The comparison of physiological and biological parameters in T-DNA double mutants of ALDH genes and wild-type plants demonstrated that mutant lines are more sensitive to heat stress and stress combinations than wild-type plants.

48 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023260
2022192
202170
202081
201980
201895