TY - JOUR. T1 - Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from those already characterized. AU - Parés, Xavier. AU - Moreno, Alberto. AU - Cederlund, Ella. AU - Höög, Jan Olov. AU - Jörnvall, Jans. PY - 1990/12/17. Y1 - 1990/12/17. N2 - The stomach form of alcohol dehydrogenase has been structurally evaluated by peptide analysis covering six separate regions of the rat enzyme. Overall, this new structure diners widely (32-40% residue differences) from the structures of three classes of alcohol dehydrogenase characterized before from the same species. Consequently, this novel enzyme constitutes a true fourth class of mammalian alcohol dehydrogenase. In particular, differences are extensive also towards class II, although enzymatic and physicochemical properties initially suggested overall similarities with class II. The new structure establishes the presence of one further alcohol dehydrogenase mammalian gene, extends ...
Mammalian alcohol dehydrogenase (ADH) constitutes a complex system with different forms and extensive multiplicity (ADH1-ADH6) that catalyze the oxidation and reduction of a wide variety of alcohols...
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. Early on in evolution, an effective method for eliminating both endogenous and exogenous formaldehyde was important and this ...
The best strategy for providing food and maintaining the environment on long-duration space missions is a bioregenerative life support system based on the growth of higher plants. Before such a system can be implemented, a better understanding of plant growth in space will have to be achieved. Little is known about the role of gravity-dependent physical processes in normal physiological function. A series of ground-based and spaceflight experiments was conducted to examine root oxygen availability in microgravity nutrient delivery systems. In spaceflight experiments Arabidopsis thaliana (L.) Heynh. plants were analyzed for changes in root medium redox potential and root alcohol dehydrogenase (ADH) activity, localization, and expression. These experiments showed ADH activity and expression increased by 89% and 136% respectively, without any change in localization. Ground experiments demonstrated the increase in ADH activity in spaceflight roots was achieved by a 28% decrease in oxygen availability.
Background: All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. This indicates that the class V ADH protein is not stable in a non-cellular environment, which is in contrast to all other human ADH enzymes. In this report we present evidence, supported with results from computational analyses performed in combination with earlier in vitro studies, why this ADH behaves in an atypical way. Results: Using a combination of structural calculations and sequence analyses, we were able to identify local structural differences between human class V ADH and other human ADHs, including an elongated beta-strands and a labile a-helix at the subunit interface region of each chain that probably disturb it. Several amino acid residues are strictly conserved in class I-IV, but altered in class V ADH. This includes a for class V ADH unique and conserved Lys51, a position directly involved ...
class I, II, IV alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, ...
After consumption, alcohol is mostly absorbed in the upper GI tract and then enters the liver via the portal vein. However, contrary to popular belief, some of it still does reach the distal small intestine, and concentrations close to the colon within an hour of drinking 2.5 standard drinks (0.8g/kg) were shown to reach 200mg/ml.[1] The majority of alcohol metabolism occurs in cells called hepatocytes, contained in the liver. At lower levels of consumption (average of 2 drinks), the body breaks down the alcohol through a process called oxidative conversion, where the enzyme alcohol dehydrogenase (ADH) turns it into the toxic compound acetaldehyde. This is then converted into acetate by another enzyme, acetaldehyde dehydrogenase (ALDH). In each step, NAD+ is reduced to NADH, resulting in the production of some reactive oxygen species. This process typically results in few negative side effects.[2] When larger amounts of alcohol are consumed, another metabolic pathway is used, known as the ...
Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene. This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes. GRCh38: Ensembl release 89: ENSG00000198099 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000037797 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide. Human ADH4 genome location and ADH4 gene details page in the UCSC Genome Browser. ...
Humans metabolize ethanol primarily through NAD+-dependent alcohol dehydrogenase (ADH) class I enzymes (i.e. ADH1A, ADH1B, and ADH1C) to acetaldehyde and then metabolize acetaldehyde primarily by NAD2-dependent aldehyde dehydrogenase 2 (ALDH2) to acetic acid.[26][27] Eastern Asians reportedly have a deficiency in acetaldehyde metabolism in a surprisingly high percentage (approaching 50%) of their populations. The issue has been most thoroughly investigated in native Japanese where persons with a single-nucleotide polymorphism (SNP) variant allele of the ALDH2 gene were found; the variant allele, encodes lysine (lys) instead of glutamic acid (glu) at amino acid 487; this renders the enzyme essentially inactive in metabolizing acetaldehyde to acetic acid.[28][29] The variant allele is variously termed glu487lys, ALDH2*2, and ALDH2*504lys. In the overall Japanese population, about 57% of individuals are homozygous for the normal allele (sometimes termed ALDH2*1), 40% are heterozygous for glu487lys, ...
Humans metabolize ethanol primarily through NAD+-dependent alcohol dehydrogenase (ADH) class I enzymes (i.e. ADH1A, ADH1B, and ADH1C) to acetaldehyde and then metabolize acetaldehyde primarily by NAD2-dependent aldehyde dehydrogenase 2 (ALDH2) to acetic acid.[27][28] Eastern Asians reportedly have a deficiency in acetaldehyde metabolism in a surprisingly high percentage (approaching 50%) of their populations. The issue has been most thoroughly investigated in native Japanese where persons with a single-nucleotide polymorphism (SNP) variant allele of the ALDH2 gene were found; the variant allele, encodes lysine (lys) instead of glutamic acid (glu) at amino acid 487; this renders the enzyme essentially inactive in metabolizing acetaldehyde to acetic acid.[29][30] The variant allele is variously termed glu487lys, ALDH2*2, and ALDH2*504lys. In the overall Japanese population, about 57% of individuals are homozygous for the normal allele (sometimes termed ALDH2*1), 40% are heterozygous for glu487lys, ...
The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11) was used to reduce the crystallization of mannitol. The addition of maltodextrin increased ADH activity and drastically changed the powder X-ray diffractogram of the spray-dried powders.
Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). This enzyme showed an unprecedented substrate scope and absolute enatioselectivity. The cofactor NADPH was used catalytically and regenerated in-situ by the biocatalyst, in the presence of 5% ethanol. The efficiency of HvADH2 for conversion of aromatic ketones was markedly influenced by the steric and electronic factors as well as the solubility of ketones in the reaction medium. Furthermore, carbonyl stretching bands frequencies ν ( ) have been measured for different ketones to understand the effect of electron withdrawing or donating properties of the ketones substituents on the reaction rate catalyzed by HvADH2. Good correlation was observed between ν ( ) of methyl aryl-ketones and the reaction rate catalyzed by HvADH2. The enzyme catalyzed the reductions of ketone ...
TY - JOUR. T1 - Molecular systematics of the genus Neotoma based on DNA sequences from intron 2 of the alcohol dehydrogenase gene. AU - Bradley, Robert. AU - Longhofer, Lisa. PY - 2006. Y1 - 2006. M3 - Article. JO - Journal of Mammalogy. JF - Journal of Mammalogy. ER - ...
TY - JOUR. T1 - Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.. AU - Qulali, M.. AU - Wolfla, C. E.. AU - Ross, R. A.. AU - Crabb, D. W.. PY - 1989. Y1 - 1989. UR - http://www.scopus.com/inward/record.url?scp=0024491855&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0024491855&partnerID=8YFLogxK. M3 - Article. C2 - 2471210. AN - SCOPUS:0024491855. VL - 290. SP - 143. EP - 153. JO - Progress in Clinical and Biological Research. JF - Progress in Clinical and Biological Research. SN - 0361-7742. ER - ...
Tobacco plants were transformed with a Nhap type Na,sup,+,/sup,/H,sup,+,/sup, antiporter gene, ,i,SynnhaP1,/i, (slr1595), from a cyanobacterium ,i,Synechocystis,/i, sp. PCC 6803. Two kinds of promoters, ,i,Arabidopsis,/i, alcohol dehydrogenase gene promoter (Adh promoter) and CaMV 35S promoter (35S promoter), were used. The transgenic plants driven by Adh promoter accumulated SynNhaP1 proteins only in root whereas the transgenic plants driven by 35S promoter accumulated SynNhaP1 proteins in all tissues. Confocal imaging of SynNhaP1-GFP fusion protein suggests the intracellular localization of SynNhaP1 in plasma membrane. Transgenic plants exhibited higher germination yields, increased biomass during developmental stage, increased seed production, and decreased intracellular Na,sup,+,/sup, content under salt-stress conditions. The transgenic plants driven by Adh promoter exhibited similar or slightly higher salt tolerance than that by 35S promoter. These results indicate the importance of ...
Multifactorial approaches can quickly and efficiently model complex, interacting natural or engineered biological systems in a way that traditional one-factor-at-a-time experimentation can fail to do. We applied a Design of Experiments (DOE) approach to model ethanol biosynthesis in yeast, which is well-understood and genetically tractable, yet complex. Six alcohol dehydrogenase (ADH) isozymes catalyze ethanol synthesis, differing in their transcriptional and post-translational regulation, subcellular localization, and enzyme kinetics. We generated a combinatorial library of all ADH gene deletions and measured the impact of gene deletion(s) and environmental context on ethanol production of a subset of this library. The data were used to build a statistical model that described known behaviors of ADH isozymes and identified novel interactions. Importantly, the model described features of ADH metabolic behavior without explicit a priori knowledge. The method is therefore highly suited to ...
The structural framework of cod liver alcohol dehydrogenase is similar to that of horse and human alcohol dehydrogenases. In contrast, the substrate pocket differs significantly, and main differences are located in three loops. Nevertheless, the substrate pocket is hydrophobic like that of the mammalian class I enzymes and has a similar topography in spite of many main-chain and side-chain differences. The structural framework of alcohol dehydrogenase is also present in a number of related enzymes like glucose dehydrogenase and quinone oxidoreductase. These enzymes have completely different substrate specificity, but also for these enzymes, the corresponding loops of the substrate pocket have significantly different structures. The domains of the two subunits in the crystals of the cod enzyme further differ by a rotation of the catalytic domains by about 6 degrees. In one subunit, they close around the coenzyme similarly as in coenzyme complexes of the horse enzyme, but form a more open cleft in ...
S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate ...
Expression-ready Human ADH5 cDNA ORF clone (HG17057-NY) with enhanced promotor in expression vector (pCMV3-N-HA) is confirmed by full-length sequence and validated in expression capability for gene expression studies or other applications. Quote for bulk production.
References for Abcams Recombinant Human ADH5 protein (ab124573). Please let us know if you have used this product in your publication
Alcohol, as a toxin, can result in cellular damage after prolonged effects. The first step toward metabolizing alcohol is to convert it to acetaldehyde. It has been found that 50% of the Pacific Rim Asian population (Chinese, Japanese, Koreans) possess an atypical alcohol dehydrogenase (ADH) known as ADH2*2 that leads to unusually rapid conversion of ethanol to acetaldehyde. This atypical ADH is less expressed in Caucasians, Africans Americans, Native Americans, and Asian Indian (Agarwal and Goedde, 1992). Since acetaldehyde is more toxic than alcohol, its increased accumulation causes flushing in the human body. Moreover, the normal aldehyde dehydrogenase (ALDH2), synthesized in the liver, oxidizes acetaldehyde into a carboxylic acid, acetic acid.[3] Mutant ALDH2 enzyme (known as ALDH2*2) in 45 to 53 percent of Japanese, Chinese, Korean, Taiwanese, and Vietnamese population, however, is only 8% as effective as the normal, wild-type enzyme (ALDH*1). This mutant allele of ALDH2 is dominant, as it ...
In the liver, ethanol is predominantly metabolised by alcohol dehydrogenase (ADH) and CYP 2E1, resulting in acetaldehyde (AA) formation. AA, the extremely toxic first intermediate of ethanol metabolism, binds rapidly to cellular proteins and also possibly to DNA. These AA adducts represent neoantigens leading to the formation of specific antibodies.26 AA has mutagenic and carcinogenic properties leading to metaplasia, inhibition of DNA repair,27 sister chromatid exchanges,28 stimulation of apoptosis, and enhanced cell injury associated with hyperregeneration.29 According to the International Agency for Research on Cancer, there is sufficient evidence to identify AA as a carcinogen in animals.. Ethanol is metabolised by the successive action of ADH and aldehyde dehydrogenase (ALDH). For both ADH and ALDH, genetic polymorphisms have been described that influence the rate of conversion of ethanol to AA and of the latter to acetate.30 It has been consistently reported that ALDH2 is the most ...
We have tested for effects of alcohol dehydrogenase (ADH) genotypes on self-reported alcohol consumption and symptoms of alcohol dependence, recorded on three occasions up to 15 years apart, in 377 male and female subjects of European descent. ADH2 genotype had significant effects on both consumptio …
Alzheimers disease ; Beta-amyloid ; Aß-binding alcohol dehydrogenase (ABAD) ; Receptor for advanced glycation end products (RAGE) ; QP552.A45R4 ; Amyloid beta-protein ; Alcohol dehydrogenase ; Cell receptors ; Alzheimers disease
Paleogenetics is an emerging field that resurrects ancestral proteins from now-extinct organisms to test, in the laboratory, models of protein function based on natural history and Darwinian evolution. Here, we resurrect digestive alcohol dehydrogenases (ADH4) from our primate ancestors to explore the history of primate-ethanol interactions. The evolving catalytic properties of these resurrected enzymes show that our ape ancestors gained a digestive dehydrogenase enzyme capable of metabolizing ethanol near the time that they began using the forest floor, about 10 million y ago. The ADH4 enzyme in our more ancient and arboreal ancestors did not efficiently oxidize ethanol. This change suggests that exposure to dietary sources of ethanol increased in hominids during the early stages of our adaptation to a terrestrial lifestyle. Because fruit collected from the forest floor is expected to contain higher concentrations of fermenting yeast and ethanol than similar fruits hanging on trees, this ...
TY - JOUR. T1 - Hominids adapted to metabolize ethanol long before human-directed fermentation. AU - Carrigan, Matthew A.. AU - Uryasev, Oleg. AU - Frye, Carole B.. AU - Eckman, Blair L.. AU - Myers, Candace R.. AU - Hurley, Thomas D.. AU - Benner, Steven A.. PY - 2015/1/13. Y1 - 2015/1/13. N2 - Paleogenetics is an emerging field that resurrects ancestral proteins from now-extinct organisms to test, in the laboratory, models of protein function based on natural history and Darwinian evolution. Here, we resurrect digestive alcohol dehydrogenases (ADH4) from our primate ancestors to explore the history of primate-ethanol interactions. The evolving catalytic properties of these resurrected enzymes show that our ape ancestors gained a digestive dehydrogenase enzyme capable of metabolizing ethanol near the time that they began using the forest floor, about 10 million y ago. The ADH4 enzyme in our more ancient and arboreal ancestors did not efficiently oxidize ethanol. This change suggests that ...
Transgenic arabidopsis plants containing the alcohol dehydrogenase (Adh) gene promoter fused to the green fluorescent protein (GFP) reporter gene were developed as biological sensors for monitoring physiological responses to unique environments. Plan
Ruth, like many Asian Americans, has at times been reluctant to drink wine because of her tendency to turn a deep shade of red after even just half a glass of red or white.. The cause of this wine flush has to do with how many Asians metabolize alchohol. Alchohol is absorbed through the stomach and small intestine. About 10 percent is eliminated by the kidneys, lungs, and sweat glands, but the rest is dealt with in the liver by two enzymes: alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). I dont know enough about the bodys chemistry to know how these two enzymes actually manage to break down the alchohol, but its enough to know that they do.. Its this second enzyme (ALDH) that is missing (or low) in up to 50 percent of Asian people, and is not present at all in most Native Americans and Inuits. People with less ALDH will often flush and sweat after drinking alcohol, and if their quantities of the enzyme are quite low, they may also become ill after drinking even small amounts ...
1. The excretion of H+ ions, with practically equivalent uptake of K+ ions (from 0·1m-potassium chloride), occurs during the aerobic oxidation of ethanol. 2. Acetaldehyde and acetic acid formed at the same time are quantitatively equal to the amount of ethanol oxidized. 3. A slow uptake of K+ ions occurs during the oxidation of acetaldehyde and a more rapid uptake during the oxidation of d-glyceraldehyde 3-phosphate. 4. The anaerobic reduction of methylene blue is studied, and the inhibitory effect of K+ and other inorganic cations on the system demonstrated. 5. The cation requirement for equal inhibitory effect is parallel with the reciprocals of the transport affinities for the physiological K-carrier (as taken from Conway & Duggan, 1958). 6. The cation inhibition of methylene blue reduction is reversed by treatment of the yeast with Teepol or by freezing-and-thawing. 7. Azide is shown to inhibit the reduction of methylene blue with intact cells. The inhibition is partially reversed by ...
SWISS-MODEL Template Library (SMTL) entry for 3cos. Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn
SORD [ENSP00000267814]. L-iditol 2-dehydrogenase; Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm; Belongs to the zinc-containing alcohol dehydrogenase family.. Synonyms: SORD, B7Z3A6, H0YKB3, H0YLA4, Q00796 .... Linkouts: STRING Pharos UniProt OMIM ...
Accepted name: alcohol dehydrogenase (nicotinoprotein). Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor. Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Systematic name: ethanol:acceptor oxidoreductase. Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].. Links to other databases: BRENDA, ...
Alcohol use that begins during adolescence affects the development of alcohol use disorders during adulthood. A new study looks at the effects of interplay between peer drinking and the functional variant rs1229984 in the alcohol dehydrogenase 1B gene (ADH1B) among adolescents. Peer drinking reduces the protective effects of this ADH1B variant.
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Three anti-horse liver alcohol dehydrogenase (HLADH) monoclonal antibodies are described. Two are specific for ADH and cross-react with class I and II enzymes from mouse, horse and Chinese hamster....
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
1A72: Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Vanillin is a potent fermentation inhibitor derived from the lignocellulosic biomass in biofuel production, and high concentrations of vanillin result in the pronounced repression of bulk translation in Saccharomyces cerevisiae. Studies on genes that are efficiently translated even in the presence of high concentrations of vanillin will be useful for improving yeast vanillin tolerance and fermentation efficiency. The BDH1 and BDH2 genes encode putative medium-chain alcohol dehydrogenase/reductases and their amino acid sequences are very similar to each other. Although BDH2 was previously suggested to be involved in vanillin tolerance, it has yet to be clarified whether Bdh1/Bdh2 actually contribute to vanillin tolerance and reductions in vanillin. Therefore, we herein investigated the effects of Bdh1 and Bdh2 on vanillin tolerance. bdh2Δ cells exhibited hypersensitivity to vanillin and slower reductions in vanillin than wild-type cells and bdh1Δ cells. Additionally, the overexpression of the BDH2 gene
If your face goes red when drinking alcohol, youre not alone. More than one in three people with East Asian heritage (Chinese, Japanese, and Korean) experience facial flushing when drinking beer, wine, or spirits.. In Asian populations, it is due to an inherited deficiency in one of the enzymes involved in the breakdown of alcohol: aldehyde dehydrogenase. This type of reaction is very rare, but not unknown, in other ethnic groups.. But there is more to this deficiency than just an embarrassing reddening of the face. There are positive and negative health implications. And it provided a lightbulb moment, helping us understand how a common treatment for alcoholism works.. How you digest alcohol. Alcohol is broken down in your liver in two steps. In the first step, the enzyme alcohol dehydrogenase converts alcohol into a rather nasty chemical called acetaldehyde. A build up of this toxic chemical is one of the reasons you feel sick when hungover.. Then a second enzyme, aldehyde dehydrogenase, ...
My research centers on molecular population genetics and evolution. I am interested in understanding the evolutionary basis for high levels of polymorphisms within species, and in determining whether natural selection contributes to the maintenance of within- species variation. I am also interested in knowing whether molecular evolution between species results from the same evolutionary forces that produce intra-species variation. Using the alcohol dehydrogenase locus (Adh) as a model system, our studies reveal how selection has contributed to the evolution of the locus over three time scales: affecting populations, affecting species, and affecting long-term molecular evolution. Finally, because our ability to acquire molecular data is limited by technology, I place a special emphasis on developing better methods for measuring genetic variation. Current projects in the lab include the role of natural selection in the evolution of codon nias, the relationship between recombination rates and ...
The present study discusses the metabolism of ethanol in the human body from the ingestion of ethanol to the excretion of its break down products water and carbon dioxide. Ethanol is a small molecule, soluble in water as well as in organic solutions. It is quickly distributed to every section in the body, where it exerts a direct toxic effect on the cells. Ethanol cannot directly leave the body efficiently so it needs other metabolic pathways. The molecule is metabolized by oxidation, predominately in the liver. The enzyme alcohol dehydrogenase catalyses the degradation of ethanol to acetaldehyde. Acetaldehyde is even more toxic than ethanol and it is degraded by the enzyme aldehyde dehydrogenase. In chronic alcoholics other chemical processes such as the cytochrome P450 system may have a bigger impact on alcohol metabolism.. The carbohydrate metabolism is extensively affected by ethanol. Most important is its restrictive effect on the gluconeogenesis leading to sustained hypoglycaemia in ...
The pattern that we developed to detect this class of enzymes is based on a conserved region that includes a histidine residue which is the second ligand of the catalytic zinc atom. This family also includes NADP-dependent quinone oxidoreductase (EC 1.6.5.5), an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [7]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The torpedo fish and mammlian synaptic vesicle membrane protein vat-1 is realted to qor. We have developed a specific pattern for this subfamily. Expert(s) to contact by email: Joernvall H ...
Method of Action. Zinc is an important metallic constituent of the enzyme carboxypeptidase A, a pancreatic enzyme active in protein degradation. Zinc is found in highest concentration in the liver, with lesser amounts found in the pancreas, kidney, and pituitary gland. Zinc absorption occurs primarily in the small intestine. Zinc-binding ligand molecules act to transport zinc across the mucosal cells of the intestine, where it is picked up by albumin molecules for transport to the liver and other organs.. Zinc is a constituent of the enzyme carbonic anhydrase. This enzyme is, in turn, a constituent of red blood cells and gastric juices, and plays an important role in the deposition of calcium salts in teeth and bones.. The enzyme alcohol dehydrogenase contains zinc and is essential for the conversion of alcohol to an aldehyde, thereby facilitating alcohol metabolism in the liver. The function of this enzyme and its relationship to the development of liver cirrhosis is conspicuously tied to ...
TY - JOUR. T1 - Alcohol dehydrogenase activity in mouse brown adipose tissue. AU - Muralidhara, D. V.. AU - Desautels, M.. PY - 1996/4/1. Y1 - 1996/4/1. N2 - The present work provides evidence for the occurrence of the enzyme alcohol dehydrogenase (ADH) in very minute concentration in mice brown adipose tissue (BAT). Mice consuming 10% ethanol for 10 days showed significantly lowered enzyme activity in brown fat while liver ADH activity was increased but not significantly. Measurements of basal and norepinephrine stimulated oxygen consumption of isolated brown adipocytes indicated that the presence of ADH in BAT of mice is unlikely to play any role in ethanol oxidation.. AB - The present work provides evidence for the occurrence of the enzyme alcohol dehydrogenase (ADH) in very minute concentration in mice brown adipose tissue (BAT). Mice consuming 10% ethanol for 10 days showed significantly lowered enzyme activity in brown fat while liver ADH activity was increased but not significantly. ...
Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. The pigeon enzyme turns out to be of class I type and the dogfish enzyme of class III type. This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. It is discernable as the major liver form at about the level in-between cartilaginous and osseous fish. The results also show early divergence within the avian orders. Structures were determined by Edman degradations, making it appropriate to acknowledge ...
The membrane-bound alcohol dehydrogenase (ADH) activity of Acetobacter pasteurianus NCI1380 was enhanced more than 10-fold by the addition of ethanol to the medium. In order to elucidate the mechanism of the ethanol induction, a gene cluster encoding the dehydrogenase and cytochrome c subunits of ADH was cloned from this strain, and its nucleotide sequence was determined. Comparison of the deduced amino acid sequences and the NH2-terminal sequences determined with purified proteins showed that the dehydrogenase and cytochrome c subunits contained typical signal peptides of 35 and 26 amino acids, respectively. Transcriptional analysis of the cloned genes by primer extension revealed that the gene cluster was transcribed from two different promoters upstream from the dehydrogenase gene. One (59 bp upstream of the ATG start codon) of the two promoters was used in the presence of ethanol, whereas the other (232 bp upstream of the ATG start codon) was used in the absence of ethanol. Immunoblot ...
Title: Effects of Trehalose on Pressure-Induced Inactivation of Yeast Alcohol Dehydrogenase. VOLUME: 12 ISSUE: 6. Author(s):Hyun Park, Gene Kidman and Dexter B. Northrop. Affiliation:Center for Drug Evaluation Division of Pharmaceutical Sciences, School of Pharmacy, University ofWisconsin-Madison, Madison, WI 53705, U.S.A.. Keywords:yeast alcohol dehydrogenase, trehalose, hydrostatic pressure, protein denaturation, barostability, thermostability, surface tension. Abstract: Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures ( < 3 kbar). The time courses for inactivation are biphasic and both phases of both isozymes are protected by trehalose. ADH-I is slightly more barostable than ADH-II which is opposite to their thermostabilities. Trehalose at 1M extends their halflives about 6-fold at 2 kbar, pH 7.5 and 25°C. In contrast, 1M sucrose provides only 4.4-fold protection under identical conditions, a finding consistent with the superior protein ...
TY - JOUR. T1 - Translation Initiation in Drosophila melanogaster Is Reduced by Mutations Upstream of the AUG Initiator Codon. AU - Feng, Yue. AU - Gunter, Lee E.. AU - Organ, Edward L.. AU - Cavener, Douglas R.. N1 - Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 1991/4. Y1 - 1991/4. N2 - The importance to in vivo translation of sequences immediately upstream of the Drosophila alcohol dehydrogenase (Adh) start codon was examined at two developmental stages. Mutations were introduced into the Adh gene in vitro, and the mutant gene was inserted into the genome via germ line transformation. An A-to-T substitution at the -3 position did not affect relative translation rates of the ADH protein at the second-instar larval stage but resulted in a 2.4-fold drop in translation of ADH at the adult stage. A second mutant gene, containing five mutations in the region -1 to -9, was designed to completely block translation initiation. However, transformant lines bearing these mutations ...
TY - JOUR. T1 - Hydride transfer in liver alcohol dehydrogenase. T2 - Quantum dynamics, kinetic isotope effects, and role of enzyme motion. AU - Billeter, S. R.. AU - Webb, S. P.. AU - Agarwal, P. K.. AU - Iordanov, T.. AU - Hammes-Schiffer, S.. PY - 2001/11/14. Y1 - 2001/11/14. N2 - The quantum dynamics of the hydride transfer reaction catalyzed by liver alcohol dehydrogenase (LADH) are studied with real-time dynamical simulations including the motion of the entire solvated enzyme. The electronic quantum effects are incorporated with an empirical valence bond potential, and the nuclear quantum effects of the transferring hydrogen are incorporated with a mixed quantum/classical molecular dynamics method in which the transferring hydrogen nucleus is represented by a three-dimensional vibrational wave function. The equilibrium transition state theory rate constants are determined from the adiabatic quantum free energy profiles, which include the free energy of the zero point motion for the ...
The purpose of this study was to investigate the effect of protein and dietary fiber levels on the activities of ehanol metabilizing enzymes of the brain in acute and chronic ethanol-treated rats. Male Sprague-Dwley rats were fed on diets containing two levels of protein(7%, 20%)) with two levels of fiber(5%, 105) for 5 weeks. Rats were orally administered 40% (v/v) ethanol(5g/body weight) 90 min before decapitation in the acute ethanol-treated groups and 25% (v/v) ethanol (5g/kg body weight) once a day for 5 weeks in the chronic ethnol-treated groups. Cytosilic alcohol dehydrogenase (ADH) activities were higher than those of mitochondrial ADH. The ADH activities were increased by 20% protein and %% fiber levels in the diet in two fractions , but were decreased by chronic ethanol treatment. Mitochondrial aldehyde dehydrogenase (ALDH) activities did not change by ethanol treatment but were increased by the 20% protein level. However, cytosilic ALDH activities were decreased by chronic ethanol ...
3.0.CO;2-T, The Genomic Basis of Postponed Senescence in Drosophila melanogaster, Evidence for premature aging in a Drosophila model of Werner syndrome, Drosophila mate copying correlates with atmospheric pressure in a speed learning situation, Male fruit flies learn to avoid interspecific courtship, Sexual experience enhances Drosophila melanogaster male mating behavior and success, tinman and bagpipe: two homeo box genes that determine cell fates in the dorsal mesoderm of Drosophila, The structure and evolution of cis-regulatory regions: the shavenbaby story, Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation, The influence of Adh function on ethanol preference and tolerance in adult Drosophila melanogaster, Genetics and genomics of alcohol responses in Drosophila, Ecological Niche Difference Associated with Varied Ethanol Tolerance between Drosophila suzukii and Drosophila melanogaster (Diptera: Drosophilidae), Deletion of a ...
Alcohol metabolism is dependent on two enzymes: alcohol dehydrogenase (ADH) that converts alcohol to acetaldehyde, and acetaldehyde dehydrogenase (ALDH) that further converts acetaldehyde to harmless products (like acetate).. About 80% of Asians have a hyper-functional alcohol dehydrogenase.3 That means Asians metabolize alcohol to acetaldehyde up to 100 times faster than others, but never really experience the buzz that normally comes with booze. Additionally, 40% have some sort of malfunction of acetaldehyde dehydrogenase (ALDH) that metabolizes further down the acetaldehyde. This is essentially a double whammy - they metabolize alcohol intake far too quickly into a toxic stage where it cant easily get out.. In practice, that glass of wine is converted to acetaldehyde too fast, and it just gets stuck inside of sufferers - then uncomfortable side effects ensue. Basically, their bodies arent fully equipped to break down alcohol in a safe and enjoyable way. Its safe to call this an alcohol ...
Looking for online definition of Alcohol metabolism in the Medical Dictionary? Alcohol metabolism explanation free. What is Alcohol metabolism? Meaning of Alcohol metabolism medical term. What does Alcohol metabolism mean?
4-Methyl pyrazole (4-MP, a specific inhibitor of alcohol dehydrogenase) reduced ethanol elimination by 30-50% and completely removed the ethanol-induced inhibition of galactose elimination in 2 control subjects. Ethanol elimination was accelerated in 2 alcoholics with adequate nutrition, but the effect of 4-MP was comparable to that in controls. In 2 other alcoholic subjects, who reported poor nutritional intake, intermediate rates of ethanol elimination were observed and 4-MP had almost no effect on ethanol or galactose elimination. These results suggest that alcohol abuse may result in an increased contribution to ethanol elimination by pathways other than that involving alcohol dehydrogenase (ADH) and that the decreased contribution from ADH, possibly potentiated by inadequate nutrition, may diminish the ethanol-induced shift in the NAD-coupled redox state. Since liver damage produced by alcohol abuse is believed to be related to changes from the normal redox state caused by ethanol, these ...
Steven Joseph Szarka (sjszarka at acs.ucalgary.ca) wrote: : Is the ADH promoter considered constitutive?, or is it up regulated : during anoxia? : I seem to get good expression in 5 ml tube cultures but lose expression : when I scale up to 100 mls in 250 mls flasks. : Thanks for any help : Steve : _______________________________________________________________________ : Steven Szarka Botany Division : Dept. of Biological Sciences : Email: sjszarka at acs.ucalgary.ca University of Calgary : FAX: (403) 289-9311 2500 University Drive NW : Phone: (403) 220-7907 Calgary, AB, Canada T2N 1N4 : _______________________________________________________________________ ...
TY - JOUR. T1 - Influence of temperature on the production of archaeal thermoactive alcohol dehydrogenases from Pyrococcus furiosus with recombinant E. coli. AU - Kube, J.. AU - Brokamp, C.. AU - Machielsen, M.P.. AU - van der Oost, J.. AU - Markl, H.. PY - 2006. Y1 - 2006. N2 - The heterologous production of a thermoactive alcohol dehydrogenase (AdhC) from Pyrococcus furiosus in Escherichia coli was investigated. E. coli was grown in a fed-batch bioreactor in minimal medium to high cell densities (cell dry weight 76 g/l, OD600 of 150). Different cultivation strategies were applied to optimize the production of active AdhC, such as lowering the cultivation temperature from 37 to 28°C, heat shock of the culture from 37 to 42°C and from 37 to 45°C, and variation of time of induction (induction at an OD600 of 40, 80 and 120). In addition to the production of active intracellular protein, inclusion bodies were always observed. The maximal activity of 30 U/l (corresponding to 6 mg/l active ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
Excessive alcohol consumption is associated with spontaneous burning pain, hyperalgesia, and allodynia. Although acetaldehyde has been implicated in the painful alcoholic neuropathy, the mechanism by which the ethanol metabolite causes pain symptoms is unknown. Acute ethanol ingestion caused delayed mechanical allodynia in mice. Inhibition of alcohol dehydrogenase (ADH) or deletion of transient receptor potential ankyrin 1 (TRPA1), a sensor for oxidative and carbonyl stress, prevented allodynia. Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia. Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1. Chronic ethanol ...
It is the simplest alcohol, and is a light, volatile, colourless, flammable, poisonous liquid with a distinctive odor that is somewhat milder and sweeter than ethanol (Wikipedia). Methanol is responsible for accidental, suicidal, and epidemic poisonings, resulting in death or permanent sequelae. Toxicity is due to the metabolic products of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase. (PMID 15627163 ). The rapid and accurate diagnosis of toxic alcohol poisoning due to methanol (methyl alcohol) is paramount in preventing serious adverse outcomes. The quantitative measurement of specific serum levels of methanol using gas chromatography is expensive, time consuming and generally only available at major tertiary-care facilities. (PMID 15862085 ...
Owades knew ... that active dry yeast has an enzyme in it called alcohol dehydrogenases (ADH) ... if you also have that enzyme in your stomach when the alcohol first hits it, the ADH will begin breaking it down before it gets into your bloodstream and, thus, your brain. And it will mitigate - not eliminate - but mitigate the effects of alcohol! Koch told me.. In his final years Owades even patented a product called Prequel, an all-natural pill similarly designed to limit drunkenness. No companies wanted to deal with the potential liabilities of the product, and Owades died in 2005 at the age of 86.. ...
In the first part of this work, the pentose phosphate pathway (PPP) was investigated as a source of NADPH in reductive whole-cell biotransformation using $\textit{Escherichia coli}$ and $\textit{Corynebacterium glutamicum}$ as hosts and glucose as reductant. The reduction of methyl acetoacetate to the chiral (R)-methyl hydroxybutyrate (MHB) served as a model reaction for NADPH-dependent reactions and was catalyzed by an alcohol dehydrogenase (ADH) from $\textit{Lactobacillus brevis}$. Partial cyclization of the PPP in $\textit{E. coli}$ and $\textit{C. glutamicum}$ was achieved by deletion of the phosphofructokinase gene $\textit{pfkA}$, which prevents fructose 6-phosphate catabolism in the glycolytic pathway. The $\textit{pfkA}$-deficient mutants carrying the $\textit{L. brevis}$ ADH showed a doubled MHB-per-glucose ratio compared to the parent strains. In $\textit{E. coli}$ the partial PPP cyclization in the Δ$\textit{pfkA}$ mutant was proven by $^{13}$C-flux analysis, which showed a negative ...
Characterization of polymorphisms of genes ADH2, ADH3, ALDH2 and CYP2E1 and relationship to the alcoholism in a Colombian population
Hyperthermophiles grow optimally at 80 ºC and above, and many of them have the ability to utilize various carbohydrates as carbon source and produce ethanol as an end product. Alcohol dehydrogenase (ADH) is a key enzyme responsible for alcohol production, catalyzing interconversions between alcohols and corresponding ketones or aldehydes. ADHs from hyperthermophiles are of great interests due to their thermostability, high activity and enantioselectivity. The gene encoding ADH from hyperthermophilic archaeon Thermococcus guaymasensis was cloned, sequenced and over-expressed. DNA fragments of the genes encoding the ADHs were amplified directly from the corresponding genomic DNA by combining the use of conventional and inverse PCRs. The entire gene was detected to be 1092 bp and the deduced amino acid sequence had a total of 364 amino acids with a calculated molecular mass of 39463 Dalton. The enzyme belonged to the family of zinc-containing ADHs with catalytic zinc only. It was verified that the ...
Drosophila has long been useful for demonstrating the principles of classical Mendelian genetics in the classroom. In recent years, the organism has also helped students understand biochemical and behavioral genetics. In this connection, this article describes the development of a set of integrated laboratory exercises and descriptive materials--a laboratory module--in biochemical genetics for use by high-school students. The module focuses on the Adh gene and its product, the alcohol dehydrogenase enzyme. Among other activities, students using the module get to measure alcohol tolerance and to assay alcohol dehydrogenase activity in Adh-negative and -positive flies. To effectively present the module in the classroom, teachers attend a month-long Dissemination Institute in the summer. During this period, they learn about other research activities that can be adapted for classroom use. One such activity that has proved popular with teachers and students utilizes Drosophila to introduce some of ...
Drosophila melanogaster Adult enhancer factor 1 (Aef1) datasheet and description hight quality product and Backed by our Guarantee
TY - JOUR. T1 - Incorporation of the genetic control of alcohol dehydrogenase into a physiologically based pharmacokinetic model for ethanol in humans. AU - Sultatos, Lester G.. AU - Pastino, Gina M.. AU - Rosenfeld, Clint A.. AU - Flynn, Edward J.. N1 - Funding Information: This work was funded by a research grant from the American Chemistry Council. All model code will be made available upon request to the authors.. PY - 2004/3. Y1 - 2004/3. N2 - The assessment of the variability of human responses to foreign chemicals is an important step in characterizing the public health risks posed by nontherapeutic hazardous chemicals and the risk of encountering adverse reactions with drugs. Of the many sources of interindividual variability in chemical response identified to date, hereditary factors are some of the least understood. Physiologically based pharmacokinetic modeling linked with Monte Carlo sampling has been shown to be a useful tool for the quantification of interindividual variability in ...
Metabolism and pharmacokinetics of 3-n-butylphthalide (NBP) in humans: the role of cytochrome P450s and alcohol dehydrogenase in biotransformation. - Xingxing Diao, Pan Deng, Cen Xie, Xiuli Li, Dafang Zhong, Yifan Zhang, Xiaoyan Chen
Genetic linkage studies with alcoholics have provided strong support for the assumption that AA plays a central role in alcohol-associated carcinogenesis. These studies found that individuals who accumulate AA because they carry certain alleles of the genes encoding ADH or ALDH have an increased cancer risk [42, 43]. As discussed above there are at least seven isozymes of human ADH that are encoded by seven genes. These isozymes are categorized into five different classes based on structural characteristics. Class I isozymes account for most of the alcohol metabolism.. For both the ADH1B and the ADH1C genes, several alleles exist that result in differences in the activity of the ADH molecules they encode. For example, the ADH1B*2 allele encodes an enzyme that is approximately 40 times more active than the enzyme encoded by the ADH1B*1 allele. Similarly, the enzyme encoded by the ADH1C*1 allele is 2.5 times more active than the enzyme encoded by the ADH1C*2 allele [44]. Individuals who carry the ...
M. J. Reimers, Hahn, M. E., and Tanguay, R. L., Two Zebrafish Alcohol Dehydrogenases Share Common Ancestry with Mammalian Class I, II, IV, and V Alcohol Dehydrogenase Genes but Have Distinct Functional Characteristics, Journal of Biological Chemistry, vol. 279, no. 37, pp. 38303 - 38312, 2004. ...
M. J. Reimers, Hahn, M. E., and Tanguay, R. L., Two Zebrafish Alcohol Dehydrogenases Share Common Ancestry with Mammalian Class I, II, IV, and V Alcohol Dehydrogenase Genes but Have Distinct Functional Characteristics, Journal of Biological Chemistry, vol. 279, no. 37, pp. 38303 - 38312, 2004. ...
To use the rs1229984 variant in the alcohol dehydrogenase 1B gene (ADH1B) as an instrument to investigate the causal role of alcohol in cardiovascular disease.Mendelian randomisation meta-analysis of 56 epidemiological studies.261 991 individuals of European descent, including 20 259 coronary heart disease cases and 10 164 stroke events. Data were available on ADH1B rs1229984 variant, alcohol phenotypes, and cardiovascular biomarkers.Odds ratio for coronary heart disease and stroke associated with the ADH1B variant in all individuals and by categories of alcohol consumption.Carriers of the A-allele of ADH1B rs1229984 consumed 17.2% fewer units of alcohol per week (95% confidence interval 15.6% to 18.9%), had a lower prevalence of binge drinking (odds ratio 0.78 (95% CI 0.73 to 0.84)), and had higher abstention (odds ratio 1.27 (1.21 to 1.34)) than non-carriers. Rs1229984 A-allele carriers had lower systolic blood pressure (-0.88 (-1.19 to -0.56) mm Hg), interleukin-6 levels (-5.2% (-7.8 to ...
To use the rs1229984 variant in the alcohol dehydrogenase 1B gene (ADH1B) as an instrument to investigate the causal role of alcohol in cardiovascular disease.Mendelian randomisation meta-analysis of 56 epidemiological studies.261 991 individuals of European descent, including 20 259 coronary heart disease cases and 10 164 stroke events. Data were available on ADH1B rs1229984 variant, alcohol phenotypes, and cardiovascular biomarkers.Odds ratio for coronary heart disease and stroke associated with the ADH1B variant in all individuals and by categories of alcohol consumption.Carriers of the A-allele of ADH1B rs1229984 consumed 17.2% fewer units of alcohol per week (95% confidence interval 15.6% to 18.9%), had a lower prevalence of binge drinking (odds ratio 0.78 (95% CI 0.73 to 0.84)), and had higher abstention (odds ratio 1.27 (1.21 to 1.34)) than non-carriers. Rs1229984 A-allele carriers had lower systolic blood pressure (-0.88 (-1.19 to -0.56) mm Hg), interleukin-6 levels (-5.2% (-7.8 to ...
Genetic variants of the alcohol-metabolizing enzyme ADH4, located on chromosome 4q22-4q23, have been related to alcohol dependence (AD) risk in previous research. The aim of this association study in a large multicenter sample of alcohol-dependent individuals and controls is to confirm ADH4 single nucleotide polymorphism (SNP) and haplotype association with AD and relevant related phenotypes. One thousand, six hundred and twenty-two (1622) inpatient subjects and 1469 control subjects with DSM-IV. AD from four addiction treatment centres were included. Characteristics of AD and related phenotypes including alcohol withdrawal, Cloningers type I and II and first ages of drinking, regular drinking and AD onset were obtained using standardized structured interviews. After subjects were genotyped for 2 ADH4 polymorphisms, single SNP case-control and haplotype analyses were conducted. Both variants-rs1800759 and rs1042364-and the A-A and C-G haplotypes were significantly related to AD across samples. ...
FRANCES, F. et al. Genetic predisposition to alcohol consumption: The case of Alcohol Dehydrogenase 1C. Cuad. med. forense [online]. 2007, n.48-49, pp.157-164. ISSN 1988-611X.. Introduction: Alcohol consumption is present in several crimes, being an extenuating or exculpating circumstance. In other cases it represents per se a penal infraction. Several genetic and environmental factors predisposing to alcohol consumption have been identified. Our aim is to study the prevalence of the Ile349Val polymorphism in the Alcohol Dehydrogenase 1C, that generates the gamma 2 isoform (slow metabolizers) and to assess its association with alcohol consumption, and to reflect upon the degree of the dimension of these genetic variants in Legal Medicine. Material and methods: We have genotyped 869 individuals from a Mediterranean Spanish population for the Ile349Val polymorphism in the ADH1C. We estimated the prevalence of this polymorphism and we studied its association with alcohol consumption. Continuous and ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
One hypothesis for the difference between the sexes is that men have a higher activity of the enzyme ADH, as I mentioned earlier, which metabolizes methanol and converts it to formaldehyde. More formaldehyde circulating in your blood would naturally have more opportunity to cause greater damage. Its possible that there is some hormonally mediated protection against the adverse effects of aspartame in women, in addition to men having higher ADH activity, but the study was not designed to answer that question. All in all however, I believe the study offers significant supporting evidence of the danger that aspartame-sweetened and other diet drinks and foods pose ...
Abreviações: Monkey ADH1Reatividade: MonkeyTipo de amostra: Serum, Plasma, Cell supernatantNivel de detecção: 0.16~10ng/mLSensibilidade: 0.09ng/mLSize: 96 TestesArmazenagem: An unopened kit can be stored at 4℃ for 1 month. If the kit is not used within 1 month, store the items separately according to the product manual. Método: This ELISA kit uses the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Monkey ADH1. Standards or samples are added to the micro ELISA plate wells and combined with the specific antibody. Then a biotinylated detection antibody specific for Monkey ADH1 and Avidin-Horseradish Peroxidase (HRP) conjugate are added successively to each micro plate well and incubated. Free components are washed away. The substrate solution is added to each well. Only those wells that contain Monkey ADH1, biotinylated detection antibody and Avidin-HRP conjugate will appear blue in color. The enzyme-substrate reaction is
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...