scispace - formally typeset
Search or ask a question
Topic

Aldehyde dehydrogenase

About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.


Papers
More filters
Journal ArticleDOI
TL;DR: Proteomic analyses suggest that liver mitochondria in old rats suffer from a decline in their capacity for energy production, due to decreased expression of OXPHOS complex I/V components and glycative damage to key fatty acid β-oxidation and TCA/urea cycle enzymes.

33 citations

Journal ArticleDOI
TL;DR: The present results for D-ADH, combined with data from the literature, establish that aldehyde oxidation, manifest as dismutation, is a widespread property of alcohol dehydrogenases with potential physiological importance in alcohol metabolism and alde Hyde detoxification.
Abstract: The ability of Drosophila alcohol dehydrogenase (D-ADH) to catalyze the oxidation of aldehydes to carboxylic acids has been re-examined. Prior studies are shown to have been compromised by a nonenzymic reaction between the aldehydic substrates and amine-containing buffers, e.g., glycine or Tris, and an amine-catalyzed addition of aldehyde to NAD+. These reactions interfere with spectrophotometric assays for monitoring aldehyde oxidation and obscure the nature and scope of D-ADH-catalyzed aldehyde oxidation, particularly at physiological pH. Use of nonreactive buffers, such as pyrophosphate or phosphate, and 1H NMR spectroscopy to monitor all the components of the reaction mixture reveals the facile dismutation of aldehydes into equimolar quantities of the corresponding acids and alcohols at both neutral and high pH. At high pH, dismutation is accompanied by a small burst of NADH production to a steady-state concentration ( < 10 microM) that represents a partitioning between NADH dissociation and aldehyde reduction. The increase in A340 is therefore not a direct measure of the aldehyde oxidation reaction, and the resulting kinetic values cannot be compared to those for alcohol dehydrogenation. The present results for D-ADH, combined with data from the literature, establish that aldehyde oxidation, manifest as dismutation, is a widespread property of alcohol dehydrogenases with potential physiological importance in alcohol metabolism and aldehyde detoxification.

33 citations

Journal ArticleDOI
TL;DR: It is concluded that treatment with disulfiram and cyanamide affects serotonin metabolism leading to increased production of 5-hydroxytryptophol, but there is a marked inter-individual variability in degree of response.
Abstract: The effect of the aldehyde dehydrogenase inhibitors disulfiram (Antabuse®) and cyanamide (calcium carbimide, Dipsan®) on the metabolism of serotonin measured as relative amounts of the metabolites 5-hydroxyindole-3-acetic acid and 5-hydroxytryptophol in urine were studied in alcoholic patients. Sixteen out of 23 patients receiving drug therapy showed elevated excretion of 5-hydroxytryptophol. However, there was a marked, 15-fold, variability in 5-hydroxytryptophol excretion rate between patients. A high degree of variability was also seen in another group of patients studied before and after introduction of drug therapy. When patients were followed during the dose interval, a time-dependent response after each single dose could be observed. The disulfiram response lasted over the course of several days whereas the response to cyanamide lasted for less than 12 hr. It is concluded that treatment with disulfiram and cyanamide affects serotonin metabolism leading to increased production of 5-hydroxytryptophol, but there is a marked inter-individual variability in degree of response.

33 citations

Journal ArticleDOI
TL;DR: The nucleotide sequence of the membrane-bound aldehyde dehydrogenase (ALDH) gene from an industrial vinegar producer, Acetobacter polyoxogenes, was determined and showed that ALDH was primarily translated as a 773-amino-acid protein and that the 44-amINO-acid sequence at the NH2-terminus was processed during maturation and localization in the membrane.
Abstract: The nucleotide sequence of the membrane-bound aldehyde dehydrogenase (ALDH) gene from an industrial vinegar producer, Acetobacter polyoxogenes, was determined. Comparison of the sequence with the NH2-terminal amino acid sequence of the mature ALDH and determination of the actual translational initiation codon by means of in vitro manipulation of the upstream and proximal regions of the cloned gene showed that ALDH was primarily translated as a 773-amino-acid protein and that the 44-amino-acid sequence at the NH2-terminus, which probably serves as a signal peptide, was processed during maturation and localization in the membrane. When ALDH was expressed in a large quantity in Escherichia coli cells after the coding region had been placed downstream of the lac promoter, the ALDH protein, which still contained the signal peptide and had no ALDH activity, was localized in the membrane fraction.

33 citations

Journal ArticleDOI
TL;DR: Missense mutations involving 24 amino acid positions in FALDH are more highly conserved among related class 3 aldehyde dehydrogenase enzymes than expected, suggesting that they are critically important for protein folding, catalysis or stability.

33 citations


Network Information
Related Topics (5)
Cell culture
133.3K papers, 5.3M citations
84% related
Gene expression
113.3K papers, 5.5M citations
84% related
Receptor
159.3K papers, 8.2M citations
83% related
Signal transduction
122.6K papers, 8.2M citations
82% related
Apoptosis
115.4K papers, 4.8M citations
82% related
Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023260
2022192
202170
202081
201980
201895