Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have studied the development of ocular aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) activities in C57BL/6J inbred male mice. Eyes were removed from freshly killed mice, enucleated, extracted, and analyzed for enzyme activities for animals of various ages during neonatal development, up to the adult stage. Activity levels were compared between mice maintained from birth in either complete darkness or on a 12-hour light/dark cycle. Ocular ALDH activity increased dramatically (greater than 30-fold) during the first 3 weeks of life. Moreover, light-adapted animals showed significantly higher ALDH activities from day 8. Ocular ADH activity also increased during development (greater than 5-fold) although the profile showed a steady increase to reach adult levels. Light-adapted mice showed no significant differences in ADH activity up to the weaning stage, as compared with mice maintained in darkness. These observations support proposals from earlier studies for major functional roles for both corneal ALDH and ADH in protecting the eye against ultraviolet light-induced damage.
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PMID:Development of aldehyde dehydrogenase and alcohol dehydrogenase in mouse eye: evidence for light-induced changes. 156 30

In sorbitol dehydrogenase only one cysteine residue, Cys-43, is reactive in both anionic buffer (phosphate) and zinc-liganding buffer (imidazole) upon carboxymethylation. This is in contrast to the situation in the structurally related liver alcohol dehydrogenase, with either of two alternative Cys residues being reactive, and is compatible with differences in zinc-binding and active site relationships between these two metalloenzymes. Unrelated aldehyde dehydrogenase, upon carboxamidomethylation, shows a third pattern, now less well defined but confirming the presence of a thiol function of Cys-302 close to the active site.
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PMID:Cysteine reactivity in sorbitol and aldehyde dehydrogenases. Differences towards the pattern in alcohol dehydrogenase. 159 5

Two types of factors can theoretically modulate alcohol metabolism toward increased acetaldehyde production. These factors are the following: (a) individual, genetically determined isoenzymes with distinct catalytic properties, and (b) modifications of enzyme activity induced by alcohol itself or liver damage. To investigate the respective roles of these factors in white individuals, we studied the alcohol dehydrogenase phenotype, together with liver alcohol dehydrogenase and aldehyde dehydrogenase activities, in 161 patients. Patients with alcoholic cirrhosis (n = 31) were compared with three types of controls: patients with nonalcoholic cirrhosis (n = 25) and excessive (n = 62) and moderate drinkers (n = 43) without liver disease. No association between alcohol dehydrogenase-3 phenotype and alcoholic cirrhosis was found. The prevalence of atypical alcohol dehydrogenase in the four groups was less than 1%. Patients with cirrhosis, regardless of its cause, had significantly lower alcohol dehydrogenase activity than the patients without cirrhosis (p less than 0.05 and p less than 0.01 vs. excessive and moderate drinkers, respectively). Among the noncirrhotic patients, alcohol dehydrogenase activity was significantly lower in the excessive drinkers than in the moderate drinkers (p less than 0.001). Aldehyde dehydrogenase activity was not different between cirrhosis-free excessive and moderate drinkers; in contrast, compared with these two groups, it was significantly lower in the two cirrhosis groups (p less than 0.01). These results suggest that no phenotypic pattern of alcohol dehydrogenase-3 associated with alcoholic cirrhosis in white patients exists, that liver alcohol dehydrogenase activity falls as a consequence of both alcohol abuse and cirrhosis and that liver aldehyde dehydrogenase activity is unaffected by alcohol abuse and only falls after the onset of cirrhosis.
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PMID:Polymorphism of alcohol dehydrogenase, alcohol and aldehyde dehydrogenase activities: implication in alcoholic cirrhosis in white patients. The French Group for Research on Alcohol and Liver. 832 17

The frequencies of the alleles encoding isozymes of alcohol dehydrogenase and aldehyde dehydrogenase were low in Northwest Coast Amerindians compared to Chinese subjects.
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PMID:Gene frequencies of alcohol dehydrogenase2 and aldehyde dehydrogenase2 in Northwest Coast Amerindians. 160 27

Cytochromes P-450 are extremely important in the oxidative metabolism of a variety of endogenous and exogenous compounds in pro- and eukaryotic organisms. Progress in understanding the structure and mechanism of action of this superfamily of enzymes has been hampered by the properties of the eukaryotic enzymes and the availability of only one well-characterized prokaryotic enzyme as a model. We report here the isolation of a Pseudomonas species which will utilize a monoterpene natural product, alpha-terpineol, as its sole source of carbon and energy. Approximately 1% of the soluble protein in the cell-free extract is a novel cytochrome P-450 (P-450terp). This enzyme and its associated iron sulfur protein electron carrier (terpredoxin) have been purified to homogeneity and their NH2-terminal amino acid sequences determined. The amino acid sequences of six tryptic peptide fragments of cytochrome P-450terp have also been determined. This sequence information was used to clone the gene encoding cytochrome P-450terp. Three clones representing approximately 8 kilobase pairs of unique sequences were selected and sequenced. Five non-overlapping open reading frames (ORFs) were found in the sequences, and the translated sequences were used to search the Protein Identification Resource for comparable proteins. The ORFs were identified as: 1) an alcohol dehydrogenase, 2) an aldehyde dehydrogenase, 3) cytochrome P-450terp, 4) terpredoxin reductase, and 5) terpredoxin. The identification of both the cytochrome P-450terp and terpredoxin DNA sequence was confirmed by the presence of each of the corresponding amino acid sequences found in the purified proteins. The five ORFs were bounded on both the 5' and 3' ends by consensus factor-independent terminator sequences. A consensus promoter sequence was found immediately 5' to the first ORF. These results indicate that we have sequenced the complete terp operon. Comparison of the amino acid sequence of cytochrome P-450terp to that of all other cytochromes P-450 has shown that it is the first member of the gene family CYP108. Preliminary characterization of the chemical and physical properties and the preparation of crystals of this new cytochrome P-450, suitable for x-ray diffraction analysis, indicate that it will be useful in comparison studies with other members of this class of proteins.
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PMID:Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. 162 18

1. Short-term intake of a 2% benzyl alcohol in the rat drinking fluid resulted in sex-dependent inhibition of hepatic alcohol dehydrogenase. 2. Benzyl alcohol intake also inhibited female but not male mitochondrial aldehyde dehydrogenase isoenzymes with the apparent low and high Km. 3. The benzyl alcohol inhibition kinetics were found non-competitive with the major differences in Vmax being confined to the cytoplasmic enzymes. 4. The velocity of the enzymatic reaction was greater for the substrate benzaldehyde than benzyl alcohol. 5. The results suggest sex-dependent hepatic alcohol dehydrogenase-substrate competition between benzyl alcohol and ethanol which may precipitate adverse metabolic interaction particularly in the susceptible female subject. 6. Modulation of the activity of this enzyme by benzyl alcohol may contribute to its toxicity as preservative in parentral injectable solutions.
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PMID:Benzyl alcohol adverse effects in the rat: implications for toxicity as a preservative in parentral injectable solutions. 168 18

The distribution of the human liver alcohol dehydrogenase, ADH2, and aldehyde dehydrogenase, ALDH2, genotypes in 21 different populations comprising Mongoloids, Caucasoids, and Negroids was determined by hybridization of the amplified genomic DNA with allele-specific oligonucleotide probes. Whereas the frequency of the ADH1(2) allele was found to be relatively high in the Caucasoids, Mexican Mestizos, Brazilian Indios, Swedish Lapps, Papua New Guineans and Negroids, the frequency of the ADH2(2) gene was considerably higher in the Mongoloids and Australian Aborigines. The atypical ALDH2 gene (ALDH2(2)) was found to be extremely rare in Caucasoids, Negroids, Papua New Guineans, Australian Aborigines and Aurocanians (South Chile). In contrast, this mutant gene was found to be widely prevalent among the Mongoloids. Individuals possessing the abnormal ALDH2 gene show alcohol-related sensitivity responses (e.g. facial flushing), have the tendency not to be habitual drinkers, and apparently suffer less from alcoholism and alcohol-related liver disease.
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PMID:Distribution of ADH2 and ALDH2 genotypes in different populations. 173 36

Ethanol was oxidized to acetate by an enzyme system using yeast alcohol dehydrogenase (YADH), yeast aldehyde dehydrogenase (YALDH), and lactic dehydrogenase (LDH) recycling NAD in two model duodenal fluids and in canine duodenal aspirate in vitro. Sufficient enzyme activities were maintained to convert as much as 34% of the original ethanol to acetate with negligible acetaldehyde accumulation.
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PMID:Multi-enzyme catalyzed rapid ethanol lowering in vitro. 175 12

The effect that variation in activities of the enzymes alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) has on the flux from 14C-ethanol to lipids was examined in third-instar larvae of Drosophila melanogaster and D. simulans. The activities of ADH and ALDH were also nutritionally manipulated by the inhibitor, cyanamide. Feeding larvae cyanamide before the flux test eliminated greater than 98% of the ALDH activity but only 40% of the ADH activity. The mean +/- SD flux control coefficient for ADH activity was 0.86 +/- 0.12, and that for ALDH activity was 0.02 +/- 0.07. This suggests that ADH is the major rate-limiting enzyme for the ethanol-to-lipid pathway in Drosophila larvae under the current experimental conditions.
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PMID:Metabolic control analysis and enzyme variation: nutritional manipulation of the flux from ethanol to lipids in Drosophila. 176 65

The effects of some tremor-producing and antitremor agents on the enzymes sequentially metabolizing ethanol and acetaldehyde in addition to biogenic-amine-derived aldehyde intermediates were studied in mouse liver preparations. Aldehyde but not alcohol dehydrogenase was differentially stimulated by the compounds studied in vitro. This effect was confined to the mitochondrial enzyme and was isoenzyme-dependent. The results indicate difference between in vitro and in vivo effects and suggest a role for mitochondrial aldehyde dehydrogenase in metabolic detoxification of endogenous biogenic aldehydes in the presence of alcohol which may explain the worsening of drug-induced tremor by ethanol.
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PMID:Effect of tremorogenic and antitumor agents on enzymes regulating a minor metabolic pathway of biogenic amines: an hypothesis for the underlying mechanism. 182 23


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