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
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
Protein Disulfide Reductase (Glutathione)
Pyruvate Synthase
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.
Copyright
It is a form of protection provided by law. In the United States this protection is granted to authors of original works of authorship, including literary, dramatic, musical, artistic, and certain other intellectual works. This protection is available to both published and unpublished works. (from Circular of the United States Copyright Office, 6/30/2008)
Organizations, Nonprofit
Encyclopedias as Topic
Computer Security
Protective measures against unauthorized access to or interference with computer operating systems, telecommunications, or data structures, especially the modification, deletion, destruction, or release of data in computers. It includes methods of forestalling interference by computer viruses or so-called computer hackers aiming to compromise stored data.
Privacy
Mycobacterium
Actinobacteria
Prephenate Dehydratase
Actinomycetales
Amino Acid Sequence
Acetoin
Butylene Glycols
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Acetoin Dehydrogenase
Receptors, Notch
A family of conserved cell surface receptors that contain EPIDERMAL GROWTH FACTOR repeats in their extracellular domain and ANKYRIN repeats in their cytoplasmic domains. The cytoplasmic domain of notch receptors is released upon ligand binding and translocates to the CELL NUCLEUS where it acts as transcription factor.
Drosophila
Drosophila Proteins
Drosophila melanogaster
Receptor, Notch2
Signal Transduction
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Amyloid Precursor Protein Secretases
Glutamate-5-Semialdehyde Dehydrogenase
Phosphotransferases (Carboxyl Group Acceptor)
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Pyrroline Carboxylate Reductases
A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
Pyruvaldehyde
Monoterpenes
Compounds with a core of 10 carbons generally formed via the mevalonate pathway from the combination of 3,3-dimethylallyl pyrophosphate and isopentenyl pyrophosphate. They are cyclized and oxidized in a variety of ways. Due to the low molecular weight many of them exist in the form of essential oils (OILS, VOLATILE).
Cyclohexenes
Acetone
Mixed Function Oxygenases
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
Lignin
The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)
Microscopy, Ultraviolet
Alcohol Dehydrogenase
Plant Stems
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 Lines
RDH11 Antibody | scrazzl.com - Simply Connecting Science
X-ray Structure of the Quinoprotein Ethanol Dehydrogenase from Pseudomonas Aeruginosa: Basis of Substrate Specificity
SDR9C7 Antibody | scrazzl.com - Simply Connecting Science
Homologies between enzymes involved in steroid and xenobiotic carbonyl reduction in vertebrates, invertebrates and procaryonts....
产品类别 一抗 | 博士德生物 BOSTER Biological Technology co.ltd
Ctbp1 - C-terminal-binding protein 1 - Mus musculus (Mouse) - Ctbp1 gene & protein
MEDLINE - Resultado p gina 1
Critical residues for structure and catalysis in short-chain dehydrogenases/reductases. - Immunology
Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in...
SDR42E1 Gene - GeneCards | D42E1 Protein | D42E1 Antibody
Expression of CtBP family protein isoforms in breast cancer and their role in chemoresistance - ePrints Soton
Biochemical properties of human dehydrogenase/reductase (SDR family) member 7. - Nuffield Department of Orthopaedics,...
retinol dehydrogenase 8 (all trans) Proteins: Novus Biologicals
Plus it
Alcohol Oxidase - AP20103AF-N | acris-antibodies.com
RCSB PDB - Protein Feature View
- Homoisocitrate dehydrogenase - Q72IW9 (HICDH THET2)
Dehydrogenase/reductase SDR family protein elisa and antibody
EMBL: CP000667.PE408
Practical Fragments: December 2013
Gentaur Molecular :GenWay \ Acyl-Coenzyme A dehydrogenase family. member 8 variant - \ 10-288-21999F
RDH16 Gene - GeneCards | RDH16 Protein | RDH16 Antibody
HEK-293T Cells Human ADHFE1 Lysate | ABIN1338769
RDH5抗体|Abcam中国|Anti-RDH5抗体
Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to...
Retinal reductase | definition of retinal reductase by Medical dictionary
1 3 propanediol dehydrogenase : définition de 1 3 propanediol dehydrogenase et synonymes de 1 3 propanediol dehydrogenase ...
cinnamyl alcohol dehydrogenase
Summary Report | CureHunter
Recombinant Human BDH2 protein, His-tagged BDH2-3452H - Creative BioMart
3-hydroxyisobutyrate dehydrogenase, mitochondrial
GRHPR - Glyoxylate reductase/hydroxypyruvate reductase - Homo sapiens (Human) - GRHPR gene & protein
Regulation of Corepressor Function by Nuclear NADH | Science
Results for the protein: P16152
Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in...
Alkohol dehidrogenase - Wikipedia bahasa Indonesia, ensiklopedia bebas
Homoisocitrate dehydrogenase - Wikipedia
Woodwards reagent K inactivation of Escherichia coli L-threonine dehydrogenase: increased absorbance at 340-350 nm is due to...
Recombinant Escherichia coli Glyoxylate/hydroxypyruvate reductase A(ghrA) - Cusabio
Pseudomonas aeruginosa ExaE protein
Summary Report | CureHunter
Cinnamyl alcohol: Uses, Interactions, Mechanism of Action | DrugBank Online
Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from...
EC 1.1.99.36
EC 1.1.1.194
RCSB PDB
- 1MGO: Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant Literature Report Page
Identification of RDH10, an All-trans Retinol Dehydrogenase, in Retinal Müller Cells | IOVS | ARVO Journals
Cancer research yields unexpected new way to produce nylon
1g72.1 | SWISS-MODEL Template Library
Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.<...
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome...
GTOP nfar0:BAD57618.1
GTOP nfar0:BAD55466.1
KEGG ENZYME: 4.2.1.115
Hydroxypyruvate as a gluconeogenic substrate in rat hepatocytes | Biochemical Journal
Anti-Human Dehydrogenase/reductase (SDR Family) Member 9 Antikörper für Immunohistochemistry (Frozen Sections) (IHC (fro))
Switch to Europe/Worldwide website
Sch475 00050 : CDS information --- DoBISCUIT
June 2021 Report on Global Alcohol Dehydrogenase Market Overview, Size, Share and Trends 2021-2026 - Herald Keeper
Analytical approaches to alcohol dehydrogenase structures
WikiGenes - RDH5 - retinol dehydrogenase 5 (11-cis/9-cis)
Publications of the Group | Max Planck Institute of Molecular Plant Physiology
SACOL RS13280 - AureoWiki
SA RS12060 - AureoWiki
anti-HAO1 antibody, Internal | GeneTex
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 ...
HSD17B4
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
Citrinin
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. ...
Acetaldehyde dehydrogenase
Alcohol flush reaction Disulfiram-like drug Oxidoreductase PDB: 1NVM; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). " ... Swift R, Davidson D. "Alcohol Hangover: Mechanisms and Mediators" (PDF). National Institute on Alcohol Abuse and Alcoholism. ... Acetaldehyde is more toxic than alcohol and is responsible for many hangover symptoms. About 50% of people of Northeast Asian ... In the first step, ethanol is converted to acetaldehyde by alcohol dehydrogenase. In the second step, the acetaldehyde is ...
8-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, ...
Hydroxysteroid dehydrogenase
... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...
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+ ...
Chlordecone 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+. ...
VAT1
It belongs to the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. In melanocytic cells VAT1 ...
Atromentin
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 ...
Alkohol dehidrogenase bahasa Indonesia, ensiklopedia bebas
... primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari ... NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase ...
Pirolohinolin hinon - Википедија, слободна енциклопедија
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem J. ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). „A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ...
Aril-alkohol dehidrogenase (NADP+) bahasa Indonesia, ensiklopedia bebas
Oksidoreduktase aril-alkohol:NADP+ (bahasa Inggris: aryl-alcohol:NADP+ oxidoreductase, aryl-alcohol dehydrogenase (NADP+), aryl ... coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP), EC 1.1.1.91) adalah ...
Methanol dehydrogenase (cytochrome c)
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". The ... cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction a primary alcohol + 2 ferricytochrome cL ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... displaystyle \rightleftharpoons } an aldehyde + 2 ferrocytochrome cL + 2 H+ A periplasmic quinoprotein alcohol dehydrogenase is ...
17β-Hydroxysteroid dehydrogenase
... are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β- ... Oxidoreductase from the Rat Adrenal Gland]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 336: 63-8. doi: ...
Alcohol oxidase
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase. It ... to differentiate is from long-chain-alcohol oxidase (LCAO), aryl-alcohol oxidase (AAO) and secondary-alcohol oxidase (SAO). As ... In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ⇌ {\ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as ...
Coniferyl-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+ ...
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) Biology portal. ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
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) Biology portal. ... Cozier GE, Giles IG, Anthony C (June 1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti ... Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K (2003). "Quinoprotein alcohol dehydrogenase is ...
Allyl-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 ...
Polyvinyl-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, ...
Perillyl-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. ...
Secondary-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 ...
Cinnamyl-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 ...
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 ...
Vanillyl-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 ...
Alcohol dehydrogenase (azurin)
... azurin oxidoreductase. This enzyme catalyses the following chemical reaction primary alcohol + azurin ⇌ {\displaystyle \ ... Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase ... "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory ... Alcohol+dehydrogenase+(azurin) at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
Aryl-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+ ...
Aryl-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 ...
Acidogenesis
H2 by pyruvate ferredoxin oxidoreductase and hydrogenase; and ethanol via NADH- and NADPH-linked alcohol dehydrogenase. By its ...
L-xylulose reductase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). ... This enzyme belongs to the superfamily of short-chain oxidoreductases, specifically those acting on the CH-OH group of donor ...
Homoisocitrate dehydrogenase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme ... The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
AKR1B1
oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ... allyl-alcohol dehydrogenase activity. • NADP-retinol dehydrogenase activity. Cellular component. • mast cell granule. • Schwann ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. The involvement in ... dependent enzyme catalyzing the reduction of various aldehydes and ketones to the corresponding alcohol. It also participates ...
Oxidoreductase
Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L- ... Alcohol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
Arachidonate 5-lipoxygenase
oxidoreductase activity. • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, ... it may also contribute to hypersensitivity responses of the respiratory system to cold air and possibly even alcohol beverages ... may then be released by the enzyme and rapidly reduced by cellular glutathione peroxidases to its corresponding alcohol, 5(S)- ...
AKR1A1 - Wicipedia
alditol:NADP+ 1-oxidoreductase activity. • electron carrier activity. • oxidoreductase activity. • alcohol dehydrogenase (NADP+ ... allyl-alcohol dehydrogenase activity. Cydrannau o'r gell. • cytosol. • extracellular exosome. • apical plasma membrane. • ...
Lactate dehydrogenase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase ...
Transferase
Within this group is alcohol sulfotransferase which has a broad targeting capacity. Due to this, alcohol sulfotransferase is ... hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. EC 2.1 includes enzymes that ... This transferase acts via the following reaction: 3'-phosphoadenylyl sulfate + an alcohol ⇌ {\displaystyle \rightleftharpoons ...
Citrate synthase
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Carnitine 3-dehydrogenase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase. ...
Iron
"Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial. Retrieved 11 February 2007.. ... It can also be dissolved in alcohol to form tincture of iron, which is used as a medicine to stop bleeding in canaries.[133] ...
3-oxoacyl-(acyl-carrier-protein) reductase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
Acetaldehyde dehydrogenase
Alcohol flush reaction. *Disulfiram-like drug. *Oxidoreductase. References[edit]. *^ a b PDB: 1NVM; Manjasetty BA, Powlowski J ... Role in metabolism of alcohol[edit]. In the liver, the enzyme alcohol dehydrogenase oxidizes ethanol into acetaldehyde, which ... National Institute on Alcohol Abuse and Alcoholism. Retrieved 26 Mar 2017.. *^ a b Xiao Q, Weiner H, Crabb DW (Nov 1996). "The ... Acetaldehyde is more toxic than alcohol and is responsible for many hangover symptoms.[5] ...
Uridine kinase
... with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
L-gulonolactone oxidase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ...
Aromatase
oxidoreductase activity. • aromatase activity. • oxidoreductase activity, acting on paired donors, with incorporation or ... Factors known to increase aromatase activity include age, obesity, insulin, gonadotropins, and alcohol. Aromatase activity is ... oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen. • electron carrier ...
ALDH2
Adams KE, Rans TS (Dec 2013). "Adverse reactions to alcohol and alcoholic beverages". Annals of Allergy, Asthma & Immunology. ... oxidoreductase activity. • aldehyde dehydrogenase [NAD(P)+ activity]. • aldehyde dehydrogenase (NAD) activity. • NAD binding. • ... alcohol metabolic process. • oxidation-reduction process. • ethanol oxidation. • carbohydrate metabolic process. • electron ... oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor. • glyceraldehyde-3-phosphate ...
Succinate dehydrogenase
... (succinate-ubiquinone oxidoreductase). The structure of SQR in a phospholipid membrane. SdhA, SdhB, ... succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction". The ...
Protease
Threonine proteases - using a threonine secondary alcohol. *Aspartic proteases - using an aspartate carboxylic acid ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Kynureninase
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
2,5-Furandicarboxylic acid
FDCA was also detected in blood plasma.[3] Recently, the enzyme furfural/HMF oxidoreductase was isolated from the bacterium ... Both of these latter materials can serve as alcohol components in the production of new polyester, and their combination with ...
நொதியம் - தமிழ் விக்கிப்பீடியா
"alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or ... 1. ஆக்சிசனேற்ற--ஒடுக்க நொதிகள் (Oxidoreductases):. ஒரு வினையில் ஆக்சிசனேற்றம் நடக்கிறதென்றால் ஒடுக்கமும் நடக்கிறதென்று பொருள். ... எ.கா: 1.1.1.1 என்பது ஆல்க்ககால் டிஐதரோச்செனேசு (Alcohol dehydrogenase) குடும்ப நொதிகளைக் குறிக்கும் நொதிஎண் ஆகும். ...
Respiratory complex I
NADH-ubiquinone oxidoreductase chain 1 EC 1.6.5.3. Pfam PF00146 9. ND2 / NU2M. NU2M_HUMAN. NADH-ubiquinone oxidoreductase chain ... NADH-ubiquinone oxidoreductase chain 4L EC 1.6.5.3. Pfam PF00420 13. ND5 / NU5M. NU5M_HUMAN. NADH-ubiquinone oxidoreductase ... NADH-ubiquinone oxidoreductase chain 3 EC 1.6.5.3. Pfam PF00507 11. ND4 / NU4M. NU4M_HUMAN. NADH-ubiquinone oxidoreductase ... Respiratory complex I, EC 1.6.5.3 (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial ...
Perilil-alkohol dehidrogenase bahasa Indonesia, ensiklopedia bebas
Oksidoreduktase perilil-alkohol:NAD+ (bahasa Inggris: perillyl-alcohol:NAD+ oxidoreductase, perillyl-alcohol dehydrogenase, ...
Cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ... The systematic name of this enzyme class is cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase. This enzyme is also called 3β- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... Wikvall K (April 1981). "Purification and properties of a 3 β-hydroxy-delta 5-C27-steroid oxidoreductase from rabbit liver ...
Galacturonokinase
... with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Cofactor (biochemistry)
Salisbury SA, Forrest HS, Cruse WB, Kennard O (August 1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". ... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus,[18] and even cadmium in ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. doi:10.1126/science.7878465. PMID 7878465.. ... They noticed that adding boiled and filtered yeast extract greatly accelerated alcoholic fermentation in unboiled yeast ...
17β-Hydroxysteroid dehydrogenase
... are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β- ... Oxidoreductase from the Rat Adrenal Gland]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 336: 63-8. doi: ...
Statin
Oxidoreductase (EC 1). *1.1 Aldose reductase. *HMG-CoA reductase. *1.3 5α-Reductase ...
Alcohol Oxidoreductases - MeSH - NCBI
All MeSH CategoriesChemicals and Drugs CategoryEnzymes and CoenzymesEnzymesOxidoreductasesAlcohol OxidoreductasesCarbohydrate ... Alcohol Oxidoreductases. A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as ... Dependent Alcohol Oxidoreductases11-beta-Hydroxysteroid Dehydrogenases +20-Hydroxysteroid Dehydrogenases +3-alpha- ... Acetoin DehydrogenaseAlcohol DehydrogenaseAldo-Keto Reductases +Carbonyl Reductase (NADPH)D-Xylulose ReductaseGlycerol-3- ...
Alcohol Oxidoreductases | Journal of Bacteriology
Alcohol oxidoreductase - Wikipedia
Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group.[1][2] ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) ... This oxidoreductase article is a stub. You can help Wikipedia by expanding it.. *v ... Functional group of an alcohol molecule. The carbon atom is attached to other carbon or hydrogen atoms. ...
Alcohol oxidoreductase - Wikipedia
Alcohol Oxidoreductases | Harvard Catalyst Profiles | Harvard Catalyst
"Alcohol Oxidoreductases" by people in Harvard Catalyst Profiles by year, and whether "Alcohol Oxidoreductases" was a major or ... "Alcohol Oxidoreductases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Alcohol Oxidoreductases" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Alcohol Oxidoreductases". ...
N'-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N
Summary Report | CureHunter
... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ... Oxidoreductases: 9264*Alcohol Oxidoreductases: 1*N-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N ... dimethyl-4-nitrosoaniline oxidoreductase alcohol - N. Subscribe to New Research on N-dimethyl-4-nitrosoaniline oxidoreductase ... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ...
Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol
Alcohol Oxidoreductases / genetics * Alcohol Oxidoreductases / metabolism * Amino Acid Substitution * Anaerobiosis * Butylene ... Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol Appl Environ ... dependent oxidoreductases. One of them has been purified and shown to be d-arabinose dehydrogenase (Ara1p), which converts (R/S ...
Transcriptional repression by suppressor of hairless involves the binding of a hairless-dCtBP complex in Drosophila
Protein - Other functions | Britannica.com
alcohol: NAD oxidoreductase. alcohol dehydrogenase. alcohol + NAD → acetaldehyde NADH. alcoholic fermentation. 1.1.1.27. L- ... Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. The table ... Enzymes that catalyze reactions in which hydrogen is transferred belong to the group known as oxidoreductases; those that ... The numbering system is as follows: the first number places the enzyme in one of six general groups-1, oxidoreductases; 2, ...
MEDLINE - Resultado p gina 1
MEDLINE - Resultado p gina 1
An unbiased cell morphology-based screen for new, biologically active small molecules.
Alcohol Oxidoreductases / chemistry. Apoptosis. Cell Line. Cell Line, Tumor. Cell Physiological Phenomena*. Cells / cytology*. ... Asher G,Lotem J,Cohen B,Sachs L,Shaul Y. Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase ... This pathway was not known to be dependent on the oxidoreductase CBR1, thus validating that the compounds discovered in such ... To initially validate that the oxidoreductase CBR1 was indeed inhibited by hydroxy-PP, we measured CBR1 catalytic activity in ...
Metal-catalyzed Oxidation of Fe2+ Dehydrogenases: consensus target sequence between Propanediol Oxidoreductase of Escherichia...
2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. These enzymes perform their ... the sequence of which is YNTPH277GVAN for propanediol oxidoreductase and YNLPH277GV for alcohol dehydrogenase 11. This ... consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas ... consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas ...
Energies | Free Full-Text | Microbial Conversion of Waste Glycerol from Biodiesel Production into Value-Added Products | HTML
... acetaldehyde/alcohol dehydrogenase; AOR, aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase ... acetaldehyde/alcohol dehydrogenase; AOR, aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase ... alcohol/acetaldehyde dehydrogenase, and d-lactate dehydrogenase [28]. Thirty-two grams per liter of d-lactate (99.9% chiral ... It is also suggested that an acetaldehyde/alcohol dehydrogenase might carry out an important role in glycerol fermentation for ...
Search Results Details (334) | Harvard Catalyst Profiles | Harvard Catalyst
gpr - L-glyceraldehyde 3-phosphate reductase - Escherichia coli (strain K12) - gpr gene & protein
Oxidoreductase - Wikipedia
Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L- ... Alcohol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
Alcohol dehydrogenase (nicotinoprotein) - Wikipedia
Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol ... Alcohol+dehydrogenase+(nicotinoprotein) at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol ...
Alcohol Dehydrogenase (acceptor), 978-613-9-96853-4, 6139968534 ,9786139968534
The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol ... quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ...
TNO Repository search for: subject:'bacterial metabolism'
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductase · Oxygenase · Unclassified drug · Bacterial metabolism · Controlled study · Enzyme activity · Nonhuman · ...
TNO Repository search for: subject:'Oxygenase'
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductases · Rats · Rats, Wistar · RNA, Messenger · Steroid Hydroxylases · Support, Non-U.S. Govt · Taurocholic Acid · ... cinnamyl alcohol · collagen type 16 · disulfiram · dodecyl sulfate sodium · eugenol · ferritin · ferrochelatase · glucose 6 ...
KEGG ENZYME: 1.1.1.90
Biomolecules | Free Full-Text | Enzyme-Catalyzed Synthesis of Unsaturated Aliphatic Polyesters Based on Green Monomers from ...
Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase ... The byproducts generated during polycondensation are water, methanol, ethanol and n-butyl alcohol, respectively. ... and n-butyl alcohol (bp = 117.7 °C). Besides, the chemical reactivity of the alkyl esters is another reason. It is well known ... We suspect that the increase of the residual alcohol amount and the decrease of the polymerization rate in dilute reaction ...
AKR1C2 aldo-keto reductase family 1 member C2 [Homo sapiens (human)] - Gene - NCBI
Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor IDA Inferred from Direct Assay. more info ... alditol:NADP+ 1-oxidoreductase activity IBA Inferred from Biological aspect of Ancestor. more info ...
KEGG ORTHOLOGY: K10617
cinnamyl alcohol dehydrogenase
Summary Report | CureHunter
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to ... cinnamyl alcohol dehydrogenase. Subscribe to New Research on cinnamyl alcohol dehydrogenase NADP-dependent enzyme that ... 12/01/2014 - "Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes ... 09/01/1999 - "Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol ...
MeSH ORA framework: R/Bioconductor packages to support MeSH over-representation analysis | BMC Bioinformatics | Full Text
More articles from Plant Biology | PNAS
CRYZ - Quinone oxidoreductase - Cavia porcellus (Guinea pig) - CRYZ gene & protein
Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such ... Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.Curated ... Quinone oxidoreductaseAdd BLAST. 328. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... A novel NADPH:quinone oxidoreductase.". Rao P.V., Krishna C.M., Zigler J.S. Jr.. J. Biol. Chem. 267:96-102(1992) [PubMed] [ ...
Frontiers | How Does Fusarium oxysporum Sense and Respond to Nicotinaldehyde, an Inhibitor of the NAD+ Salvage Biosynthesis...
Surprisingly, alcohol dehydrogenases were significantly up-regulated more than any other dehydrogenases, including aldehyde ... the high concentrations of the latter provoked the expression of alcohol dehydrogenases that in yeast can act to reduce NADH ... Cells responded to NA by up-regulation of oxidoreductases, with hardly any up-regulation of the classic response to oxidative ... Cells responded to NA by up-regulation of oxidoreductases, with hardly any up-regulation of the classic response to oxidative ...
Dehydrogenases8
- We have studied two enzymes of a newly described family of dehydrogenases with high sequence homology, 1,2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. (udl.cat)
- Surprisingly, alcohol dehydrogenases were significantly up-regulated more than any other dehydrogenases, including aldehyde dehydrogenases. (frontiersin.org)
- the high concentrations of the latter provoked the expression of alcohol dehydrogenases that in yeast can act to reduce NADH and increase NAD + amounts, respectively. (frontiersin.org)
- 2. Jörnvall, H. Differences between alcohol dehydrogenases. (qmul.ac.uk)
- As an alternative to (thermodynamically disfavoured) nicotinamide-dependent alcohol dehydrogenases, alcohol oxidases make use of molecular oxygen but their application is under-represented in synthetic biotransformations. (springer.com)
- Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD + /NADH cofactor that does not dissociate during the catalytic process. (qmul.ac.uk)
- Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. (hmdb.ca)
- NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. (creative-enzymes.com)
NADH1
- In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. (umassmed.edu)
Enzyme13
- Alcohol dehydrogenase E (AdhE) is an Fe-enzyme that, under anaerobic conditions, is involved in dissimilation of glucose. (udl.cat)
- Zymomonas mobilis is endowed with two isoenzymes of fermentative alcohol dehydrogenase, a zinc-containing enzyme (ADH I) and an iron-containing enzyme (ADH II). (udl.cat)
- Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. (wikipedia.org)
- In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + acceptor \rightleftharpoons an aldehyde + reduced acceptor Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor. (morebooks.de)
- This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. (morebooks.de)
- The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. (morebooks.de)
- [ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.com)
- [ 9 ] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty alcohol to aldehyde and fatty acid. (medscape.com)
- The dissociation constants for the enzyme-NAD+ complex and for the enzyme-alcohol complexes obtained from the kinetic quotients satisfactorily correspond to the dissociation constants obtained by use of other techniques. (thebiogrid.org)
- It is suggested that the non-linear curves may be attributed to a structural change in the enzyme itself, caused by the alcohol. (thebiogrid.org)
- This study demonstrates the function of the FaQR enzyme in the biosynthesis of HDMF as enone oxidoreductase and provides a foundation for the improvement of strawberry flavor and the biotechnological production of HDMF. (plantcell.org)
- This conventional biosensor is produced by forming an electrode system having a working electrode and a counter electrode on an electrically insulating base plate by a screen printing method or the like and subsequently forming an enzyme reaction layer including a hydrophilic polymer, an oxidoreductase and an electron acceptor above the electrode system. (google.com)
- Hoog JO, von Bahr-Lindstrom H, Heden LO, Holmquist B, Larsson K, Hempel J, Vallee BL, Jornvall H: Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. (hmdb.ca)
Acceptor2
- Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. (morebooks.de)
- The biosensor comprises an electrode system including a working electrode and a counter electrode formed on an electrically insulating base plate, and a reaction layer containing at least an oxidoreductase and an electron acceptor, wherein the electron acceptor is a sodium salt. (google.com)
Quinone2
- A novel NADPH:quinone oxidoreductase. (uniprot.org)
- Sequence analysis of two peptide fragments showed total identity with the protein sequence of a strongly ripening-induced, auxin-dependent putative quinone oxidoreductase, Fragaria × ananassa quinone oxidoreductase (FaQR). (plantcell.org)
NADP1
- The concentrations of (2R,3R)-2,3-butanediol are mostly dependent on Bdh1p activity, while those of (meso)-2,3-butanediol are also influenced by the activity of NADP(H)-dependent oxidoreductases. (nih.gov)
Acetaldehyde4
- Ethanolamine lyase produces acetaldehyde, which is converted by the oxidoreductase EutE to acetyl-coenzyme A, which enters the carbon pool of the cell. (asm.org)
- Alternatively, acetaldehyde can be converted to alcohol by another specialized oxidoreductase, EutG. (asm.org)
- It is proven that alcohol dehydrogenase oxidizes ethanol to acetaldehyde, which is responsible for some hangover symptoms. (steadyhealth.com)
- The identified enzymes involved in acetaldehyde production included alcohol dehydrogenase (ADH) and xanthine oxidoreductase (XO) in the cytosolic fraction and the flavoenzyme NADPH oxidase and catalase in the microsomal fraction [1]. (thefreedictionary.com)
Oxidation5
- Oxidation of aldehydes is considered to be generally a detoxification reaction because it is based on removing the electrophilic products of alcohol oxidation. (steadyhealth.com)
- In Sjögren-Larsson syndrome , FALDH deficiency impairs fatty alcohol oxidation and leads to accumulation of 16- and 18-carbon-long aliphatic alcohols. (medscape.com)
- Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. (medscape.com)
- In this review, the mechanism of copper-containing and flavoprotein alcohol oxidases is discussed in view of their ability to accept electronically activated or non-activated alcohols and their propensity towards over-oxidation of aldehydes yielding carboxylic acids. (springer.com)
- In flavoprotein oxidases, the oxidation proceeds via two half reactions, where the alcohol is first oxidised by a two-electron transfer during the reductive half reaction , yielding reduced flavin. (springer.com)
Allyl-alcohol dehyd2
- Creative Enzymes is one of the few companies in the world that provides spectrophotometric assays for allyl-alcohol dehydrogenase. (biocatalogue.org)
- With specialized knowledge in oxidoreductases, especially the ones such as allyl-alcohol dehydrogenase, Creative Enzymes successfully demonstrated the first-in-class test quality and service reliability. (biocatalogue.org)
MeSH1
- Alcohol Oxidoreductases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Aryl-alcohol2
- The fungus secretes aryl-alcohol oxidase and Mn2+-oxidizing peroxidase, two kinds of oxidoreductases characteristic of ligninolytic basidiomycetes. (csic.es)
- Aryl-alcohol oxidase (AAO, EC 1.1.3.7) generates H2O2 for lignin degradation at the expense of benzylic and other π system-containing primary alcohols, which are oxidized to the corresponding aldehydes. (upc.edu)
Alcohols3
- Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. (thebiogrid.org)
- The kinetic coefficients determined from secondary plots are consistent with an 'equilibrium random-order' mechanism for extremely low alcohol concentrations and for all alcohols, the transformation of the ternary complexes being the rate-limiting step of the reaction. (thebiogrid.org)
- In a related fashion, alcohol oxidases convert primary and secondary alcohols to aldehydes and ketones, respectively. (springer.com)
NADPH1
- The aryl hydrocarbon receptor (AHR) nuclear translocator (ARNT), as the AHR's heterodimerization partner, and NADPH-cytochrome P450 oxidoreductase (POR), as the key electron donor for all microsomal P450s, are independent and indispensable components in the adaptive and toxic responses to polycyclic aromatic hydrocarbons. (aspetjournals.org)
Aromatic1
- We report here the molecular cloning and characterization of the corresponding cDNA, CAD 1-5, which encodes this novel aromatic alcohol dehydrogenase. (deepdyve.com)
Metabolism4
- Two decades later, Sjögren-Larsson syndrome was shown to be an inborn error of lipid metabolism caused by deficient activity of fatty alcohol:NAD oxidoreductase. (medscape.com)
- Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which results in defective metabolism of both fatty aldehyde and fatty alcohol. (medscape.com)
- the role of decreased gastric alcohol dehydrogenase and first pass metabolism. (thefreedictionary.com)
- Rizzo W.B., Craft D.A., Dammann A.L., Phillips M.W., Fatty alcohol metabolism in cultured human fibroblasts. (springer.com)
Kinetics2
- 5. Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. (qmul.ac.uk)
- Electron-withdrawing substituents resulted in lower quantum mechanics stacking energies between aldehyde and the tyrosine side chain, contributing to product release, in agreement with the ping-pong mechanism observed in 3-chloro- and 3-fluorobenzyl alcohol kinetics analysis. (upc.edu)
ENCODES1
- This gene encodes class V alcohol dehydrogenase, which is a member of the alcohol dehydrogenase family. (genecards.org)
Aldehyde dehydrogenase2
- Experts are saying that Aldehyde dehydrogenase (ALDH) is functioning often in tandem with Alcohol dehydrogenase. (steadyhealth.com)
- Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (medscape.com)
Substrate4
- Kinetic studies of yeast alcohol dehydrogenase with NAD+ and ethanol, hexanol or decanol as substrates invariably result in non-linear Lineweaver-Burk plots if the alcohol is the variable substrate. (thebiogrid.org)
- Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. (freepatentsonline.com)
- Such biosensor can quantitate various substrates if an adequate oxidoreductase fit for the measuring substrate is adopted. (google.com)
- Ligand diffusion studies on Pleurotus eryngii AAO showed a T-shaped stacking interaction between the Tyr92 side chain and the alcohol substrate at the catalytically competent position for concerted hydride and proton transfers. (upc.edu)
Electron1
- Pyruvate-ferredoxin oxidoreductase and quinol-fumarate reductase contain ferredoxin domains that bind [Fe-S] clusters and are involved in electron transport. (ebscohost.com)
Gene4
- ADH6 (Alcohol Dehydrogenase 6 (Class V)) is a Protein Coding gene. (genecards.org)
- GO annotations related to this gene include oxidoreductase activity and alcohol dehydrogenase (NAD) activity . (genecards.org)
- Here we present gene distribution and phylogenetic analyses of the genes encoding the hybrid-cluster protein, A-type flavoprotein, glucosamine-6-phosphate isomerase, and alcohol dehydrogenase E. These four genes have a limited distribution among sequenced prokaryotic and eukaryotic genomes and were previously implicated in gene transfer events affecting eukaryotes. (diva-portal.org)
- Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. (hmdb.ca)
Methanol1
- Biodiesel itself is composed of mono-alkyl esters of vegetable oils or animal fats and is produced by transesterification with a monohydric alcohol (methanol) [ 3 ]. (mdpi.com)
CDNA1
- Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. (hmdb.ca)
Synthesis2
- [ 14 ] In cultured skin keratinocytes, elevated fatty alcohol is diverted into the synthesis of wax esters and alkyldiacylglycerol lipids. (medscape.com)
- Synthesis of pyruvate: ferredoxin oxidoreductase and alcohol dehydrogenase E enzymes during Giardia intestinalis excystation. (ebscohost.com)
Chemistry1
- Evidence for a fatty alcohol cycle, The Journal of biological chemistry 262 (1987) 17412-17419. (springer.com)
Transferases1
- Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. (britannica.com)
Liver1
- a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. (qmul.ac.uk)
Mediator1
- 8. The biosensor of claim 7 , wherein the oxidoreductase and the mediator are immobilized on the working electrode. (google.com)
Oxidase2
- 5. The biosensor of claim 4 , wherein the oxidoreductase is glucose oxidase. (google.com)
- More specifically, it relates to a glucose biosensor having glucose oxidase immobilized thereon or a biosensor having an oxidoreductase immobilized thereon. (google.com)