DiseasesChemicals and DrugsPsychiatry and PsychologyGeographicals
NAD (+) and NADP (+) Dependent Alcohol OxidoreductasesAlcohol OxidoreductasesAlcohol DrinkingOxidoreductasesAlcoholsProtein Disulfide Reductase (Glutathione)Pyruvate SynthaseNADH, NADPH OxidoreductasesSjogren-Larsson SyndromeIchthyosisAldehyde OxidoreductasesFatty AlcoholsSwedenLeukotriene AntagonistsIchthyosis, Lamellar
NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases
Alcohol Oxidoreductases
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).
Alcohol Drinking
Behaviors associated with the ingesting of alcoholic beverages, including social drinking.
Oxidoreductases
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)
Alcohols
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)
Protein Disulfide Reductase (Glutathione)
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.
Pyruvate Synthase
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
NADH, NADPH Oxidoreductases
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.
Sjogren-Larsson Syndrome
An autosomal recessive neurocutaneous disorder characterized by severe ichthyosis MENTAL RETARDATION; SPASTIC PARAPLEGIA; and congenital ICHTHYOSIS. It is caused by mutation of gene encoding microsomal fatty ALDEHYDE DEHYDROGENASE leading to defect in fatty alcohol metabolism.
Ichthyosis
Any of several generalized skin disorders characterized by dryness, roughness, and scaliness, due to hypertrophy of the stratum corneum epidermis. Most are genetic, but some are acquired, developing in association with other systemic disease or genetic syndrome.
Aldehyde Oxidoreductases
Oxidoreductases that are specific for ALDEHYDES.
Fatty Alcohols
Usually high-molecular-weight, straight-chain primary alcohols, but can also range from as few as 4 carbons, derived from natural fats and oils, including lauryl, stearyl, oleyl, and linoleyl alcohols. They are used in pharmaceuticals, cosmetics, detergents, plastics, and lube oils and in textile manufacture. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Sweden
Leukotriene Antagonists
A class of drugs designed to prevent leukotriene synthesis or activity by blocking binding at the receptor level.
Ichthyosis, Lamellar
A chronic, congenital ichthyosis inherited as an autosomal recessive trait. Infants are usually born encased in a collodion membrane which sheds within a few weeks. Scaling is generalized and marked with grayish-brown quadrilateral scales, adherent at their centers and free at the edges. In some cases, scales are so thick that they resemble armored plate.

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)

MicroRNA-137 Targets Carboxyl-terminal Binding Protein 1 in Melanoma Cell LinesMicroRNA-137 Targets Carboxyl-terminal Binding Protein 1 in Melanoma Cell Lines
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 ...
http://www.ijbs.com/v07p0133.htm
RDH11 Antibody | scrazzl.com - Simply Connecting Science
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 ...
http://scrazzl.com/874691/rdh11-antibody
X-ray Structure of the Quinoprotein Ethanol Dehydrogenase from Pseudomonas Aeruginosa: Basis of Substrate SpecificityX-ray Structure of the Quinoprotein Ethanol Dehydrogenase from Pseudomonas Aeruginosa: Basis of Substrate Specificity
JPT Peptide Technologies is a DIN ISO 9001:2015 certified and GCLP compliant integrated provider of innovative peptide based catalog products and custom services.
https://www.jpt.com/literature/X-ray-Structure-of-the-Quinoprotein-Ethanol-Dehydrogenase-from-Pseudomonas-Aeruginosa-Basis-of-Substrate-Specificity/
SDR9C7 Antibody | scrazzl.com - Simply Connecting Science
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 ...
http://scrazzl.com/872765/sdr9c7-antibody
Homologies between enzymes involved in steroid and xenobiotic carbonyl reduction in vertebrates, invertebrates and procaryonts....
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
https://www.ndorms.ox.ac.uk/publications/108344
产品类别 一抗 | 博士德生物 BOSTER Biological Technology co.ltd
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,. ...
http://www.boster.com.cn/product/index/cate/39.html
Ctbp1 - C-terminal-binding protein 1 - Mus musculus (Mouse) - Ctbp1 gene & proteinCtbp1 - C-terminal-binding protein 1 - Mus musculus (Mouse) - Ctbp1 gene & protein
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.
http://www.uniprot.org/uniprot/O88712
MEDLINE - Resultado p gina 1
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 ...
http://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&format=standard.pft&indexSearch=EX&exprSearch=D08.811.682.047.150.270.500&lang=p&base=MEDLINE
Critical residues for structure and catalysis in short-chain dehydrogenases/reductases. - Immunology
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
https://www.immunology.ox.ac.uk/publications/108576
Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in...
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.
https://www.kennedy.ox.ac.uk/publications/108890
SDR42E1 Gene - GeneCards | D42E1 Protein | D42E1 AntibodySDR42E1 Gene - GeneCards | D42E1 Protein | D42E1 Antibody
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
http://www.genecards.org/cgi-bin/carddisp.pl?gene=SDR42E1
Expression of CtBP family protein isoforms in breast cancer and their role in chemoresistance - ePrints SotonExpression of CtBP family protein isoforms in breast cancer and their role in chemoresistance - ePrints Soton
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 ...
https://eprints.soton.ac.uk/166261/
Biochemical properties of human dehydrogenase/reductase (SDR family) member 7. - Nuffield Department of Orthopaedics,...
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
https://www.ndorms.ox.ac.uk/publications/443444
retinol dehydrogenase 8 (all trans) Proteins: Novus Biologicalsretinol dehydrogenase 8 (all trans) Proteins: Novus Biologicals
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
https://www.novusbio.com/proteins/retinol-dehydrogenase-8-%28all-trans%29?showGrid=true
Plus itPlus it
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 ...
http://cancerres.aacrjournals.org/content/66/8_Supplement/141.1
Alcohol Oxidase - AP20103AF-N | acris-antibodies.com
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.
https://www.acris-antibodies.com/antibodies/primary-antibodies/alcohol-oxidase-ap20103af-n.htm
RCSB PDB - Protein Feature View - Homoisocitrate dehydrogenase - Q72IW9 (HICDH THET2)RCSB PDB - Protein Feature View - Homoisocitrate dehydrogenase - Q72IW9 (HICDH THET2)
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.
http://www.rcsb.org/pdb/protein/Q72IW9
Dehydrogenase/reductase SDR family protein elisa and antibodyDehydrogenase/reductase SDR family protein elisa and antibody
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.
https://www.mybiosource.com/protein_family.php?root=dehydrogenase-reductase-sdr-family-protein
EMBL: CP000667.PE408
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 ...
http://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-id?query=CP000667.PE408&db=EMBL&ident=ACNUC7421
Practical Fragments: December 2013Practical Fragments: December 2013
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 ...
http://practicalfragments.blogspot.com/2013_12_01_archive.html
Gentaur Molecular :GenWay \ Acyl-Coenzyme A dehydrogenase family. member 8 variant - \ 10-288-21999FGentaur Molecular :GenWay \ Acyl-Coenzyme A dehydrogenase family. member 8 variant - \ 10-288-21999F
Gentaur molecular products has all kinds of products like :search , GenWay \ Acyl-Coenzyme A dehydrogenase family. member 8 variant - \ 10-288-21999F for more molecular products just contact us
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RDH16 Gene - GeneCards | RDH16 Protein | RDH16 AntibodyRDH16 Gene - GeneCards | RDH16 Protein | RDH16 Antibody
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
http://www.genecards.org/cgi-bin/carddisp.pl?gene=RDH16
HEK-293T Cells Human ADHFE1 Lysate | ABIN1338769HEK-293T Cells Human ADHFE1 Lysate | ABIN1338769
Lysate und Produkte wie ADHFE1 293T Cell Transient Overexpression Lysate(Denatured) bestellen auf www.antikoerper-online.de. Jetzt Produkt ABIN1338769 bestellen.
https://www.antikoerper-online.de/lysate/1338769/ADHFE1+293T+Cell+Transient+Overexpression+LysateDenatured/
RDH5抗体|Abcam中国|Anti-RDH5抗体RDH5抗体|Abcam中国|Anti-RDH5抗体
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。
http://www.abcam.cn/rdh5-antibody-ab101457.html
Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to...
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 ...
https://indiana.pure.elsevier.com/en/publications/cloning-and-sequence-analysis-of-a-cdna-for-3-hydroxyisobutyrate-
Retinal reductase | definition of retinal reductase by Medical dictionaryRetinal reductase | definition of retinal reductase by Medical dictionary
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?
https://medical-dictionary.thefreedictionary.com/retinal+reductase
1 3 propanediol dehydrogenase : définition de 1 3 propanediol dehydrogenase et synonymes de 1 3 propanediol dehydrogenase ...1 3 propanediol dehydrogenase : définition de 1 3 propanediol dehydrogenase et synonymes de 1 3 propanediol dehydrogenase ...
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
http://dictionnaire.sensagent.leparisien.fr/1+3+propanediol+dehydrogenase/en-en/
cinnamyl alcohol dehydrogenase Summary Report | CureHuntercinnamyl alcohol dehydrogenase Summary Report | CureHunter
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
http://www.curehunter.com/public/keywordSummaryC018656-cinnamyl-alcohol-dehydrogenase.do
Recombinant Human BDH2 protein, His-tagged BDH2-3452H - Creative BioMart
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 ...
https://www.creativebiomart.net/description_10342_12.htm
3-hydroxyisobutyrate dehydrogenase, mitochondrial3-hydroxyisobutyrate dehydrogenase, mitochondrial
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 ...
https://pharos.nih.gov/idg/targets/P31937
GRHPR - Glyoxylate reductase/hydroxypyruvate reductase - Homo sapiens (Human) - GRHPR gene & proteinGRHPR - Glyoxylate reductase/hydroxypyruvate reductase - Homo sapiens (Human) - GRHPR gene & protein
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.
http://www.uniprot.org/uniprot/Q9UBQ7
Regulation of Corepressor Function by Nuclear NADH | ScienceRegulation of Corepressor Function by Nuclear NADH | Science
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. ...
https://science.sciencemag.org/content/295/5561/1895?ijkey=c54648027407e6bcea614bfcbaf75ce93eaf3835&keytype2=tf_ipsecsha
Results for the protein: P16152Results for the protein: P16152
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 ...
http://bioinf.umbc.edu/dmdm/gene_prot_page.php?search_type=protein&id=118519
Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in...Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in...
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. ...
http://www.biochemj.org/content/302/1/11
Alkohol dehidrogenase - Wikipedia bahasa Indonesia, ensiklopedia bebasAlkohol dehidrogenase - Wikipedia bahasa Indonesia, ensiklopedia bebas
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: ...
https://id.wikipedia.org/wiki/Oksidoreduktase_alkohol:NAD%2B
Homoisocitrate dehydrogenase - WikipediaHomoisocitrate dehydrogenase - Wikipedia
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. ...
https://en.wikipedia.org/wiki/Homoisocitrate_dehydrogenase
Woodwards reagent K inactivation of Escherichia coli L-threonine dehydrogenase: increased absorbance at 340-350 nm is due to...
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 ...
https://www.meta.org/papers/woodwards-reagent-k-inactivation-of-escherichia/8745417
Recombinant Escherichia coli Glyoxylate/hydroxypyruvate reductase A(ghrA) - CusabioRecombinant Escherichia coli Glyoxylate/hydroxypyruvate reductase A(ghrA) - Cusabio
Purchase Recombinant Escherichia coli Glyoxylate/hydroxypyruvate reductase A(ghrA). It is produced in Yeast. High purity. Good price.
https://www.cusabio.com/Recombinant-Protein/Recombinant-Escherichia-coli-Glyoxylatehydroxypyruvate-reductase-AghrA-547959.html
Pseudomonas aeruginosa ExaE protein Summary Report | CureHunterPseudomonas aeruginosa ExaE protein Summary Report | CureHunter
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
http://www.curehunter.com/public/keywordSummaryC433522-Pseudomonas-aeruginosa-ExaE-protein.do
Cinnamyl alcohol: Uses, Interactions, Mechanism of Action | DrugBank OnlineCinnamyl alcohol: Uses, Interactions, Mechanism of Action | DrugBank Online
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....
https://go.drugbank.com/drugs/DB14186
Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from...Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from...
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 ...
https://portalrecerca.uab.cat/en/publications/class-iv-mammalian-alcohol-dehydrogenase-structural-data-of-the-r
EC 1.1.99.36EC 1.1.99.36
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, ...
http://www.sbcs.qmul.ac.uk/iubmb/enzyme/EC1/1/99/36.html
EC 1.1.1.194EC 1.1.1.194
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]. ...
http://www.sbcs.qmul.ac.uk/iubmb/enzyme/EC1/1/1/194.html
RCSB PDB - 1MGO: Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant Literature Report PageRCSB PDB - 1MGO: Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant Literature Report Page
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
http://www.rcsb.org/pdb/explore/litView.do?structureId=1MGO
Identification of RDH10, an All-trans Retinol Dehydrogenase, in Retinal Müller Cells | IOVS | ARVO JournalsIdentification of RDH10, an All-trans Retinol Dehydrogenase, in Retinal Müller Cells | IOVS | ARVO Journals
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) ...
http://iovs.arvojournals.org/article.aspx?articleid=2123876
Cancer research yields unexpected new way to produce nylonCancer research yields unexpected new way to produce nylon
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 ...
http://www.innovations-report.com/html/reports/life-sciences/cancer-research-yields-unexpected-produce-nylon-202765.html
1g72.1 | SWISS-MODEL Template Library
SWISS-MODEL Template Library (SMTL) entry for 1g72.1. CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION
https://swissmodel.expasy.org/templates/1g72
Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.<...
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 - ...
https://indiana.pure.elsevier.com/en/publications/regulation-of-the-expression-of-the-rat-alcohol-dehydrogenase-gen
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome...negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome...
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome Database
https://rgd.mcw.edu/rgdweb/ontology/annot.html?acc_id=GO:0062003
GTOP nfar0:BAD57618.1
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 ...
http://spock.genes.nig.ac.jp/~genome/cgi-bin/mas.pl.cgi?org=nfar0&gene=BAD57618.1
GTOP nfar0:BAD55466.1
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 ...
http://spock.genes.nig.ac.jp/~genome/cgi-bin/mas.pl.cgi?org=nfar0&gene=BAD55466.1
KEGG ENZYME: 4.2.1.115
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 ...
http://www.genome.jp/dbget-bin/www_bget?enzyme+4.2.1.115
Hydroxypyruvate as a gluconeogenic substrate in rat hepatocytes | Biochemical JournalHydroxypyruvate as a gluconeogenic substrate in rat hepatocytes | Biochemical Journal
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.. ...
http://www.biochemj.org/content/146/1/277
Anti-Human Dehydrogenase/reductase (SDR Family) Member 9 Antikörper für Immunohistochemistry (Frozen Sections) (IHC (fro))Anti-Human Dehydrogenase/reductase (SDR Family) Member 9 Antikörper für Immunohistochemistry (Frozen Sections) (IHC (fro))
Top performende anti-Human Dehydrogenase/reductase (SDR Family) Member 9 Antikörper für Immunohistochemistry (Frozen Sections) (IHC (fro)) vergleichen & kaufen.
http://www.antikoerper-online.de/c21-steroid-hormone-metabolic-process-pathway-50/dhrs9-antibody-13757/human-ihc-fro-151238/
Switch to Europe/Worldwide website
ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
https://www.acris-antibodies.com/target/alcohol-dehydrogenase-4-antibody-adh4-antibody.htm?ab_ag_reactivity=Rt&ab_applications=E
Sch475 00050 : CDS information --- DoBISCUIT
putative quinate/shikimate dehydrogenase [putative shikimate 5-dehydrogenase] ATGGTCAAGGACTCGTATCTCGTCGGGCTGATCGGCGCCGGGATCGGCCCGTCGCTCAGC CCGGCACTGCACGAGCGGGAGGCCGACCGGCAGGGCCTGCGCTATCTGTACCGGCTGATC GACATCGACGCGCTCGGTGTCGGGCCGCAGGCGGTGGGGGACCTCGTACGAGCCGCCCGC GACCTGGGCTTCGACGGGCTGAACATCACGCATCCCTGCAAGCAGCTCGTCATCGGGCAT CTGGACGCGCTCGCCCCGCAGGCCGAGGCGCTCGGCGCGGTGAACACCGTCGTCTTCGAG GGCGGGCGTGCGGTCGGGCACAACACCGATGTCACCGGGTTCGCCGCCTCGTTCGCCCGT GGGCTGCCGGATGCCCCGCTGGAGCGGGTCGTGCAGTTGGGCGCGGGGGGAGCGGGGGCG GCCGTCGCGCATGCCATGCTCACGCTCGGGGCCGGGCACGTCACCGTCGTCGATGCCATG CCGGACCGGTCGGCGGACCTCGCCGCCTCGCTGAACCGGCACTTCGGTGCGGGGCGGGCC GCTGCCGCGGGCCCGGAGCGGCTGGCGGCGCTGCTCGGCGGTGCGGACGGCATCGTGCAT GCCACGCCGACGGGGATGGCCGCTCATCCGGGGCTGCCGCTTCCCGGTGAGTTGCTGCAT CCCGGGTTGTGGGTGGCCGAGGTGGTGTACCGGCCGTTGGAGACCGAGTTGCTGCGTGCC GCTCGGGCGGCGGGGTGTGCGGTTCTCGATGGTGGGGGGATGGCTGTTTTCCAGGCCGCG GACGCGTTTCGGCTGTTCACGGGGCGGGAGCCGGACGCGGTGCGGATGCTTGCGGATATT ...
http://www.bio.nite.go.jp/pks/feature/view/Sch475_00050
June 2021 Report on Global Alcohol Dehydrogenase Market Overview, Size, Share and Trends 2021-2026 - Herald Keeper
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 ...
https://heraldkeeper.com/market/june-2021-report-on-global-alcohol-dehydrogenase-market-overview-size-share-and-trends-2021-2026-999711.html
Analytical approaches to alcohol dehydrogenase structuresAnalytical approaches to alcohol dehydrogenase structures
Analytical approaches to alcohol dehydrogenase structures / M.T. Gheorghe; I. Lindh; W.J. Griffiths; J. Sjovall; T. Bergman; William Griffiths ...
https://cronfa.swan.ac.uk/Record/cronfa37636
WikiGenes - RDH5 - retinol dehydrogenase 5 (11-cis/9-cis)WikiGenes - RDH5 - retinol dehydrogenase 5 (11-cis/9-cis)
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
https://www.wikigenes.org/e/gene/e/5959.html
Publications of the Group | Max Planck Institute of Molecular Plant Physiology
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 ...
https://www.mpimp-golm.mpg.de/2491196/publications-of-the-group-alseekh?page=1&year=2016
SA RS12060 - AureoWikiSA RS12060 - AureoWiki
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 201.9) ...
http://aureowiki.med.uni-greifswald.de/SA_RS12060
SA RS01030 - AureoWikiSA RS01030 - AureoWiki
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 180.6) ...
http://aureowiki.med.uni-greifswald.de/SA_RS01030
anti-HAO1 antibody, Internal | GeneTexanti-HAO1 antibody, Internal | GeneTex
HAO1 antibody, Internal (hydroxyacid oxidase (glycolate oxidase) 1) for WB. Anti-HAO1 pAb (GTX81144) is tested in Human, Mouse samples. 100% Ab-Assurance.
http://www.genetex.com/HAO1-antibody-Internal-GTX81144.html
Alcohol oxidoreductaseAlcohol oxidoreductase
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) Portal: Biology v t e v t e (EC ... 1.1, All stub articles, Oxidoreductase stubs, EC 1.1 stubs). ...
https://en.wikipedia.org/wiki/Alcohol_oxidoreductase
Alcohol dehydrogenase (nicotinoprotein)Alcohol dehydrogenase (nicotinoprotein)
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) Portal: Biology ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(nicotinoprotein)
Methanol dehydrogenase (nicotinoprotein)Methanol dehydrogenase (nicotinoprotein)
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 ...
https://en.wikipedia.org/wiki/Methanol_dehydrogenase_(nicotinoprotein)
HSD17B4HSD17B4
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
https://en.wikipedia.org/wiki/HSD17B4
CitrininCitrinin
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. ...
https://en.wikipedia.org/wiki/Citrinin
Long-chain-alcohol oxidaseLong-chain-alcohol oxidase
Other names in common use include long-chain fatty alcohol oxidase, fatty alcohol oxidase, fatty alcohol:oxygen oxidoreductase ... NAD+ oxidoreductase and requires NAD+. Yeast have low levels of fatty alcohol dehydrogenase.) The long-chain alcohol is then ... This alcohol is oxidized by long-chain fatty alcohol oxidase in yeast. (This is different from the pathway found in mammalian ... Lee T (April 1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry ...
https://en.wikipedia.org/wiki/Long-chain-alcohol_oxidase
Long-chain-alcohol dehydrogenaseLong-chain-alcohol dehydrogenase
NAD+ oxidoreductase. Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This ... Lee T (April 1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction a long-chain ...
https://en.wikipedia.org/wiki/Long-chain-alcohol_dehydrogenase
Acetaldehyde dehydrogenaseAcetaldehyde dehydrogenase
Alcohol flush reaction Disulfiram-like drug Oxidoreductase PDB: 1NVM​; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). " ... Swift R, Davidson D (1998). "Alcohol Hangover: Mechanisms and Mediators" (PDF). Alcohol Health and Research World. 22 (1): 54- ... 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 ...
https://en.wikipedia.org/wiki/Acetaldehyde_dehydrogenase
Alcohol oxidaseAlcohol oxidase
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called methanol oxidase and ... aryl-alcohol oxidase (AAO) and secondary-alcohol oxidase (SAO). Alcohol oxidases catalyzes the oxidation of primary alcohols to ... In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ⇌ {\ ... Sometimes, this enzyme is called short-chain alcohol oxidase (SCAO) to differentiate it from long-chain-alcohol oxidase (LCAO ...
https://en.wikipedia.org/wiki/Alcohol_oxidase
Alcohol dehydrogenase (acceptor)Alcohol dehydrogenase (acceptor)
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 ...
https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor)
8-Hydroxygeraniol dehydrogenase8-Hydroxygeraniol dehydrogenase
... 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, ...
https://en.wikipedia.org/wiki/8-Hydroxygeraniol_dehydrogenase
Hydroxysteroid dehydrogenaseHydroxysteroid dehydrogenase
... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...
https://en.wikipedia.org/wiki/Hydroxysteroid_dehydrogenase
Coniferyl-alcohol dehydrogenaseConiferyl-alcohol dehydrogenase
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+ ...
https://en.wikipedia.org/wiki/Coniferyl-alcohol_dehydrogenase
Polyvinyl-alcohol dehydrogenase (acceptor)Polyvinyl-alcohol dehydrogenase (acceptor)
... acceptor oxidoreductase. Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. ... oxidized polyvinyl alcohol + reduced acceptor Thus, the two substrates of this enzyme are polyvinyl alcohol and acceptor, ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) (EC 1.1.99.23) is an enzyme that catalyzes the chemical reaction ...
https://en.wikipedia.org/wiki/Polyvinyl-alcohol_dehydrogenase_(acceptor)
Aryl-alcohol dehydrogenase (NADP+)Aryl-alcohol dehydrogenase (NADP+)
The systematic name of this enzyme class is aryl-alcohol:NADP+ oxidoreductase. Other names in common use include aryl alcohol ... 2. Purification and properties of aryl-alcohol: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. (in German). 8 ( ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, an aryl-alcohol dehydrogenase (NADP+) (EC 1.1.1.91) is an enzyme that catalyzes the chemical reaction an ...
https://en.wikipedia.org/wiki/Aryl-alcohol_dehydrogenase_(NADP )
Carbonyl reductase (NADPH)Carbonyl reductase (NADPH)
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+ ...
https://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH)
Allyl-alcohol dehydrogenaseAllyl-alcohol dehydrogenase
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 ...
https://en.wikipedia.org/wiki/Allyl-alcohol_dehydrogenase
Polyvinyl-alcohol oxidasePolyvinyl-alcohol oxidase
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, ...
https://en.wikipedia.org/wiki/Polyvinyl-alcohol_oxidase
Perillyl-alcohol dehydrogenasePerillyl-alcohol dehydrogenase
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. ...
https://en.wikipedia.org/wiki/Perillyl-alcohol_dehydrogenase
Secondary-alcohol oxidaseSecondary-alcohol oxidase
... 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 ...
https://en.wikipedia.org/wiki/Secondary-alcohol_oxidase
Cinnamyl-alcohol dehydrogenaseCinnamyl-alcohol dehydrogenase
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 ...
https://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase
Alcohol dehydrogenase (NAD(P)+)Alcohol dehydrogenase (NAD(P)+)
The systematic name of this enzyme class is alcohol:NAD(P)+ oxidoreductase. Other names in common use include retinal reductase ... In enzymology, an alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71) is an enzyme that catalyzes the chemical reaction an alcohol + ... Alcohol dehydrogenase Fidge NH, Goodman DS (1968). "The enzymatic reduction of retinal to retinol in rat intestine". J. Biol. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NAD(P) )
Vanillyl-alcohol oxidaseVanillyl-alcohol oxidase
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 ...
https://en.wikipedia.org/wiki/Vanillyl-alcohol_oxidase
Aryl-alcohol dehydrogenaseAryl-alcohol dehydrogenase
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+ ...
https://en.wikipedia.org/wiki/Aryl-alcohol_dehydrogenase
Aryl-alcohol oxidaseAryl-alcohol oxidase
... 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 ...
https://en.wikipedia.org/wiki/Aryl-alcohol_oxidase
3-hydroxybenzyl-alcohol dehydrogenase3-hydroxybenzyl-alcohol dehydrogenase
NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction 3- ... Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108- ...
https://en.wikipedia.org/wiki/3-hydroxybenzyl-alcohol_dehydrogenase
Chlordecone reductaseChlordecone reductase
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+. ...
https://en.wikipedia.org/wiki/Chlordecone_reductase
VAT1VAT1
It belongs to the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. In melanocytic cells VAT1 ...
https://en.wikipedia.org/wiki/VAT1
AtromentinAtromentin
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 ...
https://en.wikipedia.org/wiki/Atromentin
Cyclic alcohol dehydrogenase (quinone)Cyclic alcohol dehydrogenase (quinone)
... cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. This enzyme ... Cyclic+alcohol+dehydrogenase+(quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... "Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM ... catalyses the following chemical reaction cyclic alcohol + quinone ⇌ {\displaystyle \rightleftharpoons } cyclic ketone + quinol ...
https://en.wikipedia.org/wiki/Cyclic_alcohol_dehydrogenase_(quinone)
Aflatoxin B1Aflatoxin B1
Now an esterase, EstA, catalyzes the hydrolysis of the acetyl, forming the primary alcohol in versiconal. The acetal in ... an oxidoreductase. Then a final recyclization occurs to form aflatoxin B1. Aflatoxin B1 is a potent genotoxic hepatocarcinogen ... Averantin is converted to averufin via a two different enzymes, a hydroxylase and an alcohol dehydrogenase. This will oxygenate ...
https://en.wikipedia.org/wiki/Aflatoxin_B1
Isocitrate dehydrogenaseIsocitrate dehydrogenase
Along with the sp3 to sp2 stereochemical change around the alpha-C, there is a ketone group that is formed from the alcohol ... Oxidoreductase Myelodysplastic syndrome#IDH1 and IDH2 mutations Oncometabolism PDB: 1CW7​; Cherbavaz DB, Lee ME, Stroud RM, ... This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed ... the alcohol group of the alpha-carbon is deprotonated and the resulting lone pair of electrons forms a ketone group on that ...
https://en.wikipedia.org/wiki/Isocitrate_dehydrogenase
Zinc in biologyZinc in biology
... and alcoholic fermentation. Carboxypeptidase cleaves peptide linkages during digestion of proteins. A coordinate covalent bond ... oxidoreductases, and isomerases (42,43). Bitanihirwe BK, Cunningham MG (November 2009). "Zinc: the brain's dark horse". Synapse ... "Molecular dynamics study of zinc binding to cysteines in a peptide mimic of the alcohol dehydrogenase structural zinc site". ...
https://en.wikipedia.org/wiki/Zinc_in_biology
L-xylulose reductaseL-xylulose reductase
Xylulose Xylitol (Note conversion of ketone to alcohol) This enzyme belongs to the superfamily of short-chain oxidoreductases, ... The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). A deficiency is responsible ...
https://en.wikipedia.org/wiki/L-xylulose_reductase
Octanol dehydrogenaseOctanol dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... Roche B, Azoulay E (1969). "Régulation des alcool-déshydrogénases chez Saccharomyces cerevisiae" [Regulation of the alcohol ... The systematic name of this enzyme class is octanol:NAD+ oxidoreductase. This enzyme is also called 1-octanol dehydrogenase. ...
https://en.wikipedia.org/wiki/Octanol_dehydrogenase
ToxicationToxication
Oxidoreductases are enzymes that catalyze the reactions that involve the transfer of electrons. Methanol in itself is toxic due ... to its central nervous system depression properties, but it can be converted to formaldehyde by alcohol dehydrogenase and then ...
https://en.wikipedia.org/wiki/Toxication
Dihydrokaempferol 4-reductaseDihydrokaempferol 4-reductase
... or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl alcohol or coniferyl alcohol or coumaryl alcohol ... 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 cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include ...
https://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase
BenzeneBenzene
Dewar James (1869). "On the oxidation of phenyl alcohol, and a mechanical arrangement adapted to illustrate structure in the ... These include cytochrome P450 2E1 (CYP2E1), quinine oxidoreductase (NQ01 or DT-diaphorase or NAD(P)H dehydrogenase (quinone 1 ... Individuals carrying variant of NAD(P)H:quinone oxidoreductase 1 (NQO1), microsomal epoxide hydrolase (EPHX) and deletion of ...
https://en.wikipedia.org/wiki/Benzene
Cinnamoyl-CoA reductaseCinnamoyl-CoA reductase
... while lignin found in dicots is typically composed of almost entirely coniferyl alcohol and sinapyl alcohol subunits. As can be ... Cinnamoyl-CoA reductase (EC 1.2.1.44), systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but ... and cinnamyl alcohol dehydrogenase (CAD) in tobacco plants" (PDF). The Plant Journal. 28 (3): 257-70. doi:10.1046/j.1365-313x. ... except in the case of sinapyl alcohol - while several CCR homologs have been shown to act on sinapoyl-CoA in vitro, it is ...
https://en.wikipedia.org/wiki/Cinnamoyl-CoA_reductase
Methanol dehydrogenaseMethanol dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... independent alcohol dehydrogenase found originally in Pseudomonas M27. This enzyme (EC. 1.1.99.8) contains a prosthetic group ... The systematic name of this enzyme class is methanol:NAD+ oxidoreductase. This enzyme participates in methane metabolism. Prior ...
https://en.wikipedia.org/wiki/Methanol_dehydrogenase
S)-limonene 7-monooxygenaseS)-limonene 7-monooxygenase
... perillyl alcohol, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired ... The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common ... perillyl alcohol + NADP+ + H2O The 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H+, and O2, whereas its 3 products ... oxygen oxidoreductase (7-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene ...
https://en.wikipedia.org/wiki/(S)-limonene_7-monooxygenase
Xanthoxin dehydrogenaseXanthoxin dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... Ponce MR, Micol JL, Serrano R, Rodriguez PL (2002). "The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of ... The systematic name of this enzyme class is xanthoxin:NAD+ oxidoreductase. Other names in common use include xanthoxin oxidase ...
https://en.wikipedia.org/wiki/Xanthoxin_dehydrogenase
Alcohol dehydrogenase (quinone)Alcohol dehydrogenase (quinone)
... 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) Portal: Biology (CS1: ... 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 ...
https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(quinone)
IronIron
It can also be dissolved in alcohol to form tincture of iron, which is used as a medicine to stop bleeding in canaries. Iron(II ... Boon EM, Downs A, Marcey D. "Proposed Mechanism of Catalase". Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial ...
https://en.wikipedia.org/wiki/Iron
Butyric acidButyric acid
Legastelois R, Jeanblanc J, Vilpoux C, Bourguet E, Naassila M (2017). "[Epigenetic mechanisms and alcohol use disorders: a ... Pyruvate is oxidized into acetyl coenzyme A catalyzed by pyruvate:ferredoxin oxidoreductase. Two molecules of carbon dioxide ( ...
https://en.wikipedia.org/wiki/Butyric_acid
Pyrococcus furiosusPyrococcus furiosus
An oxidoreductase species in P. furiosus that does not contain tungsten is pyruvate ferredoxin oxidoreductase, or POR, which ... Ma, Kesen, Adams, Michael W. W. (15 February 1999). "An Unusual Oxygen-Sensitive, Iron- and Zinc-Containing Alcohol ... The next oxidoreductase to be discovered was glyceraldehyde-3-phosphate ferredoxin oxidoreductase, or GAPOR, which utilizes ... Another oxidoreductase is formaldehyde ferredoxin oxidoreductase, or FOR, which catalyzes the oxidation of aldehydes into ...
https://en.wikipedia.org/wiki/Pyrococcus_furiosus
DehydrogenaseDehydrogenase
The systematic name of an oxidoreductase is "donor:acceptor oxidoreductase", but when possible it is more conveniently named as ... This happens frequently when an alcohol is the substrate; when the proton on the oxygen leaves, the free electrons on the ... Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of ... A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron ...
https://en.wikipedia.org/wiki/Dehydrogenase
List of medical mnemonicsList of medical mnemonics
... alcohol, sedatives, barbiturates Acute metabolic changes - pH, hypo/hyper Na, Ca, acute liver or renal failure Trauma - brain ... Oxidoreductases 2 - Transferases 3 - Hydrolases 4 - Lyases 5 - Isomerases 6 - Ligases 7 - Translocases LMNOP: Lasix (furosemide ... Alcohol Trauma (cardiac contusion) Recent surgery (post CABG) Ischemia Atrial enlargement Lone or idiopathic Fever, anemia, ... alcohol, other drugs, sexual risks) Allergies Medications Preexisting medical conditions Trauma Hhistory of hospitalizations ...
https://en.wikipedia.org/wiki/List_of_medical_mnemonics
OxidoreductaseOxidoreductase
EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases) EC 1.2 includes oxidoreductases ... CH-CH oxidoreductases) EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, ... Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified ... Superfamilies of single-pass transmembrane oxidoreductases in Membranome database Media related to Oxidoreductases at Wikimedia ...
https://en.wikipedia.org/wiki/Oxidoreductase
Mycena galopusMycena galopus
Engler M, Anke T, Sterner O (1997). "Pterulinic acid and pterulone, two novel inhibitors of NADH:ubiquinone oxidoreductase ( ... an enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis) presumably ... ubiquinone oxidoreductase (complex I) produced by a Pterula species. I. Production, isolation and biological activities". ...
https://en.wikipedia.org/wiki/Mycena_galopus
BorrelidinBorrelidin
The BorI gene product, a cytochrome 450 hydroxylase catalyzes the oxidation of the C12 methyl group into an allylic alcohol, ... which can undergo further oxidation by the gene products of BorI or BorK, an oxidoreductase, to form the formyl intermediate. ...
https://en.wikipedia.org/wiki/Borrelidin
Lactate dehydrogenaseLactate dehydrogenase
Biology portal Dehydrogenase Lactate Oxidoreductase This article incorporates text from the public domain Pfam and InterPro: ... Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase ...
https://en.wikipedia.org/wiki/Lactate_dehydrogenase
List of enzymesList of enzymes
EC 1.1.1.1 Alcohol dehydrogenase (NADP) EC 1.1.1.2 Homoserine dehydrogenase EC 1.1.1.3 Aminopropanol oxidoreductase EC 1.1.1.4 ...
https://en.wikipedia.org/wiki/List_of_enzymes
Fructose 5-dehydrogenaseFructose 5-dehydrogenase
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... "Enzymatic studies on the oxidation of sugar and sugar alcohol. I Purification and properties of particle-bound fructose ... The systematic name of this enzyme class is D-fructose:acceptor 5-oxidoreductase. Other names in common use include fructose 5- ... dehydrogenase (acceptor), D-fructose dehydrogenase, and D-fructose:(acceptor) 5-oxidoreductase. Ameyama M; Adachi O (1982). "[ ...
https://en.wikipedia.org/wiki/Fructose_5-dehydrogenase
Potent inhibitors of a shikimate pathway enzyme from Mycobacterium tuberculosis: combining mechanism- and modeling-based designPotent inhibitors of a shikimate pathway enzyme from Mycobacterium tuberculosis: combining mechanism- and modeling-based design
Alcohol Oxidoreductases / antagonists & inhibitors* * Alcohol Oxidoreductases / chemistry* * Alcohol Oxidoreductases / ...
https://pubmed.ncbi.nlm.nih.gov/21454647/
Sol Genomics Network
Molecular Function: oxidoreductase activity (GO:0016491). 210. 2. 118636. Alcohol dehydrogenase GroES-like. Alcohol ... Alcohol dehydrogenase. zinc-binding. GroES-like. 41. 5. 129101. Alcohol dehydrogenase GroES-like. Alcohol dehydrogenase ... Molecular Function: oxidoreductase activity (GO:0016491). Alcohol dehydrogenase. zinc-binding. GroES-like. 41. ... Alcohol dehydrogenase superfamily. zinc-containing. - Molecular Function: zinc ion binding (GO:0008270). - ...
https://www.sgn.cornell.edu/search/unigene.pl?unigene_id=SGN-U272530
Sjogren-Larsson Syndrome - United Leukodystrophy FoundationSjogren-Larsson Syndrome - United Leukodystrophy Foundation
Fatty Alcohol: NAD+ Oxidoreductase Deficiency. *FAO deficiency. *Fatty aldehyde dehydrogenase deficiency. *FALDH deficiency ...
https://ulf.org/leukodystrophies/sjogren-larsson-syndrome/
Genetics of Sjogren-Larsson Syndrome Medication: Retinoids, Leukotriene inhibitorsGenetics of Sjogren-Larsson Syndrome Medication: Retinoids, Leukotriene inhibitors
Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ... Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide ... Abnormal fatty alcohol metabolism in cultured keratinocytes from patients with Sjogren-Larsson syndrome. J Lipid Res. 2008 Feb ... oxidoreductase activity. J Clin Invest. 1988 Mar. 81(3):738-44. [QxMD MEDLINE Link]. [Full Text]. ...
https://emedicine.medscape.com/article/949023-medication
Publication Year: 2019 / Subject: aluminum / Subject term: biosynthesis / Text Availability: Citation in PubAg - PubAg Search...Publication Year: 2019 / Subject: aluminum / Subject term: biosynthesis / Text Availability: Citation in PubAg - PubAg Search...
ENZYME - 1.1.1.192 long-chain-alcohol dehydrogenaseENZYME - 1.1.1.192 long-chain-alcohol dehydrogenase
fatty alcohol oxidoreductase.. Reaction catalysed. a long-chain primary fatty alcohol + H2O + 2 NAD(+) <=> a long-chain fatty ...
https://enzyme.expasy.org/EC/1.1.1.192
The International System Classification of Enzymes and Enzyme Naming System - Articles FactoryThe International System Classification of Enzymes and Enzyme Naming System - Articles Factory
The second 1 means that the enzyme belongs to the first subclass of oxidoreductases and catalyzes the oxidation of alcohol. ... Oxidoreductases. All enzymes that can catalyze the oxidation-reduction reaction of a substrate are called oxidoreductases. In ... The third 1 indicates that the enzyme belongs to the first subclass of the first subclass of oxidoreductases; the hydrogen ... The first 1 means that the enzyme belongs to the first category, that is, oxidoreductases. ...
https://www.articlesfactory.com/articles/health/the-international-system-classification-of-enzymes-and-enzyme-naming-system.html
Transcriptome analysis of the sex pheromone gland of the noctuid moth Heliothis virescens | BMC Genomics | Full TextTranscriptome analysis of the sex pheromone gland of the noctuid moth Heliothis virescens | BMC Genomics | Full Text
The systematic name of this group of enzymes is alcohol:NADP+ oxidoreductase, oxidizing alcohols using NAPD+ (alcohol + NADP ... The fatty acyl CoA pheromone precursor may be reduced to the corresponding alcohol by an alcohol-generating Fatty Acyl ... The reverse reaction is catalyzed through alcohol oxidases, and both enzymes are more generally described as alcohol ... The alcohol-generating FAR from B. mori was shown by functional expression to produce the pheromone bombykol from its precursor ...
https://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-11-29
ExplorEnz: EC 1.14.13.229ExplorEnz: EC 1.14.13.229
tert-butyl alcohol,NADPH:oxygen oxidoreductase. Comments:. The enzyme, characterized from the bacterium Aquincola ... Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol ... tert-butyl alcohol + NADPH + H+ + O2 = 2-methylpropane-1,2-diol + NADP+ + H2O. ... L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase ...
https://www.enzyme-database.org/query.php?ec=1.14.13.229
RCSB PDB - 4QUK: Crystal Structure of Cinnamyl-Alcohol Dehydrogenase 2 Mutant K169ARCSB PDB - 4QUK: Crystal Structure of Cinnamyl-Alcohol Dehydrogenase 2 Mutant K169A
Crystal Structure of Cinnamyl-Alcohol Dehydrogenase 2 Mutant K169A ... Classification: OXIDOREDUCTASE. *Organism(s): Medicago truncatula. *Expression System: Escherichia coli BL21(DE3) ... The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in ... The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in ...
https://www.rcsb.org/structure/4QUK
HOMD :: SEQF2043HOMD :: SEQF2043
Uncharacterized oxidoreductases%2C Fe-dependent alcohol dehydrogenase family. 161. SEQF2043,FP929034.1. CBK69886.1 jb [NA] [AA ...
https://www.homd.org/genome/explorer?gid=SEQF2043&anno=ncbi
Mahmoud Ahmed - Publications - UTMB Health Research Expert ProfilesMahmoud Ahmed - Publications - UTMB Health Research Expert Profiles
Ahmed, M. S., Aleksunes, L. M., Boeuf, P., Chung, M. K., Daoud, G., Desoye, G., Díaz, P., Golos, T. G., Illsley, N. P., Kikuchi, K., Komatsu, R., Lao, T., Morales-Prieto, D. M., Nanovskaya, T., Nobuzane, T., Roberts, C. T., Saffery, R., Tamura, I., Tamura, K., Than, N. G., & 8 othersTomi, M., Umbers, A., Wang, B., Weedon-Fekjaer, M. S., Yamada, S., Yamazaki, K., Yoshie, M. & Lash, G. E., 2013, In: Placenta. 34, SUPPL, p. S6-S10. Research output: Contribution to journal › Article › peer-review ...
https://researchexperts.utmb.edu/en/persons/mahmoud-ahmed/publications/
SCOPe 2.07: Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domainSCOPe 2.07: Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domain
Quinone oxidoreductase [51747] (3 species). *. Species Escherichia coli [TaxId:562] [51748] (1 PDB entry). ... Timeline for Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domain: *Family c.2.1.1: Alcohol dehydrogenase-like, C- ... Family c.2.1.1: Alcohol dehydrogenase-like, C-terminal domain appears in SCOPe 2.06. *Family c.2.1.1: Alcohol dehydrogenase- ... Putative zinc-binding alcohol dehydrogenase [102131] (1 species). *. Species Mouse (Mus musculus) [TaxId:10090] [102132] (1 PDB ...
http://scop.berkeley.edu/sunid=51736&ver=2.07
DeCSDeCS
NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases [D08.811.682.047.820] NAD (+) and NADP (+) Dependent Alcohol ... Alcohol Oxidoreductases - Preferred Concept UI. M0000651. Scope note. A subclass of enzymes which includes all dehydrogenases ... Alcohol Oxidoreductases Entry term(s). Carbonyl Reductase Carbonyl Reductases Ketone Reductase Ketone Reductases ... Alcohol oxidoreductases Entry term(s):. Carbonyl Reductase. Carbonyl Reductases. Ketone Reductase. Ketone Reductases. ...
https://decs.bvsalud.org/en/ths/resource/?id=434&filter=ths_exact_term&q=ALCOHOL+OXIDOREDUCTASES
Asymmetric reduction of a variety of ketones with a recombinant carbonyl reductase: Identification of the gene encoding a...
Alcohol Oxidoreductases Engineering & Materials Science 100% * Gene encoding Engineering & Materials Science 72% ...
https://okayama.pure.elsevier.com/en/publications/asymmetric-reduction-of-a-variety-of-ketones-with-a-recombinant-c
IMSEAR at SEARO: Regulation of tricarboxylic acid cycle dehydrogenases in Mycobacterium phlei.
Alcohol Oxidoreductases --metabolism. en_US. dc.subject.mesh. Citric Acid Cycle. en_US. ...
https://imsear.searo.who.int/handle/123456789/27481?mode=full
protein deficiencyprotein deficiency
Alcohol Oxidoreductases. 1. + 74. Metalloproteins. 1. + 75. Thyroxine. 1. + 76. Adenine Phosphoribosyltransferase. 1. + ...
https://lookfordiagnosis.com/results.php?symptoms=protein+deficiency&lang=1&parent=%2F&mode=F&therapy_ap=1
Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism ...Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism ...
... oxidoreductases (aryl alcohol oxidases and vanillyl-alcohol oxidases; AA3 and AA4, respectively) and other AAs (AA5, AA7 and ... 51]. Briefly, veratryl alcohol (VA) was used as a substrate and the reaction was performed in pH 5.6 PBS. The LiP activity was ... Members of the GMC oxidoreductase superfamily were believed to provide hydrogen peroxide for lignin peroxidase (LiP) and MnP to ...
https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-019-1406-y
CoP: Co-expressed Biological Processes
F:aldehyde-lyase activity, oxidoreductase activity, acting on CH-OH group of donors, FAD binding;P:cellular alcohol metabolic ... glucose-methanol-choline (GMC) oxidoreductase family protein. ...
http://webs2.kazusa.or.jp/kagiana/cgi-bin/ginfo.cgi?query=At1g24260&organism=ath
MICROBIOCAPTEURS CONDUCTIMETRIQUES UTILISANT DES OXYDOREDUCTASES De la conception à lapplication à lenvironnement et l...MICROBIOCAPTEURS CONDUCTIMETRIQUES UTILISANT DES OXYDOREDUCTASES De la conception à l'application à l'environnement et l...
... we developed biosensors based on three oxidoreductases (alcohol oxidase, lactate oxidase and formaldehyde dehydrogenase) for ... Conductometric biosensors using oxidoreductases. From design to implementation to the environmental and food analysis. ...
https://theses.hal.science/tel-00866085
Xanthine Oxidase | Profiles RNS
Oxidoreductases [D08.811.682]. *Alcohol Oxidoreductases [D08.811.682.047]. *Xanthine Oxidase [D08.811.682.047.928] ...
https://profiles.rush.edu/display/17499
Estradiol Dehydrogenases | Profiles RNS
Oxidoreductases [D08.811.682]. *Alcohol Oxidoreductases [D08.811.682.047]. *Hydroxysteroid Dehydrogenases [D08.811.682.047.436] ...
https://profiles.ouhsc.edu/display/7480
Xanthine Oxidase | Profiles RNS
Oxidoreductases [D08.811.682]. *Alcohol Oxidoreductases [D08.811.682.047]. *Xanthine Oxidase [D08.811.682.047.928] ...
https://researchers.childrensmercy.org/display/17067
DeCS Ingl s
D08.811.682 Oxidoreductases .. D08.811.682.047 Alcohol Oxidoreductases .. D08.811.682.047.239 Glucose Oxidase .. E01 Diagnosis ...
http://trigramas.bireme.br/cgi-bin/mx/[email protected]?collection=DeCSi&lang=p&minsim=0.30&maxrel=10&text=Micronefrin
Code System Concept
NAD - Fatty alcohol-nicotinamide adenine nucleotide oxidoreductase Active Synonym false false 1235376011 Fatty alcohol- ... nicotinamide adenine nucleotide oxidoreductase Active Synonym false false 147056016 Long-chain-alcohol dehydrogenase Active ... Long-chain-alcohol dehydrogenase (substance). Code System Preferred Concept Name. Long-chain-alcohol dehydrogenase (substance) ...
https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=88689003
UMLS. CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM - Terms starting with 'U' - MEDINDEX.AM
alcohol oxidoreductase; 75. glutathione analog [synthetic or natural compounds which resemble glutathione in structure and/or ... alcohol oxidoreductase; 70. glutamyltransferase [ ] (UMLS (CSP) C0678107) =Amino Acid, Peptide, or Protein; Enzyme ; = ... amine oxidoreductase; 5. Glucocorticoid deficiency [ ] (UMLS (ICD9CM) C1955741) GLUCOCORTICOID DEFICIENT; =Disease or Syndrome ... NAD(P)H oxidoreductase; 34. glucose tolerance [physiological ability of the body to properly metabolize glucose. ( CSP )] (UMLS ...
http://www.medindex.am/glossary/index.php/list/UMLS.+CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM/,G,L,U.xhtml
研究者詳細 - 今泉 和彦
Purpose : Alcohol dehydrogenase (ADH；alcohol:NAD+ oxidoreductase) is the principal enzyme responsible for ethanol oxidation. ... and a relationship between alcohol drinking volume (=alcohol consumption) and the degree of alcohol intoxication. This article ... alcohol: NAD+ oxidoreductase, EC1.1.1.1) activities and plasma zinc levels in rats. The weaned male Sprague Dawley rats were ... 目的］飲酒（＝エタノール摂取）によって生体内に取り込まれたアルコールは、胃および小腸か
https://w-rdb.waseda.jp/html/100002283_ja.html
Browse
alcohol dehydrogenase-like oxidoreductase protein 62.15 334 aa 393 1e-108 Ralstonia solanacearum GMI1000 Bacteria normal 1 ...
https://exploration.weizmann.ac.il/perl/pandatox1_0.mperl?submit=show_homologs&locus_tag=Plav_0046&replicon_accession=NC_009719
Medical Terminology & Phrases - Medword TranscriptionMedical Terminology & Phrases - Medword Transcription
Fatty alcohol:NAD+ oxidoreductase deficiency; Fatty aldehyde dehydrogenase deficiency; Fatty liver of pregnancy, acute; Fauces ... Fetal alcohol effects (FAE); Fetal alcohol syndrome (FAS); Fetal alcohol syndrome (FAS) diagnosis; Fetal circulation; Fetal ... fetal alcohol syndrome); FAS (fetal alcohol syndrome) diagnosis; Fascia; Fasciculation; Fasciitis; Fasciitis, eosinophilic ( ... Fear of drinking alcohol; Fear of dust; Fear of feces; Fear of flowers; Fear of flying; Fear of fur; Fear of ghosts; Fear of ...
http://www.medword.mobi/medterms_fTEXT.html
ReductaseFatty AlcoholENZYMEAldehydeQuinoneÁlcoolFetal alcoholReactionBacterialSubstrateOxidationSaccharomycesSusceptibilityConsumptionDrugsAcidReactionsReductionPrimaryResponseTreatmentQuinone oxidoreductaseDehydrogenasesEnzymesOxidaseCinnamyl-alcohol dehydNADHAlcoholsSynthaseAldehyde oxidoreductasesProteinReductasePyruvate ferredoxinMetabolismPurificationYeastKetonesPolyolGigasEthanolOxidasesCoenzymeMoietyLiver alcohol dehydActivityAbuse and AlcoholismAlcoholismAcceptorActingFattyBenzylDeficiencyEPHX1HepaticCarbon dioxide
Reductase3
  • The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in the conversion of cinnamic acid derivatives into monolignol building blocks for lignin polymers in plant cell walls. (rcsb.org)
  • Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. (ox.ac.uk)
  • Ladenstein, R., Winberg, J.-O., Benach, J., Medium- and shortchain dehydrogenase/reductase gene and protein families: Structure-function relationships in short-chain alcohol dehydrogenases (2008) Cell. (cnr.it)
Fatty Alcohol3
  • Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. (medscape.com)
  • Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (medscape.com)
  • fatty alcohol oxidoreductase. (expasy.org)
ENZYME3
  • Depending on the substrate, the enzyme also catalyses EC 1.14.19.48 , tert -amyl alcohol desaturase. (enzyme-database.org)
  • 2-ketoisovalerate ferredoxin oxidoreductase (VOR) is a key enzyme in hyperthermophiles catalyzing the coenzyme A-dependent oxidative decarboxylation of aliphatic amino acid-derived 2-keto acids. (scirp.org)
  • The enzyme purified under anaerobic conditions from a hyperthermophilic archaeon, Thermococcus profundus, is a hetero-octamer (αβγδ) 2 consisting of four different subunits, α = 45 kDa, β = 31 kDa, γ = 22 kDa and δ = 13 kDa, respectively, and it has three [4Fe-4S] clusters per αβγδ-protomer, similar to other ferredoxin oxidoreductases. (scirp.org)
Aldehyde2
  • reducing aldehyde of vanillin to vanillyl alcohol. (southcentraltechsales.com)
  • While choline is an essential nutrient for the host, contributing to cell membrane function, methyl transfer events, and neurotransmission, gut anaerobes use choline as a source of carbon and energy, cleaving its C−N bond to generate acetaldehyde, which is further processed by alcohol dehydrogenase CutO and aldehyde oxidoreductase CutF to give ethanol and acetyl coenzyme A, and trimethylamine (TMA), a uniquely microbial metabolite. (tissueandcells.com)
Quinone6
  • NAD(P)H: quinone oxidoreductase 1 (NQO1) C609T polymorphism and the risk of eight cancers for Japanese. (cdc.gov)
  • Correlative polymorphism of NAD(P)H: quinone oxidoreductase (NQO1) with telomere shortening in colorectal cancer. (cdc.gov)
  • Role of epoxide hydrolase, NAD(P)H:quinone oxidoreductase, cytochrome P450 2E1 or alcohol dehydrogenase genotypes in susceptibility to colorectal cancer. (cdc.gov)
  • NAD(P)H:quinone oxidoreductase 1 (NQO1) Pro187Ser polymorphism and the risk of lung, bladder, and colorectal cancers: a meta-analysis. (cdc.gov)
  • The influence of fruit and vegetable consumption and genetic variation on NAD(P)H:quinone oxidoreductase (NQO1) phenotype in an endoscopy-based population. (cdc.gov)
  • NAD(P)H:quinone oxidoreductase 1 (NQO1) Pro187Ser polymorphism and colorectal cancer predisposition in the ethnic Kashmiri population. (cdc.gov)
Álcool1
  • Quando substratos polissacarídicos foram adicionados à cultura, diversas atividades enzimáticas relacionadas à degradação de lignina, em menor ou maior grau, foram detectadas: lacase, peroxidase, manganês-peroxidase, celobiose-quinona oxidoreductase e álcool veratrílico-oxidase. (unicamp.br)
Fetal alcohol1
  • For example, people with fetal alcohol syndrome, other developmental disabilities, and other brain disorders are vulnerable to the development of TDs, even after receiving only 1 dose of the causative agent. (medscape.com)
Reaction2
  • All enzymes that can catalyze the oxidation-reduction reaction of a substrate are called oxidoreductases. (articlesfactory.com)
  • The 2-ketoisovalerate ferredoxin oxidoreductase (VOR) catalyzes a reaction to produce acetyl CoA in the presence of coenzyme A from these 2-keto acids through oxidative decarboxylation. (scirp.org)
Bacterial2
  • The bacterial gene, encoding alpha-acetolactate decarboxylase (alpha-ALDC), was expressed in a bottom-fermenting brewer's yeast under the control of a modified Saccharomyces cerevisiae alcohol dehydrogenase (ADHI) promoter which lacks the upstream regions from -800 bp to -1500 bp. (aalto.fi)
  • Alcohol and bacterial pneumonia. (rutgers.edu)
Substrate1
  • alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis (1992) J. Org. (cnr.it)
Oxidation1
  • Screening of microorganisms producing cold-active oxidoreductases to be applied in enantioselective alcohol oxidation. (angenechem.com)
Saccharomyces1
  • On the other hand,Saccharomyces cerevisiae mutants have been selected as vanillyl alcohol hyperproducers: vanillyl alcohol productivity of the best selected mutant is twice as high as wild-type strain productivity. (southcentraltechsales.com)
Susceptibility1
  • Acute hepatic renal toxicity from low doses of acetaminophen in the absence of alcohol abuse or malnutrition: evidence for increased susceptibility to drug toxicity due to cardiopulmonary and renal insufficiency. (rutgers.edu)
Consumption1
  • Alcohol consumption and chronic obstructive pulmonary disease. (rutgers.edu)
Drugs2
  • Alcohol, drugs of abuse, and immune functions. (rutgers.edu)
  • This buildup, in combination with nongenetic factors such as certain drugs, alcohol, and dieting, leads to the signs and symptoms of hereditary coproporphyria and harderoporphyria. (medlineplus.gov)
Acid2
  • Standard curves for vanillic acid (compound 1a), vanillin (compound 3a), vanillyl alcohol (compound 4a), and guaiacol (compound 2) were established over the range of 0.3 to 8 mg. (southcentraltechsales.com)
  • v) of 5.0 ml for vanillyl alcohol, 8.1 ml for vanillic acid, 13.2 ml for vanillin, 16.1 ml for o-anisic acid, and 18.7 ml for guaiacol. (southcentraltechsales.com)
Reactions1
  • 3. Vanillyl-alcohol oxidase and laccase-catalyzed reactions have been reported for the selective production of vanillin … Soc. (southcentraltechsales.com)
Reduction2
  • No. HCl OH HO H 3CO Vanillin, 1 Vanillyl alcohol, 2 4 (3) Either LiAlH4 and NaBH4 could be used for this reduction, but sodium borohydride is the reagent of choice … Note 2: In contrast, lithium aluminum hydride reacts explosively with water to yield hydrogen gas and basic salts of Li(I) and Al(III). (southcentraltechsales.com)
  • https://doi.org/10.1007/BF02936481, Over 10 million scientific documents at your fingertips, Not logged in The mechanism for the reduction of vanillin by NaBH4 The flavoprotein vanillyl alcohol oxidase (VAO) acts on a wide range of phenolic compounds and converts both creosol and vanillylamine to vanillin with high yield. (southcentraltechsales.com)
Primary1
  • In this work, we developed biosensors based on three oxidoreductases (alcohol oxidase, lactate oxidase and formaldehyde dehydrogenase) for primary alcohols, lactate and formaldehyde analysis. (hal.science)
Response2
  • Encodes an aromatic alcohol:NADP+ oxidoreductase whose mRNA levels are increased in response to treatment with a variety of phytopathogenic bacteria. (edu.au)
  • Alcohol and the response of upper airway resistance to a changing respiratory drive in normal man. (rutgers.edu)
Treatment1
  • Alcohol and HIV interactions in the natural history and treatment of HIV/AIDS. (rutgers.edu)
Quinone oxidoreductase3
  • Therefore, we determined whether polymorphisms in the genes coding for microsomal epoxide hydrolase (EPHX1), NAD(P)H:quinone oxidoreductase (NQO1), cytochrome P450 2E1 (CYP2E1) and alcohol dehydrogenase (ADH3) predispose to the development of CRC. (nih.gov)
  • Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins. (dbcls.jp)
  • quinone oxidoreductase I (NQO1), microsomal epoxide hydrolase (mEH), catechol-O-methyltransferase (COMT), uridine diphosphate-glucuronosyltransferase (UGT)] were selected for the present analysis based on their putative role in xenobiotic metabolism. (escholarship.org)
Dehydrogenases2
  • Analysis of the sequence suggests that the sequenced protein was a mixture of at least 3 of the different isoforms of alcohol dehydrogenases found in yeast. (uniprot.org)
  • Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. (umbc.edu)
Enzymes6
  • Multiplication of enzyme efficiencies with the relative quantities of individual enzymes in cytosol resulted in a rough estimate of their contributions to total alcohol metabolite formation. (nih.gov)
  • Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (uams.edu)
  • In summary, this work provides the first examples of enzymes showing "alcohol aminase" activity. (hims-biocat.eu)
  • Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a member of the xanthine oxidase (XO) family of mononuclear Mo-enzymes that catalyzes the oxidation of aldehydes to carboxylic acids. (rcsb.org)
  • These cells express the highest levels of the major ethanol-oxidizing enzymes, alcohol dehydrogenase (ADH), which is located in the cytosol, and cytochrome P450 2E1 (CYP2E1), which resides in the smooth endoplasmic reticulum (ER) (figure 1). (nih.gov)
  • NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. (umbc.edu)
Oxidase7
  • 2. Sakai, K., Hamada, N. and Watanabe, Y. Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by hydrophobic and dye-ligand chromatographies. (qmul.ac.uk)
  • Disclosed is an enzyme electrode having an oxidoreductase (for instance, glucose oxidase, cholesterol oxidase, fructosylamine oxidase and glucose dehydrogenase) and an electron-transfer protein (for instance, cytochrome C, cytochrome b562 and cytochrome c551), as well as a sensor utilizing the enzyme electrode as working electrode. (freepatentsonline.com)
  • 4. The enzyme electrode of claim 1, wherein the oxidoreductase is selected from the group consisting of glucose oxidase, cholesterol oxidase, lactate oxidase, alcohol oxidase, galactose oxidase, bilirubin oxidase, fructosylamine oxidase, glucose dehydrogenase, alcohol dehydrogenase and glucose-3-dehydrogenase. (freepatentsonline.com)
  • Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M (2019) Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols Adv. Synth. (indoxproject.eu)
  • Aryl alcohol oxidase (AAO) is a fungal flavoenzyme capable of oxidizing aromatic primary alcohols into their correspondent aldehydes through a stereoselective hydride abstraction. (indoxproject.eu)
  • Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT (2019) Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols Catal. (indoxproject.eu)
  • Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ (2018) Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase Adv. Synth. (indoxproject.eu)
Cinnamyl-alcohol dehyd1
NADH5
  • Enzima que oxida un aldehído en presencia de NAD+ y agua formando un ácido y NADH. (bvsalud.org)
  • In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. (lookformedical.com)
  • An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. (lookformedical.com)
  • Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. (umbc.edu)
  • In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. (umbc.edu)
Alcohols5
  • In Sjögren-Larsson syndrome , FALDH deficiency impairs fatty alcohol oxidation and leads to accumulation of 16- and 18-carbon-long aliphatic alcohols. (medscape.com)
  • 4. Suzuki, T. Oxidation of secondary alcohols by polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. (qmul.ac.uk)
  • Herein, we harnessed the promiscuous alcohol dehydrogenase (ADH) activity of LysEDH to create new variants that exhibited enhanced catalytic activity for the reduction of substituted benzaldehydes and arylaliphatic aldehydes to primary alcohols. (hims-biocat.eu)
  • Aldose reductase (NADP+ 1-oxidoreductase, EC 1.1.1.21) is a sugar alcohol synthase enzyme that transforms glucose or galactose into sugar alcohols (polyols). (edu.pl)
  • The efficient lignin oxidation system of this fungus requires cyclic redox reactions involving the reduction of aryl-aldehydes to the corresponding alcohols by aryl-alcohol dehydrogenase. (biomedcentral.com)
Synthase1
  • 7. The organism of claim 1, further comprising at least one enzyme or polypeptide selected from the group consisting of a corrinoid protein, a methyltetrahydrofolate:corrinoid protein methyltransferase, a corrinoid iron-sulfur protein, a nickel-protein assembly protein, a ferredoxin, an acetyl-CoA synthase, a carbon monoxide dehydrogenase, a pyruvate ferredoxin oxidoreductase, and a hydrogenase. (patentsencyclopedia.com)
Aldehyde oxidoreductases1
  • Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. (enzyme-database.org)
Protein5
  • We report here the cloning of an aryl-alcohol dehydrogenase cDNA from the white-rot fungus Phanerochaete chrysosporium , its expression in Escherichia coli and the biochemical characterization of the encoded GST and His 6 tagged protein. (biomedcentral.com)
  • 1. An enzyme electrode having an oxidoreductase and an electron-transfer protein. (freepatentsonline.com)
  • 9. The enzyme electrode of claim 1, wherein the oxidoreductase is glucose dehydrogenase and the electron-transfer protein is cytochrome b562. (freepatentsonline.com)
  • 14. The enzyme electrode of claim 1, wherein the oxidoreductase is glucose dehydrogenase having pyrroloquinoline quinone as coenzyme (PQQGDH) and the electron-transfer protein is cytochrome b562. (freepatentsonline.com)
  • RESULTS: Three bacterial proteins were consistently detected among all the culture[1]positive and PCR-positive cases tested, namely SDR family NAD(P)-dependent oxidoreductase protein (32kDa), 3-hydroxyacyl-CoA dehydrogenase Burkholderia sp. (iium.edu.my)
Reductase1
  • Increased intracellular polar alcohol levels promote lens fiber extension, vacuole formation, and opacification, while Aldose reductase inhibition prevents sugar cataract development. (edu.pl)
Pyruvate ferredoxin1
  • Both nitazoxanide and its active metabolite (tizoxanide) interfere with the pyruvate:ferredoxin 2-oxidoreductase. (arogga.com)
Metabolism5
  • 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)
  • This includes investigating roles of various factors such as acetaldehyde, cytochrome P450 2E1 (CYP2E1), vascular endothelial growth factor (VEGF), impaired immune function, and alcohol-induced impaired metabolism of s-adenosylmethionine (SAMe), folate, betaine, iron, and vitamin A. (nih.gov)
  • As the reduction of vanillin to vanillyl alcohol is an undesired trait in Pseudomonas strains engineered to accumulate vanillin, connecting the strain 9.1 phenotype with a genotype would increase the fundamental understanding and genetic engineering potential of microbial vanillin metabolism. (omicsdi.org)
  • After a brief overview of alcohol metabolism in the liver, this article will summarize the mechanisms through which excessive alcohol consumption contributes to the development of various types of alcohol-induced liver damage. (nih.gov)
Purification1
  • 3. Suzuki, T. Purification and some properties of polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. (qmul.ac.uk)
Yeast2
  • Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solution. (nih.gov)
  • [9] A few decades later, when studying the fermentation of sugar to alcohol by yeast , Louis Pasteur concluded that this fermentation was caused by a vital force contained within the yeast cells called "ferments", which were thought to function only within living organisms. (wikipedia.org)
Ketones1
Polyol1
  • The distribution of polyol: NADP oxidoreductase in mammalian tissues. (wikidata.org)
Gigas1
  • The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically competent form an equatorial oxo ligand instead of the sulfido ligand. (rcsb.org)
Ethanol2
  • 5-HT receptor antagonists do not reduce ethanol preference in sardinian alcohol-preferring (sP) rats. (rutgers.edu)
  • Beverage alcohol (i.e., ethanol) is chiefly metabolized in the main parenchymal cells of the liver (i.e., hepatocytes) that make up about 70 percent of the liver mass (Jones 1996). (nih.gov)
Oxidases1
  • In addition to the copper radical oxidases, the FAD-dependent extracellular aryl-alcohol oxidases (Aaop) catalyze the oxidation of aryl-alcohol derivatives into their corresponding aldehydes with the concomitant reduction of O 2 to H 2 O 2 [ 6 , 10 ]. (biomedcentral.com)
Coenzyme2
  • Proton nuclear magnetic resonance and fluorescence studies of the interaction between inhibitors and horse liver alcohol dehydrogenase-reduced pyridine coenzyme binary complex. (nih.gov)
  • 2. The enzyme electrode of claim 1, wherein the oxidoreductase is an oxidoreductase having pyrroloquinoline quinone as coenzyme. (freepatentsonline.com)
Moiety1
  • The two adducts present a direct interaction between the molybdenum and one of the carbon atoms of the alcohol moiety, which constitutes the first structural evidence for such a bond in a biological system. (rcsb.org)
Liver alcohol dehyd4
  • Activity of NMN+, nicotinamide ribose and analogs in alcohol oxidation promoted by horse-liver alcohol dehydrogenase. (nih.gov)
  • The conformation of adenosine diphosphoribose and 8-bromoadenosine diphosphoribose when bound to liver alcohol dehydrogenase. (nih.gov)
  • Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. (nih.gov)
  • Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. (umbc.edu)
Activity7
  • The "Hot Paper" reports on the generation of oxidoreductases that possess both alcohol dehydrogenase and amine dehydrogenase activity. (hims-biocat.eu)
  • Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity Chem. (hims-biocat.eu)
  • The diagnostic significance of serum alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase activity in prostate cancer patients. (edu.pl)
  • Serum alcohol dehydrogenase and aldehyde dehydrogenase activity in the course of hepatitis C. (edu.pl)
  • The activity of class I, II, III, and IV alcohol dehyrogenase isoenzymes and aldehyde dehydrogenase in endometrial cancer. (edu.pl)
  • Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with liver cancer. (edu.pl)
  • ATP-dependent catalytic activity' This would follow previous terms such as: GO:0016723 'oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor', as well as many specific terms e.g. (geneontology.org)
Abuse and Alcoholism1
  • The National Institute on Alcohol Abuse and Alcoholism (NIAAA), National Cancer Institute (NCI), and Office of Dietary Supplements (ODS) invite research grant applications that will employ an integrative approach using state-of-the-art technologies to gain insight into the molecular and biochemical mechanisms by which chronic alcohol consumption leads to the development of cancers of various organs such as oral cavity, pharynx, larynx, esophagus, stomach, large intestine, liver, and breast. (nih.gov)
Alcoholism1
  • Alcohol and Alcoholism, Suppl No. 2, 1994. (rutgers.edu)
Acceptor1
  • EC 1.1.99.8 alcohol dehydrogenase (acceptor). (kegg.jp)
Acting3
  • Oxidoreductases Acting on CH-NH Group Donors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
  • This graph shows the total number of publications written about "Oxidoreductases Acting on CH-NH Group Donors" by people in this website by year, and whether "Oxidoreductases Acting on CH-NH Group Donors" was a major or minor topic of these publications. (ouhsc.edu)
  • Below are the most recent publications written about "Oxidoreductases Acting on CH-NH Group Donors" by people in Profiles. (ouhsc.edu)
Fatty4
  • [ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.com)
  • [ 14 ] In cultured skin keratinocytes, elevated fatty alcohol is diverted into the synthesis of wax esters and alkyldiacylglycerol lipids. (medscape.com)
  • [ 15 ] Accumulation of fatty alcohol and related lipid products disrupts formation of the intercellular membranes in the stratum corneum, which is critical for epidermal water barrier. (medscape.com)
  • Fatty alcohol and aldehyde may likewise alter the normal integrity of myelin membranes in the brain, leading to white-matter disease and spasticity. (medscape.com)
Benzyl2
  • As a proof‐of‐principle, we performed an unprecedented one‐pot "hydrogen‐borrowing" cascade to convert benzyl alcohol to benzylamine using a single enzyme. (hims-biocat.eu)
  • Benzyl alcohol dehydrogenase. (umbc.edu)
Deficiency1
  • 1. Have a known or suspected diagnosis of any of the other forms of classic CAH including 11-beta-hydroxylase deficiency, 17-alpha-hydroxylase deficiency, 3-beta-hydroxysteroid dehydrogenase deficiency, P450 side-chain cleavage deficiency, or P450 oxidoreductase deficiency. (nih.gov)
EPHX11
  • 6. Role of NQO1C609T and EPHX1 gene polymorphisms in the association of smoking and alcohol with sporadic distal colorectal adenomas: results from the UKFSS Study. (nih.gov)
Hepatic1
  • Chronic and excessive alcohol consumption produces a wide spectrum of hepatic lesions, the most characteristic of which are steatosis, hepatitis, and fibrosis/cirrhosis. (nih.gov)
Carbon dioxide1
  • They are produced from the amyloses and sucroses, as by the action of heat and acids of ferments, and are themselves decomposed by fermentation into alcohol and carbon dioxide. (leparisien.fr)
Sjogren-Larsson Syndrome - United Leukodystrophy Foundation
Sjogren-Larsson Syndrome - United Leukodystrophy Foundation (ulf.org)
Genetics of Sjogren-Larsson Syndrome Medication: Retinoids, Leukotriene inhibitors
Genetics of Sjogren-Larsson Syndrome Medication: Retinoids, Leukotriene inhibitors (emedicine.medscape.com)
The International System Classification of Enzymes and Enzyme Naming System - Articles Factory
The International System Classification of Enzymes and Enzyme Naming System - Articles Factory (articlesfactory.com)
Transcriptome analysis of the sex pheromone gland of the noctuid moth Heliothis virescens | BMC Genomics | Full Text
Transcriptome analysis of the sex pheromone gland of the noctuid moth Heliothis virescens | BMC Genomics | Full Text (bmcgenomics.biomedcentral.com)
HOMD :: SEQF2043
HOMD :: SEQF2043 (homd.org)
Mahmoud Ahmed - Publications - UTMB Health Research Expert Profiles
Mahmoud Ahmed - Publications - UTMB Health Research Expert Profiles (researchexperts.utmb.edu)
Sol Genomics Network
Sol Genomics Network (sgn.cornell.edu)
Publications | Centre de recherche CERVO
Publications | Centre de recherche CERVO (cervo.ulaval.ca)
Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism ...
Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism ... (biotechnologyforbiofuels.biomedcentral.com)
Mitochondrial Trifunctional Protein, alpha Subunit | Profiles RNS
Mitochondrial Trifunctional Protein, alpha Subunit | Profiles RNS (researchers.childrensmercy.org)
17-Hydroxysteroid Dehydrogenases | Profiles RNS
17-Hydroxysteroid Dehydrogenases | Profiles RNS (profiles.ouhsc.edu)
研究者詳細 - 今泉 和彦
研究者詳細 - 今泉 和彦 (w-rdb.waseda.jp)
CoP: Co-expressed Biological Processes
CoP: Co-expressed Biological Processes (webs2.kazusa.or.jp)
CAS 100-19-6 | Ethanone, 1-(4-nitrophenyl)- | CAS Number 100-19-6 | angenechem.com
CAS 100-19-6 | Ethanone, 1-(4-nitrophenyl)- | CAS Number 100-19-6 | angenechem.com (angenechem.com)
Use of a modified alcohol dehydrogenase, ADH1, promoter in construction of diacetyl non-producing brewer's yeast<...
Use of a modified alcohol dehydrogenase, ADH1, promoter in construction of diacetyl non-producing brewer's yeast<... (research.aalto.fi)
DEFEROXAMINE HYDROCHLORIDE
DEFEROXAMINE HYDROCHLORIDE (drugs.ncats.io)
Pyrroloquinoline quinone (PQQ) - an unproved supplement | Leaders in Pharmaceutical Business Intelligence (LPBI) Group
Pyrroloquinoline quinone (PQQ) - an unproved supplement | Leaders in Pharmaceutical Business Intelligence (LPBI) Group (pharmaceuticalintelligence.com)
Terminal RI - SophiA Biblioteca Web
Terminal RI - SophiA Biblioteca Web (repositorio.unicamp.br)
PDB 7UDD | Chain HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND 2,2,2- TRIFLUOROETHANOL AT 150 K | 7UDD_A | 3D...
PDB 7UDD | Chain HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND 2,2,2- TRIFLUOROETHANOL AT 150 K | 7UDD_A | 3D... (corona-1.cansar.icr.ac.uk)
(emedicine.medscape.com)
Ichthyosis Workup: Laboratory Studies, Imaging Studies, Other Tests
Ichthyosis Workup: Laboratory Studies, Imaging Studies, Other Tests (emedicine.medscape.com)