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)

Thermoanaerobium brockii was shown to catabolize glucose via the Embden-Meyerhof-Parnas pathway into ethanol, acetic acid, H(2)-CO(2), and lactic acid. Radioactive tracer studies, employing specifically labeled [(14)C]glucose, demonstrated significant fermentation of (14)CO(2) from C-3 and C-4 of the substrate exclusively. All extracts contained sufficient levels of activity (expressed in micromoles per minute per milligram of protein at 40 degrees C) to assign a catabolic role for the following enzymes: glucokinase, 0.40; fructose-1,6-diphosphate aldolase, 0.23; glyceraldehyde-3-phosphate dehydrogenase, 1.73; pyruvate kinase, 0.36; lactate dehydrogenase (fructose-1,6-diphosphate activated), 0.55; pyruvate dehydrogenase (coenzyme A acetylating), 0.53; hydrogenase, 3.3; phosphotransacetylase, 0.55; acetaldehyde dehydrogenase (coenzyme A acetylating), 0.15; ethanol dehydrogenase, 1.57; and acetate kinase, 1.50. All pyridine nucleotide-linked oxidoreductases examined were specific for nicotinamide adenine dinucleotide, except ethanol dehydrogenase which displayed both nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-linked activities. Fermentation product balances and cell growth yields supported the glucose catabolic pathway described. Representative balanced end product yields (in moles per mole of glucose fermented) were: ethanol, 0.94; l-lactate, 0.84; acetate, 0.20; CO(2), 1.31; and H(2), 0.50. Growth yields of 16.4 g of cells per mole of glucose were demonstrated. Both growth and end product yields varied significantly in accordance with the specific medium composition and incubation time.
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PMID:Glucose fermentation pathway of Thermoanaerobium brockii. 676 5

A strain of Escherichia coli with a mutation in the ana gene was shown to lack acetaldehyde dehydrogenase and alcohol dehydrogenase. The requirement of this strain for an external oxidant to grow anaerobically on glucose shows that the reduction of acetyl-CoA is the principal means of reoxidation of NADH produced during glycolysis in E. coli. Further mutants derived from the ana strain were shown to be affected in the enzymes involved in the fermentation of pyruvate (pyruvate formate-lyase, phosphotransacetylase, acetate kinase). A gene controlling acetate kinase (ackB) activity has been located at 39 min on the chromosomal map. Evidence is presented that anaerobic nitrite reduction with pyruvate involves at least the dehydrogenase subunit of the pyruvate dehydrogenase complex.
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PMID:Mutants of Escherichia coli K12 with defects in anaerobic pyruvate metabolism. 703 67

Significant quantitative differences in end-product yields by two strains of Clostridium thermocellum and one strain of Thermoanaerobium brockii were observed during cellobiose fermentation. Most notably, the ethanol/H(2) and lactate/acetate ratios were drastically higher for T. brockii as compared with C. thermocellum strains LQRI and AS39. Exogenous H(2) addition (0.4 to 1.0 atm) during culture growth increased the ethanol/acetate ratio of both T. brockii and AS39 but had no effect on LQRI. All strains had an operative Embden-Meyerhof glycolytic pathway and displayed catabolic activities of fructose-1,6-diphosphate-activated lactate dehydrogenase, coenzyme A acetylating pyruvate and acetaldehyde dehydrogenase, hydrogenase, ethanol dehydrogenase, and acetate kinase. Enzyme kinetic properties (apparent K(m), V(max), and Q(10) values) and the specificity of electron donors/acceptors for different oxidoreductases involved in pyruvate conversion to fermentation products were compared in the three strains. Both species contained ferredoxin-linked pyruvate dehydrogenase and pyridine nucleotide oxidoreductases. Ferredoxin-nicotinamide adenine dinucleotide (NAD) reductase activity was significantly higher in T. brockii than in AS39 and was not detectable in LQRI. H(2) production and hydrogenase activity were inversely related to ferredoxin-NAD reductase activity in the three strains. Ferredoxin-NAD phosphate reductase activity was present in cell extracts of both species. Alcohol dehydrogenase activity in C. thermocellum was NAD dependent, unidirectional, and inhibited by low concentrations of NAD and ethanol. Ethanol dehydrogenase activity of T. brockii was both NAD and NADP linked, reversible, and not inhibited by low levels of reaction products. The high lactate yield of T. brockii correlated with increased fructose-1,6-diphosphate. The relation of catabolic enzyme activity and quantitative differences in intracellular electron flow and fermentation product yields of these thermophilic bacteria is discussed.
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PMID:Ethanol production by thermophilic bacteria: relationship between fermentation product yields of and catabolic enzyme activities in Clostridium thermocellum and Thermoanaerobium brockii. 743 65

Individuals with the atypical aldehyde dehydrogenase ALDH2 allele, both homozygous and heterozygous status, are alcohol sensitive and have a markedly reduced risk of developing alcoholic diseases. Genetic abnormalities of the ALDH1 locus are also associated with alcohol flushing. The ALDH3 and ALDHx loci are polymorphic and their variations may affect the development of alcoholic diseases. The variations of alcohol dehydrogenase ADH2 and ADH3 loci have no profound effects on alcohol sensitivity. The newly identified ADH6 gene has hormone response elements, and it may cause the gender difference in alcoholic problems.
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PMID:Genetic polymorphisms of alcohol metabolizing enzymes related to alcohol sensitivity and alcoholic diseases. 769 85

Our previous experiments have shown that the appetite or preference for alcohol is affected by the rat strain and nutritional status, such as dietary protein levels. To determine the affected factors in alcohol preference, the alcohol metabolism in SHRSP (stroke-prone spontaneously hypertensive rats) and WKY (Wistar-Kyoto) rats fed with the standard level (15%) or low level (5%) purified egg protein diet (PEP) was investigated. The animals were kept on the experimental diets for 4 weeks. After 12 h fasting, a 15% ethanol solution was given in a dose of 100 mg ethanol per 100 g body weight with a gastric probe to all animals and the blood ethanol and acetaldehyde levels were determined. Compared with 15% PEP diet-fed SHRSP, WKY showed higher levels of blood ethanol and acetaldehyde. Furthermore, the same results were also observed in SHRSP and WKY fed with 5% PEP diet. On the other hand, regardless of the rat strain, rats fed a low level protein diet showed higher blood ethanol and acetaldehyde levels. We also found that there was no significant change in alcohol dehydrogenase (ADH) activity and acetaldehyde dehydrogenase (ALDH) activity between SHRSP and WKY. However, both SHRSP and WKY fed a 15% PEP diet showed higher ADH and ALDH activity compared with rats fed the 5% PEP diet. These results suggested that the affected factors of preference for alcohol may be correlated with blood ethanol and acetaldehyde levels after alcohol intake.
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PMID:Comparative study of alcohol metabolism in stroke-prone spontaneously hypertensive rats and Wistar-Kyoto rats fed normal or low levels of dietary protein. 775 73

A fragment of the Salmonella typhimurium ethanolamine utilization operon was cloned and characterized. The 6.3-kb nucleotide sequence encoded six complete open reading frames, termed cchA, cchB, eutE, eutJ, eutG, and eutH. In addition, the nucleotide sequences of two incomplete open reading frames, termed eutX and eutI, were also determined. Comparison of the deduced amino acid sequences and entries in the GenBank database indicated that eutI encodes a phosphate acetyltransferase-like enzyme. The deduced amino acid sequences of the EutE and EutG proteins revealed a significant degree of homology with the Escherichia coli alcohol dehydrogenase AdhE sequence. Mutations in eutE or eutG completely abolished the ability of mutants to utilize ethanolamine as a carbon source and reduced the ability to utilize ethanolamine as a nitrogen source. The product of eutE is most probably an acetaldehyde dehydrogenase catalyzing the conversion of acetaldehyde into acetyl coenzyme A. The product of the eutG gene, an uncommon iron-containing alcohol dehydrogenase, may protect the cell from unconverted acetaldehyde by converting it into an alcohol. The deduced amino acid sequence of cchA resembles that of carboxysome shell proteins from Thiobacillus neapolitanus and Synechococcus sp. as well as that of the PduA product from S. typhimurium. CchA and CchB proteins may be involved in the formation of an intracellular microcompartment responsible for the metabolism of ethanolamine. The hydrophobic protein encoded by the eutH gene possesses some characteristics of bacterial permeases and might therefore be involved in the transport of ethanolamine. Ethanolamine-utilization mutants were slightly attenuated in a mouse model of S. typhimurium infection, indicating that ethanolamine may be an important source of nitrogen and carbon for S. typhimurium in vivo.
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PMID:Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. 786 11

Acute alcohol ingestion can induce drug interactions, either pharmacokinetic or pharmacodynamic. Metabolically, they especially result from interference in the enzymatic systems which catalyse ethanol oxidation, the blocking of alcohol dehydrogenase, blocking of the microsomal oxidation system of ethanol with accumulation of the xenobiotic and risk of overdose, and blocking of acetaldehyde dehydrogenase with an antabuse effect. Pharmacodynamically, the main interactions result from the action of drugs having a sedative effect, such as tranquilizers but also antidepressants, neuroleptics, analgesics, H1 antihistamines, central antihypertensive drugs (CNS depressant?), etc. This sedative effect is increased by ethanol, which can be dangerous in at-risk situations.
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PMID:[Acute alcoholic intoxication and drugs]. 790 15

Entamoeba histolytica ferments glucose to ethanol under the anaerobic conditions of the human colon. There is special interest in this metabolic pathway because it provides an opportunity for parasite-specific chemotherapy. Peptide sequences from a 97-kDa E. histolytica protein, which was originally isolated because of extracellular matrix binding properties, were used to clone and sequence a gene that was found to encode an E. histolytica alcohol dehydrogenase and acetaldehyde dehydrogenase (EhADH2). The EhADH2 cDNA clone had an open reading frame encoding 870 amino acids with a predicted molecular weight of 95,758. The EhADH2 cDNA clone was identical in 48% of its amino acids to the multifunctional enzyme (alcohol dehydrogenase, acetyl-CoA reductase, and pyruvate-formate-lyase-deactivase) encoded by the Escherichia coli adhE gene. The isolation of the EhADH2 protein helps define a new family of ADH enzymes that may be specific to anaerobic and facultatively anaerobic organisms.
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PMID:Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. 793 3

A bifunctional 95 kDa polypeptide (EhADH2) harbouring acetaldehyde dehydrogenase and alcohol dehydrogenase activities was purified to homogeneity from trophozoite extracts of the protozoan parasite Entamoeba histolytica. Kinetic studies revealed that the enzyme utilizes NAD+ rather than NADP+ as cofactor. Km values for acetyl-CoA, acetaldehyde and ethanol were found to be 0.015, 0.15 and 80 mM respectively in the presence of 0.2 mM NAD+. The primary structure of EhADH2 as deduced from respective amoebic DNA sequences showed striking similarity to the trifunctional AdhE protein of Escherichia coli and the bifunctional AAD protein of Clostridium acetobutylicum. Alignment with a number of aldehyde dehydrogenases and alcohol dehydrogenases from various species suggested that the two catalytic functions of EhADH2 are located on separate parts of the molecule. By cross-linking experiments and electron-microscopic analysis, native EhADH2 was found to be organized in a homopolymeric fashion consisting of more than 20 associated promoters which form rods about 50-120 nm in length.
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PMID:Purification and molecular characterization of the NAD(+)-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica. 798 Apr 41

The Long-Evans Cinnamon (LEC) rat is a mutant strain established from Long-Evans rats. LEC rats display hereditary hepatitis and spontaneous hepatocellular carcinoma (HCC). We first tried to examine effects of ethanol consumption on the development of HCC, and fed a Lieber's liquid diet containing 5% ethanol to LEC rats. However the rats died within 2 weeks because of acute alcohol intoxication. In LEC rats, the concentration of ethanol and acetaldehyde in blood was significantly higher, and liver alcohol dehydrogenase activity was slightly lower and acetaldehyde dehydrogenase activities were remarkably suppressed compared to those of Wistar rats. These results suggest that LEC rats have hereditary deficiencies of ethanol and acetaldehyde metabolizing enzymes.
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PMID:Abnormal ethanol metabolism in Long-Evans Cinnamon rats, a mutant strain developing spontaneous hepatoma. 800 22


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