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.
It is a form of protection provided by law. In the United States this protection is granted to authors of original works of authorship, including literary, dramatic, musical, artistic, and certain other intellectual works. This protection is available to both published and unpublished works. (from Circular of the United States Copyright Office, 6/30/2008)
Organizations which are not operated for a profit and may be supported by endowments or private contributions.
Exclusive legal rights or privileges applied to inventions, plants, etc.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Protective measures against unauthorized access to or interference with computer operating systems, telecommunications, or data structures, especially the modification, deletion, destruction, or release of data in computers. It includes methods of forestalling interference by computer viruses or so-called computer hackers aiming to compromise stored data.
The privacy of information and its protection against unauthorized disclosure.
The state of being free from intrusion or disturbance in one's private life or affairs. (Random House Unabridged Dictionary, 2d ed, 1993)
A genus of gram-positive, aerobic bacteria. Most species are free-living in soil and water, but the major habitat for some is the diseased tissue of warm-blooded hosts.
A bacterial genus of the order ACTINOMYCETALES.
Class of BACTERIA with diverse morphological properties. Strains of Actinobacteria show greater than 80% 16S rDNA/rRNA sequence similarity among each other and also the presence of certain signature nucleotides. (Stackebrandt E. et al, Int. J. Syst. Bacteriol. (1997) 47:479-491)
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.
An order of gram-positive, primarily aerobic BACTERIA that tend to form branching filaments.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.
A family of conserved cell surface receptors that contain EPIDERMAL GROWTH FACTOR repeats in their extracellular domain and ANKYRIN repeats in their cytoplasmic domains. The cytoplasmic domain of notch receptors is released upon ligand binding and translocates to the CELL NUCLEUS where it acts as transcription factor.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
A notch receptor that plays an important role in CELL DIFFERENTIATION in a variety of cell types. It is the preferentially expressed notch receptor in mature B-LYMPHOCYTES.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.
An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.
A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
An organic compound used often as a reagent in organic synthesis, as a flavoring agent, and in tanning. It has been demonstrated as an intermediate in the metabolism of acetone and its derivatives in isolated cell preparations, in various culture media, and in vivo in certain animals.
Proteins obtained from ESCHERICHIA COLI.
A dye used as a reagent in the determination of vitamin C.
A plant genus of the family LAMIACEAE having characteristic flavor.
Compounds with a core of 10 carbons generally formed via the mevalonate pathway from the combination of 3,3-dimethylallyl pyrophosphate and isopentenyl pyrophosphate. They are cyclized and oxidized in a variety of ways. Due to the low molecular weight many of them exist in the form of essential oils (OILS, VOLATILE).
Six-carbon alicyclic hydrocarbons which contain one or more double bonds in the ring. The cyclohexadienes are not aromatic, in contrast to BENZOQUINONES which are sometimes called 2,5-cyclohexadiene-1,4-diones.
A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)
Microscopy in which the image is formed by ultraviolet radiation and is displayed and recorded by means of photographic film.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Parts of plants that usually grow vertically upwards towards the light and support the leaves, buds, and reproductive structures. (From Concise Dictionary of Biology, 1990)
Isomeric forms and derivatives of PROPANOL (C3H7OH).
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.

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)

1. Lee Y, Jeon K, Lee JT, Kim S, Kim VN. MicroRNA maturation: stepwise processing and subcellular localization. Embo J. 2002;21(17):4663-4670 2. Chen K, Rajewsky N. The evolution of gene regulation by transcription factors and microRNAs. Nat Rev Genet. 2007;8(2):93-103 3. Pillai RS, Bhattacharyya SN, Filipowicz W. Repression of protein synthesis by miRNAs: how many mechanisms?. Trends Cell Biol. 2007;17(3):118-126 4. Walker GJ, Indsto JO, Sood R. et al. Deletion mapping suggests that the 1p22 melanoma susceptibility gene is a tumor suppressor localized to a 9-Mb interval. Genes Chromosomes Cancer. 2004;41(1):56-64 5. Bemis LT, Chen R, Amato CM. et al. MicroRNA-137 targets microphthalmia-associated transcription factor in melanoma cell lines. Cancer Res. 2008;68(5):1362-1368 6. Chinnadurai G. The transcriptional corepressor CtBP: a foe of multiple tumor suppressors. Cancer Res. 2009;69(3):731-734 7. Haflidadottir BS, Bergsteinsdottir K, Praetorius C, Steingrimsson E. miR-148 regulates Mitf in ...
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC 1.1.1.300, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
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EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Evidence is reported for the existence of a structurally and functionally related and probably evolutionarily conserved class of membrane-bound liver carbonyl reductases/hydroxysteroid dehydrogenases involved in steroid and xenobiotic carbonyl metabolism. Carbonyl reduction was investigated in liver microsomes of 8 vertebrate species, as well as in insect larvae total homogenate and in purified 3 alpha-hydroxysteroid dehydrogenase preparations of the procaryont Pseudomonas testosteroni, using the ketone compound 2-methyl-1,2 di-(3-pyridyl)-1-propanone (metyrapone) as substrate. The enzyme activities involved in the metyrapone metabolism were screened for their sensitivity to several steroids as inhibitors. In all fractions tested, steroids of the adrostane or pregnane class strongly inhibited xenobiotic carbonyl reduction, whereas only in the insect and procaryotic species could ecdysteroids inhibit this reaction. Immunoblot analysis with antibodies against the respective microsomal mouse liver
Estradiol 17-beta-dehydrogenase 11,1.1.1.62,17-beta-hydroxysteroid dehydrogenase 11,17-beta-HSD 11,17bHSD11,17betaHSD11,17-beta-hydroxysteroid dehydrogenase XI,17-beta-HSD XI,17betaHSDXI,Cutaneous T-cell lymphoma-associated antigen HD-CL-03,CTCL-associated antigen HD-CL-03,Dehydrogenase/reductase SDR family member 8,Retinal short-chain dehydrogenase/reductase 2,retSDR2,Short chain dehydrogenase/reductase family 16C member 2,HSD17B11,DHRS8,PAN1B,SDR16C2,PSEC0029,UNQ207/PRO233,. ...
Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
BACKGROUND: (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol [(R)-3,5-BTPE] is a valuable chiral intermediate for Aprepitant (Emend) and Fosaprepitant (Ivemend). Biocatalyzed asymmetric reduction is a preferred approach to synthesize highly optically active (R)-3,5-BTPE. However, the product concentration and productivity of reported (R)-3,5-BTPE synthetic processes remain unsatisfied. RESULTS: A NADPH-dependent carbonyl reductase from Lactobacillus kefir (LkCR) was discovered by genome mining for reduction of 3,5-bis(trifluoromethyl) acetophenone (3,5-BTAP) into (R)-3,5-BTPE with excellent enantioselectivity. In order to synthesize (R)-3,5-BTPE efficiently, LkCR was coexpressed with glucose dehydrogenase from Bacillus subtilis (BsGDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L (R)-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). Then, four different linker peptides were used for the fusion expression of ...
Short-chain dehydrogenases/reductases form a large, evolutionarily old family of NAD(P)(H)-dependent enzymes with over 60 genes found in the human genome. Despite low levels of sequence identity (often 10-30%), the three-dimensional structures display a highly similar alpha/beta folding pattern. We have analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3beta/17beta-hydroxysteroid dehydrogenase and selected mutants. Structure determination of the wild-type enzyme at 1.2-A resolution by x-ray crystallography and docking analysis was used to interpret the biochemical data. Enzyme kinetic data from mutagenetic replacements emphasize the critical role of residues Thr-12, Asp-60, Asn-86, Asn-87, and Ala-88 in coenzyme binding and catalysis. The data also demonstrate essential interactions of Asn-111 with active site residues. A general role of its side chain interactions for maintenance of the active site configuration to
The major metabolic pathways involved in synthesis and disposition of carbonyl and hydroxyl group containing compounds are presented, and structural and functional characteristics of the enzyme families involved are discussed. Alcohol and aldehyde dehydrogenases (ADH, ALDH) participate in oxidative pathways, whereas reductive routes are accomplished by members of the aldo-keto reductase (AKR), short-chain dehydrogenases/reductases (SDR) and quinone reductase (QR) superfamilies. A wealth of biochemical, genetic and structural data now establishes these families to constitute important phase I enzymes.
Complete information for SDR42E1 gene (Protein Coding), Short Chain Dehydrogenase/Reductase Family 42E, Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Background information. CtBP proteins have roles in the nucleus as transcriptional co-repressors, and in the cytoplasm in the maintenance of vesicular membranes. CtBPs are expressed from two genes, CTBP1 and CTBP2, mRNA products of which are alternatively spliced at their 5 ends to generate distinct protein isoforms. Extensive molecular and cellular analyses have identified CtBPs as regulators of pathways critical for tumour initiation, progression, and response to therapy. However little is known of the expression or regulation of CtBP isoforms in human cancer, nor the relative contribution of CTBP1 and CTBP2 to the tumour cell phenotype. Results. Expression of CtBP proteins, and CTBP1 and CTBP2 mRNA splice forms in breast cancer cell lines and tumour tissue were examined. CtBP1 proteins are identifiable as a single band on western blots and are ubiquitously detectable in breast tumour samples, by both western blotting and immunohistochemistry. CtBP1 is present in 6 of 6 breast cancer cell ...
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
592 Drug resistance caused by overexpression of P-glycoprotein (P-gp), the MDR1 gene product, limits the therapeutic outcome in cancer patients. Although modulation of multidrug resistance (MDR) by pharmacological agents, antibodies, antisense oligonucleotides, siRNA, and inhibitors of signal transduction have been reported, clinical benefits have been disappointing. We and others have sought to understand the regulation of MDR1 gene expression as another approach to this problem. CtBP1 (C-terminal-binding protein 1) is a transcriptional co-regulator that plays an important role in oncogenesis. Recently, it was reported that CtBP1 could serve as both a co-activator and co-repressor of transcription. In this study, we determined the effect of CtBP1 on transcription of the MDR1 gene. Chromatin immunoprecipitation (ChIP) experiments demonstrated that CtBP1 bound to the promoter and coding regions of the MDR1 gene, but not to the non-coding regions. Knockdown of CtBP1 expression by siRNA repressed ...
Alcohol Oxidase, 10 mg. Alcohol Oxidase (AOX) is a homooctameric flavoprotein consisting of eight identical subunits of ~74 kD, each containing a flavin adenine dinucleotide molecule (FAD) as a prosthetic group (van der Klei et al.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Shop Dehydrogenase/reductase SDR family protein ELISA Kit, Recombinant Protein and Dehydrogenase/reductase SDR family protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
CP000667.PE408 Location/Qualifiers FT CDS_pept 469214..469912 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Strop_0408 FT /product=short-chain dehydrogenase/reductase SDR FT /note=PFAM: short-chain dehydrogenase/reductase SDR FT /db_xref=EnsemblGenomes-Gn:Strop_0408 FT /db_xref=EnsemblGenomes-Tr:ABP52893 FT /db_xref=InterPro:IPR002347 FT /db_xref=InterPro:IPR036291 FT /db_xref=UniProtKB/TrEMBL:A4X1Z3 FT /protein_id=ABP52893.1 FT /translation=MVNLDGLRVAVTGAGRASGRLLATAFAEHGAQVFVSARDEVAARR FT TTDSIRQRGRGRGEAFVCDLTSPDSVRAFAAALTDRTDHLDVLVNNGAGYLHGVDLGDV FT EDDHIIATIGGTATGTVLLTKHLLALLRASTRPDIVNMISACGEVGHHRSEAHPAFYAA FT KHAQAGFAEIMSHRLRVEGIRVISLFPPDFVQHGPRVASNNLTAQSVVDCVLFAVSQPR FT DCFIREFRFE gtggtgaatc tcgacggact acgggttgct gtcaccggcg ccgggcgcgc ctccggacgc 60 ctcctggcga ccgccttcgc cgagcacggc gcgcaggtgt ttgtctccgc ccgtgatgag 120 gtggcagcca gacgcaccac ggattcgatc cggcagcgtg ggcgggggag aggcgaagcc 180 ttcgtctgtg acctgaccag ccccgactcg gtacgcgcgt tcgcggcggc gttgaccgac 240 cgcaccgacc ...
But experimentalists should not get too cocky: the next paper, by Jamie Simpson and collaborators at Monash University, describes some of the things that can go wrong. An STD NMR screen of the antimicrobial target ketopantoate reductase (KPR) using the same Maybridge library of 500 compounds revealed 196 hits! The 47 with the strongest STD signals were then tested in a 1H/15N-HSQC NMR assay, leading to 14 hits, of which 4 gave measurable IC50 values in an enzymatic assay. Unfortunately, follow-up SAR was disappointing, and subsequent experiments revealed that aggregation was to blame: when the biochemical experiments were rerun in the presence of 0.01% Tween-20, only a single fragment gave a measurable IC50 value. The researchers redid their STD-NMR screen in the presence of detergent, resulting in 71 hits, all of which were tested in the biochemical screen. This led to the identification of a new (and fairly potent) hit that had previously been missed. This nicely illustrates the fact that ...
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Complete information for RDH16 gene (Protein Coding), Retinol Dehydrogenase 16 (All-Trans), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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RDH5兔多克隆抗体(ab101457)可与人样本反应并经WB, IHC实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
TY - JOUR. T1 - Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases. AU - Rougraff, P. M.. AU - Zhang, B.. AU - Kuntz, M. J.. AU - Harris, Robert. AU - Crabb, David. PY - 1989. Y1 - 1989. N2 - A 1.7-kilobase pair cDNA clone encoding 3-hydroxyisobutyrate dehydrogenase has been isolated by screening a rat liver λgt11 library with a 17-base oligonucleotide probe which corresponds to a portion of the N-terminal amino acid sequence of rabbit liver 3-hydroxyisobutyrate dehydrogenase. The cDNA contains an open reading frame of 1038 base pairs which includes an amino acid sequence that matches the N-terminal 35 amino acid sequence of rabbit 3-hydroxyisobutyrate dehydrogenase at 33 residues. The cDNA predicts a 300-amino acid mature protein with an amino acid composition and molecular weight very similar to that of rabbit liver 3-hydroxyisobutyrate dehydrogenase. Northern blot ...
Looking for online definition of retinal reductase in the Medical Dictionary? retinal reductase explanation free. What is retinal reductase? Meaning of retinal reductase medical term. What does retinal reductase mean?
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants
BDH2; 3-hydroxybutyrate dehydrogenase, type 2; dehydrogenase/reductase (SDR family) member 6 , DHRS6; 3-hydroxybutyrate dehydrogenase type 2; FLJ13261; PRO20933; SDR15C1; short chain dehydrogenase/reductase family 15C; member 1; UCPA OR; UNQ6308; oxidoreductase UCPA; R-beta-hydroxybutyrate dehydrogenase; dehydrogenase/reductase SDR family member 6; dehydrogenase/reductase (SDR family) member 6; short chain dehydrogenase/reductase family 15C, member 1; DHRS6; EFA6R; UCPA-OR ...
This gene encodes a mitochondrial 3-hydroxyisobutyrate dehydrogenase enzyme. The encoded protein plays a critical role in the catabolism of L-valine by catalyzing the oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde. [provided by RefSeq, Nov 2011 ...
Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
The corepressor CtBP (carboxyl-terminal binding protein) is involved in transcriptional pathways important for development, cell cycle regulation, and transformation. We demonstrate that CtBP binding to cellular and viral transcriptional repressors is regulated by the nicotinamide adenine dinucleotides NAD+ and NADH, with NADH being two to three orders of magnitude more effective. Levels of free nuclear nicotinamide adenine dinucleotides, determined using two-photon microscopy, correspond to the levels required for half-maximal CtBP binding and are considerably lower than those previously reported. Agents capable of increasing NADH levels stimulate CtBP binding to its partners in vivo and potentiate CtBP-mediated repression. We propose that this ability to detect changes in nuclear NAD+/NADH ratio allows CtBP to serve as a redox sensor for transcription. ...
CBR1_HUMAN RecName: Full=Carbonyl reductase [NADPH] 1; AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)]; AltName: Full=NADPH-dependent carbonyl reductase 1; AltName: Full=Prostaglandin 9-ketoreductase; AltName: Full=Prostaglandin-E(2) 9-reductase ...
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues. ...
Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari golongan dehidrogenase yang berfungsi sebagai katalisator oksidasi alkohol dengan aldehid atau keton, dengan reduksi NAD+ menjadi NADH. ADH merupakan protein yang mengandung Zn yang bereaksi pada alkohol primer dan sekunder atau asetal-hemi, dan alkohol sekunder siklik.[1] Reaksi yang terjadi: ...
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis. ...
L-Threonine dehydrogenase (TDH) from Escherichia coli is rapidly inactivated and develops a new absorbance peak at 347 nm when incubated with N-ethyl-5-phenylisoxazolium-3-sulfonate (Woodwards reagent K, WRK). The cofactors, NAD+ or NADH (1.5 mM), provide complete protection against inactivation; L-threonine (60 mM) is approximately 50% as effective. Tryptic digestion of WRK-modified TDH followed by HPLC fractionation (pH 6.2) yields four 340-nm-absorbing peptides, two of which are absent from enzyme incubated with WRK and NAD+. Peptide I has the sequence TAICGTDVH (TDH residues 35-43), whereas peptide II is TAICGTDVHIY (residues 35-45). Peptides not protected are TMLDTMNHGGR (III, residues 248-258) and NCRGGRTHLCR (IV, residues 98-108). Absorbance spectra of these WRK-peptides were compared with WRK adducts of imidazole, 2-hydroxyethanethiolate, and acetate. Peptides III and IV have pH-dependent lambda max values (340-350 nm), consistent with histidine modification. Peptide I has ...
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Pseudomonas aeruginosa ExaE protein: a response regulator of a two-component regulatory system for controling expression quinoprotein ethanol dehydrogenase; isolated from Pseudomonas aeruginosa; amino acid sequence in first source
Cinnamyl alcohol is a naturally occurring compound that is found within cinnamon. Due to the low levels found in cinnamon, cinnamyl alcohol is usually supplied as DB14184 within commercial products....
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 ...
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, ...
Accepted name: coniferyl-alcohol dehydrogenase. Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+. Other name(s): CAD. Systematic name: coniferyl-alcohol:NADP+ oxidoreductase. Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-27-4. References:. 1. Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849-1853.. 2. Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. [PMID: 1250]. ...
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
RDH10 is a specific all-trans retinol dehydrogenase identified in the RPE and now in the Müller cells. 14 We propose that one of the possible physiological functions of RDH10 is to synthesize the all-trans retinal chromophore for RGR and thus to act as a functional partner of RGR in the photic visual cycle. As RGR is known to be expressed in both the RPE and Müller cells, it was necessary to determine whether RDH10 co-expresses with RGR in both the RPE and Müller cells. Western blot analysis demonstrated that RDH10 is expressed at a high level in the RPE and a lower level in the retina (Fig. 2) . The anti-RDH10 antibody stained a cell type in the inner retina. The morphology of the stained cells and their location in the retina are consistent with those of Müller cells. 16 To further confirm the observation, we used rMC-1 cells, a well-established and characterized retinal Müller cell line. 19 RDH10 expression in this cell line was detected at both the mRNA and protein levels (Fig. 4) ...
Reitman and colleagues had a hunch that the genetic mutation seen in cancer might trigger a similar functional change to a closely related enzyme found in yeast and bacteria (homoisocitrate dehydrogenase), which would create the elusive 2-hydroxyadipate dehydrogenase necessary for green adipic acid production.. They were right. The functional mutation observed in cancer could be constructively applied to other closely related enzymes, creating a beneficial outcome - in this case the missing link that could enable adipic acid production from cheap sugars. The next step will be to scale up the overall adipic acid production process, which remains a considerable undertaking.. Its exciting that sequencing cancer genomes can help us to discover new enzyme activities, Reitman said. Even genetic changes that occur in only a few patients could reveal useful new enzyme functions that were not obvious before.. Yan, a professor in the Department of Pathology and senior author of the study, said the ...
SWISS-MODEL Template Library (SMTL) entry for 1g72.1. CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION
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 - ...
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome Database
GT:ID BAD57618.1 GT:GENE BAD57618.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 2940013..2940783 GB:FROM 2940013 GB:TO 2940783 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD57618.1 LENGTH 256 SQ:AASEQ MDKDSFRKLFDLSGRTAIVTGGTRGIGLAIAEGFACAGANLVVASRKPEACEQAAARLRELGAQAVGVPTHLGEIDSLRALVDTAVSAFGGIDIVVNNAANALAQPLATMAPEAVDKSFGVNVQGPLFLVQAALPHLRASAHAAVLNLGSVAALQFAPGLSMYAAGKAALLSFTRAMAAEFAADGIRVNAMAPGAVNTDMVRKNPPEFIAAMAQAPLLRRIAEPDEMVGAALLLCSDAGSFITGQTFLVDGGTVAR GT:EXON 1,1-256:0, BL:SWS:NREP 1 BL:SWS:REP 12-,256,DHRS4_RABIT,4e-36,36.8,242/260, PROS 150-,178,PS00061,ADH_SHORT,PDOC00060, SEG 97-,102,nnaana, BL:PDB:NREP 1 BL:PDB:REP 9-,255,1vl8B,1e-34,34.4,247/252, RP:PDB:NREP 1 RP:PDB:REP 10-,256,2ae1A,8e-44,30.6,245/252, RP:PFM:NREP 1 RP:PFM:REP 15-,180,PF00106,2e-21,42.2,166/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP 16-,181,PF00106,2.2e-34,30.9,162/167,adh_short, GO:PFM:NREP 2 GO:PFM ...
GT:ID BAD55466.1 GT:GENE BAD55466.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 643418..644293 GB:FROM 643418 GB:TO 644293 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD55466.1 LENGTH 291 SQ:AASEQ MSRWDTANIPDQSGRTFIVTGANSGLGAVAARALARAGADVVLACRNLTKAEKVAAEIGARATVRELDLADLASVRAFAAGTERVDVLINNAGVMAVPHRTTADGFEMQIGTNHLGHFALTGLLLDKITDRVVTVSSGAHAVGRIDLADLNWERRRYQRWLAYGQSKLANLLFAYELQRRLGAAGSPILSVAAHPGYAATELQSHTETFLDSVMNVGNRILAQTAEMGALPELFAATMPVEPGAFYGPTGLGGMRGYPGRCGSTKASRDERVAGELWALSERLTGVTYSFD GT:EXON 1,1-291:0, BL:SWS:NREP 1 BL:SWS:REP 7-,286,RDH13_MOUSE,2e-38,40.5,269/334, SEG 25-,44,glgavaaralaragadvvla, BL:PDB:NREP 1 BL:PDB:REP 14-,205,2japC,4e-08,39.4,180/246, RP:PDB:NREP 2 RP:PDB:REP 13-,91,2ag5C,1e-05,23.4,77/244, RP:PDB:REP 68-,205,3ce6B,5e-13,8.1,136/485, RP:PFM:NREP 1 RP:PFM:REP 46-,143,PF00106,3e-05,38.8,98/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP ...
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pyloris pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes ...
At concentrations of 2mM and above hydroxypyruvate produced no glucose with isolated rat liver cells, although it was rapidly utilized. At a lower concentration of hydroxypyruvate or in the presence of substrates which generate reducing equivalents (ethanol or butyrate), appreciable amounts of glucose were formed from hydroxypyruvate. A possible explanation for this phenomenon is discussed.. ...
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ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
putative quinate/shikimate dehydrogenase [putative shikimate 5-dehydrogenase] ATGGTCAAGGACTCGTATCTCGTCGGGCTGATCGGCGCCGGGATCGGCCCGTCGCTCAGC CCGGCACTGCACGAGCGGGAGGCCGACCGGCAGGGCCTGCGCTATCTGTACCGGCTGATC GACATCGACGCGCTCGGTGTCGGGCCGCAGGCGGTGGGGGACCTCGTACGAGCCGCCCGC GACCTGGGCTTCGACGGGCTGAACATCACGCATCCCTGCAAGCAGCTCGTCATCGGGCAT CTGGACGCGCTCGCCCCGCAGGCCGAGGCGCTCGGCGCGGTGAACACCGTCGTCTTCGAG GGCGGGCGTGCGGTCGGGCACAACACCGATGTCACCGGGTTCGCCGCCTCGTTCGCCCGT GGGCTGCCGGATGCCCCGCTGGAGCGGGTCGTGCAGTTGGGCGCGGGGGGAGCGGGGGCG GCCGTCGCGCATGCCATGCTCACGCTCGGGGCCGGGCACGTCACCGTCGTCGATGCCATG CCGGACCGGTCGGCGGACCTCGCCGCCTCGCTGAACCGGCACTTCGGTGCGGGGCGGGCC GCTGCCGCGGGCCCGGAGCGGCTGGCGGCGCTGCTCGGCGGTGCGGACGGCATCGTGCAT GCCACGCCGACGGGGATGGCCGCTCATCCGGGGCTGCCGCTTCCCGGTGAGTTGCTGCAT CCCGGGTTGTGGGTGGCCGAGGTGGTGTACCGGCCGTTGGAGACCGAGTTGCTGCGTGCC GCTCGGGCGGCGGGGTGTGCGGTTCTCGATGGTGGGGGGATGGCTGTTTTCCAGGCCGCG GACGCGTTTCGGCTGTTCACGGGGCGGGAGCCGGACGCGGTGCGGATGCTTGCGGATATT ...
At the beginning of 2020, COVID-19 disease began to spread around the world, millions of people worldwide were infected with COVID-19 disease, and major countries around the world have implemented foot prohibitions and work stoppage orders. Except for the medical supplies and life support products industries, most industries have been greatly impacted, and Alcohol Dehydrogenase industries have also been greatly affected.. GET FREE SAMPLE PDF : https://www.wiseguyreports.com/sample-request/6274794-global-alcohol-dehydrogenase-market-report-2021. This Report covers the manufacturers data, including: shipment, price, revenue, gross profit, interview record, business distribution etc., these data help the consumer know about the competitors better. This report also covers all the regions and countries of the world, which shows a regional development status, including market size, volume and value, as well as price data ...
Analytical approaches to alcohol dehydrogenase structures / M.T. Gheorghe; I. Lindh; W.J. Griffiths; J. Sjovall; T. Bergman; William Griffiths ...
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Kerchev, P.; Waszczak, C.; Lewandowska, A.; Willems, P.; Shapiguzov, A.; Li, Z.; Alseekh, S.; Mühlenbock, P.; Hoeberichts, F.A.; Huang, J. et al.; Van Der Kelen, K.; Kangasjärvi, J.; Fernie, A. R.; De Smet, R.; Van de Peer, Y.; Messens, J.; Van Breusegem, F.: Lack of GLYCOLATE OXIDASE1, but not GLYCOLATE OXIDASE2, attenuates the photorespiratory phenotype of CATALASE2-deficient Arabidopsis. Plant Physiology 171 (3), pp. 1704 - 1719 (2016 ...
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 173.2) ...
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 201.9) ...
HAO1 antibody, Internal (hydroxyacid oxidase (glycolate oxidase) 1) for WB. Anti-HAO1 pAb (GTX81144) is tested in Human, Mouse samples. 100% Ab-Assurance.
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 ...
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
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. ...
Alcohol flush reaction Disulfiram-like drug Oxidoreductase PDB: 1NVM​; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). " ... Swift R, Davidson D. "Alcohol Hangover: Mechanisms and Mediators" (PDF). National Institute on Alcohol Abuse and Alcoholism. ... Acetaldehyde is more toxic than alcohol and is responsible for many hangover symptoms. About 50% of people of Northeast Asian ... In the first step, ethanol is converted to acetaldehyde by alcohol dehydrogenase. In the second step, the acetaldehyde is ...
... 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, ...
... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...
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 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 ...
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 ...
... primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari ... NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase ...
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem J. ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). „A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ...
Oksidoreduktase aril-alkohol:NADP+ (bahasa Inggris: aryl-alcohol:NADP+ oxidoreductase, aryl-alcohol dehydrogenase (NADP+), aryl ... coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP), EC 1.1.1.91) adalah ...
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". The ... cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction a primary alcohol + 2 ferricytochrome cL ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... displaystyle \rightleftharpoons } an aldehyde + 2 ferrocytochrome cL + 2 H+ A periplasmic quinoprotein alcohol dehydrogenase is ...
... are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β- ... Oxidoreductase from the Rat Adrenal Gland]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 336: 63-8. doi: ...
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase. It ... to differentiate is from long-chain-alcohol oxidase (LCAO), aryl-alcohol oxidase (AAO) and secondary-alcohol oxidase (SAO). As ... In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ⇌ {\ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as ...
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+ ...
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 US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
... membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase. ... Alcohol+dehydrogenase+(quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Cozier GE, Giles IG, Anthony C (June 1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti ... Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K (2003). "Quinoprotein alcohol dehydrogenase is ...
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: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 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 ...
... azurin oxidoreductase. This enzyme catalyses the following chemical reaction primary alcohol + azurin ⇌ {\displaystyle \ ... Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase ... "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... Alcohol+dehydrogenase+(azurin) at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
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 ...
H2 by pyruvate ferredoxin oxidoreductase and hydrogenase; and ethanol via NADH- and NADPH-linked alcohol dehydrogenase. By its ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). ... This enzyme belongs to the superfamily of short-chain oxidoreductases, specifically those acting on the CH-OH group of donor ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme ... The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ... allyl-alcohol dehydrogenase activity. • NADP-retinol dehydrogenase activity. Cellular component. • mast cell granule. • Schwann ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. The involvement in ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. It also participates ...
Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L- ... Alcohol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
oxidoreductase activity. • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, ... it may also contribute to hypersensitivity responses of the respiratory system to cold air and possibly even alcohol beverages ... may then be released by the enzyme and rapidly reduced by cellular glutathione peroxidases to its corresponding alcohol, 5(S)- ...
alditol:NADP+ 1-oxidoreductase activity. • electron carrier activity. • oxidoreductase activity. • alcohol dehydrogenase (NADP+ ... allyl-alcohol dehydrogenase activity. Cydrannau o'r gell. • cytosol. • extracellular exosome. • apical plasma membrane. • ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase ...
Within this group is alcohol sulfotransferase which has a broad targeting capacity. Due to this, alcohol sulfotransferase is ... hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. EC 2.1 includes enzymes that ... This transferase acts via the following reaction: 3'-phosphoadenylyl sulfate + an alcohol ⇌ {\displaystyle \rightleftharpoons ...
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... 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 carnitine:NAD+ 3-oxidoreductase. ...
"Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial. Retrieved 11 February 2007.. ... It can also be dissolved in alcohol to form tincture of iron, which is used as a medicine to stop bleeding in canaries.[133] ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
Alcohol flush reaction. *Disulfiram-like drug. *Oxidoreductase. References[edit]. *^ a b PDB: 1NVM​; Manjasetty BA, Powlowski J ... Role in metabolism of alcohol[edit]. In the liver, the enzyme alcohol dehydrogenase oxidizes ethanol into acetaldehyde, which ... National Institute on Alcohol Abuse and Alcoholism. Retrieved 26 Mar 2017.. *^ a b Xiao Q, Weiner H, Crabb DW (Nov 1996). "The ... Acetaldehyde is more toxic than alcohol and is responsible for many hangover symptoms.[5] ...
... with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ...
oxidoreductase activity. • aromatase activity. • oxidoreductase activity, acting on paired donors, with incorporation or ... Factors known to increase aromatase activity include age, obesity, insulin, gonadotropins, and alcohol. Aromatase activity is ... oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen. • electron carrier ...
Adams KE, Rans TS (Dec 2013). "Adverse reactions to alcohol and alcoholic beverages". Annals of Allergy, Asthma & Immunology. ... oxidoreductase activity. • aldehyde dehydrogenase [NAD(P)+ activity]. • aldehyde dehydrogenase (NAD) activity. • NAD binding. • ... alcohol metabolic process. • oxidation-reduction process. • ethanol oxidation. • carbohydrate metabolic process. • electron ... oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor. • glyceraldehyde-3-phosphate ...
... (succinate-ubiquinone oxidoreductase). The structure of SQR in a phospholipid membrane. SdhA, SdhB, ... succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction". The ...
Threonine proteases - using a threonine secondary alcohol. *Aspartic proteases - using an aspartate carboxylic acid ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
FDCA was also detected in blood plasma.[3] Recently, the enzyme furfural/HMF oxidoreductase was isolated from the bacterium ... Both of these latter materials can serve as alcohol components in the production of new polyester, and their combination with ...
"alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or ... 1. ஆக்சிசனேற்ற--ஒடுக்க நொதிகள் (Oxidoreductases):. ஒரு வினையில் ஆக்சிசனேற்றம் நடக்கிறதென்றால் ஒடுக்கமும் நடக்கிறதென்று பொருள். ... எ.கா: 1.1.1.1 என்பது ஆல்க்ககால் டிஐதரோச்செனேசு (Alcohol dehydrogenase) குடும்ப நொதிகளைக் குறிக்கும் நொதிஎண் ஆகும். ...
NADH-ubiquinone oxidoreductase chain 1 EC 1.6.5.3. Pfam PF00146 9. ND2 / NU2M. NU2M_HUMAN. NADH-ubiquinone oxidoreductase chain ... NADH-ubiquinone oxidoreductase chain 4L EC 1.6.5.3. Pfam PF00420 13. ND5 / NU5M. NU5M_HUMAN. NADH-ubiquinone oxidoreductase ... NADH-ubiquinone oxidoreductase chain 3 EC 1.6.5.3. Pfam PF00507 11. ND4 / NU4M. NU4M_HUMAN. NADH-ubiquinone oxidoreductase ... Respiratory complex I, EC 1.6.5.3 (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial ...
Oksidoreduktase perilil-alkohol:NAD+ (bahasa Inggris: perillyl-alcohol:NAD+ oxidoreductase, perillyl-alcohol dehydrogenase, ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase. This enzyme is also called 3β- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... Wikvall K (April 1981). "Purification and properties of a 3 β-hydroxy-delta 5-C27-steroid oxidoreductase from rabbit liver ...
... with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus,[18] and even cadmium in ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. doi:10.1126/science.7878465. PMID 7878465.. ... They noticed that adding boiled and filtered yeast extract greatly accelerated alcoholic fermentation in unboiled yeast ...
... are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β- ... Oxidoreductase from the Rat Adrenal Gland]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 336: 63-8. doi: ...
Oxidoreductase (EC 1). *1.1 Aldose reductase. *HMG-CoA reductase. *1.3 5α-Reductase ...
All MeSH CategoriesChemicals and Drugs CategoryEnzymes and CoenzymesEnzymesOxidoreductasesAlcohol OxidoreductasesCarbohydrate ... Alcohol Oxidoreductases. A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as ... Dependent Alcohol Oxidoreductases11-beta-Hydroxysteroid Dehydrogenases +20-Hydroxysteroid Dehydrogenases +3-alpha- ... Acetoin DehydrogenaseAlcohol DehydrogenaseAldo-Keto Reductases +Carbonyl Reductase (NADPH)D-Xylulose ReductaseGlycerol-3- ...
Regulation of a Glycerol-Induced Quinoprotein Alcohol Dehydrogenase by σ54 and a LuxR-Type Regulator in Azospirillum brasilense ...
Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group.[1][2] ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) ... This oxidoreductase article is a stub. You can help Wikipedia by expanding it.. *v ... Functional group of an alcohol molecule. The carbon atom is attached to other carbon or hydrogen atoms. ...
Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal v t e v t e. ...
"Alcohol Oxidoreductases" by people in Harvard Catalyst Profiles by year, and whether "Alcohol Oxidoreductases" was a major or ... "Alcohol Oxidoreductases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Alcohol Oxidoreductases" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Alcohol Oxidoreductases". ...
... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ... Oxidoreductases: 9264*Alcohol Oxidoreductases: 1*N-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N ... dimethyl-4-nitrosoaniline oxidoreductase alcohol - N. Subscribe to New Research on N-dimethyl-4-nitrosoaniline oxidoreductase ... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ...
Alcohol Oxidoreductases / genetics * Alcohol Oxidoreductases / metabolism * Amino Acid Substitution * Anaerobiosis * Butylene ... Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol Appl Environ ... dependent oxidoreductases. One of them has been purified and shown to be d-arabinose dehydrogenase (Ara1p), which converts (R/S ...
Alcohol Oxidoreductases * Amino Acid Sequence * Animals * DNA-Binding Proteins / metabolism* * Drosophila / embryology ...
alcohol: NAD oxidoreductase. alcohol dehydrogenase. alcohol + NAD → acetaldehyde NADH. alcoholic fermentation. 1.1.1.27. L- ... Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. The table ... Enzymes that catalyze reactions in which hydrogen is transferred belong to the group known as oxidoreductases; those that ... The numbering system is as follows: the first number places the enzyme in one of six general groups-1, oxidoreductases; 2, ...
Alcohol Oxidoreductases); EC 1.1.- (glycolic acid dehydrogenase); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde ...
Alcohol Oxidoreductases); EC 1.1.1.36 (acetoacetyl-CoA reductase); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC ...
Alcohol Oxidoreductases / chemistry. Apoptosis. Cell Line. Cell Line, Tumor. Cell Physiological Phenomena*. Cells / cytology*. ... Asher G,Lotem J,Cohen B,Sachs L,Shaul Y. Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase ... This pathway was not known to be dependent on the oxidoreductase CBR1, thus validating that the compounds discovered in such ... To initially validate that the oxidoreductase CBR1 was indeed inhibited by hydroxy-PP, we measured CBR1 catalytic activity in ...
2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. These enzymes perform their ... the sequence of which is YNTPH277GVAN for propanediol oxidoreductase and YNLPH277GV for alcohol dehydrogenase 11. This ... consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas ... consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas ...
... acetaldehyde/alcohol dehydrogenase; AOR, aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase ... acetaldehyde/alcohol dehydrogenase; AOR, aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase ... alcohol/acetaldehyde dehydrogenase, and d-lactate dehydrogenase [28]. Thirty-two grams per liter of d-lactate (99.9% chiral ... It is also suggested that an acetaldehyde/alcohol dehydrogenase might carry out an important role in glycerol fermentation for ...
Predicted oxidoreductases (Related to aryl-alcohol dehydrogenases). Klebsiella pneumoniae IS22. 346. +39. ... oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: EcoCyc ,p>Inferred from Direct ...
Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L- ... Alcohol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
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 US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
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. ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ...
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductase · Oxygenase · Unclassified drug · Bacterial metabolism · Controlled study · Enzyme activity · Nonhuman · ...
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductases · Rats · Rats, Wistar · RNA, Messenger · Steroid Hydroxylases · Support, Non-U.S. Govt · Taurocholic Acid · ... cinnamyl alcohol · collagen type 16 · disulfiram · dodecyl sulfate sodium · eugenol · ferritin · ferrochelatase · glucose 6 ...
p-hydroxybenzyl alcohol dehydrogenase;. benzyl alcohol dehydrogenase;. coniferyl alcohol dehydrogenase. Class. Oxidoreductases; ... Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase ...
Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase ... The byproducts generated during polycondensation are water, methanol, ethanol and n-butyl alcohol, respectively. ... and n-butyl alcohol (bp = 117.7 °C). Besides, the chemical reactivity of the alkyl esters is another reason. It is well known ... We suspect that the increase of the residual alcohol amount and the decrease of the polymerization rate in dilute reaction ...
Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor IDA Inferred from Direct Assay. more info ... alditol:NADP+ 1-oxidoreductase activity IBA Inferred from Biological aspect of Ancestor. more info ...
p-cumic alcohol:NAD+ oxidoreductase. Definition. p-Cumic alcohol + NAD+ ,=, 4-Isopropylbenzaldehyde + NADH + H+. ...
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to ... cinnamyl alcohol dehydrogenase. Subscribe to New Research on cinnamyl alcohol dehydrogenase NADP-dependent enzyme that ... 12/01/2014 - "Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes ... 09/01/1999 - "Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol ...
Alcohol Oxidoreductases (+35). Autoradiography (+14). Carbohydrate Metabolism (+38). PA0374. Chromosomes (+4). Escherichia coli ...
Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP+ oxidoreductase Imre E. Somssich, Petra Wernert, ...
Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such ... Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.Curated ... Quinone oxidoreductaseAdd BLAST. 328. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... A novel NADPH:quinone oxidoreductase.". Rao P.V., Krishna C.M., Zigler J.S. Jr.. J. Biol. Chem. 267:96-102(1992) [PubMed] [ ...
Surprisingly, alcohol dehydrogenases were significantly up-regulated more than any other dehydrogenases, including aldehyde ... the high concentrations of the latter provoked the expression of alcohol dehydrogenases that in yeast can act to reduce NADH ... Cells responded to NA by up-regulation of oxidoreductases, with hardly any up-regulation of the classic response to oxidative ... Cells responded to NA by up-regulation of oxidoreductases, with hardly any up-regulation of the classic response to oxidative ...
  • We have studied two enzymes of a newly described family of dehydrogenases with high sequence homology, 1,2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. (udl.cat)
  • Surprisingly, alcohol dehydrogenases were significantly up-regulated more than any other dehydrogenases, including aldehyde dehydrogenases. (frontiersin.org)
  • the high concentrations of the latter provoked the expression of alcohol dehydrogenases that in yeast can act to reduce NADH and increase NAD + amounts, respectively. (frontiersin.org)
  • 2. Jörnvall, H. Differences between alcohol dehydrogenases. (qmul.ac.uk)
  • As an alternative to (thermodynamically disfavoured) nicotinamide-dependent alcohol dehydrogenases, alcohol oxidases make use of molecular oxygen but their application is under-represented in synthetic biotransformations. (springer.com)
  • 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. (qmul.ac.uk)
  • Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. (hmdb.ca)
  • NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. (creative-enzymes.com)
  • In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. (umassmed.edu)
  • Alcohol dehydrogenase E (AdhE) is an Fe-enzyme that, under anaerobic conditions, is involved in dissimilation of glucose. (udl.cat)
  • Zymomonas mobilis is endowed with two isoenzymes of fermentative alcohol dehydrogenase, a zinc-containing enzyme (ADH I) and an iron-containing enzyme (ADH II). (udl.cat)
  • Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. (wikipedia.org)
  • In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + acceptor \rightleftharpoons an aldehyde + reduced acceptor Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor. (morebooks.de)
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. (morebooks.de)
  • The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. (morebooks.de)
  • [ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.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)
  • The dissociation constants for the enzyme-NAD+ complex and for the enzyme-alcohol complexes obtained from the kinetic quotients satisfactorily correspond to the dissociation constants obtained by use of other techniques. (thebiogrid.org)
  • It is suggested that the non-linear curves may be attributed to a structural change in the enzyme itself, caused by the alcohol. (thebiogrid.org)
  • This study demonstrates the function of the FaQR enzyme in the biosynthesis of HDMF as enone oxidoreductase and provides a foundation for the improvement of strawberry flavor and the biotechnological production of HDMF. (plantcell.org)
  • This conventional biosensor is produced by forming an electrode system having a working electrode and a counter electrode on an electrically insulating base plate by a screen printing method or the like and subsequently forming an enzyme reaction layer including a hydrophilic polymer, an oxidoreductase and an electron acceptor above the electrode system. (google.com)
  • Hoog JO, von Bahr-Lindstrom H, Heden LO, Holmquist B, Larsson K, Hempel J, Vallee BL, Jornvall H: Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. (hmdb.ca)
  • Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. (morebooks.de)
  • The biosensor comprises an electrode system including a working electrode and a counter electrode formed on an electrically insulating base plate, and a reaction layer containing at least an oxidoreductase and an electron acceptor, wherein the electron acceptor is a sodium salt. (google.com)
  • A novel NADPH:quinone oxidoreductase. (uniprot.org)
  • Sequence analysis of two peptide fragments showed total identity with the protein sequence of a strongly ripening-induced, auxin-dependent putative quinone oxidoreductase, Fragaria × ananassa quinone oxidoreductase (FaQR). (plantcell.org)
  • The concentrations of (2R,3R)-2,3-butanediol are mostly dependent on Bdh1p activity, while those of (meso)-2,3-butanediol are also influenced by the activity of NADP(H)-dependent oxidoreductases. (nih.gov)
  • Ethanolamine lyase produces acetaldehyde, which is converted by the oxidoreductase EutE to acetyl-coenzyme A, which enters the carbon pool of the cell. (asm.org)
  • Alternatively, acetaldehyde can be converted to alcohol by another specialized oxidoreductase, EutG. (asm.org)
  • It is proven that alcohol dehydrogenase oxidizes ethanol to acetaldehyde, which is responsible for some hangover symptoms. (steadyhealth.com)
  • The identified enzymes involved in acetaldehyde production included alcohol dehydrogenase (ADH) and xanthine oxidoreductase (XO) in the cytosolic fraction and the flavoenzyme NADPH oxidase and catalase in the microsomal fraction [1]. (thefreedictionary.com)
  • Oxidation of aldehydes is considered to be generally a detoxification reaction because it is based on removing the electrophilic products of alcohol oxidation. (steadyhealth.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)
  • Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. (medscape.com)
  • In this review, the mechanism of copper-containing and flavoprotein alcohol oxidases is discussed in view of their ability to accept electronically activated or non-activated alcohols and their propensity towards over-oxidation of aldehydes yielding carboxylic acids. (springer.com)
  • In flavoprotein oxidases, the oxidation proceeds via two half reactions, where the alcohol is first oxidised by a two-electron transfer during the reductive half reaction , yielding reduced flavin. (springer.com)
  • Creative Enzymes is one of the few companies in the world that provides spectrophotometric assays for allyl-alcohol dehydrogenase. (biocatalogue.org)
  • With specialized knowledge in oxidoreductases, especially the ones such as allyl-alcohol dehydrogenase, Creative Enzymes successfully demonstrated the first-in-class test quality and service reliability. (biocatalogue.org)
  • Alcohol Oxidoreductases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • The fungus secretes aryl-alcohol oxidase and Mn2+-oxidizing peroxidase, two kinds of oxidoreductases characteristic of ligninolytic basidiomycetes. (csic.es)
  • Aryl-alcohol oxidase (AAO, EC 1.1.3.7) generates H2O2 for lignin degradation at the expense of benzylic and other π system-containing primary alcohols, which are oxidized to the corresponding aldehydes. (upc.edu)
  • Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. (thebiogrid.org)
  • The kinetic coefficients determined from secondary plots are consistent with an 'equilibrium random-order' mechanism for extremely low alcohol concentrations and for all alcohols, the transformation of the ternary complexes being the rate-limiting step of the reaction. (thebiogrid.org)
  • In a related fashion, alcohol oxidases convert primary and secondary alcohols to aldehydes and ketones, respectively. (springer.com)
  • The aryl hydrocarbon receptor (AHR) nuclear translocator (ARNT), as the AHR's heterodimerization partner, and NADPH-cytochrome P450 oxidoreductase (POR), as the key electron donor for all microsomal P450s, are independent and indispensable components in the adaptive and toxic responses to polycyclic aromatic hydrocarbons. (aspetjournals.org)
  • We report here the molecular cloning and characterization of the corresponding cDNA, CAD 1-5, which encodes this novel aromatic alcohol dehydrogenase. (deepdyve.com)
  • 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)
  • the role of decreased gastric alcohol dehydrogenase and first pass metabolism. (thefreedictionary.com)
  • Rizzo W.B., Craft D.A., Dammann A.L., Phillips M.W., Fatty alcohol metabolism in cultured human fibroblasts. (springer.com)
  • 5. Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. (qmul.ac.uk)
  • Electron-withdrawing substituents resulted in lower quantum mechanics stacking energies between aldehyde and the tyrosine side chain, contributing to product release, in agreement with the ping-pong mechanism observed in 3-chloro- and 3-fluorobenzyl alcohol kinetics analysis. (upc.edu)
  • This gene encodes class V alcohol dehydrogenase, which is a member of the alcohol dehydrogenase family. (genecards.org)
  • Experts are saying that Aldehyde dehydrogenase (ALDH) is functioning often in tandem with Alcohol dehydrogenase. (steadyhealth.com)
  • Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (medscape.com)
  • Kinetic studies of yeast alcohol dehydrogenase with NAD+ and ethanol, hexanol or decanol as substrates invariably result in non-linear Lineweaver-Burk plots if the alcohol is the variable substrate. (thebiogrid.org)
  • Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. (freepatentsonline.com)
  • Such biosensor can quantitate various substrates if an adequate oxidoreductase fit for the measuring substrate is adopted. (google.com)
  • Ligand diffusion studies on Pleurotus eryngii AAO showed a T-shaped stacking interaction between the Tyr92 side chain and the alcohol substrate at the catalytically competent position for concerted hydride and proton transfers. (upc.edu)
  • Pyruvate-ferredoxin oxidoreductase and quinol-fumarate reductase contain ferredoxin domains that bind [Fe-S] clusters and are involved in electron transport. (ebscohost.com)
  • ADH6 (Alcohol Dehydrogenase 6 (Class V)) is a Protein Coding gene. (genecards.org)
  • GO annotations related to this gene include oxidoreductase activity and alcohol dehydrogenase (NAD) activity . (genecards.org)
  • Here we present gene distribution and phylogenetic analyses of the genes encoding the hybrid-cluster protein, A-type flavoprotein, glucosamine-6-phosphate isomerase, and alcohol dehydrogenase E. These four genes have a limited distribution among sequenced prokaryotic and eukaryotic genomes and were previously implicated in gene transfer events affecting eukaryotes. (diva-portal.org)
  • Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. (hmdb.ca)
  • Biodiesel itself is composed of mono-alkyl esters of vegetable oils or animal fats and is produced by transesterification with a monohydric alcohol (methanol) [ 3 ]. (mdpi.com)
  • Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. (hmdb.ca)
  • [ 14 ] In cultured skin keratinocytes, elevated fatty alcohol is diverted into the synthesis of wax esters and alkyldiacylglycerol lipids. (medscape.com)
  • Synthesis of pyruvate: ferredoxin oxidoreductase and alcohol dehydrogenase E enzymes during Giardia intestinalis excystation. (ebscohost.com)
  • Evidence for a fatty alcohol cycle, The Journal of biological chemistry 262 (1987) 17412-17419. (springer.com)
  • Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. (britannica.com)
  • a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. (qmul.ac.uk)
  • 8. The biosensor of claim 7 , wherein the oxidoreductase and the mediator are immobilized on the working electrode. (google.com)
  • 5. The biosensor of claim 4 , wherein the oxidoreductase is glucose oxidase. (google.com)
  • More specifically, it relates to a glucose biosensor having glucose oxidase immobilized thereon or a biosensor having an oxidoreductase immobilized thereon. (google.com)