Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.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)Aldehyde Dehydrogenase: An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.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.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).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.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.Glutaredoxins: A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.NAD (+) and NADP (+) Dependent Alcohol OxidoreductasesOxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Protein Disulfide-Isomerases: Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.Aldehyde Reductase: An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.Oxidoreductases Acting on Sulfur Group Donors: Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.FlavoproteinsThioredoxins: Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.Oxidoreductases Acting on Aldehyde or Oxo Group Donors: A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.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.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Quinone Reductases: NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.Electron Transport Complex II: A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.Nanoarchaeota: A kingdom of hyperthermophilic ARCHAEA found in diverse environments.Wolinella: A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Thioredoxin-Disulfide Reductase: A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Succinate Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Acetaldehyde: A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.Oxidoreductases Acting on CH-CH Group Donors: A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.Ecological and Environmental Processes: Ecosystem and environmental activities, functions, or events.Electron Transport: The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)Glucose Oxidase: An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.AcroleinBenzaldehydesSequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Pleurotus: A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)NAD(P)H Dehydrogenase (Quinone): A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.Ferredoxin-NADP Reductase: An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.Flavin-Adenine Dinucleotide: A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)Electron Transport Complex I: A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.15-Oxoprostaglandin 13-Reductase: (5Z)-(15S)-11 alpha-Hydroxy-9,15-dioxoprostanoate:NAD(P)+ delta(13)-oxidoreductase. An enzyme active in prostaglandin E and F catabolism. It catalyzes the reduction of the double bond at the 13-14 position of the 15-ketoprostaglandins and uses NADPH as cofactor. EC 1.3.1.48.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.Flavins: Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)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.Kinetics: The rate dynamics in chemical or physical systems.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Iron-Sulfur Proteins: A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Disulfiram: A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.Oxidoreductases Acting on CH-NH2 Group Donors: Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.Prokaryotic Cells: Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.Xanthine Dehydrogenase: An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.Protochlorophyllide: A photo-active pigment localized in prolamellar bodies occurring within the proplastids of dark-grown bean leaves. In the process of photoconversion, the highly fluorescent protochlorophyllide is converted to chlorophyll.KetonesBinding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Electrons: Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.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)FMN Reductase: An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.Bacterial Proteins: Proteins found in any species of bacterium.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Alkadienes: Acyclic branched or unbranched hydrocarbons having two carbon-carbon double bonds.Periplasm: The space between the inner and outer membranes of a cell that is shared with the cell wall.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Sulfhydryl Compounds: Compounds containing the -SH radical.Isomerases: A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.PQQ Cofactor: A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.Flavodoxin: A low-molecular-weight (16,000) iron-free flavoprotein containing one molecule of flavin mononucleotide (FMN) and isolated from bacteria grown on an iron-deficient medium. It can replace ferredoxin in all the electron-transfer functions in which the latter is known to serve in bacterial cells.Rhodobacter capsulatus: Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.Sugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Glutathione Reductase: Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Cyanamide: A cyanide compound which has been used as a fertilizer, defoliant and in many manufacturing processes. It often occurs as the calcium salt, sometimes also referred to as cyanamide. The citrated calcium salt is used in the treatment of alcoholism.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Periplasmic Proteins: Proteins found in the PERIPLASM of organisms with cell walls.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Recombinant Proteins: Proteins prepared by recombinant DNA technology.Archaea: One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.Oxidoreductases, O-Demethylating: Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Succinic Acid: A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Genes, Bacterial: The functional hereditary units of BACTERIA.Ferredoxins: Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Fumarates: Compounds based on fumaric acid.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Anaerobiosis: The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Metalloproteins: Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Selenocysteine: A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.Bacteria: One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Oxidative Stress: A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).Selenoproteins: Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.Sequence Homology: The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.Quinones: Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Electron Transport Complex III: A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.Electron Spin Resonance Spectroscopy: A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Clostridium: A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Alkenes: Unsaturated hydrocarbons of the type Cn-H2n, indicated by the suffix -ene. (Grant & Hackh's Chemical Dictionary, 5th ed, p408)Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Ubiquinone: A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.Sjogren-Larsson Syndrome: An autosomal recessive neurocutaneous disorder characterized by severe ichthyosis MENTAL RETARDATION; SPASTIC PARAPLEGIA; and congenital ICHTHYOSIS. It is caused by mutation of gene encoding microsomal fatty ALDEHYDE DEHYDROGENASE leading to defect in fatty alcohol metabolism.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.GlyceraldehydeAldehyde-Lyases: Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.Molecular Weight: The sum of the weight of all the atoms in a molecule.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.Chemistry, Organic: The study of the structure, preparation, properties, and reactions of carbon compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Iridium: A metallic element with the atomic symbol Ir, atomic number 77, and atomic weight 192.22.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Aerobiosis: Life or metabolic reactions occurring in an environment containing oxygen.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Hydrogenation: Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)Metabolic Networks and Pathways: Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Fungal Proteins: Proteins found in any species of fungus.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

Nitrate-dependent regulation of acetate biosynthesis and nitrate respiration by Clostridium thermoaceticum. (1/1279)

Nitrate has been shown to shunt the electron flow in Clostridium thermoaceticum from CO2 to nitrate, but it did not influence the levels of enzymes involved in the Wood-Ljungdahl pathway (J. M. Frostl, C. Seifritz, and H. L. Drake, J. Bacteriol. 178:4597-4603, 1996). Here we show that under some growth conditions, nitrate does in fact repress proteins involved in the Wood-Ljungdahl pathway. The CO oxidation activity in crude extracts of nitrate (30 mM)-supplemented cultures was fivefold less than that of nitrate-free cultures, while the H2 oxidation activity was six- to sevenfold lower. The decrease in CO oxidation activity paralleled a decrease in CO dehydrogenase (CODH) protein level, as confirmed by Western blot analysis. Protein levels of CODH in nitrate-supplemented cultures were 50% lower than those in nitrate-free cultures. Western blots analyses showed that nitrate also decreased the levels of the corrinoid iron-sulfur protein (60%) and methyltransferase (70%). Surprisingly, the decrease in activity and protein levels upon nitrate supplementation was observed only when cultures were continuously sparged. Northern blot analysis indicates that the regulation of the proteins involved in the Wood-Ljungdahl pathway by nitrate is at the transcriptional level. At least a 10-fold decrease in levels of cytochrome b was observed with nitrate supplementation whether the cultures were sparged or stoppered. We also detected nitrate-inducible nitrate reductase activity (2 to 39 nmol min-1 mg-1) in crude extracts of C. thermoaceticum. Our results indicate that nitrate coordinately represses genes encoding enzymes and electron transport proteins in the Wood-Ljungdahl pathway and activates transcription of nitrate respiratory proteins. CO2 also appears to induce expression of the Wood-Ljungdahl pathway genes and repress nitrate reductase activity.  (+info)

Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. (2/1279)

A marked difference in hepatic activity of aldehyde oxidase between rats and monkeys was found to be responsible for the previously reported marked species difference in the metabolism of Zaleplon in vivo. In the postmitochondrial fractions, S-9s, from liver homogenates of these animals, Zaleplon was transformed in the presence of NADPH into the side chain oxidation product, N-desethyl-Zaleplon, and the aromatic ring oxidation product, 5-oxo-Zaleplon. In the rat S-9, N-desethyl-Zaleplon and 5-oxo-Zaleplon were a major and a very minor metabolites, respectively. However, in the monkey S-9, Zaleplon was transformed into 5-oxo-Zaleplon at a much higher rate than that for N-desethyl-Zaleplon formation. N-Desethyl-Zaleplon was formed in the monkey S-9 at a rate almost equal to that in the rat S-9. N-Desethyl-5-oxo-Zaleplon was formed at a minor rate only in the monkey S-9 through N-desethyl-Zaleplon as an obligatory intermediate. The hepatic activity for the formation of 5-oxo-Zaleplon in the monkey and rat was localized in cytosol and did not require NADPH. Sensitivity to various inhibitors and requirement of water as oxygen source, using H218O, strongly suggested that the hepatic cytosolic formation of 5-oxo-Zaleplon was mediated by aldehyde oxidase. N-Desethyl-Zaleplon was formed in the presence of NADPH by microsomes from the liver of rats and monkeys, and its formation was strongly suggested using various cytochrome P-450 inhibitors to be mediated by a number of cytochrome P-450 isoforms, such as 3A, 2C, and 2D subfamilies.  (+info)

A genetic linkage map of rat chromosome 9 with a new locus for variant activity of liver aldehyde oxidase. (3/1279)

A genetic linkage map of rat chromosome 9 consisting of five loci including a new biochemical marker representing a genetic variation of the activity of the liver aldehyde oxidase, (Aox) was constructed. Linkage analysis of the five loci among 92 backcross progeny of (WKS/Iar x IS/Iar)F1 x WKS/Iar revealed significant linkages between these loci. Minimizing crossover frequency resulted in the best gene order: Aox-D9Mit4-Gls-Cryg-Tp53l1. The homologues of the Cryg, Gls, and Aox genes have been mapped on mouse chromosome 1 and human chromosome 2q. The present findings provide further evidence for the conservation of synteny among these regions of rat, mouse, and human chromosomes.  (+info)

Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. (4/1279)

Pseudomonas aeruginosa ATCC 17933 grown aerobically on ethanol produces a soluble cytochrome c550 together with a quinoprotein ethanol dehydrogenase. A 3.2 kb genomic DNA fragment containing the gene encoding cytochrome c550 was cloned and sequenced. Two other complete and two truncated ORFs were also identified. A truncated ORF encoding the quinoprotein ethanol dehydrogenase (exaA) was found upstream of the cytochrome c550 gene (exaB) and in reverse orientation. An ORF encoding a NAD(+)-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c550 gene and in the same orientation. Another ORF showed similarity to the pqqA gene and a truncated ORF similarity to the pqqB gene, both involved in the biosynthesis of the prosthetic group PQQ. The organization of these genes was found to be different from the well-studied methanol oxidation system in methylotrophic bacteria. The deduced amino acid sequence of cytochrome c550 from P. aeruginosa showed some similarity to cytochrome c6 of the alga Chlamydomonas reinhardtii and the haem domain of quinohaemoprotein alcohol dehydrogenases of acetic acid bacteria, but no similarity to the soluble cytochrome cL of the quinoprotein methanol oxidation system of methylotrophs could be detected. A mutant of P. aeruginosa with an interrupted cytochrome c550 gene was unable to grow on ethanol, which proves that cytochrome c550 is an essential component of the ethanol oxidation system in this organism.  (+info)

Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (5/1279)

Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3.  (+info)

Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver. (6/1279)

A barbiturate-sensitive aldehyde reductase was purified to homogeneity from rat liver and shown to metabolize the cancer-chemotherapeutic antibiotic daunorubicin. The aldehyde reductase may have important roles in the metabolism of exogeneous drugs as well as the aldehyde derivatives of the biogenic amines.  (+info)

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (7/1279)

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)

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (8/1279)

In order to investigate the effects of trace elements on different metabolic pathways, the thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been cultivated on various carbon substrates in the presence and absence of molybdate. When grown on glucose (but neither on glutamate nor casein hydrolysate) as sole carbon source, the lack of molybdate results in serious growth inhibition. By analysing cytosolic fractions of glucose adapted cells for molybdenum containing compounds, an aldehyde oxidoreductase was detected that is present in the cytosol to at least 0.4% of the soluble protein. With Cl2Ind (2,6-dichlorophenolindophenol) as artificial electron acceptor, the enzyme exhibits oxidizing activity towards glyceraldehyde, glyceraldehyde-3-phosphate, isobutyraldehyde, formaldehyde, acetaldehyde and propionaldehyde. At its pH-optimum (6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant. The protein has an apparent molecular mass of 177 kDa and consists of three subunits of 80.5 kDa (alpha), 32 kDa (beta) and 19.5 kDa (gamma). It contains close to one Mo, four Fe, four acid-labile sulphides and four phosphates per protein molecule. Methanol extraction revealed the existence of 1 FAD per molecule and 1 molybdopterin per molecule, which was identified as molybdopterin guanine dinucleotide on the basis of perchloric acid cleavage and thin layer chromatography. EPR-spectra of the aerobically prepared enzyme exhibit the so-called 'desulpho-inhibited'-signal, known from chemically modified forms of molybdenum containing proteins. Anaerobically prepared samples show both, the signals arising from the active molybdenum-cofactor as well as from the two [2Fe-2S]-clusters. According to metal-, cofactor-, and subunit-composition, the enzyme resembles the members of the xanthine oxidase family. Nevertheless, the melting point and long-term thermostability of the protein are outstanding and perfectly in tune with the growth temperature of S. acidocaldarius (80 degrees C). The findings suggest the enzyme to function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylated Entner-Doudoroff pathway and thereby may attribute a new physiological role to this class of enzyme.  (+info)

1FFU: The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
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.
CP000667.PE356 Location/Qualifiers FT CDS 407150..408517 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0356" FT /product="glutamyl-tRNA reductase" FT /EC_number="1.2.1.70" FT /note="PFAM: glutamyl-tRNA reductase; Shikimate/quinate FT 5-dehydrogenase" FT /db_xref="EnsemblGenomes-Gn:Strop_0356" FT /db_xref="EnsemblGenomes-Tr:ABP52841" FT /db_xref="GOA:A4X1U1" FT /db_xref="InterPro:IPR000343" FT /db_xref="InterPro:IPR006151" FT /db_xref="InterPro:IPR015895" FT /db_xref="InterPro:IPR015896" FT /db_xref="InterPro:IPR036291" FT /db_xref="InterPro:IPR036343" FT /db_xref="InterPro:IPR036453" FT /db_xref="UniProtKB/Swiss-Prot:A4X1U1" FT /protein_id="ABP52841.1" FT /translation="MKLLVVGASYRTAPVAALERLTVAPADLSRVLTRLVAQPYVSEAV FT LVSTCNRVEVYAVVSGFHGGLGDICAVLAESTGCQPAALADHLYVHFDAAAVNHVFRVA FT VGLDSMVVGEAQILGQLRDAYHWASEAETVGRLLHELMQQALRVGKRAHSETGIDRAGQ FT SVVTAALGLATELLHSDLACRPALVVGAGAMGSLGVATLARLGAGPVSVTNRGVDRAIR FT LAESYGATAVPIADLTATLSTVDIVVAATAAPEAVLTRAVVTQALAGRNPSRGPLVLLD FT ...
Description of disease Fatty aldehyde dehydrogenase deficiency. Treatment Fatty aldehyde dehydrogenase deficiency. Symptoms and causes Fatty aldehyde dehydrogenase deficiency Prophylaxis Fatty aldehyde dehydrogenase deficiency
Shop Alcohol-forming fatty acyl-CoA reductase ELISA Kit, Recombinant Protein and Alcohol-forming fatty acyl-CoA reductase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
A 3.2 kb fragment of an indigenous Anabaena azollae plasmid was isolated and fully sequenced. Sequence analysis identified an open reading frame of 1110-bp that showed high similarity (56-71%) with glutathione dependent formaldehyde dehydrogenase genes (gdfaldh) from various bacteria. The identity of the gene was confirmed by expressing the gene in Escherichia coli with a pET-32 (a) vector followed by enzyme assay. Adjacent to the gdfaldh a second gene was detected that showed high similarity (53%) with an S-formylglutathione hydrolase (fgh) gene from the methylotrophic bacterium Paracoccus denitrificans. The presence of gdfaldh and fgh-like genes adjacent to each other may suggest that the corresponding gene products interact in a common metabolic pathway involved in removing exogenous or endogenous formaldehyde ...
Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. Early on in evolution, an effective method for eliminating both endogenous and exogenous formaldehyde was important and this ...
Birds clean and lubricate their feathers with waxes that are produced in the uropygial gland, a holocrine gland located on their back above the tail. The type and the composition of the secreted wax esters are dependent on the bird species, for instance the wax ester secretion of goose contains branched-chain fatty acids and unbranched fatty alcohols, whereas that of barn owl contains fatty acids and alcohols both of which are branched. Alcohol-forming fatty acyl-CoA reductases (FAR) catalyze the reduction of activated acyl groups to fatty alcohols that can be esterified with acyl-CoA thioesters forming wax esters. cDNA sequences encoding fatty acyl-CoA reductases were cloned from the uropygial glands of barn owl (Tyto alba), domestic chicken (Gallus gallus domesticus) and domestic goose (Anser anser domesticus). Heterologous expression in Saccharomyces cerevisiae showed that they encode membrane associated enzymes which catalyze a NADPH dependent reduction of acyl-CoA thioesters to fatty alcohols. By
ENCODES a protein that exhibits fatty-acyl-CoA reductase (alcohol-forming) activity (ortholog); INVOLVED IN ether lipid biosynthetic process (ortholog); glycerophospholipid biosynthetic process (ortholog); long-chain fatty-acyl-CoA metabolic process (ortholog); ASSOCIATED WITH Peroxisomal Fatty Acyl-CoA Reductase 1 Disorder (ortholog); FOUND IN integral component of peroxisomal membrane (ortholog); peroxisome (ortholog)
Figure 2. A, The observed NADP+ in the binding pocket of SbCCR1. NADP+ and all interacting residues are represented as stick models. The backbone of SbCCR1 is represented as a ribbon diagram, and dashed lines represent hydrogen bonds or ionic interactions. All residues that contribute to NADP+ binding are labeled according to their single-letter abbreviations and numbered according to sequence positions. The catalytic triad, composed of Ser-149, Tyr-183, and Lys-187, is in close proximity to the nicotinamide ring and serves to promote hydride transfer to hydroxycinnamoyl-CoA substrates. B, Coniferaldehyde docked into the putative phenylpropanoid-binding region of SbCCR1. The backbone of SbCCR1 is represented by a ribbon diagram, with protruding side chains that contribute to coniferaldehyde binding modeled as sticks. Coniferaldehyde, which is the product of the reaction with the preferred substrate feruloyl-CoA, is shown in gray. Kinetics experiments with T154A and Y310F mutants revealed that ...
Fingerprint Dive into the research topics of Enhancement of activity and stability of the formaldehyde dehydrogenase by immobilizing onto phenyl-functionalized mesoporous silica. Together they form a unique fingerprint. ...
In contrast to the published description of S. mucosus [7], which suggests a strictly aerobic and chemoheterotrophic metabolism, the genome reveals an astonishing metabolic versatility. Besides genes for the degradation of organic substrates, we also found genes encoding enzymes for the utilization of alternative electron donors enabling facultative lithotrophic growth: a Sox multienzyme complex encoded by the genes salmuc_00587 - 00597 could be utilized for the oxidation of thiosulfate to sulfate, while molecular hydrogen may be utilized as electron donor by a multimeric uptake hydrogenase of the [NiFe]-type (salmuc_04814 - 04830). A further potential substrate is carbon monoxide, which might be oxidized by an aerobic-type carbon monoxide dehydrogenase encoded by the genes salmuc_05576 - 05578. Additional genes encoding subunits of carbon monoxide dehydrogenase were found dispersed at several sites in the genome. The metabolic plasticity of this species is further reflected in a multiple ...
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Previous studies have shown that the steady state mRNA levels of RALDH2 are significantly increased during recovery from induced myopia.17 In the present study, RALDH2 protein expression was compared in 4-day control (C) and recovering (R) eyes by Western blot with chick specific anti-RALDH2 antibodies (Fig. 4A). The 4-day time point was used since RALDH2 mRNA levels were shown previously to be significantly increased at this time point.17 Quantification of the band intensities demonstrated that RALDH2 protein levels were significantly increased in 4-day recovering choroids (3.65 ± 0.45 RALDH2 IOD/8-mm punch) compared to controls (1.62 ± 0.31 RALDH2 IOD/8-mm punch; P , 0.05, paired t-test; n = 4) (Figs. 4A, 4B). RALDH2 protein expression in 8-mm posterior choroidal punches was examined subsequently at several time points throughout the recovery process (0 hours to 15 days; Fig. 5). RALDH2 was detected in control and recovering choroids at all time points examined as an approximately 55 kDa ...
Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Jaspers, M. H. J.; Pflanz, R.; Riedel, D.; Kawelke, S.; Feussner, I.; Schuh, R.: The fatty acyl-CoA reductase Waterproof mediates airway clearance in Drosophila. Developmental Biology 385 (1), pp. 23 - 31 (2014 ...
Complete information for FAR2P1 gene (Pseudogene), Fatty Acyl-CoA Reductase 2 Pseudogene 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Formaldehyde is an ubiquitous air pollutant in indoor and outdoor atmospheres. Possible sources are disinfectants, paints, resins, particle boards, tobbaco smoke and combustion processes. It is used in large amounts in the plastics manufacturing industry. The German government has set the maximum allowed workspace concentration, MAK-value, to 0.5 ppm (v/v). For non-occupational indoor environments 0.1 ppm (v/v) are recommended. Traditional systems for the determination of formaldehyde in air consist of a sampling step (e.g. washer, adsorber) followed by a quantification step (optical, enzymatic, or titration). There are only few reports where formaldehyde is determined directly in the gas phase in one step. We present an electrochemical enzyme biosensor that can detect gaseous formaldehyde directly without a separate sampling step. NAD-dependent formaldehyde dehydrogenase converts formaldehyde to formic acid. The formed NADH is oxidised by a redox mediator (e.g. naphthoquinone). The latter is ...
Anna was looking forward to receiving her third year trophy, and she was worried about what would happen to her partner in the show without her. Every co-dependent, desire-to-please/fix/make OK alarm sounded in my body; I wanted my girls there even if I was sweating it out and pushing George into the world at that very moment! I did not want to disappoint them... but if Emre was with me as labor coach, was that feasible? Practical? Prudent? Yes, I had a dance mom on standby, willing to come and pick them up and do their hair... but I dont know her well, neither do my girls, and while Anna would be old enough to handle this upheaval in stride, would little Gianna manage? What if one of them got hurt or fell ill while backstage? What to do!? My husband helped me to discern that I was stressing out over the possibility of separation; the actual separation into unchartered territory would create more anxiety for me during labor and that was exactly what I didnt need. Furthermore, my concerns were ...
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Looking for online definition of retinaldehyde dehydrogenase 1 in the Medical Dictionary? retinaldehyde dehydrogenase 1 explanation free. What is retinaldehyde dehydrogenase 1? Meaning of retinaldehyde dehydrogenase 1 medical term. What does retinaldehyde dehydrogenase 1 mean?
TY - JOUR. T1 - Betaine aldehyde dehydrogenase in plants. AU - Fitzgerald, T. L.. AU - Waters, D. L E. AU - Henry, R. J.. PY - 2009/3. Y1 - 2009/3. N2 - Plant betaine aldehyde dehydrogenases (BADHs) have been the target of substantial research, especially during the last 20 years. Initial characterisation of BADH as an enzyme involved in the production of glycine betaine (GB) has led to detailed studies of the role of BADH in the response of plants to abiotic stress in vivo, and the potential for transgenic expression of BADH to improve abiotic stress tolerance. These studies have, in turn, yielded significant information regarding BADH and GB function. Recent research has identified the potential for BADH as an antibiotic-free marker for selection of transgenic plants, and a major role for BADH in 2-acetyl-1-pyrroline-based fragrance associated with jasmine and basmati style aromatic rice varieties.. AB - Plant betaine aldehyde dehydrogenases (BADHs) have been the target of substantial ...
Preparations of sheep liver cytoplasmic aldehyde dehydrogenase obtained by published methods were found by analytical isoelectric focusing in the pH range 5-8 to contain 5-10% by weight of the mitochondrial aldehyde dehydrogenase. Under the conditions used the pI of the cytoplasmic enzyme is 6.2 and that of the mitochondrial enzyme 6.6. The mitochondrial enzyme can be removed from the preparation by selective precipitation of the cytoplasmic enzyme with (NH4)2SO4. Kinetic experiments and inhibition experiments with disulfiram show that the properties of the two sheep liver enzymes are so different that the presence of 10% mitochondrial enzyme in preparations of the cytoplasmic enzyme can introduce serious errors into results. Our results suggest that the presence of 10 microM-disulfiram in assays may completely inactivate the pure cytoplasmic enzyme. This result is in contrast with a previous report [kitson (1978) Biochem. U. 175, 83-90]. ...
Introduction: Diminished NO production and altered NO bioavailability promote vascular inflammation and atherosclerosis. S-nitrosoglutathione reductase (GSNOR) controls cellular NO balance by degrading S-nitrosoglutathione (GSNO), which is a major source of nitric oxide (NO) bioactivity. GSNOR inhibition increases protein S-nitrosylation and potentiates NO action. The role of GSNOR in vascular inflammation is undefined, and the purpose of our investigation was to determine if GSNOR targeting dampens inflammation and reduces atherosclerosis.. Methods and results: We evaluated vascular inflammation and atherosclerosis in wild type (WT) and GSNOR-deficient (GSNOR-/-) mice. TNF-induced NFκB activation was reduced by 40% (p,0.05) in endothelial cells (ECs) isolated from GSNOR-/- compared to WT mice, which was accompanied by attenuated expression of P-selectin, E-selectin, and VCAM-1 (,34% reduction, p,0.05). Decreased EC adhesion molecule expression led to a 45% reduction in leukocyte rolling in the ...
Data are presented concerning the basic metabolism sites, the reaction paths crossing in them and regulatory and toxical effect of formaldehyde and nitric oxide being mediated through them. In particular, they include: glutathione-formaldehyde-dependent dehydrogenase path of S-nitrosoglutathione reduction, semi-carbaside-sensitive amino-oxidase (SSAO) and NO-synthase systems; transformation of thioproline and metallothioneines, including nitrosation reactions. Possibilities of hexamethylenetetramine synthesis in the organism as well as its metabolism in conditions of formaldehyde hyperproduction and nitrosative stress are discussed. The role of metabolism sites, common for formaldehyde and nitric oxi-de, in the mechanisms of toxical effect of these compounds and development of pathologic states is considered.. Key words: nitric oxide, formaldehyde, glutathione-dependent formaldehyde dehydrogenase, S-nitrosoglutathione reductase, semicarbaside-sensitive aminoxidase, thioproline, hexamethy-lene ...
Expression of alcohol-forming fatty acyl-CoA reductases in E. coli can result in the biosynthesis of fatty alcohols from endogenous E. coli fatty acids, but the levels were quite low [19]. To improve the production of fatty alcohols, Steen et al. carried out a further genetic modification of E. coli, and achieved an increased titer (~60 mg/L) of the medium chain fatty alcohols (C12 or C14 alcohols) [3]. In their strategy, they employed thioesterases with different substrate specificities to tailor the composition of the FFAs, and used the aldehyde-forming fatty acyl-CoA reductase Acr1 for the conversion of fatty acyl-CoAs to fatty aldehydes. The synthesized fatty aldehydes can be further converted to fatty alcohols by an unknown alcohol dehydrogenase/aldehyde reductase of E. coli [6].. However, Steen et al. just obtained a small quantity of C16/18 alcohol, though they used the thioesterase TesA, which was capable of yielding a large proportion of C16/18 FFA [3]. As aforementioned, expression of ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Potassium atom in PDB 2wme: Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa
TY - JOUR. T1 - Levels of retinoic acid and retinaldehyde dehydrogenase expression in eyes of the Mitf-vit mouse model of retinal degeneration.. AU - Duncan, T.. AU - Swint, C.. AU - Smith, S. B.. AU - Wiggert, B. N.. PY - 1999/6/28. Y1 - 1999/6/28. N2 - PURPOSE: Several reports have characterized the retinal degeneration observed in the Mitf(vit) mutant mouse. Despite these reports, the factor(s) that may cause or modulate the degeneration still are not well defined; however, it is known that the photoreceptors of Mitf(vit) mice die through an apoptotic mechanism. We reported previously that retinoid metabolism in the RPE of Mitf(vit)++ mice is perturbed. Retinoids regulate genes via the RAR and RXR nuclear receptor pathway that are involved in numerous cellular responses including apoptosis. It is possible that retinoic acid (RA) modulates the retinal degeneration observed in the Mitf(vit) mice. The purpose of this study was to evaluate the levels of RA in whole eyes, as well as its ...
In 1957, Sjögren and Larsson described a cohort of Swedish patients with an unusual combination of symptoms that included of congenital ichthyosis, intellectual disability, and spastic diplegia or tetraplegia. Family studies indicated that Sjögren-Larsson syndrome (SLS) was a genetic disorder with autosomal recessive inheritance.
Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.
Carbon monoxide dehydrogenases (CODHs) catalyze the reversible oxidation of carbon monoxide by reaction with water to yield carbon dioxide, two protons, and two electrons. Two principal types of CODHs can be distinguished. Ni,Fe-containing CODHs contain a [NiFe(4)S(4)OH( x )] cluster within their active site, to which the direct binding of the substrates water and carbon dioxide has been revealed by protein X-ray crystallography. n-Butyl isocyanide is a slow-turnover substrate of CODHs, whose oxidation at the active site shows several parallels to the oxidation of carbon monoxide. Here, we report the crystal structure of CODH-II from Carboxydothermus hydrogenoformans resulting from the enzymatic oxidation of n-butyl isocyanide to n-butyl isocyanate at its active site cluster. The high resolution of the structure (d (min) = 1.28 A) revealed n-butyl isocyanate bound to the active site cluster and identified a novel type of Ni-C bond in CODHs. The structure suggests the occurrence of tetrahedral in ...
Heme-dependent feedback inhibition of rate-limiting ALA-synthesis of plant tetrapyrrole biosynthesis depends on binding of heme to glutamyl-tRNA reductase-binding protein.
The invention provides a method of chemically-mechanically polishing a substrate comprising tungsten through use of a composition comprising a tungsten etchant, an inhibitor of tungsten etching, and water, wherein the inhibitor of tungsten polishing is a polymer, copolymer, or polymer blend comprising at least one repeating group comprising at least one nitrogen-containing heterocyclic ring or a tertiary or quaternary nitrogen atom. The invention further provides a chemical-mechanical polishing composition particularly useful in polishing tungsten-containing substrates.
Betaine aldehyde dehydrogenase (BADH) is important enzyme which plays a dual role in cereals. It acts as an osmoprotectant and has an important role during abiotic stress. In addition it also influences the fragrance in rice. Therefore, this gene has both agronomical and breeding values. An 8pb deletion in exon 7 cause a premature termination codon in BADH2 resulting a mutate badh2 allele; which ultimately elevates the level of 2AP leading fragrance in fragrant rice (Bradbury et al., 2008). Unlike rice wheat is a hexaploid and has two BADH homologs i.e. BADH1 and BADH2. Our genomic data shows that there are three alleles for BADH homologs. One allele is present in the progenitors and these indicates that, these allele is inheritate from each of the progenitors during polyploidy in hexaploid wheat. Our data show that a total of 4 and 14 SNPs are present among the genomes in BADH2 and BADH1respectivly. Investigation on two different tissues (i.e. leaves and seeds), at two different time point (i.e. 14 DPA
S-hydroxymethylglutathione dehydrogenase from Paecilomyces variotii No. 5 strain (NBRC 109023), isolated as a formaldehyde-degrading fungus, was purified by a procedure that included ammonium sulfate precipitation, DEAE-Sepharose and hydroxyapatite chromatography and isoelectrofocusing. Approximately 122-fold purification was achieved with a yield of 10.5%. The enzyme preparation was homogeneous as judged by sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE). The molecular mass of the purified enzyme was estimated to be 49 kDa by SDS-PAGE and gel filtration, suggesting that it is a monomer. Enzyme activity was optimal at pH 8.0 and was stable in the range of pH 7.0-10. The optimum temperature for activity was 40°C and the enzyme was stable up to 40°C. The isoelectric point was pH 5.8. Substrate specificity was very high for formaldehyde. Besides formaldehyde, the only aldehyde or alcohol tested that served as a substrate was pyruvaldehyde. Enzyme activity was enhanced by several divalent
Supported Au catalysts have been studied extensively for CO oxidation. These catalysts are known to catalyze this reaction even at sub-ambient temperatures. While recent literature demonstrates catalytic activity of gold nanoparticles |2 |nm, the next stage in fine tuning this catalysis process is to develop gold clusters prepared with atomic precision. Such atomically precise gold catalysts supported on TiO2 hitherto have not been investigated for CO oxidation. The main objective of this work is to synthesize atomically-precise Au38 clusters in a flask-based method using principles of wet chemistry, to characterize these clusters using various advanced spectroscopic techniques, and to test these clusters as potential catalytic materials for CO oxidation. Furthermore, we have tested TiO2-supported Au38 clusters and a commercially purchased Au/TiO2 catalyst for CO oxidation at 30 °C and 60 °C, and used DRIFTS as a probe spectroscopic technique to correlate kinetics with the mechanism occurring on the
ID ADHE_ECOLI Reviewed; 891 AA. AC P0A9Q7; P17547; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 22-NOV-2017, entry version 109. DE RecName: Full=Aldehyde-alcohol dehydrogenase; DE Includes: DE RecName: Full=Alcohol dehydrogenase; DE Short=ADH; DE EC=1.1.1.1; DE Includes: DE RecName: Full=Acetaldehyde dehydrogenase [acetylating]; DE Short=ACDH; DE EC=1.2.1.10; DE Includes: DE RecName: Full=Pyruvate-formate-lyase deactivase; DE Short=PFL deactivase; GN Name=adhE; Synonyms=ana; OrderedLocusNames=b1241, JW1228; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11. RX PubMed=2695398; DOI=10.1016/0378-1119(89)90483-6; RA Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.; RT "Cloning and sequence analysis of the fermentative alcohol- RT dehydrogenase-encoding gene of ...
Interest in the biochemistry of nickel has been stimulated by recent discoveries of its essentiality to various microorganisms, plants, and animals and of the existence of several nickel metalloenzymes in plants and microorganisms. Signs of nickel deprivation have been described for six animal species-chick, cow, goat, minipig, rat, and sheep. Included among the more consistent signs of deficiency in mammals are depressed growth, unthriftiness characterized by rough hair coat, and an altered iron metabolism leading to depressed hematopoiesis. The predominant sign of nickel deficiency for microorganisms is depressed growth, and for plants is depressed nitrogen utilization. In plants and microorganisms, nickel is known to function in several metalloenzymes including urease, several hydrogenases, and carbon monoxide dehydrogenase. In higher animals, the evidence showing that nickel is essential has not defined its metabolic function. The finding of nickel metalloenzymes in lower forms of life ...
S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate ...
J:104523 Ribes V, Wang Z, Dolle P, Niederreither K, Retinaldehyde dehydrogenase 2 (RALDH2)-mediated retinoic acid synthesis regulates early mouse embryonic forebrain development by controlling FGF and sonic hedgehog signaling. Development. 2006 Jan;133(2):351-61 ...
Antabuse, also called disulfiram, is a famous drug for the treatment of alcohol and drug addiction. Its working mechanism is based on inhibition of the acetaldehyde dehydrogenase (the enzyme responsible for the split of acetaldehyde- the enzyme, which helps to digest alcohol.
Further information can be found in the Supplemental Methods.. Animals. Mice were housed in a pathogen-free, temperature- and light-controlled animal facility under a 12-hour light/dark cycle. ALDH2-/- LDLR-/- mice were obtained by crossing ALDH2-/- mice (a gift from Jun Ren and Aijun Sun, Zhongshan Hospital affiliated with Fudan University, Shanghai, China) (37, 40) and LDLR-/- mice (Jackson Laboratory). ALDH2-/-APOE-/- mice were obtained by crossing ALDH2-/- mice and APOE-/- mice (Shanghai Model Organisms). All mice used in the present study were on a C57BL/6 background. For atherosclerotic study, 6-week-old mice were fed Western Diet (Research Diets, catalog D12079B) for 12 weeks or 26 weeks (26-week experiment was done in duplicate). The number of mice studied in each experiment is shown in the figure legends.. Cell culture. HEK 293T cell lines were purchased from the CAS Cell Bank and cultured in DMEM containing 10% FBS. Isolation of bone marrow-derived macrophages (BMDMs) followed a ...
mag:amb2922 K03738 aldehyde:ferredoxin oxidoreductase [EC:1.2.7.5] , (GenBank) Tungsten-containing aldehyde ferredoxin oxidoreductase (A) MSWTGKFLRIDLTNGSVKTEELNRAWARQYLGQRGLATKYFAEEVDPKVDPLSPANKMIF TTGPLTGTAASTGGRYSVVTKGPLTNCIACSNSGGFFGNELKNAGWDMIIVEGRSPKPVY LSIENETVEIRDAAEFWGKTVWETENGLKARHQDPMLRVATIGAAGEKGVLYACIVNDLH RAAGRSGVGAVMGSKNLKAIAVRGTRGVTVKDPDRFIKATIEQKKVLADNAVTGQGLPKY GTQVLMNVINEIGAMPTRNFKEVQFEGAHKISAEAMHEPRATDGKANLATNGACFGCTIA CGRISRMDPGHFSITSRPQYKEPSGGVEYEAAWAMGSDCGVDDLEACTFANFMCNEHGID PISFGSTLAAAMEMFEMGVITKEQTGGVELKFGSAEALVKMAELTGKGEGFGLELGQGSR RLCAKYGHPELSMTVKSQEFPAYDPRGIQGMGLTYATSNRGACHLRSYTVASEVLGIPFK SDPLATDGKAALVKAFQDATAAFDASGICIFTTFAWSLENLAPQIDAACEGEWTPEILLE VGERIWTLERQFNLAAGMTAADDTLPKRLLKDAAKTGPAKGLTSGLEKMLPEYYQLRGWT TDGVPTTETLKRLQLA ...
Semantic Scholar extracted view of Aldehyde dehydrogenase activity and level of dopamine in certain sections of the brain of rats preferring and refusing ethanol by Kharchenko Nk
Sci. Rep. Aldehyde dehydrogenase enzymes (ALDHs) are very common proteins involved in the oxidation of aliphatic and aromatic aldehydes to their corresponding…
Sjögren-Larsson syndrome presents with ichtyosis, spastic diplegia and cognitive deficits. It is caused by a deficiency of fatty aldehyde dehydrogenase. Treatments are limited to symptomatic therapies; for example, ziluteon (an inhibitor of 5-lipoxygenase) can reduce pruritus.. In a recent article, bezafibrate has been shown to induce the expression of the deficient protein in fibroblasts from some patients. This discovery could become of clinical importance ...
NCT 501 (CAS: 1802088-50-1)is a potent and selective theophylline-based inhibitor of aldehyde dehydrogenase 1A1 (ALDH1A1), inhibits hALDH1A1 with IC50 of 40 nM, typically shows better selectivity over other ALDH isozymes and other dehydrogenases (hALDH1B1
FUJIWARA Ken , DAVAADASH Bulgan , YATABE Megumi , KIKUCHI Motoshi , HORIGUCHI Kotaro , KUSUMOTO Kenji , KOUKI Tom , YASHIRO Takashi Medical molecular morphology : official journal of the Japanese Society for Clinical Molecular Morphology 41(3), 126-131, 2008-09-01 医中誌Web 参考文献20件 ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ... Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a ...
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 ethanol:acceptor oxidoreductase. This enzyme ... catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes ...
"Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry / FEBS. 271 (1): ...
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 ...
The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... In enzymology, a carboxylate reductase (EC 1.2.99.6) is an enzyme that catalyzes the chemical reaction an aldehyde + acceptor ... oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, tungsten. White H, Strobl G, Feicht R ...
... 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.. ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common ... H+ The 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP+, whereas its 3 products are long-chain acyl-CoA, ... is an enzyme that catalyzes the chemical reaction a long-chain aldehyde + CoA + NADP+ ⇌ {\displaystyle \rightleftharpoons } a ...
... the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin Oxidoreductase". ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Other names in common use include aldehyde dismutase, and cannizzanase. As of late 2007, only one structure has been solved for ... Kato N, Shirakawa K, Kobayashi H, Sakazawa C (1983). "The dismutation of aldehydes by a bacterial enzyme". Agric. Biol. Chem. ... The systematic name of this enzyme class is formaldehyde:formaldehyde oxidoreductase. ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include ... oxidoreductase. Two major classes of the carbon monoxide dehydrogenase (CODH) enzymes have been identified. CODH containing a ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is formylmethanofuran:acceptor oxidoreductase. This enzyme is also called ... formylmethanofuran:(acceptor) oxidoreductase. This enzyme participates in folate biosynthesis. It has 2 cofactors: molybdenum, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Mandal SK, Datta Chaudhuri B (1987). "Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental ... The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase. This ... Huang DY, Furukawa A, Ichikawa Y (1999). "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... T; Akaba, S; Oritani, T; Delarue, M; Bellini, C; Caboche, M; Koshiba, T (1998). "Higher activity of an aldehyde oxidase in the ... The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include ... Marion-Poll A, Caboche M, Kamiya Y, Koshiba T (1998). "Molecular cloning and characterization of aldehyde oxidases in ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (CoA-acetylating). This enzyme participates in ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme ...
... these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, ... This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. Some proteins of this family contain a potassium ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547-51. PMID 2498333 ... channel beta chain regulatory domain; these are reported to have oxidoreductase activity. AKR1 Steroidogenic enzyme Bohren KM, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating). Other names in common use include MtPDC (mitochondrial ... lipoamide 2-oxidoreductase (decarboxylating and, acceptor-acetylating), pyruvic acid dehydrogenase, and pyruvic dehydrogenase. ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase. Yagi T (October 1969). "Formate: ... cytochrome oxidoreductase of Desulfovibrio vulgaris". J. Biochem. Tokyo. 66 (4): 473-8. PMID 4982127. Yagi T (1979). " ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ...
The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H- ... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase. Structural studies[edit]. As of late 2007, ...
Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. ... Microsomal fatty aldehyde dehydrogenase catalyzes the oxidation of aliphatic aldehyde derived from ether glycerolipid ... Isolation of animal cell mutants defective in long-chain fatty aldehyde dehydrogenase. Sensitivity to fatty aldehydes and ... Identification of fatty aldehyde dehydrogenase in the breakdown of phytol to phytanic acid. Mol Genet Metab. 2004 May. 82(1):33 ...
In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin ... The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a ... Roy R, Dhawan IK, Johnson MK, Rees DC, Adams MW (2006-04-15). Handbook of Metalloproteins: Aldehyde Ferredoxin Oxidoreductase ( ...
Aldehyde ferredoxin oxidoreductase, N-terminal domain superfamily (IPR036503). Short name: Ald_Fedxn_OxRdtase_N_sf ... Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [PMID: 9242907] contain a tungsten cofactor and an 4Fe4S cluster ... Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.. Science 267 1463-9 1995 ... formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from ...
Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ...
Three different types of tungsten-containing aldehyde oxidizing enzymes aldehyde ferredoxin oxidoreductase (AOR), formaldehyde ... Detailed kinetic analyses of FOR indicate that C4 - C6 dialdehyde or acid-substituted aldehyde may serve as the physiological ... ferredoxin oxidoreductase (FOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) have previously been isolated ...
eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (N) ... eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (A) ... aldehyde oxidoreductase, ethanolamine utilization protein (P77445). Identification. Name:. aldehyde oxidoreductase, ...
ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. The identification of the gene from ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ... Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid. Author. Venkitasubramanian Padmesh, Daniels Lacy, Das ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ATP and NADPH dependent reduction of carboxylic acids ...
... the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase ... the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase ...
Aldehyde Oxidoreductases. LinkOut - more resources. Medical. *Genes and Gene Therapy - MedlinePlus Health Information ... Aldehyde oxidase as a cell marker for internal organs in Drosophila melanogaster.. Janning W. ...
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. By MK Chan, S Mukund, A Kletzin, MW ...
Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1). ... Aldehyde ferredoxin oxidoreductase, domains 2 & 3 family protein. Escherichia coli 1-176-05_S3_C2. Loading... ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC ...
... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... Zhang, Y.; Li, Y.; Du, C.; Liu, M.; Cao, Z. Inactivation of aldehyde dehydrogenase: A key factor for engineering 1,3- ... By inactivating aldehyde dehydrogenase (ADH), the enzyme responsible for ethanol formation in K. pneumoniae YMU2, less ethanol ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ... Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a ...
Alcohol Oxidoreductases); EC 1.1.- (glycolic acid dehydrogenase); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde ...
Aldehyde Oxidoreductases); EC 1.2.99.2 (carbon monoxide dehydrogenase); P6YC3EG204 (Vitamin B 12). ... NADPH Oxidoreductases); EC 1.6.4.- (thioredoxin glutathione reductase); K848JZ4886 (Cysteine). ...
Aldehyde Oxidoreductases / genetics * Aldehyde Oxidoreductases / metabolism* * Chloroplasts / physiology* * Esters * Metabolic ...
The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and ...
Classification: OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A)). *Organism(s): Escherichia coli (strain K12) ...
Classification: OXIDOREDUCTASE (NAD(A)-ALDEHYDE(D)). *Organism(s): Homo sapiens. *Deposited: 1983-06-20 Released: 1983-10-27 ...
... 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.. ...
Aldehyde Oxidoreductases / genetics* * Amino Acid Sequence * Bacterial Proteins / genetics* * Bacterial Proteins / metabolism ...
Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With unknown physiological acceptors. ... Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the ... Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from ... Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. ...
Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With NAD+ or NADP+ as acceptor. ... an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+ [RN:R01486]. ... The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit ...
... aldehyde ferredoxin oxidoreductase (AOR) (17), and tungsten oxidoreductases of unknown function WOR4 and WOR5. The clade ... Tungsten-dependent aldehyde oxidoreductase: a new family of enzymes containing the pterin cofactor. Metal Ions Biol Syst 39:673 ... Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus. J Bacteriol 192:4143-4152. doi: ... Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267:1463-1469. doi:10.1126/ ...
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray ...