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)
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
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
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).
Oxidoreductases that are specific for KETONES.
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.
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.
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
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).
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.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC (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 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.
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.
A kingdom of hyperthermophilic ARCHAEA found in diverse environments.
A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.
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.
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.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC
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.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Ecosystem and environmental activities, functions, or events.
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
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)
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.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC was formerly listed as EC and EC
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
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.
(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
Oxidoreductases that are specific for ALDEHYDES.
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)
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)
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)
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)
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
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.
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.
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.
Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.
Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
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.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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 and EC
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.
The space between the inner and outer membranes of a cell that is shared with the cell wall.
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.
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.
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.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
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.
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
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Proteins found in any species of bacterium.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Compounds containing the -SH radical.
Proteins found in the PERIPLASM of organisms with cell walls.
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.
Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.
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.
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)
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.
Compounds based on fumaric acid.
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.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC
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)
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
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.
The rate dynamics in chemical or physical systems.
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)
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.
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.
The functional hereditary units of BACTERIA.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
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.
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)
An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC
Proteins prepared by recombinant DNA technology.
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.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
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).
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.
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.
A species of gram-positive bacteria that is a common soil and water saprophyte.
The relationships of groups of organisms as reflected by their genetic makeup.
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.
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.
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)
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.
Proteins obtained from ESCHERICHIA COLI.
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.
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.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
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.
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.
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.
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)
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.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
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.
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)
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).
Life or metabolic reactions occurring in an environment containing oxygen.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
Proteins found in any species of fungus.
Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed)
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
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.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
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.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Mutagenesis where the mutation is caused by the introduction of foreign DNA sequences into a gene or extragenic sequence. This may occur spontaneously in vivo or be experimentally induced in vivo or in vitro. Proviral DNA insertions into or adjacent to a cellular proto-oncogene can interrupt GENETIC TRANSLATION of the coding sequences or interfere with recognition of regulatory elements and cause unregulated expression of the proto-oncogene resulting in tumor formation.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
The genetic complement of a BACTERIA as represented in its DNA.
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
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.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
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.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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).
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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.
The sum of the weight of all the atoms in a molecule.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Elements of limited time intervals, contributing to particular results or situations.

Profound variation in dihydropyrimidine dehydrogenase activity in human blood cells: major implications for the detection of partly deficient patients. (1/8900)

Dihydropyrimidine dehydrogenase (DPD) is responsible for the breakdown of the widely used antineoplastic agent 5-fluorouracil (5FU), thereby limiting the efficacy of the therapy. To identify patients suffering from a complete or partial DPD deficiency, the activity of DPD is usually determined in peripheral blood mononuclear cells (PBM cells). In this study, we demonstrated that the highest activity of DPD was found in monocytes followed by that of lymphocytes, granulocytes and platelets, whereas no significant activity of DPD could be detected in erythrocytes. The activity of DPD in PBM cells proved to be intermediate compared with the DPD activity observed in monocytes and lymphocytes. The mean percentage of monocytes in the PBM cells obtained from cancer patients proved to be significantly higher than that observed in PBM cells obtained from healthy volunteers. Moreover, a profound positive correlation was observed between the DPD activity of PBM cells and the percentage of monocytes, thus introducing a large inter- and intrapatient variability in the activity of DPD and hindering the detection of patients with a partial DPD deficiency.  (+info)

Dihydropyrimidine dehydrogenase deficiency and fluorouracil-related toxicity. (2/8900)

Dihydropyrimidine dehydrogenase (DPD) is the initial and rate-limiting enzyme of 5-fluorouracil (5-FU) catabolism. We report lymphocytic DPD data concerning a group of 53 patients (23 men, 30 women, mean age 58, range 36-73), treated by 5-FU-based chemotherapy in different French institutions and who developed unanticipated 5-FU-related toxicity. Lymphocyte samples (standard collection procedure) were sent to us for DPD determination (biochemical method). Among the whole group of 53 patients, 19 had a significant DPD deficiency (DD; below 150 fmol min(-1) mg(-1) protein, i.e. less than 70% of the mean value observed from previous population study). There was a greater majority of women in the DD group (15 out of 19, 79%) compared with the remaining 34 patients (15 out of 34, 44%, P<0.014). Toxicity was often severe, leading to patient death in two cases (both women). The toxicity score (sum of WHO grading, theoretical range 0-20) was twice as high in patients with marked DD (below 100 pmol min(-1) mg(-1) protein, n = 11, mean score = 13.2) compared with patients with moderate DD (between 150 and 100 pmol min(-1) mg(-1) protein, n = 8, mean score = 6.8), P = 0.008. In the DD group, there was a high frequency of neurotoxic syndromes (7 out of 19, 37%). The two deceased patients both had severe neurotoxicity. The occurrence of cardiac toxicity was relatively rare (1 out of 19, 5%). These data suggest that women are particularly prone to DPD deficiency and allow a more precise definition of the DD toxicity profile.  (+info)

Phase I study of eniluracil, a dihydropyrimidine dehydrogenase inactivator, and oral 5-fluorouracil with radiation therapy in patients with recurrent or advanced head and neck cancer. (3/8900)

5-Fluorouracil (5-FU) is an effective enhancer of radiation therapy (RT) in head and neck cancers. Due to rapid, predominantly hepatic metabolism by dihydropyrimidine dehydrogenase (DPD) and suggested clinical benefit from prolonged drug exposure, 5-FU is commonly given by continuous infusion. Eniluracil is a novel DPD-inactivator designed to prolong the half-life of 5-FU and provide sustained plasma concentrations of 5-FU with oral dosing. We conducted a Phase I study of the safety and efficacy of eniluracil given with oral 5-FU in patients receiving concurrent RT for recurrent or advanced squamous cell carcinomas of the head and neck. Thirteen patients with recurrent, metastatic, or high-risk (defined as an expected 2-year survival rate of <10%) head and neck cancer were enrolled and treated with concomitant chemoradiotherapy on an every-other-week schedule. Eniluracil at a fixed dose [20 mg twice a day (BID)] was given for 7 consecutive days (days 1-7). 5-FU and RT were given on 5 consecutive days (days 2-6). One patient was treated with once-daily RT (2.0 Gy fractions). The remaining patients received hyperfractionated RT (1.5-Gy fractions BID). The initial dose of 5-FU was 2.5 mg/m2 given BID. Dose escalation in patient cohorts was scheduled at 2.5-mg/m2 increments, with intrapatient dose escalation permitted. Lymphocyte DPD activity and serum 5-FU and uracil concentrations were monitored during two cycles. DPD activity was completely or nearly completely inactivated in all patients. Sustained, presumed therapeutic concentrations of 5-FU were observed at a dose of 5.0 mg/m2 given BID. Cumulative dose-limiting myelosuppression (both neutropenia and thrombocytopenia) was observed during the fourth and fifth cycles following administration of 5.0 mg/m2 5-FU BID. One patient died of neutropenic sepsis during cycle 4. Other late cycle toxicities included diarrhea, fatigue, and mucositis. Grade 3 mucositis was observed in 4 patients, but no grade 4 mucositis or grade 3 or 4 dermatitis was observed. A second patient death occurred during cycle 1 of treatment. No specific cause of death was identified. The study was subsequently discontinued. Cumulative myelosupression was the significant dose-limiting toxicity of oral 5-FU given with the DPD-inactivator eniluracil on an every-other-week schedule. Clinical radiation sensitization was not observed, based on the absence of dose-limiting mucositis and dermatitis. Alternative dosing schedules need to be examined to determine the most appropriate use of eniluracil and 5-FU as radiation enhancers.  (+info)

Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe. (4/8900)

We have investigated the extent to which functional expression of the plant alternative oxidase (from Sauromatum guttatum) in Schizosaccharomyces pombe affects yeast growth. When cells are cultured on glycerol, the maximum specific growth rate is decreased from 0.13 to 0.11 h-1 while growth yield is lowered by 20% (from 1. 14 x 10(8) to 9.12 x 10(7) cells ml-1). Kinetic studies suggest that the effect on growth is mitochondrial in origin. In isolated mitochondria we found that the alternative oxidase actively competes with the cytochrome pathway for reducing equivalents and contributes up to 24% to the overall respiratory activity. Metabolic control analysis reveals that the alternative oxidase exerts a considerable degree of control (22%) on total electron flux. Furthermore, the negative control exerted by the alternative oxidase on the flux ratio of electrons through the cytochrome and alternative pathways is comparable with the positive control exerted on this flux-ratio by the cytochrome pathway. To our knowledge, this is the first paper to report a phenotypic effect because of plant alternative oxidase expression. We suggest that the effect on growth is the result of high engagement of the non-protonmotive alternative oxidase in yeast respiration that, consequently, lowers the efficiency of energy conservation and hence growth.  (+info)

Analysis of the nitrous oxide reduction genes, nosZDFYL, of Achromobacter cycloclastes. (5/8900)

The structural gene, nosZ, for the monomeric N2O reductase has been cloned and sequenced from the denitrifying bacterium Achromobacter cycloclastes. The nosZ gene encodes a protein of 642 amino acid residues and the deduced amino acid sequence showed homology to the previously derived sequences for the dimeric N2O reductases. The relevant DNA region of about 3.6 kbp was also sequenced and found to consist of four genes, nosDFYL based on the similarity with the N2O reduction genes of Pseudomonas stutzeri. The gene product of A. cycloclastes nosF (299 amino acid residues) has a consensus ATP-binding sequence, and the nos Y gene encodes a hydrophobic protein (273 residues) with five transmembrane segments, suggesting the similarity with an ATP-binding cassette (ABC) transporter which has two distinct domains of a highly hydrophobic region and ATP-binding sites. The nosL gene encodes a protein of 193 amino acid residues and the derived sequence showed a consensus sequence of lipoprotein modification/processing site. The expression of nosZ gene in Escherichia coli cells and the comparison of the translated sequences of the nosDFYL genes with those of bacterial transport genes for inorganic ions are discussed.  (+info)

Alternative oxidase inhibitors potentiate the activity of atovaquone against Plasmodium falciparum. (6/8900)

Recent evidence suggests that the malaria parasite Plasmodium falciparum utilizes a branched respiratory pathway including both a cytochrome chain and an alternative oxidase. This branched respiratory pathway model has been used as a basis for examining the mechanism of action of two antimalarial agents, atovaquone and proguanil. In polarographic assays, atovaquone immediately reduced the parasite oxygen consumption rate in a concentration-dependent manner. This is consistent with its previously described role as an inhibitor of the cytochrome bc1 complex. Atovaquone maximally inhibited the rate of P. falciparum oxygen consumption by 73% +/- 10%. At all atovaquone concentrations tested, the addition of the alternative oxidase inhibitor, salicylhydroxamic acid, resulted in a further decrease in the rate of parasite oxygen consumption. At the highest concentrations of atovaquone tested, the activities of salicylhydroxamic acid and atovaquone appear to overlap, suggesting that at these concentrations, atovaquone partially inhibits the alternative oxidase as well as the cytochrome chain. Drug interaction studies with atovaquone and salicylhydroxamic acid indicate atovaquone's activity against P. falciparum in vitro is potentiated by this alternative oxidase inhibitor, with a sum fractional inhibitory concentration of 0.6. Propyl gallate, another alternative oxidase inhibitor, also potentiated atovaquone's activity, with a sum fractional inhibitory concentration of 0.7. Proguanil, which potentiates atovaquone activity in vitro and in vivo, had a small effect on parasite oxygen consumption in polarographic assays when used alone or in the presence of atovaquone or salicylhydroxamic acid. This suggests that proguanil does not potentiate atovaquone by direct inhibition of either branch of the parasite respiratory chain.  (+info)

Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan. (7/8900)

Three Mycobacterium smegmatis mutants selected for resistance to triclosan each had a different mutation in InhA, an enoyl reductase involved in fatty acid synthesis. Two expressed some isoniazid resistance. A mutation originally selected on isoniazid also mediated triclosan resistance, as did the wild-type inhA gene on a multicopy plasmid. Replacement of the mutant chromosomal inhA genes with wild-type inhA eliminated resistance. These results suggest that M. smegmatis InhA, like its Escherichia coli homolog FabI, is a target for triclosan.  (+info)

A phosphonate-induced gene which promotes Penicillium-mediated bioconversion of cis-propenylphosphonic acid to fosfomycin. (8/8900)

Penicillium decumbens is able to epoxidize cis-propenylphosphonic acid (cPA) to produce the antibiotic fosfomycin [FOM; also referred to as phosphonomycin and (-)-cis-1,2-epoxypropylphosphonic acid], a bioconversion of considerable commercial significance. We sought to improve the efficiency of the process by overexpression of the genes involved. A conventional approach of isolating the presumed epoxidase and its corresponding gene was not possible since cPA epoxidation could not be achieved with protein extracts. As an alternative approach, proteins induced by cPA were detected by two-dimensional gel electrophoresis. The observation that a 31-kDa protein (EpoA) was both cPA induced and overaccumulated in a strain which more efficiently converted cPA suggested that it might take part in the bioconversion. EpoA was purified, its amino acid sequence was partially determined, and the corresponding gene was isolated from cosmid and cDNA libraries with oligonucleotide probes. The DNA sequence for this gene (epoA) contained two introns and an open reading frame encoding a peptide of 277 amino acids having some similarity to oxygenases. When the gene was subcloned into P. decumbens, a fourfold increase in epoxidation activity was achieved. epoA-disruption mutants which were obtained by homologous recombination could not convert cPA to FOM. To investigate the regulation of the epoA promoter, the bialaphos resistance gene (bar, encoding phosphinothricin acetyltransferase) was used to replace the epoA-coding region. In P. decumbens, expression of the bar reporter gene was induced by cPA, FOM, and phosphorous acid but not by phosphoric acid.  (+info)

Fingerprint Dive into the research topics of MPP,sup,+,/sup,-induced neuronal death in rats involves tyrosine 33 phosphorylation of WW domain-containing oxidoreductase WOX1. Together they form a unique fingerprint. ...
Bhate, Radha H and Ramasarma, T (2010) Catalase-dependent release of half of the consumed oxygen during the activity of potato mitochondrial alternative oxidase confirms H2O2 as the product of oxygen reduction. In: Archives of Biochemistry and Biophysics, 495 (1). pp. 95-96. ...
We investigated the role of the WW domain-containing oxidoreductase (wwox) gene in the embryonic development of zebrafish, with particular emphasis on intracellular Ca2+ dynamics because Ca2+ is an important intracellular messenger. Comparisons between zebrafish wwox and human WWOX sequences identified highly conserved domain structures. wwox was expressed in developing heart tissues in the zebrafish embryo. Moreover, wwox knockdown induced pericardial edema with similarities to conditions observed in human breast cancer. The wwox knockdown embryos with the edema died within a week. High Ca2+ levels were observed at the boundary between the edema and yolk in wwox knockdown embryos.
Shop Nitric oxide reductase transcription regulator ELISA Kit, Recombinant Protein and Nitric oxide reductase transcription regulator Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
WWOX, WW domain-containing oxidoreductase, is a tumor suppressor that is altered in many human cancers, including breast cancer. Wwox interacts with the ErbB4 receptor, reduces nuclear translocation of the cleaved intracellular domain of ErbB4, and inhibits its transactivation function mediated thro …
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Discover why STEAP1 (six-transmembrane epithelial antigen of prostate 1) is a therapeutic target and overexpressed in prostate cancer.
References for Abcams Recombinant Human WWOX protein (ab86687). Please let us know if you have used this product in your publication
View Notes - BISC 120 Section 3 review guide from BISC 120 at USC. MIDTERM 3 Review sheet This document lists SOME of the topics that were covered in lectures or in the relevant chapters of the
BISC219, Genetics Lab, models investigative science. We cannot provide individualized materials for you to design experiments to investigate questions you come up with on your own because of cost, time constraints, and your inexperience in using some of the tools. Nevertheless, we want you to learn first hand this semseter how scientists use genetic principles and techniques to answer basic and nuanced questions about gene structure and function and how that knowledge can be applied more broadly and communicated to the scientific community. Although your instructors have defined the questions and designed the experiments that will be used to address those questions, you must be able to, at any point in an investigation, describe what you are doing (summary of the experimental design and where you are in the process of completing the experiments), why you are doing it (experimental question(s) and goals), and what it means if x happens versus y when you collect your data (have a hypothesis ...
Please complete a brief survey BEFORE leaving lab 12 to help us assess your background knowledge and expectations for lab. You can access this survey at {]. This survey is totally anonymous and not used to evaluate, you so please do not guess! Thank you for completing the survey. The labs for BISC 110/112 are designed to familiarize you with how experimental science is designed, performed and how it is communicated. Over the course of the semester, you will be designing and performing experiments that reinforce concepts covered in the lecture portion of the class. Your job will be to think like scientists when designing experiments to answer hypothesize driven questions about basic cellular processes. You will learn to perform the experiments properly, to keep good records of your results, and to communicate the results and conclusions of your work, both orally and in written reports ...
Study Flashcards On BISC104 Chapter 4 at Quickly memorize the terms, phrases and much more. makes it easy to get the grade you want!
The Escherichia coli peptide methionine sulfoxide reductase gene (msrA) encodes a single-subunit polypeptide of 212 amino acid residues (M. A. Rahman, H. Nelson, H. Weissbach, and N. Brot, J. Biol. Chem. 267:15549-15551, 1992). RNA blot analysis showed that the gene is transcribed into an mRNA of about 850 nucleotides. The promoter region was characterized, and the transcription initiation site was identified by primer extension. The synthesis of the MsrA protein increased about threefold in a growth-phase-dependent fashion. In an attempt to define the in vivo role of msrA, a chromosomal disruption was constructed. This mutant was more sensitive to oxidative stress, suggesting that oxidation of methionine in proteins plays an important role in oxidative damage. ...
The SCOP classification for the Peptide methionine sulfoxide reductase superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
TY - JOUR. T1 - Nitrate, nitrite and nitric oxide reductases. T2 - From the last universal common ancestor to modern bacterial pathogens. AU - Vázquez-Torres, Andrés. AU - Baumler, Andreas J. PY - 2016/2/1. Y1 - 2016/2/1. N2 - The electrochemical gradient that ensues from the enzymatic activity of cytochromes such as nitrate reductase, nitric oxide reductase, and quinol oxidase contributes to the bioenergetics of the bacterial cell. Reduction of nitrogen oxides by bacterial pathogens can, however, be uncoupled from proton translocation and biosynthesis of ATP or NH4 +, but still linked to quinol and NADH oxidation. Ancestral nitric oxide reductases, as well as cytochrome c oxidases and quinol bo oxidases evolved from the former, are capable of binding and detoxifying nitric oxide to nitrous oxide. The NO-metabolizing activity associated with these cytochromes can be a sizable source of antinitrosative defense in bacteria during their associations with host cells. Nitrosylation of terminal ...
Numerous hits in PSI-BLAST to peptide methionine sulfoxide reductases; e.g. residues 2-155 are 50% similar to PMSR_MYCGE, and residues 5-157 are 45% similar to PMSR_HELPY. Similar correlations exist to PMSR_NEIGO, PMSR_BRANA, PMSR_ARATH, PMSR_ECOLI, PMSR_YEAST, and PMSR_BOVIN ...
TY - JOUR. T1 - Dioxygen and nitric oxide reactivity of a reduced heme/non-heme diiron(II) complex [(5L)Fe(II)···Fe(II)-Cl]+. Using a tethered tetraarylporphyrin for the development of an active site reactivity model for bacterial nitric oxide reductase. AU - Ju, Telvin D.. AU - Woods, Amina S.. AU - Cotter, Robert J.. AU - Moënne-Loccoz, Pierre. AU - Karlin, Kenneth D.. PY - 2000/1/1. Y1 - 2000/1/1. N2 - We present here a first-generation model and initial reactivity (with O2 and NO) study for the heme/non-heme diiron active site chemistry of nitric oxide reductase (NOR), a denitrifying bacterial enzyme which converts nitric oxide to nitrous oxide (2NO + 2e- + 2H+ → N2O + H2O). This research is also pertinent because of the considerable recent biological, chemical and industrial interest in NO and nitrogen oxides. The study employs the binucleating ligand 5L, with tetradentate tris(2-pyridyl-methyl)amine (TMPA) chelate tethered to a tetraarylporphyrin (with three 2,6-difluorophenyl meso ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Arsenic atom in PDB 1l1d: Crystal Structure Of the C-Terminal Methionine Sulfoxide Reductase Domain (Msrb) of N. Gonorrhoeae Pilb
Sigma-Aldrich offers abstracts and full-text articles by [Petr Galuszka, Jitka Frébortová, Tomás Werner, Mamoru Yamada, Miroslav Strnad, Thomas Schmülling, Ivo Frébort].
TY - CHAP. T1 - Nitrous oxide reductase. AU - DellAcqua, Simone. AU - Pauleta, Sofia R.. AU - Moura, Isabel Maria Andrade Martins Galhardas de. N1 - Sem PDF. PY - 2013. Y1 - 2013. M3 - Chapter. SN - 978-1-4614-1532-9. T3 - Encyclopedia of Metalloproteins. BT - Nitrous oxide reductase. A2 - Kretsinger, R.H.. A2 - Uversky, V. N.. A2 - Permyakov, E.A.. PB - Springer. ER - ...
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Preincubation of the oxidized form of the flavoenzyme mercuric reductase with the reducing substrate, NADPH, or with a high concentration of cysteine (30 mM) results in a substantial increase of the catalytic activity as measured in a standard spectrophotometric assay. Also NADH has some activating effect but NADP+ or EDTA have no effect. In the presence of 1 mM cysteine only one equivalent of NADPH per FAD seems to be required for full activation which occurs after an incubation time of about 10 min. Activated mercuric reductase appears to be stable under anaerobic conditions but eventually returns to the original level of activity in the presence of oxygen. The activated state seems to be stabilized by 1 mM cysteine. Activation of mercuric reductase does not seem to be correlated with a change in the number of reactive thiol groups. The chemical nature of the activation process is not yet understood.. Stopped-flow studies have shown that the nonactivated enzyme is practically inactive prior to ...
Cordas, Cristina M., Americo G. Duarte, Jose J. G. Moura, and Isabel Moura. Electrochemical behaviour of bacterial nitric oxide reductase-Evidence of low redox potential non-heme Fe-B gives new perspectives on the catalytic mechanism. Biochimica Et Biophysica Acta-Bioenergetics. 1827.3 (2013): 233-238 ...
The research report on Global Oxidoreductases Market Analysis 2019, evaluates the market based on SWOT analysis and Porters Five Forces Model, which analyzes the degree of competition in the global market by considering several micro and macro factors. The Global Oxidoreductases marketing research report is a comprehensive study of the current trends in the market, industry growth drivers, challenges, and restraints. It also provides data regarding the competitive landscape and geographical distribution of the Global Oxidoreductases market, along with an analysis of recent developments.. The Global Oxidoreductases market is anticipated to develop from xx USD billion 2019 to USD xx billion by 2024, at a CAGR of y% during the estimate time.. To Get Sample Copy of Report visit at : Complete Global Oxidoreductases Market 2019 research report is isolated according to major ...
Larvae of the leaf beetle subtribe Chrysomelina sensu stricto repel their enemies by displaying glandular secretions that contain defensive compounds. These repellents can be produced either de novo (iridoids) or by using plant-derived precursors (e.g. salicylaldehyde). The autonomous production of …
Degradation of the plant hormone cytokinin is controlled by cytokinin oxidase/dehydrogenase (CKX) enzymes. The molecular and cellular behavior of these proteins is still largely unknown. In this study, we show that CKX1 is a type-II single-pass membrane protein that predominantly localizes to the endoplasmic reticulum (ER). This indicates that this CKX isoform is a bona fide ER protein directly controlling the cytokinin which triggers the signaling from the ER. By using various approaches, we demonstrate that CKX1 forms homodimers and homooligomers in vivo. The N-terminal part of CKX1 was necessary and sufficient for the protein oligomerization as well as for targeting and retention in the ER. Moreover, we show that protein-protein interaction is largely facilitated by transmembrane helices and depends on a functional GxxxG-like interaction motif. Importantly, mutations rendering CKX1 monomeric interfere with its steady-state localization in the ER and cause a loss of the CKX1 biological ...
File scanned at 300 ppi (Monochrome, 8-bit Grayscale, 24-bit Color) using ScandAll PRO 1.8.1 on a Fi-6670 in PDF format. CVista PdfCompressor 4.0 was used for pdf compression and textual OCR ...
Plants can alter rates of electron transport through the alternative oxidase (AOX) pathway in response to environmental cues, thus modulating respiratory efficiency, but the 18O discrimination method necessary for measuring electron partitioning in vivo has been restricted to laboratory settings. To overcome this limitation, we developed a field-compatible analytical method. Series of plant tissue subsamples were incubated in 12 mL septum-capped vials for 0.5-4 h before aliquots of incubation air were injected into 3.7 mL evacuated storage vials. Vials were stored for up to 10 months before analysis by mass spectrometry. Measurements were corrected for unavoidable contamination. Additional mathematical tools were developed for detecting and addressing non-linearity (whether intrinsic or due to contamination) in the data used to estimate discrimination values. Initial contamination in the storage vials was 0.03 ± 0.01 atm; storing the gas samples at -17 °C eliminated further contamination ...
Complete information for SDR42E1 gene (Protein Coding), Short Chain Dehydrogenase/Reductase Family 42E, Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
1GRX: NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Shop Dehydrogenase/reductase SDR family protein ELISA Kit, Recombinant Protein and Dehydrogenase/reductase SDR family protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
CP000667.PE408 Location/Qualifiers FT CDS_pept 469214..469912 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Strop_0408 FT /product=short-chain dehydrogenase/reductase SDR FT /note=PFAM: short-chain dehydrogenase/reductase SDR FT /db_xref=EnsemblGenomes-Gn:Strop_0408 FT /db_xref=EnsemblGenomes-Tr:ABP52893 FT /db_xref=InterPro:IPR002347 FT /db_xref=InterPro:IPR036291 FT /db_xref=UniProtKB/TrEMBL:A4X1Z3 FT /protein_id=ABP52893.1 FT /translation=MVNLDGLRVAVTGAGRASGRLLATAFAEHGAQVFVSARDEVAARR FT TTDSIRQRGRGRGEAFVCDLTSPDSVRAFAAALTDRTDHLDVLVNNGAGYLHGVDLGDV FT EDDHIIATIGGTATGTVLLTKHLLALLRASTRPDIVNMISACGEVGHHRSEAHPAFYAA FT KHAQAGFAEIMSHRLRVEGIRVISLFPPDFVQHGPRVASNNLTAQSVVDCVLFAVSQPR FT DCFIREFRFE gtggtgaatc tcgacggact acgggttgct gtcaccggcg ccgggcgcgc ctccggacgc 60 ctcctggcga ccgccttcgc cgagcacggc gcgcaggtgt ttgtctccgc ccgtgatgag 120 gtggcagcca gacgcaccac ggattcgatc cggcagcgtg ggcgggggag aggcgaagcc 180 ttcgtctgtg acctgaccag ccccgactcg gtacgcgcgt tcgcggcggc gttgaccgac 240 cgcaccgacc ...
Here is the best resource for homework help with BISC 307L : General Physiology at USC. Find BISC307L study guides, notes, and practice tests from USC.
Bacteria NosR protein: amino acid sequence given in first source; regulatory component necessary for expression of nitrous oxide reductase in denitrifying
F-, [araD139]B/r, Δ(argF-lac)169, λ-, bioA24, zbh-428::Tn10, flhD5301, Δ(fruK-yeiR)725(fruA25), relA1, rpsL150(strR), bisC9::Mu cts, deoC1 ...
Conrath, K., A. S. Pereira, C. E. Martins, C. G. Timóteo, P. Tavares, S. Spinelli, J. Kinne, C. Flaudrops, C. Cambillau, S. Muyldermans, et al., Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase., Protein Sci, vol. 18, issue 3, pp. 619-28, 2009 Mar. ...
Conrath, K., A. S. Pereira, C. E. Martins, C. G. Timóteo, P. Tavares, S. Spinelli, J. Kinne, C. Flaudrops, C. Cambillau, S. Muyldermans, et al., Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase., Protein Sci, vol. 18, issue 3, pp. 619-28, 2009 Mar. ...
This page contains information on the chemical Ammonium, (p-(1,4-dihydro-3,5-dimethoxycarbonyl-2,6-dimethyl-4-pyridyl)phenyl)trimet hyl-, iodide including: 2 synonyms/identifiers.
WWOX gene plays an important role in the altered metabolism of cancer cells which are known to use glucose differently than normal cells.
An article highlighting the INDOX project objectives and main outcomes has been included in the BIOECONOMY INNOVATION -CommBeBiz magazine 2016-2017, a publication covering bioeconomy trends in markets, policy, and research social innovations.. CommBeBiz is H2020 funded initiative working with FP7 and H2020 project partners at all stages of their ideas and research development to enable more effective and speedier transfer of knowledge to the marketplace, to policy-players and for the public good. ...
An article highlighting the INDOX project objectives and main outcomes has been included in the BIOECONOMY INNOVATION -CommBeBiz magazine 2016-2017, a publication covering bioeconomy trends in markets, policy, and research social innovations.. CommBeBiz is H2020 funded initiative working with FP7 and H2020 project partners at all stages of their ideas and research development to enable more effective and speedier transfer of knowledge to the marketplace, to policy-players and for the public good. ...
Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing. PLoS One. 2010 Jul 09; 5(7):e11497 ...
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
M. genitalium was first isolated from the urine of two male patients with nongonococcal urethritis (28) and subsequently, along with M. pneumoniae, from throat specimens of pneumonia patients (4) and from synovial fluid of a patient with polyarthritis (29). Although Jensen et al. (18) recently used a cell culture system to isolate M. genitalium from urethral specimens, routine isolation of this fastidious pathogen from humans has been very difficult. Nevertheless, mounting PCR evidence reinforces its association with urethritis and other sexually transmitted diseases (26). With a limited genome size of 580 kb (12), M. genitalium is the smallest self-replicating microorganism reported to date. M. pneumoniae, which causes primary atypical pneumonia in humans, is closely related genetically to M. genitalium and has a genome size of 816 kb (15). Both Mycoplasmaspecies are limited metabolically and are deficient in genes common to other pathogenic bacteria, particularly genes related to cell wall ...
We have previously shown that WW domain-containing oxidoreductase (WWOX) has tumour-suppressing effects and that its expression is frequently reduced in pancreatic carcinoma. In this study, we examined WWOX expression in intraductal papillary mucinous neoplasm of the pancreas (IPMN) to assess the function of WWOX in pancreatic duct tumourigenesis using immunohistochemistry and methylation-specific polymerase chain reaction analysis. Among 41 IPMNs including intraductal papillary mucinous adenomas (IPMAs) and intraductal papillary mucinous carcinomas (IPMCs), loss or reduced WWOX immunoreactivity was detected in 3 (15%) of 20 IPMAs and 17 (81%) of 21 IPMCs. In addition, hypermethylation of the WWOX regulatory site was detected in 1 (33%) of 3 WWOX(−) IPMAs and 9 (53%) of 17 WWOX(−) IPMCs, suggesting that hypermethylation may possibly be important in the suppression of WWOX expression. Reduction of WWOX expression was significantly correlated with a higher Ki-67 labelling index but was not correlated
Isopenicillin N synthase (IPNS) is a non-heme iron-dependent enzyme belonging to the oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV). N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 ⇌ {\displaystyle \rightleftharpoons } isopenicillin N + 2 H2O This reaction is a key step in the biosynthesis of penicillin and cephalosporin antibiotics. The active sites of most isopenicillin N synthases contain an iron ion. This enzyme is also called isopenicillin N synthetase. A Fe(II) metal ion in the active site of the enzyme is coordinated by at least two histidine residues, an aspartate residue, a glutamine residue, and two water molecules in the absence of a bound substrate. Just two histidine residues and one aspartic acid residue are entirely conserved. Therefore, it is highly significant that these two histidine residues, His214 and His270, and one aspartic acid residue, Asp216, are precisely the ones ...
TY - JOUR. T1 - Expression analysis of alternative oxidase gene (aox1) with enhanced green fluorescent protein as marker in citric acid-producing Aspergillus niger. AU - Kirimura, Kohtaro. AU - Ogawa, Satoshi. AU - Hattori, Takasumi. AU - Kino, Kuniki. N1 - Funding Information: We express our thanks to Dr. Y. Niwa of the University of Shizuoka and Professor K. Kitamoto of the University of Tokyo for supplying the plasmid pBEGFP-F harboring the egfp gene. This work was partly supported by the 21COE program Practical Nano-Chemistry from MEXT, Japan.. PY - 2006/9. Y1 - 2006/9. N2 - In a citric acid-producing filamentous fungus Aspergillus niger WU-2223L, a cyanide- and antimycin A-insensitive and salicylhydroxamic acid-sensitive respiratory pathway functions in the mitochondria besides the cytochrome pathway and is catalyzed by alternative oxidase (AOX). We constructed an A. niger transformant strain AOXEGFP-1 expressing a fusion gene, aox1-egfp, encoding AOX and enhanced green fluorescent ...
References for Abcams Anti-Methionine Sulfoxide Reductase B antibody (ab71175). Please let us know if you have used this product in your publication
The alternative oxidase (AOX) of the soybean (Glycine max L.) inner mitochondrial membrane is encoded by a multigene family (Aox) with three known members. Here, the Aox2 and Aox3 primary translation products, deduced from cDNA analysis, were found to be 38.1 and 36.4 kD, respectively. Direct N-terminal sequencing of partially purified AOX from cotyledons demonstrates that the mature proteins are 31.8 and 31.6 kD, respectively, implying that processing occurs upon import of these proteins into the mitochondrion. Sequence comparisons show that the processing of plant AOX proteins occurs at a characteristic site and that the AOX2 and AOX3 proteins are more similar to one another than to other AOX proteins, including soybean AOX1. Transcript analysis using a polymerase chain reaction-based assay in conjunction with immunoblot experiments indicates that soybean Aox genes are differentially expressed in a tissue-dependent manner. Moreover, the relative abundance of both Aox2 transcripts and protein ...
SWISS-MODEL Repository entry for B2SQI9 (MSRA_XANOP), Peptide methionine sulfoxide reductase MsrA. Xanthomonas oryzae pv oryzae (strain PXO99A)
SWISS-MODEL Repository entry for C3LNU9 (MSRB_VIBCM), Peptide methionine sulfoxide reductase MsrB. Vibrio cholerae serotype O1 (strain M66-2)
TY - JOUR. T1 - WWOX suppresses autophagy for inducing apoptosis in methotrexate-treated human squamous cell carcinoma. AU - Tsai, C. W.. AU - Lai, F. J.. AU - Sheu, H. M.. AU - Lin, Y. S.. AU - Chang, T. H.. AU - Jan, M. S.. AU - Chen, S. M.. AU - Hsu, P. C.. AU - Huang, T. T.. AU - Huang, T. C.. AU - Sheen, M. C.. AU - Chen, S. T.. AU - Chang, W. C.. AU - Chang, N. S.. AU - Hsu, L. J.. PY - 2013/9. Y1 - 2013/9. N2 - Squamous cell carcinoma (SCC) cells refractory to initial chemotherapy frequently develop disease relapse and distant metastasis. We show here that tumor suppressor WW domain-containing oxidoreductase (WWOX) (also named FOR or WOX1) regulates the susceptibility of SCC to methotrexate (MTX) in vitro and cure of SCC in MTX therapy. MTX increased WWOX expression, accompanied by caspase activation and apoptosis, in MTX-sensitive SCC cell lines and tumor biopsies. Suppression by a dominant-negative or small interfering RNA targeting WWOX blocked MTX-mediated cell death in sensitive ...
ENOX2 Protein As Indicator of Cancerous Cells. Ecto-Nicotinamide Adenine Dinucleotide Oxidase Disulfide-Thiol Exchanger 2 (ENOX2), also known as Tumor-Associated Nicotinamide Adenine Dinucleotide Oxidase (tNOX), is specific for cancer by coating the surfaces of malignant cells and disrupting apoptosis signals to execute programmed cell death of the malignant cell. ENOX2 allows immature cancer cells to enlarge to a normal size. Essentially, cancers cells cannot survive or grow without ENOX2.. ENOX2 is produced only by cancer cells and not healthy normal cells. A distinct function of ENOX2 is the oxidation of NADH to NAD+ in an oscillating fashion. This process is accomplished within a period of 24 minutes, completing 60 cycles in a 24 hour period. This 60 cycles of 24 minutes is considered a regular oscillation of the biological clock. The period of oscillation in a cancerous cell is reduced to 22 minutes. 1. Detection of ENOX2 in the Serum with the ONCOblot® Test. The presence of ENOX2 in the ...
BDH2; 3-hydroxybutyrate dehydrogenase, type 2; dehydrogenase/reductase (SDR family) member 6 , DHRS6; 3-hydroxybutyrate dehydrogenase type 2; FLJ13261; PRO20933; SDR15C1; short chain dehydrogenase/reductase family 15C; member 1; UCPA OR; UNQ6308; oxidoreductase UCPA; R-beta-hydroxybutyrate dehydrogenase; dehydrogenase/reductase SDR family member 6; dehydrogenase/reductase (SDR family) member 6; short chain dehydrogenase/reductase family 15C, member 1; DHRS6; EFA6R; UCPA-OR ...
The major enzyme of the methionine sulfoxide reductase (Msr) system is MsrA. Senescing msrAknockout mother yeast cells accumulated significant amounts of protein-carbonyl both at 5 generation-old...
mouse Steap protein: six-transmembrane epithelial antigen of the prostate, prostate stem cell antigen, and prostate-specific membrane antigen; RefSeq NM_027399
Supplementary Materialsijms-20-05857-s001. = 7.4), Tf may bind two atoms of Fe3+ tightly. may be the receptor of can bind easily, and initiates Pyrithioxin dihydrochloride the clathrin-mediated endocytosis with the help of the TfR trafficking proteins [16]. Using the entry of protons, the pH in endosome filled with diferric Tf/TfR1 complicated decreases, producing a conformational alter in discharge and Tf of Fe3+ [17]. Subsequently, the apo-Tf/TfR complicated returns towards the cell surface area for another routine, whilst Fe3+ is normally decreased to Fe2+ by way of a reductase called six-transmembrane epithelial antigen from the prostate 3 ((PRV) over the hosts iron fat burning capacity [27], it really is of great importance to clarify the partnership between aquatic trojan infection as well as the iron fat burning capacity, which may donate to illuminating the antiviral iron-withholding strategies in aquatic pets and exploiting iron-related medications or feed chemicals for the avoidance ...
Looking for online definition of oxidoreductases in the Medical Dictionary? oxidoreductases explanation free. What is oxidoreductases? Meaning of oxidoreductases medical term. What does oxidoreductases mean?
Quantum chemical calculations of active-site models of nitrous oxide reductase (N2OR) have been undertaken to elucidate the mechanism of N-O bond cleavage mediated by the supported tetranuclear Cu4S core (Cu-Z) found in the enzymatic active site. Using either a minimal model previously employed by Gorelsky et al. (J. Am. Chem. Soc. 128:278-290, 2006) or a more extended model including key residue side chains in the active-site second shell, we found two distinct mechanisms. In the first model, N2O binds to the fully reduced Cu-Z in a bent mu-(1,3)-O,N bridging fashion between the Cu-I and Cu-IV centers and subsequently extrudes N-2 while generating the corresponding bridged mu-oxo species. In the second model, substrate N2O binds loosely to one of the coppers of Cu-Z in a terminal fashion, i.e., using only the oxygen atom; loss of N-2 generates the same mu-oxo copper core. The free energies of activation predicted for these two alternative pathways are sufficiently close to one another that ...
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
Principal Investigator:KITA Kiyoshi, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for General Scientific Research (C), Research Field:General medical chemistry
Here, I will present the recently discovered regulation of nos genes through the two-component system NasST. NasS is a nitrate sensor and NasT is a transcription antiterminator. Mutation of nasS induced both N2O reductase activity and transcription of nos genes (nosRZD), in cells of B. diazoefficiens incubated in the absence of nitrate. The NasS_NasT protein complex was dissociated in vitro by the addition of nitrate, suggesting the release of NasT, which is known to bind the leader RNA of the target gene, thereby preventing hairpin formation and allowing complete transcription. Disruption of nasT led to a marked decrease in nos transcription in B. diazoefficiens cells incubated with nitrate, indicating that NasST system regulates nos transcription in response to nitrate. Although analysis of the region upstream nosR and nosZ genes revealed no regulatory hairpin structures similar to those present in the leader RNA of other genes regulated by NasT, we could confirm binding of purified NasT with ...
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Predicted to have L-methionine-(S)-S-oxide reductase activity and peptide-methionine (S)-S-oxide reductase activity. Predicted to be involved in cellular response to oxidative stress. Predicted to localize to cytoplasm. Orthologous to human MSRA (methionine sulfoxide reductase A ...
Short-chain dehydrogenases/reductases (SDRs) constitute a large family of NAD(P)(H)-dependent oxidoreductases, sharing sequence motifs and displaying similar mechanisms. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, cofactor, hormone and xenobiotic metabolism as well as in redox sensor mechanisms. Sequence identities are low, and the most conserved feature is an alpha/beta folding pattern with a central beta sheet flanked by 2 - 3 alpha-helices from each side, thus a classical Rossmannfold motif for nucleotide binding. The conservation of this element and an active site, often with an Asn-Ser-Tyr-Lys tetrad, provides a platform for enzymatic activities encompassing several EC classes, including oxidoreductases, epimerases and lyases. The common mechanism is an underlying hydride and proton transfer involving the nicotinamide and typically an active site tyrosine residue, whereas substrate specificity is determined by a variable C-terminal segment. Relationships exist with ...
The major metabolic pathways involved in synthesis and disposition of carbonyl and hydroxyl group containing compounds are presented, and structural and functional characteristics of the enzyme families involved are discussed. Alcohol and aldehyde dehydrogenases (ADH, ALDH) participate in oxidative pathways, whereas reductive routes are accomplished by members of the aldo-keto reductase (AKR), short-chain dehydrogenases/reductases (SDR) and quinone reductase (QR) superfamilies. A wealth of biochemical, genetic and structural data now establishes these families to constitute important phase I enzymes.
This gene encodes a major catalytic subunit of succinate-ubiquinone oxidoreductase, a complex of the mitochondrial respiratory chain. The complex is composed of four nuclear-encoded subunits and is localized in the mitochondrial inner membrane. Mutations …
Characterization of Apoptosis-Related Oxidoreductases from Neurospora crassa. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Top performende anti-Human Dehydrogenase/reductase (SDR Family) Member 9 Antikörper für Immunohistochemistry (Frozen Sections) (IHC (fro)) vergleichen & kaufen.
TY - CONF. T1 - Oxidation of hemicellulose derived oligosaccharides with carbohydrate oxidoreductases. AU - Karppi, Johanna. PY - 2018/7/8. Y1 - 2018/7/8. M3 - Poster. T2 - Oxizymes. Y2 - 8 July 2018 through 10 July 2018. ER - ...
The IUPHAR/BPS Guide to Pharmacology. myeloperoxidase - 1.-.-.- Oxidoreductases. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
2010).10 There are six main classes of enzymes, as follows (Schomburg et al., 2014): EC 1 Oxidoreductases catalyse reactions in which a substrate donates one or more electrons to an electron acceptor, becoming oxidized in the process. In reality all of the enzymes A1210477 in classes 1-3 satisfy the definition of transferases. However, as these three classes are all large compared. with the other three groups, it is convenient to break them into three classes, and to reserve the name transferase for enzymes that are not oxidoreductases or hydrolases. In addition to the name synthetase for ligases, the name synthase can be used for any enzyme when it is appropriate to use a name that emphasizes the name of the product synthesizes. Metzler (1980) pointed out that find more using two such similar names in contrasting ways was a source of confusion. 11 There is also a difference between the way enzymes in EC 6 are named: ligases are named according to the substrates that are joined, whereas ...
A hemorragia pulmonar induzida por exercício (HPIE) é caracterizada pela presença de sangue no trato respiratório anterior e posterior, sendo considerada por muitos autores como a principal causa na redução...
Dr. Dhar was Adjunct Associate Professor at San Diego State University Biology Department. He has studied viral diseases of shrimp for the past eight years, with a foc..
View Original Article Here Any CIO worth his or her salt knows the importance of getting physicians engaged; the big question is how to
MetabolismEnergy metabolismElectron transportcytochrome aa3 quinol oxidase, subunit IV (TIGR02901; EC 1.10.3.-; HMM-score: 104.3) ...
MetabolismEnergy metabolismElectron transportcytochrome aa3 quinol oxidase, subunit III (TIGR02897; EC 1.10.3.-; HMM-score: 359) ...
oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of ...
If your organization is one of the many that need to do some remedial work in the area of lifecycle management, heres a look at some of the things you need to know.
Les reaccions d'aquest tipus són catalitzades per un grup d'enzims anomenat oxidoreductases. El nom correcte d'aquests enzims ... Les reaccions redox catalitzades per oxidoreductases són vitals en totes les àrees del metabolisme, però especialment quan té ... H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction». J. Biol. Chem. ... aquest tipus d'enzims s'anomenen oxidoreductases de classe A, mentre que els enzims de classe B transfereixen l'àtom d'hidrogen ...
"Oxidoreductases from Trametes spp. in biotechnology: A wealth of catalytic activity". Food Technology and Biotechnology. 45 (3 ...
The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H- ... 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, ... 2002). "The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals ...
The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). ... This enzyme belongs to the superfamily of short-chain oxidoreductases, specifically those acting on the CH-OH group of donor ...
... oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme ... The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ...
Oxidoreductase. References[edit]. This article incorporates text from the public domain Pfam and InterPro IPR015409 ...
oxidoreductase activity. • iron ion binding. • ferric iron binding. • protein binding. • amino acid binding. • monooxygenase ... oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one ...
... s, which belong to the oxidoreductase family, are found in archaea, bacteria, fungi, and plants.[5] They are ... The systematic name of this enzyme class is hydrogen-sulfide:acceptor oxidoreductase. Other names in common use include ... assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase. ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase. ...
Oxidoreductases: peroxidases (EC 1.11). *Catalase. *Cytochrome c peroxidase. *Eosinophil peroxidase ...
The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
Oxidoreductases: alcohol oxidoreductases (EC 1.1). 1.1.1: NAD/NADP acceptor. *3-hydroxyacyl-CoA dehydrogenase ...
... (succinate-ubiquinone oxidoreductase). The structure of SQR in a phospholipid membrane. SdhA, SdhB, ... succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction". The ...
EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
NADH-ubiquinone oxidoreductase chain 1 EC Pfam PF00146 9. ND2 / NU2M. NU2M_HUMAN. NADH-ubiquinone oxidoreductase chain ... NADH-ubiquinone oxidoreductase chain 4L EC Pfam PF00420 13. ND5 / NU5M. NU5M_HUMAN. NADH-ubiquinone oxidoreductase ... NADH-ubiquinone oxidoreductase chain 3 EC Pfam PF00507 11. ND4 / NU4M. NU4M_HUMAN. NADH-ubiquinone oxidoreductase ... Respiratory complex I, EC (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial ...
The systematic name of this enzyme class is L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called ... This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and ...
The systematic name of this enzyme class is cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase. This enzyme is also called 3β- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... Wikvall K (April 1981). "Purification and properties of a 3 β-hydroxy-delta 5-C27-steroid oxidoreductase from rabbit liver ... hydroxy-Δ5-C27-steroid oxidoreductase. The human version of this enzyme is known as hydroxy-Δ-5-steroid dehydrogenase, 3 β- and ...
oxidoreductase activity. • electron carrier activity. • 2 iron, 2 sulfur cluster binding. • 3 iron, 4 sulfur cluster binding. • ... Kita K, Oya H, Gennis RB, Ackrell BA, Kasahara M (January 1990). "Human complex II (succinate-ubiquinone oxidoreductase): cDNA ... succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction". The ...
oxidoreductase activity. • mRNA binding. • folate reductase activity. • translation repressor activity, nucleic acid binding. • ...
oxidoreductase activity. • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, ...
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14). 1.14.11: 2-oxoglutarate. *Prolyl hydroxylase ...
... protein-disulfide isomerase/oxidoreductase, thiol:protein-disulfide oxidoreductase, and thiol-protein disulphide oxidoreductase ... The systematic name of this enzyme class is glutathione:protein-disulfide oxidoreductase. Other names in common use include ... This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as ... glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein- ...
... s are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ...
oxidoreductase activity. • histone demethylase activity (H3-K27 specific). • histone demethylase activity. • zinc ion binding. ... oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one ...
The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...
oxidoreductase activity. • glutathione peroxidase activity. • peroxidase activity. Cellular component. • extracellular region. ...
oxidoreductase activity. • protein heterodimerization activity. • GO:0001948 protein binding. • Polyphenol oxidase. • ...
... oxygen oxidoreductase) is an enzyme with systematic name naphthalene-1,2-diol:oxygen oxidoreductase.[1][2][3] This enzyme ...
Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are ... Homology to other disulfide oxidoreductases". J. Biol. Chem. 262 (36): 17313-8. PMID 3693355. Pons G, Raefsky-Estrin C, ... functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases". Archives of Biochemistry ...
Amino acid oxidoreductases are oxidoreductases, a type of enzyme, that act upon amino acids. They constitute the majority of ... Examples include: Glutamate dehydrogenase Nitric oxide synthase Amino+Acid+Oxidoreductases at the US National Library of ...
CH-CH oxidoreductases are oxidoreductase enzymes that convert single bonds and double bonds between two carbon atoms. They are ... 2-reductase Oxidoreductases+Acting+on+CH-CH+Group+Donors at the US National Library of Medicine Medical Subject Headings (MeSH ...
Overgenomen van "" ...
All MeSH CategoriesChemicals and Drugs CategoryEnzymes and CoenzymesEnzymesOxidoreductasesAlcohol OxidoreductasesCarbohydrate ... Alcohol Oxidoreductases. A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as ... Dependent Alcohol Oxidoreductases11-beta-Hydroxysteroid Dehydrogenases +20-Hydroxysteroid Dehydrogenases +3-alpha- ...
Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. The ... A multimeric oxidoreductase complex according to the invention encompasses an oxidoreductase enzyme or protein within any one ... Oxidoreductase Complexes:. In one embodiment of the invention an isolated multimeric oxidoreductase complex includes at least ... B. subtilis and E. coli are not known to include multimeric oxidoreductase enzyme complexes containing cytochrome C homologs ...
Quinone oxidoreductases of the plasma membrane.. Morré DJ1.. Author information. 1. Department of Medicinal Chemistry and ...
Cytochrome P450 oxidoreductase deficiency is a disorder of hormone production. Explore symptoms, inheritance, genetics of this ... The breakdown of retinoic acid requires cytochrome P450 oxidoreductase; if a shortage of cytochrome P450 oxidoreductase ... Cytochrome P450 oxidoreductase deficiency is caused by mutations in the POR gene. This gene provides instructions for making ... Arlt W. P450 oxidoreductase deficiency and Antley-Bixler syndrome. Rev Endocr Metab Disord. 2007 Dec;8(4):301-7. Review. ...
Oxidoreductase definition, any of a class of enzymes that act as a catalyst, some of them conjointly, causing the oxidation and ... oxidoreductase. (ŏk′sĭ-dō-rĭ-dŭk′tās′, -tāz′). n.. *An enzyme that catalyzes an oxidation-reduction. ...
ASM journals are the most prominent publications in the field, delivering up-to-date and authoritative coverage of both basic and clinical microbiology.. About ASM , Contact Us , Press Room. ASM is a member of. ...
Products containing OXIDO REDUCTASES made by company: Emmaya Naturals There are no products in the database that match your ...
Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group.[1][2] ... This oxidoreductase article is a stub. You can help Wikipedia by expanding it.. *v ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) ... Retrieved from "" ...
Oxidoreductase in Plant Plasmalemma. * Redox Components in the Plant Plasma Membrane Ian M. Møller, Per Askerlund, Christer ... The workshop came at a time when the study of the plasma membrane oxidoreductase activity was beginning to attract more ... On the Occurrence of Oxidoreductases in the Apoplast of Leguminosae and Gramineae and their Significance in the Study of ... The presence and role of other oxidoreductases in the plasma membrane was documented, especially in regard to peroxide ...
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.
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.
Fermentation Klebsiella pneumoniae 1,3-propanediol propanediol oxidoreductase This is a preview of subscription content, log in ... Johnson, E.A. & Lin, E.C.C. 1987 Klebsiella pneumoniae 1,3-propanediol: NAD+ oxidoreductase. Journal of Bacteriology 169, 2050- ... 3-propanediol oxidoreductase (E.C. The fermentation process is composed of an aerobic batch phase on glucose and ... 3-propanediol oxidoreductase formation. A fast change from an aerobic to an anaerobic environment led to a redox imbalance, ...
Putative oxidoreductase FAD-binding subunit. B. 278. Sulfurisphaera tokodaii str. 7. Mutation(s): 0 Gene Names: ST0562, STK_ ... Putative oxidoreductase iron-sulfur subunit. C. 168. Sulfurisphaera tokodaii str. 7. Mutation(s): 0 Gene Names: ST0561, STK_ ... Putative oxidoreductase molybdopterin-binding subunit. A. 706. Sulfurisphaera tokodaii str. 7. Mutation(s): 0 Gene Names: ... GAOR1-3 belong to the xanthine oxidoreductase superfamily, and are composed of a molybdo-pyranopterin subunit (L), a flavin ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Oxidoreductases are enzymes that catalyze oxidation/reduction reactions by transferring electrons, hydrogens, or oxygens from a ...
... quinone oxidoreductase (complex I) pumps protons across the inner membrane of mitochondria or the plasma membrane of many ... Energy converting NADH:quinone oxidoreductase (complex I) Annu Rev Biochem. 2006;75:69-92. doi: 10.1146/annurev.biochem. ... NADH:quinone oxidoreductase (complex I) pumps protons across the inner membrane of mitochondria or the plasma membrane of many ...
Oxidoreductases a schema:Intangible ;. schema:name "Oxidoreductases"@en ;. . ... Photosystem II : the light-driven water : plastoquinone oxidoreductase. Author:. Thomas John Wydrzynski; Kimiyuki Satoh. ... schema:name "Photosystem II : the light-driven water : plastoquinone oxidoreductase"@en ;. schema:productID "62713887" ;. ... Add tags for "Photosystem II : the light-driven water : plastoquinone oxidoreductase". Be the first. ...
... Mohammad S. Eram,1,2 ... Mohammad S. Eram, Erica Oduaran, and Kesen Ma, "The Bifunctional Pyruvate Decarboxylase/Pyruvate Ferredoxin Oxidoreductase from ...
"Alcohol Oxidoreductases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Alcohol Oxidoreductases" by people in Harvard Catalyst ... Below are the most recent publications written about "Alcohol Oxidoreductases" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Alcohol Oxidoreductases". ...
NADPH-FMN oxidoreductase. Gene Name. frp. Organism. Vibrio harveyi. Amino acid sequence. ,lcl,BSEQ0011865,NADPH-flavin ... Oxidoreductase activity. Specific Function. Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide ... Lei B, Liu M, Huang S, Tu SC: Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene ...
OxidoreductaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ... FAD-dependent oxidoreductaseImported. ,p>Information which has been imported from another database using automatic procedures ... oxidoreductase activity, acting on the CH-CH group of donors Source: InterPro ... tr,B3TMR1,B3TMR1_9ACTN FAD-dependent oxidoreductase OS=Actinomadura kijaniata GN=KijD3 PE=1 SV=1 ...
Quinone oxidoreductaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p ... tr,C9JH92,C9JH92_HUMAN Quinone oxidoreductase (Fragment) OS=Homo sapiens OX=9606 GN=CRYZ PE=1 SV=1 ...
Monkey Oxidoreductase Activity. Polyclonal Antibody - TRXR1 Antibody - Western Blotting, UniProt ID Q16881, Entrez ID 7296 # ... the first having oxidoreductase activity and the second being a potential DNA binding domain (3,5). While AIF is redox-active ... the first having oxidoreductase activity and the second being a potential DNA binding domain (3,5). While AIF is redox-active ... the nucleus via its DNA binding and an anti-apoptotic activity via the scavenging of free radicals through its oxidoreductase ...
Disulphide oxidoreductase protein. Ab157065 is a full length protein produced in Escherichia coli and has been validated… ... Recombinant E. coli Disulphide oxidoreductase protein. See all Disulphide oxidoreductase proteins and peptides. ... Disulphide oxidoreductase (DsbA) is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli ...
... oxidoreductase Antibody Products from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and ... Anti-P450 (cytochrome) oxidoreductase Antibody Products. Anti-P450 (cytochrome) oxidoreductase antibodies are readily available ... P450 (cytochrome) oxidoreductase is a reported synonym of the human protein cytochrome p450 oxidoreductase, encoded by the ...
From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold. Steven G. Van Lanen, John S. ... From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold ... From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold ... From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold ...
Author summary Mitochondrial pathologies which result from mutations in the nuclear DNA remain incurable and often lead to death. As mitochondria play various roles in cellular and tissue-specific contexts, the symptoms of mitochondrial pathologies can differ between patients. Thus, diagnosis and treatment of mitochondrial disorders remain challenging. To enhance this, the generation of new models that explore and define the consequences of mitochondria insufficiencies is of central importance. Here, we present a mia40a zebrafish mutant as a model for mitochondrial dysfunction, caused by an imbalance in mitochondrial protein biogenesis. This mutant shares characteristics with existing reports on mitochondria dysfunction, and has led us to identify novel phenotypes such as enlarged mitochondrial clusters in skeletal muscles. In addition, our transcriptomics and proteomics data contribute important findings to the existing knowledge on how faulty mitochondria impinge on vertebrate development in molecular
  • NADH:quinone oxidoreductase (complex I) pumps protons across the inner membrane of mitochondria or the plasma membrane of many bacteria. (
  • Your search returned 13 NADH:ubiquinone oxidoreductase core subunit S1 ELISA ELISA Kit across 6 suppliers. (
  • The NADH:quinone oxidoreductase, also called rotenone-sensitive NADH dehydrogenase (complex I) (NDH-1), is the largest complex of the respiratory chain and is responsible for the transfer of electrons from NADH to quinones, coupled with proton or sodium translocation across the membrane. (
  • NADH:quinone oxidoreductase, or Complex I, is a multi-subunit membrane-bound enzyme in the respiratory chain of many pro- and eukaryotes. (
  • NADH-FMN Oxidoreductase antibody LS-C185137 is an unconjugated rabbit polyclonal antibody to photobacterium fischeri NADH-FMN Oxidoreductase. (
  • V. cholerae has a unique redox driven respiration-linked sodium pump, Na⁺ translocating NADH:quinone oxidoreductase (NQR). (
  • oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor that interferes with the action of any such enzyme incorporating one atom of oxygen and using NADH or NADPH as one donor (EC 1.14.13. (
  • Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group . (
  • Alcohol Oxidoreductases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • This graph shows the total number of publications written about "Alcohol Oxidoreductases" by people in Harvard Catalyst Profiles by year, and whether "Alcohol Oxidoreductases" was a major or minor topic of these publication. (
  • Below are the most recent publications written about "Alcohol Oxidoreductases" by people in Profiles. (
  • GAOR1-3 belong to the xanthine oxidoreductase superfamily, and are composed of a molybdo-pyranopterin subunit (L), a flavin subunit (M), and an iron-sulfur subunit (S), forming an LMS hetero-trimer unit. (
  • A homologous, structurally and most likely functionally similar subunit is also found in F420H2 oxidoreductases and in complex membrane-bound hydrogenases. (
  • P450 (cytochrome) oxidoreductase is a reported synonym of the human protein 'cytochrome p450 oxidoreductase', encoded by the gene POR. (
  • Type II enzymes, including both drug-metabolizing and some steroidogenic enzymes, require electron donation from a two-flavin protein, P450 oxidoreductase (POR). (
  • Interaction of human NAD(P)H:quinone oxidoreductase 1 (NQO1) with the tumor suppressor protein p53 in cells and cell-free systems. (
  • The D-lactate oxidoreductase (cytochrome c -dependent dehydrogenase, DLDH, EC1.1.2.4) is a FAD- and Zn 2+ -containing membrane-associated protein found in yeast and bacteria. (
  • Oxidative folding is catalyzed by protein disulfide isomerase ( PDI ) and PDI -related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). (
  • Recombinant Disulfide Oxidoreductase (rDsbA), produced from E.Coli is a periplasmic protein and thioredoxin superfamily member which introduces disulfide bonds directly into substrate proteins by donating the disulfide bond in its active-site Cys30-Pro31-His32-Cys33 to a pair of cysteines in substrate proteins. (
  • One such protein is CYPOR (cytochrome P450 oxidoreductase), which is involved in an extremely avid NO consumption by a colorectal cancer cell line [ 15 ]. (
  • Recommended name: Glucose-fructose oxidoreductase domain-containing protein 2. (
  • Cytochrome P450 oxidoreductase (POR) is a 2-flavin protein that transfers electrons from NADPH via its FAD and FMN moieties to all microsomal cytochrome P450 enzymes, including steroidogenic and drug-metabolizing P450s. (
  • Amino acid oxidoreductases are oxidoreductases, a type of enzyme, that act upon amino acids. (
  • This gene provides instructions for making the enzyme cytochrome P450 oxidoreductase, which plays a critical role in the formation of steroid hormones . (
  • We report a Klebsiella pneumoniae DSM2026 fermentation procedure for the efficient production of a key enzyme of 1,3-propanediol formation: 1,3-propanediol oxidoreductase (E.C. (
  • Lei B, Liu M, Huang S, Tu SC: Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. (
  • By applying an understanding of the mechanisms by which substrate properties influence enzyme activity, a set of semi-quantitative physicochemical criteria (redox potential, hydrophobicity, steric bulk and pKa) was formulated, against which the oxidoreductase degradation susceptibility of twenty-five representative OCs was assessed. (
  • An oxidoreductase enzyme, abundant in tumors, can be catalytically activated by a synthetic cofactor to convert a prodrug to a cytotoxic DNA binding species in human subjects. (
  • A procedure for the purification of the enzyme NADPH:protochlorophyllide oxidoreductase is described. (
  • Succinate:quinone oxidoreductase, or succinate dehydrogenase (complex II), is an enzyme of the tricarboxylic acid cycle, which oxidizes succinate and reduces quinones, without proton translocation. (
  • oxygen oxidoreductase, an aa 3 -type enzyme (complex IV), receives these electrons and transfers them to oxygen. (
  • NAD(P)H:quinone oxidoreductase 1 (NQO1) is a key enzyme involved in metabolism of quinones and may perform multiple functions within the cell. (
  • Conclusions: Considerable species differences in xanthine oxidoreductase activity exist, contrasting with the smaller variations in antioxidant enzyme activities. (
  • We undertook an in-vitro genetic screen of key thiol-disulfide oxidoreductases then completed secondary screens to identify those with mHTT decreasing properties. (
  • Cytochrome P450 oxidoreductase deficiency is a disorder of hormone production. (
  • The hormonal changes associated with cytochrome P450 oxidoreductase deficiency can affect the development of the reproductive system, skeleton, and other parts of the body. (
  • The signs and symptoms of cytochrome P450 oxidoreductase deficiency vary from mild to severe. (
  • People with moderate cytochrome P450 oxidoreductase deficiency usually do not have skeletal abnormalities. (
  • The severe form of cytochrome P450 oxidoreductase deficiency is sometimes called Antley-Bixler syndrome with genital anomalies and disordered steroidogenesis. (
  • Some women who are pregnant with fetuses affected by cytochrome P450 oxidoreductase deficiency experience mild symptoms of the disorder even though they themselves do not have the disorder. (
  • The prevalence of cytochrome P450 oxidoreductase deficiency is unknown. (
  • Researchers suspect that cytochrome P450 oxidoreductase deficiency is underdiagnosed and that mild cases of this disorder may be relatively common. (
  • Because the signs and symptoms can be difficult to detect, people with mild cytochrome P450 oxidoreductase deficiency may never come to medical attention. (
  • Cytochrome P450 oxidoreductase deficiency is caused by mutations in the POR gene. (
  • Mutations in the POR gene reduce the activity of cytochrome P450 oxidoreductase, which disrupts the production of steroid hormones. (
  • In a woman who is pregnant with an affected fetus, abnormal levels of sex hormones in the fetus may cause her to have mild, temporary signs and symptoms of cytochrome P450 oxidoreductase deficiency. (
  • Cytochrome P450 oxidoreductase is also needed for the production of cholesterol. (
  • Mutations in the POR gene can disrupt the production of cholesterol, which likely impairs normal bone formation in the severe form of cytochrome P450 oxidoreductase deficiency. (
  • if a shortage of cytochrome P450 oxidoreductase prevents retinoic acid from being broken down, the resulting excess of that molecule can stimulate the abnormal growth and fusion of bones. (
  • Anti-P450 (cytochrome) oxidoreductase antibodies are readily available from several suppliers. (
  • Your search returned 316 P450 (cytochrome) oxidoreductase Antibodies across 36 suppliers. (
  • Cytochrome P450 oxidoreductase (POR) is the only obligate electron donor for all of the hepatic microsomal CYP enzymes. (
  • Mutations were in the genes encoding the type I tetraheme cytochrome c 3 ( cycA ), Fe hydrogenase ( hydB ), and molybdopterin oxidoreductase ( mopB ). (
  • The main idea of investigation is focused on application of recombinant thermotolerant methylotrophic yeast Hansenula polymorpha "tr6," overproducing D-lactate: cytochrome c oxidoreductase (EC, D - lactate cytochrome c oxidoreductase, D-lactate dehydrogenase (cytochrome), DLDH). (
  • In addition to 6-fold overexpression of DLDH under a strong constitutive promoter ( prAOX ), the strain of H. polymorpha "tr6" ( gcr1 catX/Δcyb2 , prAOX_DLDH ) is characterized by impairment in glucose repression of AOX promoter, devoid of catalase and L-lactate-cytochrome oxidoreductase activities. (
  • Overexpression of DLDH coupling with the deletion of L-lactate-cytochrome oxidoreductase activity opens possibility for usage of the strain as a base for construction of bioreactor for removing D-lactate from fermented products due to oxidation to nontoxic pyruvate. (
  • Five types of terminal oxygen reductases are known in prokaryotes: three types of heme-copper reductases ( 64 ), the cytochrome bd (quinol:oxygen oxidoreductase) ( 13 ), and the so-called alternative oxidase (quinol:oxygen oxidoreductase), which harbors a di-iron center ( 78 ). (
  • Purification of this activity yielded CYPOR (cytochrome P450 oxidoreductase). (
  • Various developmental abnormalities and medical conditions are attributed to metabolic deficiencies that arise from variation in POR , encoding NADPH-cytochrome P450 oxidoreductase [(CYPOR) E.C.]. (
  • WWOX (WW domain containing oxidoreductase), a putative tumor suppressor gene that mapsto the common fragile site FRA16D on chromosome 16q23.3-24.1, is altered in breast, esophageal, and ovarian cancer. (
  • The ΔOx mutant had the transposon located in the MAP3464 gene, a putative oxidoreductase gene whose expression is upregulated upon bacterial contact with MDBK cells. (
  • To our knowledge, no study investigates the association of genetic variant distributions of WW domain-containing oxidoreductase (WWOX) gene with development of invasive cancer, clinicopathologic variables and patient survival in uterine cervical cancer for Taiwanese women. (
  • Relationship between NAD(P)H:quinone oxidoreductase 1 (NQO1) levels in a series of stably transfected cell lines and susceptibility to antitumor quinones. (
  • NAD(P)H quinone oxidoreductase 1 (NQO1, EC ) is a ubiquitous flavoenzyme that catalyzes two electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor . (
  • NAD(P)H:quinone oxidoreductase 1 (NQO1) is a two-electron reductase that has been implicated in the bioactivation of antitumor quinones. (
  • Y-700 [1-[3-Cyano4-(2,2- dimethylpropoxy)phenyl]-1H-pyrazole-4-carboxylic acid]: a potent xanthine oxidoreductase inhibitor with hepatic excretion," Journal of Pharmacology and Experimental Therapeutics, vol. (
  • The aim of this study was to confirm the renoprotective effect of xanthine oxidoreductase (XOR) inhibitor, topiroxostat, compared with another XOR inhibitor, febuxostat, under decreased angiotensin II type 1a (AT1a) receptor expression in the model of renal injury caused by adenine. (
  • NADPH: protochlorophyllide oxidoreductase (POR) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide, a key regulatory reaction in the chlorophyll biosynthetic pathway. (
  • Oxidoreductases are enzymes that catalyze oxidation/reduction reactions by transferring electrons, hydrogens, or oxygens from a reductant molecule to an oxidant molecule. (
  • Quinone oxidoreductases are a class of membrane enzymes that catalyse the oxidation or reduction of membrane-bound quinols/quinones. (
  • NAD(P)H:quinone oxidoreductase 1: role as a superoxide scavenger. (
  • Siegel, D., Bolton, E.M., Burr, J.A., Liebler, D.C. & Ross, D. The reduction of alpha-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of alpha-tocopherolhydroquinone as a cellular antioxidant. (
  • Disclosed is an artificial oxidoreductase having a structure wherein a metal ion binds to a polypeptide having 6 to 13 amino acids. (
  • Catalytic properties of NAD(P)H:quinone acceptor oxidoreductase: study involving mouse, rat, human, and mouse-rat chimeric enzymes. (
  • NAD(P):quinone acceptor oxidoreductase (quinone reductase) (DT-diaphorase, EC is involved in the process of reductive activation of cytotoxic antitumor quinones and nitrobenzenes. (
  • Pharmacogenetics of P450 oxidoreductase: implications in drug metabolism and therapy. (
  • During an analysis of the C. bescii genome sequence for oxidoreductase-type enzymes, evidence was uncovered to suggest that the primary redox metabolism of C. bescii has a completely uncharacterized aspect involving tungsten, a rarely-used element in biology. (
  • A fast change from an aerobic to an anaerobic environment led to a redox imbalance, which resulted in the abrupt activation of the anaerobic branch of glycerol utilization, with the occurrence of a high 1,3-propanediol-oxidoreductase activity. (
  • The concentrations of (2R,3R)-2,3-butanediol are mostly dependent on Bdh1p activity, while those of (meso)-2,3-butanediol are also influenced by the activity of NADP(H)-dependent oxidoreductases. (
  • Effects of topiroxostat and febuxostat on urinary albumin excretion and plasma xanthine oxidoreductase activity in db/db mice," European Journal of Pharmacology, vol. (
  • XO activity was measured as xanthine oxidoreductase (XOR) activity using a method described previously [35]. (
  • The goals of the new project of Prof. ArmenTrchounian's entilted "Redox regulation of activity of microbial oxidoreductases used in bioelectrochemical devices" will be focused on the acivity stimulation of already screened microbial oxidoreducases and optimization of the bioelectrochemical system. (
  • GFOD2 has several biochemical functions, for example, oxidoreductase activity. (
  • Xanthine oxidoreductase activity may be an important free radical source. (
  • In view of the large differences in xanthine oxidoreductase in various species, the activity of these antioxidant enzymes was investigated. (
  • Ahluwalia, ""Repurposing" of xanthine oxidoreductase as a nitrite reductase: a new paradigm for therapeutic targeting in hypertension," Antioxidants & Redox Signaling, vol. (
  • Among them, class I ER oxidoreductase, a plant PDI ortholog, has been studied in a wide variety of plants. (
  • In mammals, electron-transfer flavoprotein:ubiquinone oxidoreductase (ETFQO) and electron-transfer flavoprotein (ETF) are functionally associated, and ETF accepts electrons from at least nine mitochondrial matrix flavoprotein dehydrogenases and transfers them to ubiquinone in the inner mitochondrial membrane. (
  • Fungi produce heme-containing peroxidases and peroxygenases, flavin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases involved in the biodegradation of lignin and other recalcitrant compounds. (
  • In this study, we expressed recombinant soybean Ero 1 ( GmERO1 a) and found that GmERO1 a oxidized multiple soybean ER oxidoreductases, in contrast to mammalian Ero 1s having a high specificity for PDI. (
  • Indeed, using ad hoc software and current computational capabilities, it is now possible to predict substrate access to the active site in biophysical simulations, and electron transfer efficiency in biochemical simulations, reducing in orders of magnitude the time of experimental work in oxidoreductase screening and engineering. (
  • Type II NAD(P)H:quinone oxidoreductases (NDH-2) catalyze the two-electron transfer from NAD(P)H to quinones, without any energy-transducing site. (
  • Computer model of the structure of bovine xanthine oxidoreductase (purple, blue) with residue FAD shown in green. (
  • Disulphide oxidoreductase (DsbA) is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. (
  • We describe some biochemical properties of quinones and quinone oxidoreductases and then look in more detail at two model membranes that can be used to study quinone oxidoreductases in a native-like membrane environment with their native lipophilic quinone substrates. (
  • an oxidoreductase catalyzing the reaction of xanthine, O 2 , and H 2 O to produce urate and superoxide. (
  • Barber EA, Liu Z, Smith SR. Organic Contaminant Biodegradation by Oxidoreductase Enzymes in Wastewater Treatment. (
  • Mechanisms underlying erythrocyte and endothelial nitrite reduction to nitric oxide in hypoxia: role for xanthine oxidoreductase and endothelial nitric oxide synthase," Circulation Research, vol. (
  • Complete restoration of invasion comparable to that for the wt bacterium was achieved by introducing a copy of the complete oxidoreductase operon into the ΔOx mutant. (
  • The engineered application of ligninolytic oxidoreductase fungal enzymes, principally white-rot laccase, lignin peroxidase, and manganese peroxidase, has been identified as a particularly promising approach for OC remediation due to their strong oxidative power, broad substrate specificity, low energy consumption, environmental benignity, and cultivability from lignocellulosic waste. (
  • Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. (
  • Quinone oxidoreductases of the plasma membrane. (
  • An Ls-isocitrate:NADP oxidoreductase has been isolated and purified from embryonic chicken liver. (
  • Variants in the Oxidoreductase PYROXD1 Cause Early-Onset Myopathy with Internalized Nuclei and Myofibrillar Disorganization. (
  • Class I ER oxidoreductases have two catalytically active domains a and a′ , containing active centers composed of Cys-Gly-His-Cys and two catalytically inactive domains b and b′ . (