Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A didelphid marsupial, the gray short-tailed opossum (Monodelphis domestica), was used as a model species to study the biochemical genetics of alcohol dehydrogenases (ADHs) and aldehyde dehydrogenase (ALDH) in corneal tissue. Isoelectric point variants of corneal ALDH (designated ALDH3) and a major soluble protein in corneal extracts were observed among eight families of animals used in studying the genetics of these proteins. Both phenotypes exhibited identical patterns following PAGE-IEF and were inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression. The data provided evidence for genetic identity of corneal ALDH with this major soluble protein, and supported biochemical evidence, recently reported for purified bovine corneal ALDH, that this enzyme constitutes a major portion of soluble corneal protein (Abedinia et al. 1990). Isoelectric point variants for corneal ADH were also observed, with patterns for the two major forms (ADH3 and ADH4) and one minor form (ADH5) being consistent with the presence of two ADH subunits (designated gamma and delta), and variant phenotypes existing for the gamma subunit. The genetics of this enzyme was studied in the eight families, and the results were consistent with codominant expression of two alleles at a single locus (designated ADH3). It is relevant that a major detoxification function has been proposed for corneal ADH and ALDH, in the oxidoreduction of peroxidic aldehydes induced by available oxygen and UV-B light (Holmes & VandeBerg, 1986a). In addition, a direct role for corneal ALDH as a UV-B photoreceptor in this anterior eye tissue has also been proposed (Abedinia et al. 1990).
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PMID:Genetics of alcohol dehydrogenase and aldehyde dehydrogenase from Monodelphis domestica cornea: further evidence for identity of corneal aldehyde dehydrogenase with a major soluble protein. 227 17

Acetaldehyde and butyraldehyde are substrates for alcohol dehydrogenase in the production of ethanol and 1-butanol by solvent-producing clostridia. A coenzyme A (CoA)-acylating aldehyde dehydrogenase (ALDH), which also converts acyl-CoA to aldehyde and CoA, has been purified under anaerobic conditions from Clostridium beijerinckii NRRL B592. The ALDH showed a native molecular weight (Mr) of 100,000 and a subunit Mr of 55,000, suggesting that ALDH is dimeric. Purified ALDH contained no alcohol dehydrogenase activity. Activities measured with acetaldehyde and butyraldehyde as alternative substrates were copurified, indicating that the same ALDH can catalyze the formation of both aldehydes for ethanol and butanol production. Based on the Km and Vmax values for acetyl-CoA and butyryl-CoA, ALDH was more effective for the production of butyraldehyde than for acetaldehyde. ALDH could use either NAD(H) or NADP(H) as the coenzyme, but the Km for NAD(H) was much lower than that for NADP(H). Kinetic data suggest a ping-pong mechanism for the reaction. ALDH was more stable in Tris buffer than in phosphate buffer. The apparent optimum pH was between 6.5 and 7 for the forward reaction (the physiological direction; aldehyde forming), and it was 9.5 or higher for the reverse reaction (acyl-CoA forming). The ratio of NAD(H)/NADP(H)-linked activities increased with decreasing pH. ALDH was O2 sensitive, but it could be protected against O2 inactivation by dithiothreitol. The O2-inactivated enzyme could be reactivated by incubating the enzyme with CoA in the presence or absence of dithiothreitol prior to assay.
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PMID:Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592. 227 27

1. On the basis of kinetic properties and sensitivity to pyrazole inhibition, it is shown that liver alcohol dehydrogenase present in human mainly corresponded to class I and in rat to class ADH-3 which differed in a number of parameters. 2. Two different aldehyde dehydrogenase (ALDH) isoenzymes were detected in both human and rat liver. The human isoenzymes corresponded to the ALDH-I and ALDH-II type. 3. In the rat, one isoenzyme had low Km and showed similar activity than in human liver but differed in their sensitivity to both disulfiran and nitrofazole inhibition whereas the other presented high Km and showed greater activity than the human one. 4. Caution must be therefore paid when extrapolating to human subjects the data on ethanol metabolism obtained with rats.
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PMID:Differences in kinetic characteristics and in sensitivity to inhibitors between human and rat liver alcohol dehydrogenase and aldehyde dehydrogenase. 227 87

Suicide inhibitors of acetylenic structure can inactive many enzymes playing an important role in the cancer cell metabolism. This type of inhibitors presents a fantastic interest because of its original inhibition mode: it is the catalytic mechanism of the enzyme itself which make the inhibitor reactive. In this way, thymidylate synthetase, ornithine decarboxylase, aldehyde dehydrogenase, aldehyde reductase are inhibit by acetylenic substrates. These very efficient compounds will allow to envisage a more selective chemotherapy of cancer.
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PMID:[Acetylenic enzyme inhibitors: their role in anticancer chemotherapy]. 228 2

Vinyl acetate is subject to microbial degradation in the environment and by pure cultures. It was hydrolyzed by samples of soil, sludge, and sewage at rates of up to 6.38 and 1 mmol/h per g (dry weight) under aerobic and anaerobic conditions, respectively. Four yeasts and thirteen bacteria that feed aerobically on vinyl acetate were isolated. The pathway of vinyl acetate degradation was studied in bacterium V2. Vinyl acetate was degraded to acetate as follows: vinyl acetate + NAD(P)+----2 acetate + NAD(P)H + H+. The acetate was then converted to acetyl coenzyme A and oxidized through the tricarboxylic acid cycle and the glyoxylate bypass. The key enzyme of the pathway is vinyl acetate esterase, which hydrolyzed the ester to acetate and vinyl alcohol. The latter isomerized spontaneously to acetaldehyde and was then converted to acetate. The acetaldehyde was disproportionated into ethanol and acetate. The enzymes involved in the metabolism of vinyl acetate were studied in extracts. Vinyl acetate esterase (Km = 6.13 mM) was also active with indoxyl acetate (Km = 0.98 mM), providing the basis for a convenient spectrophotometric test. Substrates of aldehyde dehydrogenase were formaldehyde, acetaldehyde, propionaldehyde, and butyraldehyde. The enzyme was equally active with NAD+ or NADP+. Alcohol dehydrogenase was active with ethanol (Km = 0.24 mM), 1-propanol (Km = 0.34 mM), and 1-butanol (Km = 0.16 mM) and was linked to NAD+. The molecular sizes of aldehyde dehydrogenase and alcohol dehydrogenase were 145 and 215 kilodaltons, respectively.
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PMID:Degradation of vinyl acetate by soil, sewage, sludge, and the newly isolated aerobic bacterium V2. 228 14

The in vivo ethanol elimination in human subjects, monkeys and rats was investigated after an oral ethanol dosage. After 0.4 g. ethanol/kg of body weight, ethanol elimination was much slower in human subjects than in monkeys. In order to detect a rise in monkey plasma ethanol concentrations as early as observed in human subjects, ethanol had to be administered at a dose of 3 g/kg body weight. Ethanol metabolism in rats was also much faster than in human subjects. However, human liver showed higher alcohol dehydrogenase activity and higher low Km aldehyde dehydrogenase activity than rat liver. Thus, our data suggest a lack of relationship between hepatic ethanol-metabolizing activities and the in vivo ethanol elimination rate.
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PMID:In vivo ethanol elimination in man, monkey and rat: a lack of relationship between the ethanol metabolism and the hepatic activities of alcohol and aldehyde dehydrogenases. 230 67

We have previously reported that a 37-kD liver protein formed an adduct with acetaldehyde in vivo when rats were fed alcohol chronically. To understand the mechanism of the formation of this protein-acetaldehyde adduct, rat hepatocytes in primary culture were treated with ethanol in vitro for several days. When cultured in hormone-enriched and trace metal-enriched Waymouth's medium, alcohol dehydrogenase activities in hepatocytes decreased only about 30% during 6 days of culture. At the end of the specified time, protein extracts of hepatocytes were immunotransblotted with rabbit immunoglobulin G that recognized acetaldehyde adduct as an epitope. The 37-kD protein-acetaldehyde adduct band could be detected within 3 days in cells that had been treated with alcohol at a steady-state concentration as low as 5 mmol/L. Although the maximal intensity was obtained at approximately 10 to 40 mmol/L ethanol, addition of cyanamide (an inhibitor of aldehyde dehydrogenase) further increased the intensity of this protein-acetaldehyde adduct band by more than twofold. A good correlation existed between acetaldehyde concentration in the medium and the intensity of the 37-kD protein-acetaldehyde adduct band. Formation of the 37-kD liver protein-acetaldehyde adduct is thus dependent on acetaldehyde, and the 37-kD protein is apparently unusually susceptible to chemical modification by acetaldehyde.
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PMID:Formation of the 37-kD protein-acetaldehyde adduct in primary cultured rat hepatocytes exposed to alcohol. 231 53

The in vivo effect of amantadine, chlorpromazine and reserpine on testicular aldehyde dehydrogenase (T-ALDH) was studied as a function of mouse strain. The effect of Leu-enkephalin and tetrahydropapaverine on rodent T-ALDH was also studied in vivo. The in vitro effect of chlorpromazine, papaverine and scopolamine on rodent subcellular T-ALDH and testicular alcohol dehydrogenase (T-ADH) were evaluated. A strain-linked difference in endogenous T-ALDH among the three mouse strains studied was determined. Individual injection of chlorpromazine or reserpine inhibited only albino ICR T-ALDH which was alleviated by pretreatment with amantadine and, thereby, suggesting antagonism between amantadine and these agents. The Leu-enkephalin administration induced T-ALDH from saline control. Tetrahydropapaverine did not influence the enzymes studied in vivo compared to an insignificant in vitro induction of T-ADH by the O-methylated analogue papaverine. Chlorpromazine noncompetitively inhibited T-ADH in vitro. The results indicate the modulation of the enzymes studied, which are involved in both detoxification of ethanol and biogenic amine-derived aldehyde intermediates, by agents affecting the endocrine system. This suggests the potential of these testicular enzymes in the evaluation of alcohol- and drug-induced endocrine adverse reactions.
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PMID:Gonadal alcohol and aldehyde dehydrogenase: in vivo and in vitro effects of psychoactive and endocrine agents. 231 66

The effect of cholinergics and an anticholinergic agent on hepatic ethanol metabolizing enzymes was studied. Short-term administration of the cholinomimetic arecoline or the anticholinergic scopolamine induced rat liver mitochondrial aldehyde dehydrogenase (L-ALDH) isoenzyme with the apparent high and low Km, respectively. In addition, scopolamine inhibited cytoplasmic L-ALDH. This suggests differential sensitivity of the L-ALDH isoenzymes to these agents. Scopolamine and the cholinomimetic pilocarpine enhanced rat and mouse liver alcohol dehydrogenase (L-ADH) in vitro, respectively. This indicates species-dependent effect of these agents on L-ADH. The results suggest interaction of the cholinergic system with ethanol metabolizing enzymes which may contribute to the peripheral action of alcohol.
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PMID:Cholinergic, anticholinergic agents and ethanol interaction. 232 54

Following daily intraperitoneal injections of ethanol at a dose of 3.5 g/kg rats developed tolerance to its hypnotic action, which was manifested in a drastic decrease of ethanol--induced sleep time and the number of animals sleeping more than 60 min. In the liver, this process was characterized by an elevated alcohol dehydrogenase activity and a decreased aldehyde dehydrogenase one, whereas that of MEOS remained unchanged.
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PMID:[System of ethanol and acetaldehyde metabolism in the rat liver during the development of ethanol tolerance]. 233 52


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