NAD (+) and NADP (+) Dependent Alcohol OxidoreductasesAlcohol 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.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 This protection is available to both published and unpublished works.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: Organizations which are not operated for a profit and may be supported by endowments or private contributions.Patents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)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.Confidentiality: The privacy of information and its protection against unauthorized disclosure.Privacy: The state of being free from intrusion or disturbance in one's private life or affairs. (Random House Unabridged Dictionary, 2d ed, 1993)Mycobacterium: A genus of gram-positive, aerobic bacteria. Most species are free-living in soil and water, but the major habitat for some is the diseased tissue of warm-blooded hosts.Rhodococcus: A bacterial genus of the order ACTINOMYCETALES.Actinobacteria: Class of BACTERIA with diverse morphological properties. Strains of Actinobacteria show greater than 80% 16S rDNA/rRNA sequence similarity among each other and also the presence of certain signature nucleotides. (Stackebrandt E. et al, Int. J. Syst. Bacteriol. (1997) 47:479-491)Prephenate Dehydratase: An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.Actinomycetales: An order of gram-positive, primarily aerobic BACTERIA that tend to form branching filaments.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Acetoin: A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.Butylene Glycols: 4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Acetoin Dehydrogenase: An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.Hydroxybutyrate DehydrogenaseReceptors, 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: A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.Drosophila Proteins: Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.Drosophila melanogaster: A species of fruit fly much used in genetics because of the large size of its chromosomes.Receptor, Notch2: A notch receptor that plays an important role in CELL DIFFERENTIATION in a variety of cell types. It is the preferentially expressed notch receptor in mature B-LYMPHOCYTES.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: Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.GlyceraldehydeGlutamate-5-Semialdehyde Dehydrogenase: An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.Phosphotransferases (Carboxyl Group Acceptor): A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.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: An organic compound used often as a reagent in organic synthesis, as a flavoring agent, and in tanning. It has been demonstrated as an intermediate in the metabolism of acetone and its derivatives in isolated cell preparations, in various culture media, and in vivo in certain animals.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.2,6-Dichloroindophenol: A dye used as a reagent in the determination of vitamin C.Mentha spicata: A plant genus of the family LAMIACEAE having characteristic flavor.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: Six-carbon alicyclic hydrocarbons which contain one or more double bonds in the ring. The cyclohexadienes are not aromatic, in contrast to BENZOQUINONES which are sometimes called 2,5-cyclohexadiene-1,4-diones.Acetone: A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis.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: Microscopy in which the image is formed by ultraviolet radiation and is displayed and recorded by means of photographic film.Alcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.Plant Stems: Parts of plants that usually grow vertically upwards towards the light and support the leaves, buds, and reproductive structures. (From Concise Dictionary of Biology, 1990)Propanols: Isomeric forms and derivatives of PROPANOL (C3H7OH).Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

1. Lee Y, Jeon K, Lee JT, Kim S, Kim VN. MicroRNA maturation: stepwise processing and subcellular localization. Embo J. 2002;21(17):4663-4670 2. Chen K, Rajewsky N. The evolution of gene regulation by transcription factors and microRNAs. Nat Rev Genet. 2007;8(2):93-103 3. Pillai RS, Bhattacharyya SN, Filipowicz W. Repression of protein synthesis by miRNAs: how many mechanisms?. Trends Cell Biol. 2007;17(3):118-126 4. Walker GJ, Indsto JO, Sood R. et al. Deletion mapping suggests that the 1p22 melanoma susceptibility gene is a tumor suppressor localized to a 9-Mb interval. Genes Chromosomes Cancer. 2004;41(1):56-64 5. Bemis LT, Chen R, Amato CM. et al. MicroRNA-137 targets microphthalmia-associated transcription factor in melanoma cell lines. Cancer Res. 2008;68(5):1362-1368 6. Chinnadurai G. The transcriptional corepressor CtBP: a foe of multiple tumor suppressors. Cancer Res. 2009;69(3):731-734 7. Haflidadottir BS, Bergsteinsdottir K, Praetorius C, Steingrimsson E. miR-148 regulates Mitf in ...
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC 1.1.1.300, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
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EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Estradiol 17-beta-dehydrogenase 11,1.1.1.62,17-beta-hydroxysteroid dehydrogenase 11,17-beta-HSD 11,17bHSD11,17betaHSD11,17-beta-hydroxysteroid dehydrogenase XI,17-beta-HSD XI,17betaHSDXI,Cutaneous T-cell lymphoma-associated antigen HD-CL-03,CTCL-associated antigen HD-CL-03,Dehydrogenase/reductase SDR family member 8,Retinal short-chain dehydrogenase/reductase 2,retSDR2,Short chain dehydrogenase/reductase family 16C member 2,HSD17B11,DHRS8,PAN1B,SDR16C2,PSEC0029,UNQ207/PRO233,. ...
Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
BACKGROUND: (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol [(R)-3,5-BTPE] is a valuable chiral intermediate for Aprepitant (Emend) and Fosaprepitant (Ivemend). Biocatalyzed asymmetric reduction is a preferred approach to synthesize highly optically active (R)-3,5-BTPE. However, the product concentration and productivity of reported (R)-3,5-BTPE synthetic processes remain unsatisfied. RESULTS: A NADPH-dependent carbonyl reductase from Lactobacillus kefir (LkCR) was discovered by genome mining for reduction of 3,5-bis(trifluoromethyl) acetophenone (3,5-BTAP) into (R)-3,5-BTPE with excellent enantioselectivity. In order to synthesize (R)-3,5-BTPE efficiently, LkCR was coexpressed with glucose dehydrogenase from Bacillus subtilis (BsGDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L (R)-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). Then, four different linker peptides were used for the fusion expression of ...
Short-chain dehydrogenases/reductases form a large, evolutionarily old family of NAD(P)(H)-dependent enzymes with over 60 genes found in the human genome. Despite low levels of sequence identity (often 10-30%), the three-dimensional structures display a highly similar alpha/beta folding pattern. We have analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3beta/17beta-hydroxysteroid dehydrogenase and selected mutants. Structure determination of the wild-type enzyme at 1.2-A resolution by x-ray crystallography and docking analysis was used to interpret the biochemical data. Enzyme kinetic data from mutagenetic replacements emphasize the critical role of residues Thr-12, Asp-60, Asn-86, Asn-87, and Ala-88 in coenzyme binding and catalysis. The data also demonstrate essential interactions of Asn-111 with active site residues. A general role of its side chain interactions for maintenance of the active site configuration to
The major metabolic pathways involved in synthesis and disposition of carbonyl and hydroxyl group containing compounds are presented, and structural and functional characteristics of the enzyme families involved are discussed. Alcohol and aldehyde dehydrogenases (ADH, ALDH) participate in oxidative pathways, whereas reductive routes are accomplished by members of the aldo-keto reductase (AKR), short-chain dehydrogenases/reductases (SDR) and quinone reductase (QR) superfamilies. A wealth of biochemical, genetic and structural data now establishes these families to constitute important phase I enzymes.
Complete information for SDR42E1 gene (Protein Coding), Short Chain Dehydrogenase/Reductase Family 42E, Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Background information. CtBP proteins have roles in the nucleus as transcriptional co-repressors, and in the cytoplasm in the maintenance of vesicular membranes. CtBPs are expressed from two genes, CTBP1 and CTBP2, mRNA products of which are alternatively spliced at their 5 ends to generate distinct protein isoforms. Extensive molecular and cellular analyses have identified CtBPs as regulators of pathways critical for tumour initiation, progression, and response to therapy. However little is known of the expression or regulation of CtBP isoforms in human cancer, nor the relative contribution of CTBP1 and CTBP2 to the tumour cell phenotype. Results. Expression of CtBP proteins, and CTBP1 and CTBP2 mRNA splice forms in breast cancer cell lines and tumour tissue were examined. CtBP1 proteins are identifiable as a single band on western blots and are ubiquitously detectable in breast tumour samples, by both western blotting and immunohistochemistry. CtBP1 is present in 6 of 6 breast cancer cell ...
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
592 Drug resistance caused by overexpression of P-glycoprotein (P-gp), the MDR1 gene product, limits the therapeutic outcome in cancer patients. Although modulation of multidrug resistance (MDR) by pharmacological agents, antibodies, antisense oligonucleotides, siRNA, and inhibitors of signal transduction have been reported, clinical benefits have been disappointing. We and others have sought to understand the regulation of MDR1 gene expression as another approach to this problem. CtBP1 (C-terminal-binding protein 1) is a transcriptional co-regulator that plays an important role in oncogenesis. Recently, it was reported that CtBP1 could serve as both a co-activator and co-repressor of transcription. In this study, we determined the effect of CtBP1 on transcription of the MDR1 gene. Chromatin immunoprecipitation (ChIP) experiments demonstrated that CtBP1 bound to the promoter and coding regions of the MDR1 gene, but not to the non-coding regions. Knockdown of CtBP1 expression by siRNA repressed ...
Alcohol Oxidase, 10 mg. Alcohol Oxidase (AOX) is a homooctameric flavoprotein consisting of eight identical subunits of ~74 kD, each containing a flavin adenine dinucleotide molecule (FAD) as a prosthetic group (van der Klei et al.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Shop Dehydrogenase/reductase SDR family protein ELISA Kit, Recombinant Protein and Dehydrogenase/reductase SDR family protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
CP000667.PE408 Location/Qualifiers FT CDS_pept 469214..469912 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0408" FT /product="short-chain dehydrogenase/reductase SDR" FT /note="PFAM: short-chain dehydrogenase/reductase SDR" FT /db_xref="EnsemblGenomes-Gn:Strop_0408" FT /db_xref="EnsemblGenomes-Tr:ABP52893" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR036291" FT /db_xref="UniProtKB/TrEMBL:A4X1Z3" FT /protein_id="ABP52893.1" FT /translation="MVNLDGLRVAVTGAGRASGRLLATAFAEHGAQVFVSARDEVAARR FT TTDSIRQRGRGRGEAFVCDLTSPDSVRAFAAALTDRTDHLDVLVNNGAGYLHGVDLGDV FT EDDHIIATIGGTATGTVLLTKHLLALLRASTRPDIVNMISACGEVGHHRSEAHPAFYAA FT KHAQAGFAEIMSHRLRVEGIRVISLFPPDFVQHGPRVASNNLTAQSVVDCVLFAVSQPR FT DCFIREFRFE" gtggtgaatc tcgacggact acgggttgct gtcaccggcg ccgggcgcgc ctccggacgc 60 ctcctggcga ccgccttcgc cgagcacggc gcgcaggtgt ttgtctccgc ccgtgatgag 120 gtggcagcca gacgcaccac ggattcgatc cggcagcgtg ggcgggggag aggcgaagcc 180 ttcgtctgtg acctgaccag ccccgactcg gtacgcgcgt tcgcggcggc gttgaccgac 240 cgcaccgacc ...
But experimentalists should not get too cocky: the next paper, by Jamie Simpson and collaborators at Monash University, describes some of the things that can go wrong. An STD NMR screen of the antimicrobial target ketopantoate reductase (KPR) using the same Maybridge library of 500 compounds revealed 196 hits! The 47 with the strongest STD signals were then tested in a 1H/15N-HSQC NMR assay, leading to 14 hits, of which 4 gave measurable IC50 values in an enzymatic assay. Unfortunately, follow-up SAR was disappointing, and subsequent experiments revealed that aggregation was to blame: when the biochemical experiments were rerun in the presence of 0.01% Tween-20, only a single fragment gave a measurable IC50 value. The researchers redid their STD-NMR screen in the presence of detergent, resulting in 71 hits, all of which were tested in the biochemical screen. This led to the identification of a new (and fairly potent) hit that had previously been missed. This nicely illustrates the fact that ...
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Complete information for RDH16 gene (Protein Coding), Retinol Dehydrogenase 16 (All-Trans), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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TY - JOUR. T1 - Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases. AU - Rougraff, P. M.. AU - Zhang, B.. AU - Kuntz, M. J.. AU - Harris, Robert. AU - Crabb, David. PY - 1989. Y1 - 1989. N2 - A 1.7-kilobase pair cDNA clone encoding 3-hydroxyisobutyrate dehydrogenase has been isolated by screening a rat liver λgt11 library with a 17-base oligonucleotide probe which corresponds to a portion of the N-terminal amino acid sequence of rabbit liver 3-hydroxyisobutyrate dehydrogenase. The cDNA contains an open reading frame of 1038 base pairs which includes an amino acid sequence that matches the N-terminal 35 amino acid sequence of rabbit 3-hydroxyisobutyrate dehydrogenase at 33 residues. The cDNA predicts a 300-amino acid mature protein with an amino acid composition and molecular weight very similar to that of rabbit liver 3-hydroxyisobutyrate dehydrogenase. Northern blot ...
Looking for online definition of retinal reductase in the Medical Dictionary? retinal reductase explanation free. What is retinal reductase? Meaning of retinal reductase medical term. What does retinal reductase mean?
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants
This gene encodes a mitochondrial 3-hydroxyisobutyrate dehydrogenase enzyme. The encoded protein plays a critical role in the catabolism of L-valine by catalyzing the oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde. [provided by RefSeq, Nov 2011 ...
Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
The corepressor CtBP (carboxyl-terminal binding protein) is involved in transcriptional pathways important for development, cell cycle regulation, and transformation. We demonstrate that CtBP binding to cellular and viral transcriptional repressors is regulated by the nicotinamide adenine dinucleotides NAD+ and NADH, with NADH being two to three orders of magnitude more effective. Levels of free nuclear nicotinamide adenine dinucleotides, determined using two-photon microscopy, correspond to the levels required for half-maximal CtBP binding and are considerably lower than those previously reported. Agents capable of increasing NADH levels stimulate CtBP binding to its partners in vivo and potentiate CtBP-mediated repression. We propose that this ability to detect changes in nuclear NAD+/NADH ratio allows CtBP to serve as a redox sensor for transcription. ...
CBR1_HUMAN RecName: Full=Carbonyl reductase [NADPH] 1; AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)]; AltName: Full=NADPH-dependent carbonyl reductase 1; AltName: Full=Prostaglandin 9-ketoreductase; AltName: Full=Prostaglandin-E(2) 9-reductase ...
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues. ...
Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari golongan dehidrogenase yang berfungsi sebagai katalisator oksidasi alkohol dengan aldehid atau keton, dengan reduksi NAD+ menjadi NADH. ADH merupakan protein yang mengandung Zn yang bereaksi pada alkohol primer dan sekunder atau asetal-hemi, dan alkohol sekunder siklik.[1] Reaksi yang terjadi: ...
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis. ...
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Pseudomonas aeruginosa ExaE protein: a response regulator of a two-component regulatory system for controling expression quinoprotein ethanol dehydrogenase; isolated from Pseudomonas aeruginosa; amino acid sequence in first source
Accepted name: alcohol dehydrogenase (nicotinoprotein). Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor. Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Systematic name: ethanol:acceptor oxidoreductase. Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].. Links to other databases: BRENDA, ...
Accepted name: coniferyl-alcohol dehydrogenase. Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+. Other name(s): CAD. Systematic name: coniferyl-alcohol:NADP+ oxidoreductase. Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-27-4. References:. 1. Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849-1853.. 2. Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. [PMID: 1250]. ...
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
RDH10 is a specific all-trans retinol dehydrogenase identified in the RPE and now in the Müller cells. 14 We propose that one of the possible physiological functions of RDH10 is to synthesize the all-trans retinal chromophore for RGR and thus to act as a functional partner of RGR in the photic visual cycle. As RGR is known to be expressed in both the RPE and Müller cells, it was necessary to determine whether RDH10 co-expresses with RGR in both the RPE and Müller cells. Western blot analysis demonstrated that RDH10 is expressed at a high level in the RPE and a lower level in the retina (Fig. 2) . The anti-RDH10 antibody stained a cell type in the inner retina. The morphology of the stained cells and their location in the retina are consistent with those of Müller cells. 16 To further confirm the observation, we used rMC-1 cells, a well-established and characterized retinal Müller cell line. 19 RDH10 expression in this cell line was detected at both the mRNA and protein levels (Fig. 4) ...
Reitman and colleagues had a hunch that the genetic mutation seen in cancer might trigger a similar functional change to a closely related enzyme found in yeast and bacteria (homoisocitrate dehydrogenase), which would create the elusive 2-hydroxyadipate dehydrogenase necessary for "green" adipic acid production.. They were right. The functional mutation observed in cancer could be constructively applied to other closely related enzymes, creating a beneficial outcome - in this case the missing link that could enable adipic acid production from cheap sugars. The next step will be to scale up the overall adipic acid production process, which remains a considerable undertaking.. "Its exciting that sequencing cancer genomes can help us to discover new enzyme activities," Reitman said. "Even genetic changes that occur in only a few patients could reveal useful new enzyme functions that were not obvious before.". Yan, a professor in the Department of Pathology and senior author of the study, said the ...
TY - JOUR. T1 - Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.. AU - Qulali, M.. AU - Wolfla, C. E.. AU - Ross, R. A.. AU - Crabb, D. W.. PY - 1989. Y1 - 1989. UR - http://www.scopus.com/inward/record.url?scp=0024491855&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0024491855&partnerID=8YFLogxK. M3 - Article. C2 - 2471210. AN - SCOPUS:0024491855. VL - 290. SP - 143. EP - 153. JO - Progress in Clinical and Biological Research. JF - Progress in Clinical and Biological Research. SN - 0361-7742. ER - ...
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome Database
GT:ID BAD57618.1 GT:GENE BAD57618.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 2940013..2940783 GB:FROM 2940013 GB:TO 2940783 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD57618.1 LENGTH 256 SQ:AASEQ MDKDSFRKLFDLSGRTAIVTGGTRGIGLAIAEGFACAGANLVVASRKPEACEQAAARLRELGAQAVGVPTHLGEIDSLRALVDTAVSAFGGIDIVVNNAANALAQPLATMAPEAVDKSFGVNVQGPLFLVQAALPHLRASAHAAVLNLGSVAALQFAPGLSMYAAGKAALLSFTRAMAAEFAADGIRVNAMAPGAVNTDMVRKNPPEFIAAMAQAPLLRRIAEPDEMVGAALLLCSDAGSFITGQTFLVDGGTVAR GT:EXON 1,1-256:0, BL:SWS:NREP 1 BL:SWS:REP 12-,256,DHRS4_RABIT,4e-36,36.8,242/260, PROS 150-,178,PS00061,ADH_SHORT,PDOC00060, SEG 97-,102,nnaana, BL:PDB:NREP 1 BL:PDB:REP 9-,255,1vl8B,1e-34,34.4,247/252, RP:PDB:NREP 1 RP:PDB:REP 10-,256,2ae1A,8e-44,30.6,245/252, RP:PFM:NREP 1 RP:PFM:REP 15-,180,PF00106,2e-21,42.2,166/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP 16-,181,PF00106,2.2e-34,30.9,162/167,adh_short, GO:PFM:NREP 2 GO:PFM ...
GT:ID BAD55466.1 GT:GENE BAD55466.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 643418..644293 GB:FROM 643418 GB:TO 644293 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD55466.1 LENGTH 291 SQ:AASEQ MSRWDTANIPDQSGRTFIVTGANSGLGAVAARALARAGADVVLACRNLTKAEKVAAEIGARATVRELDLADLASVRAFAAGTERVDVLINNAGVMAVPHRTTADGFEMQIGTNHLGHFALTGLLLDKITDRVVTVSSGAHAVGRIDLADLNWERRRYQRWLAYGQSKLANLLFAYELQRRLGAAGSPILSVAAHPGYAATELQSHTETFLDSVMNVGNRILAQTAEMGALPELFAATMPVEPGAFYGPTGLGGMRGYPGRCGSTKASRDERVAGELWALSERLTGVTYSFD GT:EXON 1,1-291:0, BL:SWS:NREP 1 BL:SWS:REP 7-,286,RDH13_MOUSE,2e-38,40.5,269/334, SEG 25-,44,glgavaaralaragadvvla, BL:PDB:NREP 1 BL:PDB:REP 14-,205,2japC,4e-08,39.4,180/246, RP:PDB:NREP 2 RP:PDB:REP 13-,91,2ag5C,1e-05,23.4,77/244, RP:PDB:REP 68-,205,3ce6B,5e-13,8.1,136/485, RP:PFM:NREP 1 RP:PFM:REP 46-,143,PF00106,3e-05,38.8,98/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP ...
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pyloris pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes ...
At concentrations of 2mM and above hydroxypyruvate produced no glucose with isolated rat liver cells, although it was rapidly utilized. At a lower concentration of hydroxypyruvate or in the presence of substrates which generate reducing equivalents (ethanol or butyrate), appreciable amounts of glucose were formed from hydroxypyruvate. A possible explanation for this phenomenon is discussed.. ...
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ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
putative quinate/shikimate dehydrogenase [putative shikimate 5-dehydrogenase] ATGGTCAAGGACTCGTATCTCGTCGGGCTGATCGGCGCCGGGATCGGCCCGTCGCTCAGC CCGGCACTGCACGAGCGGGAGGCCGACCGGCAGGGCCTGCGCTATCTGTACCGGCTGATC GACATCGACGCGCTCGGTGTCGGGCCGCAGGCGGTGGGGGACCTCGTACGAGCCGCCCGC GACCTGGGCTTCGACGGGCTGAACATCACGCATCCCTGCAAGCAGCTCGTCATCGGGCAT CTGGACGCGCTCGCCCCGCAGGCCGAGGCGCTCGGCGCGGTGAACACCGTCGTCTTCGAG GGCGGGCGTGCGGTCGGGCACAACACCGATGTCACCGGGTTCGCCGCCTCGTTCGCCCGT GGGCTGCCGGATGCCCCGCTGGAGCGGGTCGTGCAGTTGGGCGCGGGGGGAGCGGGGGCG GCCGTCGCGCATGCCATGCTCACGCTCGGGGCCGGGCACGTCACCGTCGTCGATGCCATG CCGGACCGGTCGGCGGACCTCGCCGCCTCGCTGAACCGGCACTTCGGTGCGGGGCGGGCC GCTGCCGCGGGCCCGGAGCGGCTGGCGGCGCTGCTCGGCGGTGCGGACGGCATCGTGCAT GCCACGCCGACGGGGATGGCCGCTCATCCGGGGCTGCCGCTTCCCGGTGAGTTGCTGCAT CCCGGGTTGTGGGTGGCCGAGGTGGTGTACCGGCCGTTGGAGACCGAGTTGCTGCGTGCC GCTCGGGCGGCGGGGTGTGCGGTTCTCGATGGTGGGGGGATGGCTGTTTTCCAGGCCGCG GACGCGTTTCGGCTGTTCACGGGGCGGGAGCCGGACGCGGTGCGGATGCTTGCGGATATT ...
Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (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): 463-471. doi: ... dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and ...
It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
The oxidoreductase encoded by mrl7 converts this alcohol into a bisaldehyde. Then CitD converts it into a carboxylic acid, via ... The mrl7 gene encodes for a NAD(P)+ dependent oxidoreductase (CitC). The first step of citrinin biosynthesis in fungi is the ... CitB oxidizes the C-atom of a methyl group bound to the aromatic ring and produces an alcohol. ...
Alcohol flush reaction Disulfiram-like drug Oxidoreductase PDB: 1NVM​; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). " ... Swift R, Davidson D. "Alcohol Hangover: Mechanisms and Mediators" (PDF). National Institute on Alcohol Abuse and Alcoholism. ... Acetaldehyde is more toxic than alcohol and is responsible for many hangover symptoms. About 50% of people of Northeast Asian ... In the liver, the enzyme alcohol dehydrogenase oxidizes ethanol into acetaldehyde, which is then further converted into the ...
It belongs to the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. In melanocytic cells VAT1 ...
... acyclic monoterpene primary alcohol:NADP+ oxidoreductase) is an enzyme with systematic name (6E)-8-hydroxygeraniol:NADP+ ... "Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa ... Ikeda, H.; Esaki, N.; Nakai, S.; Hashimoto, K.; Uesato, S.; Soda, K.; Fujita, T. (1991). "Acyclic monoterpene primary alcohol: ... 8-hydroxygeraniol dehydrogenase (EC 1.1.1.324, 8-hydroxygeraniol oxidoreductase, CYP76B10, G10H, CrG10H, SmG10H, ...
... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...
The systematic name of this enzyme class is secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR. As of ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a chlordecone reductase (EC 1.1.1.225) is an enzyme that catalyzes the chemical reaction chlordecone alcohol + ... the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+. ...
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 ...
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 ...
... primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari ... NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase ...
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem J. ... Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). „A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature ...
... 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: ...
Oksidoreduktase perilil-alkohol:NAD+ (bahasa Inggris: perillyl-alcohol:NAD+ oxidoreductase, perillyl-alcohol dehydrogenase, ...
The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem. J. ... cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction a primary alcohol + 2 ferricytochrome cL ... Salisbury, S.A.; Forrest, H.S.; Cruse, W.B.T.; Kennard, O. (1979). "A novel coenzyme from bacterial primary alcohol ... displaystyle \rightleftharpoons } an aldehyde + 2 ferrocytochrome cL + 2 H+ A periplasmic quinoprotein alcohol dehydrogenase is ...
The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase. It ... 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 donor with oxygen as ... Suye S (1997). "Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003". Curr. Microbiol. 34 (6): ...
H2 by pyruvate ferredoxin oxidoreductase and hydrogenase; and ethanol via NADH- and NADPH-linked alcohol dehydrogenase. By its ...
This enzyme is an oxidoreductase, specifically a metal-dependent alcohol dehydrogenase that plays a role in anaerobic glycerol ... Marshall, J. H.; May, J. W.; Sloan, J. (1985). "Purification and Properties of Glycerol: NAD+ 2-Oxidoreductase (Glycerol ... Glycerol dehydrogenase (EC 1.1.1.6, also known as NAD+-linked glycerol dehydrogenase, glycerol: NAD+ 2-oxidoreductase, GDH, ... GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form ...
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" ...
The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD. Mansell RL ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a coniferyl-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction coniferyl ... the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+ ...
Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (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) Molecular and ... Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A. (1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase ...
... 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) Molecular and Cellular ... Cozier, G.E.; Giles, I.G.; Anthony, C. (1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti ... Chinnawirotpisan, P.; Theeragool, G.; Limtong, S.; Toyama, H.; Adachi, O.O.; Matsushita, K. (2003). "Quinoprotein alcohol ...
The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. Otsuka K (1958). "Triphosphopyridine nucleotide ... In enzymology, an allyl-alcohol dehydrogenase (EC 1.1.1.54) is an enzyme that catalyzes the chemical reaction allyl alcohol + ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...
The systematic name of this enzyme class is polyvinyl-alcohol:oxygen oxidoreductase. Other names in common use include ... In enzymology, a polyvinyl-alcohol oxidase (EC 1.1.3.30) is an enzyme that catalyzes the chemical reaction polyvinyl alcohol + ... whereas its two products are oxidized polyvinyl alcohol and H2O2. This enzyme belongs to the family of oxidoreductases, ... Shimao M, Nishimura Y, Kato N, Sakazawa C (1985). "Localization of Polyvinyl Alcohol Oxidase Produced by a Bacterial Symbiont, ...
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 ...
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) Molecular and Cellular Biology ...
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. ...
... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ... Oxidoreductases: 9264*Alcohol Oxidoreductases: 1*N-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N ... dimethyl-4-nitrosoaniline oxidoreductase alcohol - N. Subscribe to New Research on N-dimethyl-4-nitrosoaniline oxidoreductase ... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ...
Alcohol Oxidoreductases / genetics * Alcohol Oxidoreductases / metabolism * Amino Acid Substitution * Anaerobiosis * Butylene ... Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol Appl Environ ... dependent oxidoreductases. One of them has been purified and shown to be d-arabinose dehydrogenase (Ara1p), which converts (R/S ...
Alcohol Oxidoreductases * Amino Acid Sequence * Animals * DNA-Binding Proteins / metabolism* * Drosophila / embryology ...
alcohol: NAD oxidoreductase. alcohol dehydrogenase. alcohol + NAD → acetaldehyde NADH. alcoholic fermentation. 1.1.1.27. L- ... Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. The table ... Enzymes that catalyze reactions in which hydrogen is transferred belong to the group known as oxidoreductases; those that ... The numbering system is as follows: the first number places the enzyme in one of six general groups-1, oxidoreductases; 2, ...
Alcohol Oxidoreductases); EC 1.1.- (glycolic acid dehydrogenase); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde ...
Alcohol Oxidoreductases / 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 ...
0 (Glucuronates); 0 (Sugar Acids); 0U46U6E8UK (NAD); 8L70Q75FXE (Adenosine Triphosphate); EC 1.1.- (Alcohol Oxidoreductases); ... "Hit-and-run" mechanism for D-glucuronate reduction catalyzed by D-mannonate:NAD oxidoreductase of Escherichia coli.. ... 0 (Sugar Acids); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.- (L-galactonate oxidoreductase); EC 1.1.1.45 (gulonate ... In the presence of superrepressed or derepressed uxuR mutations, mannonic hydrolyase (uxuA) and oxidoreductase relationship ...
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 ...
Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (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) Molecular and ... Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A. (1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase ...
... 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 ...
Alcohol Oxidoreductases. 1. 2018. 172. 0.050. Why? Tumor Microenvironment. 2. 2017. 1526. 0.050. Why? ...
Predicted oxidoreductases (Related to aryl-alcohol dehydrogenases). Klebsiella pneumoniae IS22. 346. +39. ... oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: EcoCyc ,p>Inferred from Direct ...
Dehydrogenases, Sugar Alcohol. *Sugar Alcohol Oxidoreductases. *Alcohol Oxidoreductases, Sugar. *Oxidoreductases, Sugar Alcohol ... "Sugar Alcohol Dehydrogenases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Sugar Alcohol Dehydrogenases" by people in Harvard Catalyst ... Below are the most recent publications written about "Sugar Alcohol Dehydrogenases" by people in Profiles. ...
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" ...
The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol ... quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ...
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductase · Oxygenase · Unclassified drug · Bacterial metabolism · Controlled study · Enzyme activity · Nonhuman · ...
Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductases · Rats · Rats, Wistar · RNA, Messenger · Steroid Hydroxylases · Support, Non-U.S. Govt · Taurocholic Acid · ... cinnamyl alcohol · collagen type 16 · disulfiram · dodecyl sulfate sodium · eugenol · ferritin · ferrochelatase · glucose 6 ...
p-hydroxybenzyl alcohol dehydrogenase;. benzyl alcohol dehydrogenase;. coniferyl alcohol dehydrogenase. Class. Oxidoreductases; ... Identification and characterization of a nicotinamide adenine dinucleotide-dependent para-hydroxybenzyl alcohol-dehydrogenase ...
Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase ... The byproducts generated during polycondensation are water, methanol, ethanol and n-butyl alcohol, respectively. ... and n-butyl alcohol (bp = 117.7 °C). Besides, the chemical reactivity of the alkyl esters is another reason. It is well known ... We suspect that the increase of the residual alcohol amount and the decrease of the polymerization rate in dilute reaction ...
Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... Tas; Predicted oxidoreductase (related to aryl-alcohol dehydrogenase) [General function prediction only]. ... oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor IDA Inferred from Direct Assay. more info ... alditol:NADP+ 1-oxidoreductase activity IBA Inferred from Biological aspect of Ancestor. more info ...
p-cumic alcohol:NAD+ oxidoreductase. Definition. p-Cumic alcohol + NAD+ ,=, 4-Isopropylbenzaldehyde + NADH + H+. ...
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to ... cinnamyl alcohol dehydrogenase. Subscribe to New Research on cinnamyl alcohol dehydrogenase NADP-dependent enzyme that ... 12/01/2014 - "Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes ... 09/01/1999 - "Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol ...
Alcohol Oxidoreductases (+35). Autoradiography (+14). Carbohydrate Metabolism (+38). PA0374. Chromosomes (+4). Escherichia coli ...