Showing papers on "Aldehyde dehydrogenase published in 1974"
TL;DR: The results show that the enzymes from the two fractions are not identical, and the level of aldehyde dehydrogenase activity found in each fraction should reflect the distribution pattern in vivo.
76 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: Alochol, acetaldehyde, NAD + - and NADP + -dependent acetaldehyde dehydrogenase activities were similarly affected by sulfhydryl compounds, changes of pH and storage at 0 and 45 °C, respectively.
61 citations
TL;DR: Barbiturates-like ethanol, as mediated by acetaldehyde-markedly modify neuroamine-derived aldehyde metabolism, thereby enhancing free glycolaldehyde levels and augmenting alkaloid formation.
23 citations
TL;DR: The path of aminoacetone metabolism in Pseudomonas sp.I.C.B. 8858 was concluded to involve l-1-aminopropan-2-ol, the O-phosphate ester of this compound, propionaldehyde and propionate as obligatory intermediates, and the aldehyde dehydrogenase-deficient mutants produced copious amounts of propional dehyde and acetaldehyde during growth on the corresponding amino alcohols.
Abstract: 1. Pseudomonas sp. N.C.I.B. 8858 grew well on d- and l-1-aminopropan-2-ol and on aminoacetone. 2. Cell-free extracts possessed high activities of inducibly formed l-1-aminopropan-2-ol-NAD + oxidoreductase, amino alcohol–ATP phosphotransferase, dl-1-aminopropan-2-ol O -phosphate phospho-lyase and aldehyde–NAD + oxidoreductase, but no 1-aminopropan-2-ol racemase or d-1-aminopropan-2-ol-NAD + oxidoreductase. 3. The amino alcohol kinase (activated by ADP) was non-stereospecific towards 1-aminopropan-2-ol and was one-third as active with ethanolamine. The phospho-lyase was active with l- and d-1-aminopropan-2-ol O -phosphate, but ethanolamine O -phosphate was only one-tenth as active as its higher homologues. The purified aldehyde dehydrogenase was active with propionaldehyde, acetaldehyde and also with methylglyoxal. The previously observed 2-oxo aldehyde dehydrogenase activity was considered to be due to the broadly specific aldehyde dehydrogenase. 4. Mutants of Pseudomonas sp. N.C.I.B. 8858 deficient in 1-aminopropan-2-ol kinase, 1-aminopropan-2-ol O -phosphate phospho-lyase, aldehyde dehydrogenase or an enzyme involved in propionate metabolism were incapable of growth on aminoacetone or 1-aminopropan-2-ol as carbon source, although all except the kinase- or phospho-lyasedeficient mutants could use these compounds and ethanolamine as nitrogen sources. The aldehyde dehydrogenase-deficient mutants produced copious amounts of propionaldehyde and acetaldehyde during growth on the corresponding amino alcohols. 5. The path of aminoacetone metabolism in Pseudomonas sp. N.C.I.B. 8858 was concluded to involve l-1-aminopropan-2-ol, the O -phosphate ester of this compound, propionaldehyde and propionate as obligatory intermediates. d-1-Aminopropan-2-ol was metabolized by the same route as the l-isomer, gratuitously inducing formation of the stereospecific l-1-aminopropan-2-ol dehydrogenase. 6. Extracts of the pseudomonad grown with ethanolamine as the nitrogen source were devoid of 1-aminopropan-2-ol dehydrogenase, the kinase and the phospho-lyase, but exhibited cobamide coenzyme-dependent deaminase activity. Mutants deficient in kinase or phospho-lyase (deaminating) grew well on ethanolamine as the nitrogen source. Ethanolamine deaminase was inactive with, but inhibited by, 1-aminopropan-2-ol.
15 citations
TL;DR: The ability of phenobarbital and 3-methylcholanthrene (3MC) to induce liver microsomal and soluble enzymes was compared in Sprague-Dawley and Long-Evans rats.
10 citations
TL;DR: The stereochemistry of hydrogen transfer between pyridine nucleotide and some intermediates of cholesterol catabolism was studied and the hydrogen transferred from NADH to 3α,7α,12α-trihydroxy-5β-cholestan-26-al and from acetaldehyde to NAD+ catalyzed by horse liver aldehyde dehydrogenase was the 4A-hydrogen.
8 citations
TL;DR: Disulfiram or related compounds were administered to rats by stomach tube and the activities of alcohol dehydrogenase and aldehyde dehydrogenases in the liver and the gastric mucosa were determined 43 h later.
Abstract: SUMMARY 1. Disulfiram or related compounds were administered to rats by stomach tube and the activities of alcohol dehydrogenase and aldehyde dehydrogenase in the liver and the gastric mucosa were determined 43 h later.
2. In liver, disulfiram did not affect alcohol dehydrogenase activity but reduced aldehyde dehydrogenase activity. The disulfiram metabolite diethyldithiocarbamate was without action.
3. In gastric mucosa, disulfiram had no effect on aldehyde dehydrogenase activity but enhanced alcohol dehydrogenase activity. Diethyldithiocarbamate had a similar effect.
4. The increase in alcohol dehydrogenase activity in the gastric mucosa might explain the hyperacetaldehydaemia produced by ethanol in disulfiram-treated patients.
7 citations
01 Jan 1974
TL;DR: Aldehyde dehydrogenases in rat liver : Properties, subcellular distribution and involvement in ethanol metabolism are studied.
Abstract: Aldehyde dehydrogenases in rat liver : Properties, subcellular distribution and involvement in ethanol metabolism
3 citations