A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Behaviors associated with the ingesting of alcoholic beverages, including social drinking.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.

The alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. I. Selection in different environments. (1/3212)

The allozyme polymorphism at the alcohol dehydrogenase locus in Drosophila melanogaster was studied in order to obtain experimental evidence about the maintenance of this polymorphism. Populations started with different initial allele frequencies from homozygous F and S lines showed a convergence of frequencies on regular food at 25 degrees, leading to values equal to those in the base populations. These results were interpreted as due to some kind of balancing selection. In populations kept at 29.8 degrees, a lower equilibrium F frequency was attained. Addition of ethanol and some other alcohols to the food gave a rapid increase in F frequency, and high humidity decreased the F frequency slightly. Combination or alternation of ethanol and high humidity had variable effects in the populations tested. For a further analysis of the allele-frequency changes, estimates were obtained for egg-to-adult survival under different conditions and for adult survival on ethanol-supplemented food. On ethanol food (both at regular and high humidity), egg-to-adult survival of SS homozygotes was considerably lower than that of the FF and FS genotypes. Under regular conditions of food, temperature and humidity, a tendency to heterozygote superiority was observed, while at high humidity a relative high survival of SS was noticed in some tests. Adult survival of SS was lower than that of FF, but FS was generally intermediate, though the degree of dominance differed between populations. The results are consistent with the hypothesis of the occurrence of selection at the Adh locus.  (+info)

Separation and properties of two acetylacetoin reductases from Bacillus cereus YUF-4. (2/3212)

The separation and purification of two kinds of acetylacetoin reductases (AACRs) from Bacillus cereus YUF-4 were examined. NADPH-linked AACR (AACR I) and NADH-linked AACR (AACR II) were separated from each other by ammonium sulfate fractionation, DEAE-cellulose chromatography, and hydroxyapatite chromatography. The former was purified 3.4-fold with a yield of 10.0%, and the latter was purified 29-fold with a yield of 15.6%. The two enzymes differ from each other in some enzymic properties such as substrate specificity.  (+info)

Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. (3/3212)

Poly(3-hydroxyalkanoates) (PHAs) are a class of microbially produced polyesters that have potential applications as conventional plastics, specifically thermoplastic elastomers. A wealth of biological diversity in PHA formation exists, with at least 100 different PHA constituents and at least five different dedicated PHA biosynthetic pathways. This diversity, in combination with classical microbial physiology and modern molecular biology, has now opened up this area for genetic and metabolic engineering to develop optimal PHA-producing organisms. Commercial processes for PHA production were initially developed by W. R. Grace in the 1960s and later developed by Imperial Chemical Industries, Ltd., in the United Kingdom in the 1970s and 1980s. Since the early 1990s, Metabolix Inc. and Monsanto have been the driving forces behind the commercial exploitation of PHA polymers in the United States. The gram-negative bacterium Ralstonia eutropha, formerly known as Alcaligenes eutrophus, has generally been used as the production organism of choice, and intracellular accumulation of PHA of over 90% of the cell dry weight have been reported. The advent of molecular biological techniques and a developing environmental awareness initiated a renewed scientific interest in PHAs, and the biosynthetic machinery for PHA metabolism has been studied in great detail over the last two decades. Because the structure and monomeric composition of PHAs determine the applications for each type of polymer, a variety of polymers have been synthesized by cofeeding of various substrates or by metabolic engineering of the production organism. Classical microbiology and modern molecular bacterial physiology have been brought together to decipher the intricacies of PHA metabolism both for production purposes and for the unraveling of the natural role of PHAs. This review provides an overview of the different PHA biosynthetic systems and their genetic background, followed by a detailed summation of how this natural diversity is being used to develop commercially attractive, recombinant processes for the large-scale production of PHAs.  (+info)

MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites. (4/3212)

MOT1 is an ATPase which can dissociate TATA binding protein (TBP)-DNA complexes in a reaction requiring ATP hydrolysis. Consistent with this observation, MOT1 can repress basal transcription in vitro. Paradoxically, however, some genes, such as HIS4, appear to require MOT1 as an activator of transcription in vivo. To further investigate the function of MOT1 in basal transcription, we performed in vitro transcription reactions using yeast nuclear extracts depleted of MOT1. Quantitation of MOT1 revealed that it is an abundant protein, with nuclear extracts from wild-type cells containing a molar excess of MOT1 over TBP. Surprisingly, MOT1 can weakly activate basal transcription in vitro. This activation by MOT1 is detectable with amounts of MOT1 that are approximately stoichiometric to TBP. With amounts of MOT1 similar to those present in wild-type nuclear extracts, MOT1 behaves as a weak repressor of basal transcription. These results suggest that MOT1 might activate transcription via an indirect mechanism in which limiting TBP can be liberated from nonpromoter sites for use at promoters. In support of this idea, excess nonpromoter DNA sequesters TBP and represses transcription, but this effect can be reversed by addition of MOT1. These results help to reconcile previous in vitro and in vivo results and expand the repertoire of transcriptional control strategies to include factor-assisted redistribution of TBP between promoter and nonpromoter sites.  (+info)

Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria. (5/3212)

Glucose 6-phosphate dehydrogenase activity in rat liver mitochondria can be released by detergent. The released activity is separated by chromatography into two peaks. One peak has the kinetic behaviour and mobility similar to the soluble sex-linked enzyme, whereas the other peak is similar to the microsomal hexose 6-phosphate dehydrogenase. There is no evidence for the existence of a new glucose 6-phosphate dehydrogenase activity in rat liver mitochondria.  (+info)

Identification of the reactive cysteine residue (Cys227) in human carbonyl reductase. (6/3212)

Carbonyl reductase is highly susceptible to inactivation by organomercurials suggesting the presence of a reactive cysteine residue in, or close to, the active site. This residue is also close to a site which binds glutathione. Structurally, carbonyl reductase belongs to the short-chain dehydrogenase/reductase family and contains five cysteine residues, none of which is conserved within the family. In order to identify the reactive residue and investigate its possible role in glutathione binding, alanine was substituted for each cysteine residue of human carbonyl reductase by site-directed mutagenesis. The mutant enzymes were expressed in Escherichia coli and purified to homogeneity. Four of the five mutants (C26A, C122A C150A and C226A) exhibited wild-type-like enzyme activity, although K(m) values of C226A for three structurally different substrates were increased threefold to 10-fold. The fifth mutant, C227A, showed a 10-15-fold decrease in kcat and a threefold to 40-fold increase in K(m), resulting in a 30-500-fold drop in kcat/K(m). NaCl (300 mM) increased the activity of C227A 16-fold, whereas the activity of the wild-type enzyme was only doubled. Substitution of serine rather than alanine for Cys227 similarly affected the kinetic constants with the exception that NaCl did not activate the enzyme. Both C227A and C227S mutants were insensitive to inactivation by 4-hydroxymercuribenzoate. Unlike the parent carbonyl compounds, the glutathione adducts of menadione and prostaglandin A1 were better substrates for the C227A and C227S mutants than the wild-type enzyme. Conversely, the binding of free glutathione to both mutants was reduced. Our findings indicate that Cys227 is the reactive residue and suggest that it is involved in the binding of both substrate and glutathione.  (+info)

Protection of mice against a lethal influenza virus challenge after immunization with yeast-derived secreted influenza virus hemagglutinin. (7/3212)

The A/Victoria/3/75 (H3N2-subtype) hemagglutinin (HA) gene was engineered for expression in Pichia pastoris as a soluble secreted molecule. The HA cDNA lacking the C-terminal transmembrane anchor-coding sequence was fused to the Saccharomyces cerevisiae alpha-mating factor secretion signal and placed under control of the methanol-inducible P. pastoris alcohol oxidase 1 (AOX1) promoter. Growth of transformants on methanol-containing medium resulted in the secretion of recombinant non-cleaved soluble hemagglutinin (HA0s). Remarkably, the pH of the induction medium had an important effect on the expression level, the highest level being obtained at pH 8.0. The gel filtration profile and the reactivity against a panel of different HA-conformation specific monoclonal antibodies indicated that HA0s was monomeric. Analysis of the N-linked glycans revealed a typical P. pastoris type of glycosylation, consisting of glycans with 10-12 glycosyl residues. Mice immunized with purified soluble hemagglutinin (HA0s) showed complete protection against a challenge with 10 LD50 of mouse-adapted homologous virus (X47), whereas all control mice succumbed. Heterologous challenge with X31 virus [A/Aichi/2/68 (H3N2-subtype)], resulted in significantly higher survival rates in the immunized group compared with the control group. These results, together with the safety, reliability and economic potential of P. pastoris, as well as the flexibility and fast adaptation of the expression system may allow development of an effective recombinant influenza vaccine.  (+info)

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (8/3212)

A Staphylococcus xylosus C2A gene cluster, which encodes enzymes in the pathway for choline uptake and dehydrogenation (cud), to form the osmoprotectant glycine betaine, was identified. The cud locus comprises four genes, three of which encode proteins with significant similarities to those known to be involved in choline transport and conversion in other organisms. The physiological role of the gene products was confirmed by analysis of cud deletion mutants. The fourth gene possibly codes for a regulator protein. Part of the gene cluster was shown to be transcriptionally regulated by choline and elevated NaCl concentrations as inducers.  (+info)

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

'Alcohol drinking' refers to the consumption of alcoholic beverages, which contain ethanol (ethyl alcohol) as the active ingredient. Ethanol is a central nervous system depressant that can cause euphoria, disinhibition, and sedation when consumed in small to moderate amounts. However, excessive drinking can lead to alcohol intoxication, with symptoms ranging from slurred speech and impaired coordination to coma and death.

Alcohol is metabolized in the liver by enzymes such as alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). The breakdown of ethanol produces acetaldehyde, a toxic compound that can cause damage to various organs in the body. Chronic alcohol drinking can lead to a range of health problems, including liver disease, pancreatitis, cardiovascular disease, neurological disorders, and increased risk of cancer.

Moderate drinking is generally defined as up to one drink per day for women and up to two drinks per day for men, where a standard drink contains about 14 grams (0.6 ounces) of pure alcohol. However, it's important to note that there are no safe levels of alcohol consumption, and any level of drinking carries some risk to health.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

In chemistry, an alcohol is a broad term that refers to any organic compound characterized by the presence of a hydroxyl (-OH) functional group attached to a carbon atom. This means that alcohols are essentially hydrocarbons with a hydroxyl group. The simplest alcohol is methanol (CH3OH), and ethanol (C2H5OH), also known as ethyl alcohol, is the type of alcohol found in alcoholic beverages.

In the context of medical definitions, alcohol primarily refers to ethanol, which has significant effects on the human body when consumed. Ethanol can act as a central nervous system depressant, leading to various physiological and psychological changes depending on the dose and frequency of consumption. Excessive or prolonged use of ethanol can result in various health issues, including addiction, liver disease, neurological damage, and increased risk of injuries due to impaired judgment and motor skills.

It is important to note that there are other types of alcohols (e.g., methanol, isopropyl alcohol) with different chemical structures and properties, but they are not typically consumed by humans and can be toxic or even lethal in high concentrations.

I believe you may have meant to ask for the definition of "pyruvate dehydrogenase complex" rather than "pyruvate synthase," as I couldn't find any relevant medical information regarding a specific enzyme named "pyruvate synthase."

Pyruvate dehydrogenase complex (PDC) is a crucial enzyme complex in the human body, playing an essential role in cellular energy production. PDC is located within the mitochondrial matrix and catalyzes the oxidative decarboxylation of pyruvate, the end product of glycolysis, into acetyl-CoA. This process connects the glycolytic pathway to the citric acid cycle (Krebs cycle) and enables the continuation of aerobic respiration for efficient energy production in the form of ATP.

The pyruvate dehydrogenase complex consists of three main enzymes: pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). Additionally, two accessory proteins, E3-binding protein (E3BP) and protein X, are part of the complex. These enzymes work together to facilitate the conversion of pyruvate into acetyl-CoA, CO2, and NADH. Dysfunction in the pyruvate dehydrogenase complex can lead to various metabolic disorders and neurological symptoms.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol+oxidoreductases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e v t e ( ... Articles with short description, Short description matches Wikidata, EC 1.1, All stub articles, Oxidoreductase stubs, EC 1.1 ...
Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol ... Alcohol+dehydrogenase+(nicotinoprotein) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme ... dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803)". Microbiology. 156 (Pt 2): 463-71. doi: ... dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and ...
Other names in common use include long-chain fatty alcohol oxidase, fatty alcohol oxidase, fatty alcohol:oxygen oxidoreductase ... NAD+ oxidoreductase and requires NAD+. Yeast have low levels of fatty alcohol dehydrogenase.) The long-chain alcohol is then ... This alcohol is oxidized by long-chain fatty alcohol oxidase in yeast. (This is different from the pathway found in mammalian ... Lee T (April 1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry ...
NAD+ oxidoreductase. Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This ... Lee T (April 1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction a long-chain ...
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called methanol oxidase and ... aryl-alcohol oxidase (AAO) and secondary-alcohol oxidase (SAO). Alcohol oxidases catalyzes the oxidation of primary alcohols to ... In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ⇌ {\ ... This is reflected in their cofactor as well-unlike alcohol dehydrogenases, which use NAD+, alcohol oxidases use FAD. SCAO is ...
The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol ... quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. This enzyme ... Alcohol dehydrogenase Ameyama M; Adachi O (1982). Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. Methods in ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ...
The oxidoreductase encoded by mrl7 converts this alcohol into a bisaldehyde. Then CitD converts it into a carboxylic acid, via ... The mrl7 gene encodes for a NAD(P)+ dependent oxidoreductase (CitC). The first step of citrinin biosynthesis in fungi is the ... CitB oxidizes the C-atom of a methyl group bound to the aromatic ring and produces an alcohol. ...
... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...
The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD. Mansell RL ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a coniferyl-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction coniferyl ... the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+ ...
... acceptor oxidoreductase. Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. ... oxidized polyvinyl alcohol + reduced acceptor Thus, the two substrates of this enzyme are polyvinyl alcohol and acceptor, ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) (EC 1.1.99.23) is an enzyme that catalyzes the chemical reaction ...
The systematic name of this enzyme class is aryl-alcohol:NADP+ oxidoreductase. Other names in common use include aryl alcohol ... 2. Purification and properties of aryl-alcohol: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. (in German). 8 ( ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, an aryl-alcohol dehydrogenase (NADP+) (EC 1.1.1.91) is an enzyme that catalyzes the chemical reaction an ...
The systematic name of this enzyme class is secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. Otsuka K (1958). "Triphosphopyridine nucleotide ... In enzymology, an allyl-alcohol dehydrogenase (EC 1.1.1.54) is an enzyme that catalyzes the chemical reaction allyl alcohol + ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...
The systematic name of this enzyme class is polyvinyl-alcohol:oxygen oxidoreductase. Other names in common use include ... In enzymology, a polyvinyl-alcohol oxidase (EC 1.1.3.30) is an enzyme that catalyzes the chemical reaction polyvinyl alcohol + ... whereas its two products are oxidized polyvinyl alcohol and H2O2. This enzyme belongs to the family of oxidoreductases, ... Shimao M, Nishimura Y, Kato N, Sakazawa C (1985). "Localization of Polyvinyl Alcohol Oxidase Produced by a Bacterial Symbiont, ...
The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction perillyl ... Ballal NR, Bhattacharyya PK, Rangachari PN (1966). "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. ...
... oxygen oxidoreductase. Other names in common use include polyvinyl alcohol oxidase, and secondary alcohol oxidase. Morita M, ... In enzymology, a secondary-alcohol oxidase (EC 1.1.3.18) is an enzyme that catalyzes the chemical reaction a secondary alcohol ... Sakai K, Hamada N, Watanabe Y (1983). "Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ...
The systematic name of this enzyme class is cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction cinnamyl ... Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase ...
The systematic name of this enzyme class is alcohol:NAD(P)+ oxidoreductase. Other names in common use include retinal reductase ... In enzymology, an alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71) is an enzyme that catalyzes the chemical reaction an alcohol + ... Alcohol dehydrogenase Fidge NH, Goodman DS (1968). "The enzymatic reduction of retinal to retinol in rat intestine". J. Biol. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
The systematic name of this enzyme class is vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2- ... A novel aromatic alcohol oxidase containing covalently bound FAD". Eur. J. Biochem. 208 (3): 651-657. doi:10.1111/j.1432- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA (1992). "Purification and characterization of vanillyl-alcohol oxidase ...
NAD+ oxidoreductase. Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, an aryl-alcohol dehydrogenase (EC 1.1.1.90) is an enzyme that catalyzes the chemical reaction an aromatic ... The systematic name of this enzyme class is aryl-alcohol: ... the two substrates of this enzyme are aromatic alcohol and NAD+ ...
... oxygen oxidoreductase. Other names in common use include aryl alcohol oxidase, veratryl alcohol oxidase, and arom. alcohol ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... In enzymology, an aryl-alcohol oxidase (EC 1.1.3.7) is an enzyme that catalyzes the chemical reaction an aromatic primary ... FARMER VC, HENDERSON ME, RUSSELL JD (1960). "Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor ...
NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction 3- ... Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108- ...
The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR. As of ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a chlordecone reductase (EC 1.1.1.225) is an enzyme that catalyzes the chemical reaction chlordecone alcohol + ... the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+. ...
It belongs to the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. In melanocytic cells VAT1 ...
... acyclic monoterpene primary alcohol:NADP+ oxidoreductase) is an enzyme with systematic name (6E)-8-hydroxygeraniol:NADP+ ... "Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa ... Ikeda H, Esaki N, Nakai S, Hashimoto K, Uesato S, Soda K, Fujita T (February 1991). "Acyclic monoterpene primary alcohol:NADP+ ... 8-hydroxygeraniol dehydrogenase (EC 1.1.1.324, 8-hydroxygeraniol oxidoreductase, CYP76B10, G10H, CrG10H, SmG10H, ...
In addition, there is another adjacent and conserved gene encoding for an alcohol dehydrogenase/oxidoreductase whose function ... and aminotransferase of 23 different atromentin-producing basidiomycetes that was in almost all cases absent from the alcohol ...
... cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. This enzyme ... Cyclic+alcohol+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... "Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM ... catalyses the following chemical reaction cyclic alcohol + quinone ⇌ {\displaystyle \rightleftharpoons } cyclic ketone + quinol ...
... ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction polyvinyl alcohol + ferricytochrome c ... vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase". ... "Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing ... Polyvinyl+alcohol+dehydrogenase+(cytochrome) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ...
Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol+oxidoreductases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e v t e ( ... Articles with short description, Short description matches Wikidata, EC 1.1, All stub articles, Oxidoreductase stubs, EC 1.1 ...
Tyrosine-dependent oxidoreductases: *Protein Drosophila alcohol dehydrogenase from c.2.1.2: Tyrosine-dependent oxidoreductases ... More info for Protein Drosophila alcohol dehydrogenase from c.2.1.2: Tyrosine-dependent oxidoreductases. Timeline for Protein ... Protein Drosophila alcohol dehydrogenase from c.2.1.2: Tyrosine-dependent oxidoreductases appears in SCOPe 2.07. ... Family c.2.1.2: Tyrosine-dependent oxidoreductases [51751] (73 proteins). also known as short-chain dehydrogenases and SDR ...
16] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of ... The definitive test for Sjögren-Larsson syndrome is measurement of FALDH or fatty alcohol:NAD oxidoreductase in cultured skin ... Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which ... Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ...
Alcohol Oxidoreductases/*metabolism (1) * Alcohol Oxidoreductases/metabolism (1) * Analysis and Design (1) ...
16] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of ... The definitive test for Sjögren-Larsson syndrome is measurement of FALDH or fatty alcohol:NAD oxidoreductase in cultured skin ... Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which ... Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ...
enables oxidoreductase activity IEA Inferred from Electronic Annotation. more info. enables zinc ion binding IBA Inferred from ... alcohol_DH_class_III; class III alcohol dehydrogenases. COG1062. Location:6 → 374. FrmA; Zn-dependent alcohol dehydrogenase [ ... alcohol dehydrogenase 2. alcohol dehydrogenase B2. alcohol dehydrogenase class-III. glutathione-dependent formaldehyde ... Title: Class III Alcohol Dehydrogenase Plays a Key Role in the Onset of Alcohol-Related/-Associated Liver Disease as an S- ...
... alcohol:NAD+ oxidoreductase #, , ├── recommended.name: alcohol dehydrogenase #, , ├── synonyms: A tibble with 41 rows #, , ├── ... alcohol:NAD+ oxidoreductase #, , ├── recommended.name: alcohol dehydrogenase #, , ├── synonyms: A tibble with 128 rows ...
Alcohol Oxidoreductases. *Alleles. *Alu Elements. *Amino Acid Sequence. *Amino Acid Substitution. *Amino Acid Transport System ...
8] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty ... Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which ... Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ... Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide ...
8] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty ... Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which ... Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ... Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide ...
Expression of aldehyde ferredoxin oxidoreductase (aor from Pyrococcus furiosus) and alcohol dehydrogenase (adhA from ... This is the first instance of an acid to alcohol conversion pathway in a cellulolytic microbe. ... to the corresponding alcohol (isobutanol and hexanol) using both crystalline cellulose and switchgrass as sources of reductant ... In contrast to the tungsten-containing oxidoreductase enzymes natively produced by P. furiosus, recombinant P. aerophilum Arr ...
Generation of a Gene Bank for Genes Conferring Alcohol Oxidoreductase Activity on Escherichia coli. Appl. Environ. Microbiol. ... alcohol reductases, amidases, cellulases, amylases, glycogen-branching enzymes, and pectate lyases [98][99][100][101][102][103] ... quorum-sensing molecules are modified and degraded by Rhodococcus erythropolis W2 by both amidolytic and novel oxidoreductase ...
Oxidoreductases [D08.811.682] * Alcohol Oxidoreductases [D08.811.682.047] * Arsenate Reductases [D08.811.682.113] * Ascorbate ... Oxidoreductases Acting on CH-CH Group Donors [D08.811.682.660] * Oxidoreductases Acting on CH-NH Group Donors [D08.811.682.662] ... Oxidoreductases Acting on CH-NH2 Group Donors [D08.811.682.664] * Oxidoreductases Acting on Sulfur Group Donors [D08.811. ... Oxidoreductases Acting on Aldehyde or Oxo Group Donors [D08.811.682.657] * ...
Ketone Reductases use Alcohol Oxidoreductases Ketone, Butylmethyl use Methyl n-Butyl Ketone ...
","oxidoreductase [Ensembl]. Zinc-binding dehydrogenase, Alcohol dehydrogenase GroES-like domain [Interproscan].","protein_ ... ","DadA family oxidoreductase [Ensembl]. FAD dependent oxidoreductase [Interproscan].","protein_coding" "AEA92996","OG1RF_10309 ... ","oxidoreductase [Ensembl]. FAD dependent oxidoreductase [Interproscan].","protein_coding" "EDJ91500","CGSHi22421_07012"," ... ","Na(+)-translocating NADH-quinone reductase subunit F [Ensembl]. Oxidoreductase NAD-binding domain, Oxidoreductase FAD- ...
Align Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 (characterized) to candidate Pf1N1B4_4506 Alcohol ...
Oxidoreductases. *5,10-Methylenetetrahydrofolate Reductase (FADH2). *Alcohol Oxidoreductases. *Arsenate Reductases. *Ascorbate ...
Examples include lactate dehydrogenase and alcohol dehydrogenase.. 8. Oxidoreductases: This broad class of enzymes catalyzes ... 1. Alcohol dehydrogenase (ADH): This enzyme catalyzes the interconversion between alcohols and aldehydes or ketones by ... These enzymes catalyze the hydrolysis or synthesis of esters by breaking or forming carbon-oxygen bonds between an alcohol and ... transferring a hydride ion from the alcohol to a cofactor, such as NAD+ or NADP+, resulting in the formation of a carbon-oxygen ...
22. ALCOHOL OXIDOREDUCTASES [ԱԼԿՈՀՈԼ-ՕՔՍԻԴՈՌԵԴՈՒԿՏԱԶՆԵՐ] 72. ALKYNES [ԱԼԿԻՆՆԵՐ] 23. ALCOHOL WITHDRAWAL DELIRIUM [ԱԼԿՈՀՈԼԱՅԻՆ ... 24. ALCOHOL, METHYL [ՍՊԻՐՏ ՄԵԹՈԼԱՅԻՆ] 74. ALLANTOIS [ԱԼԱՆՏՈԻՍԱՅԻՆ ԹԱՂԱՆԹ] 25. ALCOHOL, PROPYL [ՍՊԻՐՏ ՊՐՈՊԻԼԱՅԻՆ] 75. ALLELES [ ... 26. ALCOHOL,ETHYL [ՍՊԻՐՏ ԷԹԻԼԱՅԻՆ] 76. ALLERGENS [ԱԼԵՐԳԵՆՆԵՐ] 27. ALCOHOLIC BEVERAGES [ԱԼԿՈՀՈԼԱՅԻՆ ԽՄԻՉՔՆԵՐ] 77. ALLERGY AND ... 20. ALCOHOL DETERRENTS [ՀԱԿԱԱԼԿՈՀՈԼԱՅԻՆ ՄԻՋՈՑՆԵՐ] 70. ALKYLATION [ԱԼԿԻԼԱՑՈՒՄ] 21. ALCOHOL DRINKING [ԱԼԿՈՀՈԼԻ ՕԳՏԱԳՈՐԾՈՒՄ] 71. ...
Alcohol Dehydrogenases. Those that can reduce aldehydes into primary alcohols and ketones into secondary alcohols. ... Oxidative Enzymes and Oxidoreductases. Those that cause or accelerate an oxidation reaction. ... Alcohol Dehydrogenases. Those that can reduce aldehydes into primary alcohols and ketones into secondary alcohols. ... Theres a long history of enzymes being used to elaborate certain goods (for example, with alcohol fermentation) and, in the ...
Ketone Reductases use Alcohol Oxidoreductases Ketone, Butylmethyl use Methyl n-Butyl Ketone ...
... alcohol reacts faster and the (R)-alcohol remains unchanged. Bottom row: In the catalytic system, the (R)-alcohol reacts faster ... Figure 10.52 Schematic representation of the operation of oxidoreductases. Left: The reductive and oxidative reactions with the ... Figure 10.12 Enantiotope-selective epoxidation of a primary allylic alcohol (77) catalyzed by a chiral titanium complex. New ... Figure 10.13 Stereoselective epoxidation of a chiral allylic alcohol (80) catalyzed by a chiral titanium complex. The new ...
2019). Lactobacillus plantarum NA136 improves the non-alcoholic fatty liver disease by modulating the AMPK/Nrf2 pathway. Appl. ... H quinone oxidoreductase-1 (NQO1), and glutamate-cysteine ligase modifier subunits (Zhao et al., 2015). We recently reported ... It is water-alcohol and polar solvents soluble. There are two forms of DHQ, the trans- and cis-form. The trans-DHQ oxidizes ... H quinone oxidoreductase-1; Nrf2, Nuclear factor erythroid 2-related factor 2; PMSF, phenylmethanesulfonyl fluoride; PI, ...
Using alcohol dehydrogenase from Lactobacillus brevis (LbADH) as a model system, we probed in our combined experimental and ... Using alcohol dehydrogenase from Lactobacillus brevis (LbADH) as a model system, we probed in our combined experimental and ... Crystal Contact Engineering Enables Efficient Capture and Purification of an Oxidoreductase by Technical Crystallization. ... Our example protein alcohol dehydrogenase from Lactobacillus brevis (LbADH) is an R-specific, nicotinamide adenine dinucleotide ...
Aldose reductase (AR, E.C. 1.1.1.21) catalyzes the re-duction of D-glucose to its corresponding sugar alcohol, sorbitol, and it ... H-requiring oxidoreductases. M16209 and M16287, as well as ONO-2235 and sorbinil,hardly affected the enzymes of carbohydrate ... alcohol dehydrogenase, 3.3% ethanol, 5mm NAD; AR inhibitors were added at 1×10-5M in final concentration,and the remaining ... dependent oxidoreduc-tases. Aldose reductases distribute widely in mammalian tissues,including lens,Schwann cells in nerve, ...
... oxidoreductase activity, acting on diphenols and related substances as donors;0.00118557239649909!GO:0016681;oxidoreductase ... alcohol group as acceptor;0.00426041658608387!GO:0050870;positive regulation of T cell activation;0.00438384994730396!GO: ... oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor;1.43054480640698e-15!GO:0006323;DNA ... oxidoreductase activity, acting on heme group of donors, oxygen as acceptor;0.00796318626903965!GO:0015002;heme-copper terminal ...
Alcohol dehydrogenase 4. General function:. Involved in oxidoreductase activity. Specific function:. Reduces acetaldehyde to ... Alcohol dehydrogenase 5. General function:. Involved in zinc ion binding. Specific function:. An alcohol + NAD(+) = an aldehyde ... 6. Alcohol dehydrogenase 3, mitochondrial. General function:. Involved in zinc ion binding. Specific function:. An alcohol + ... External NADH-ubiquinone oxidoreductase 2, mitochondrial. General function:. Involved in oxidoreductase activity. Specific ...
Conversion of furfural to furoic acid and furfuryl alcohol by Neurospora ascospores journal, January 1970 * Eilers, Frederick I ... Silencing of NADPH-Dependent Oxidoreductase Genes (yqhD and dkgA) in Furfural-Resistant Ethanologenic Escherichia coli journal ... Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase journal, May 2002 * ... Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase journal, April 2002 ...
","Alcohol dehydrogenase, C-terminal; Alcohol dehydrogenase, N-terminal [Interproscan].","protein_coding" "PTI_13G02500.1","No ... ","NADP-dependent oxidoreductase domain [Interproscan].","protein_coding" "EOD26818","No alias","Emiliania huxleyi","Major ... ","Putative CDP-alcohol phosphatidyltransferase class-I family protein","protein_coding" "lcl,VRMN01000002.1_cds_KAA8496982.1_ ... ","NADH:ubiquinone oxidoreductase 76 kDa subunit","protein_coding" "lcl,LHPG02000004.1_cds_PRW59237.1_7536","PRW59237"," ...
  • [ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.com)
  • Orthologous to human ADH5 (alcohol dehydrogenase 5 (class III), chi polypeptide). (nih.gov)
  • A mutant of the thermostable NAD(+)-dependent (S)-stereospecific alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) which has a single substitution, Trp95Leu, located at the substrate binding pocket, was fully characterized to ascertain the role of Trp95 in discriminating between chiral secondary alcohols suggested by the wild-type SsADH crystallographic structure. (cnr.it)
  • Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. (wikipedia.org)
  • Au sein de celle-ci, les actions combinées de trois enzymes, lipase, lipoxygénase (LOX) et hydroperoxyde lyase (HPL), convertissent un substrat lipidique (acides C 18:2 et C 18:3 ) en molécules volatiles à courte chaine. (ac.be)
  • Two decades later, Sjögren-Larsson syndrome was shown to be an inborn error of lipid metabolism caused by deficient activity of fatty alcohol:NAD oxidoreductase. (medscape.com)
  • Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which results in defective metabolism of both fatty aldehyde and fatty alcohol. (medscape.com)
  • Sjögren-Larsson syndrome can also be diagnosed by directly demonstrating defective fatty alcohol oxidation in a skin-biopsy sample using a histochemical staining method. (medscape.com)
  • In Sjögren-Larsson syndrome , FALDH deficiency impairs fatty alcohol oxidation and leads to accumulation of 16- and 18-carbon-long aliphatic alcohols. (medscape.com)
  • The definitive test for Sjögren-Larsson syndrome is measurement of FALDH or fatty alcohol:NAD oxidoreductase in cultured skin fibroblasts. (medscape.com)
  • [ 8 ] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty alcohol to aldehyde and fatty acid. (medscape.com)
  • Figure 1.9 Kekulé formulas and the bond matrices of acetaldehyde and "vinyl alcohol. (e-bookshelf.de)
  • [ 14 ] Accumulation of fatty alcohol and related lipid products disrupts formation of the intercellular membranes in the stratum corneum, which is critical for epidermal water barrier. (medscape.com)
  • [ 13 ] In cultured skin keratinocytes, elevated fatty alcohol is diverted into the synthesis of wax esters and alkyldiacylglycerol lipids. (medscape.com)
  • Aldose reductase (AR, E.C. 1.1.1.21) catalyzes the re-duction of D-glucose to its corresponding sugar alcohol, sorbitol, and it belongs to a larger family of aldehyde reductases that are monomeric, nicotineamide adenine dinucleotide phosphate (NADPH)-dependent oxidoreduc-tases. (necrosulfonamideinhibitor.com)
  • [ 9 ] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty alcohol to aldehyde and fatty acid. (medscape.com)
  • Furthermore, the genome shows a versatile set of other oxidoreductase genes putatively involved in lignin oxidation and conversion, including 5 glyoxal oxidases, 19 quinone-oxidoreductases and 12 aryl-alcohol oxidases. (bvsalud.org)
  • In Sjögren-Larsson syndrome , FALDH deficiency impairs fatty alcohol oxidation and leads to accumulation of 16- and 18-carbon-long aliphatic alcohols. (medscape.com)
  • Among the processes in which enzymes play a vital role is fermentation, which takes place in the production of alcohol or the baking of bread and also plays a part in numerous other natural phenomena, such as the purification of wastewater. (encyclopedia.com)
  • More specifically, it relates to a glucose biosensor having glucose oxidase immobilized thereon or a biosensor having an oxidoreductase immobilized thereon. (justia.com)
  • Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which results in defective metabolism of both fatty aldehyde and fatty alcohol. (medscape.com)
  • [ 14 ] In cultured skin keratinocytes, elevated fatty alcohol is diverted into the synthesis of wax esters and alkyldiacylglycerol lipids. (medscape.com)
  • Fatty alcohol and aldehyde may likewise alter the normal integrity of myelin membranes in the brain, leading to white-matter disease and spasticity. (medscape.com)
  • Toward understanding the genetics of alcohol drinking through transcriptome meta-analysis. (nih.gov)
  • This includes investigating roles of various factors such as acetaldehyde, cytochrome P450 2E1 (CYP2E1), vascular endothelial growth factor (VEGF), impaired immune function, and alcohol-induced impaired metabolism of s-adenosylmethionine (SAMe), folate, betaine, iron, and vitamin A. (nih.gov)
  • 7. Oxidative modification of hepatic mitochondria protein thiols: effect of chronic alcohol consumption. (nih.gov)
  • The National Institute on Alcohol Abuse and Alcoholism (NIAAA), National Cancer Institute (NCI), and Office of Dietary Supplements (ODS) invite research grant applications that will employ an integrative approach using state-of-the-art technologies to gain insight into the molecular and biochemical mechanisms by which chronic alcohol consumption leads to the development of cancers of various organs such as oral cavity, pharynx, larynx, esophagus, stomach, large intestine, liver, and breast. (nih.gov)
  • Alcohol further exacerbates mitochondrial oxidative stress induced by overnutrition and promotes the development of metabolic diseases. (karger.com)
  • 1. Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. (qmul.ac.uk)
  • In contrast, other oxidoreductases depending on initial MnP activity showed generally lower transcript levels on RZ than on heartwood. (bvsalud.org)