Oxidoreductases. Medical search

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 1.8.4.2.

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 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.

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 1.6.4.5

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 1.1.3.4.

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 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.

A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.

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 1.3.1.48.

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 1.6.8.1 and EC 1.5.1.29.

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 1.6.4.2.

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 1.1.1.37.

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 1.1.1.21.

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)

... 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 ...

https://en.wikipedia.org/wiki/Amino_acid_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 ... Portal: Biology v t e (EC 1.3, All stub articles, Oxidoreductase stubs). ...

https://en.wikipedia.org/wiki/CH–CH_oxidoreductases

CH-CH oxidoreductases) EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, ... EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases) EC 1.2 includes oxidoreductases ... Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified ... Superfamilies of single-pass transmembrane oxidoreductases in Membranome database Media related to Oxidoreductases at Wikimedia ...

https://en.wikipedia.org/wiki/Oxidoreductase

Bacterial thiol disulfide oxidoreductases (TDOR) are bacterial enzymes which, along with unfolded proteins, are pumped out of a ...

https://en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases

Oxalate oxidoreductases (EC 1.2.7.10) (OOR) are a relatively recently discovered group of enzymes that break down oxalate, a ... Oxalate+oxidoreductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Wikipedia ... The first one to have been characterized has the systematic name oxalate:ferredoxin oxidoreductase. This enzyme catalyses the ... Pierce E, Becker DF, Ragsdale SW (December 2010). "Identification and characterization of oxalate oxidoreductase, a novel ...

https://en.wikipedia.org/wiki/Oxalate_oxidoreductase

... (HAO) is an enzyme found in the prokaryote Nitrosomonas europaea. It plays a critically important ... Portal: Biology v t e (EC 1.7.3, Heme enzymes, Enzymes of known structure, All stub articles, Oxidoreductase stubs). ... Hooper AB, Balny C (1982). "Reaction of oxygen with hydroxylamine oxidoreductase of Nitrosomonas: fast kinetics". FEBS Lett. ... Cedervall, Peder; Hooper, Alan B.; Wilmot, Carrie M. (2013-09-10). "Structural Studies of Hydroxylamine Oxidoreductase Reveal a ...

https://en.wikipedia.org/wiki/Hydroxylamine_oxidoreductase

Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e v t e (EC ... 1.1, All stub articles, Oxidoreductase stubs, EC 1.1 stubs). ...

https://en.wikipedia.org/wiki/Alcohol_oxidoreductase

... (NOR or NXR) is an enzyme involved in nitrification. It is the last step in the process of aerobic ... Spieck E, Muller S, Engel A, Mandelkow E, Patel H (1996). "Two-dimensional structure of membrane-bound nitrite oxidoreductase ... Meincke M, Bock E, Kastrau D, Kroneck PMH (1992). "Nitrite oxidoreductase from Nitrobacter hamburgensis: redox centers and ...

https://en.wikipedia.org/wiki/Nitrite_oxidoreductase

... (EC 1.7.99.8, HAO (ambiguous)) is an enzyme with systematic name hydrazine:acceptor oxidoreductase. ... Hydrazine+oxidoreductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.7.99). ... Schalk J, de Vries S, Kuenen JG, Jetten MS (May 2000). "Involvement of a novel hydroxylamine oxidoreductase in anaerobic ... reduced acceptor Hydrazine oxidoreductase is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria. ...

https://en.wikipedia.org/wiki/Hydrazine_oxidoreductase

Thiol oxidoreductases are proteins that redox control by utilizing catalytic cysteine (Cys) residues for oxidation or reduction ... Some form functional complexes/modules, where one thiol oxidoreductase acts on another. For example, thioredoxin reductase ... Fomenko, Dmitri E.; Gladyshev, Vadim N. (February 2012). "Comparative Genomics of Thiol Oxidoreductases Reveals Widespread and ...

https://en.wikipedia.org/wiki/Thiol_oxidoreductase

Portal: Biology v t e (Oxidoreductases, All stub articles, Enzyme stubs). ...

https://en.wikipedia.org/wiki/OmcS_oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur ... The systematic name of this enzyme class is (3Z)-phytochromobilin:ferredoxin oxidoreductase. Other names in common use include ... In enzymology, a phytochromobilin:ferredoxin oxidoreductase (EC 1.3.7.4) is an enzyme that catalyzes the chemical reaction (3Z ...

https://en.wikipedia.org/wiki/Phytochromobilin:ferredoxin_oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur ... In enzymology, a phycocyanobilin:ferredoxin oxidoreductase (PcyA, EC 1.3.7.5) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is (3Z)-phycocyanobilin:ferredoxin oxidoreductase. This enzyme participates in ...

https://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase

... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index page lists ...

https://en.wikipedia.org/wiki/NADH-CoQ_oxidoreductase

... (EC 1.1.1.328, nboR (gene)) is an enzyme with systematic name 3,3'-bipyridine-2,2',5,5',6,6'-hexol ... Nicotine+blue+oxidoreductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles ... Mihasan M, Chiribau CB, Friedrich T, Artenie V, Brandsch R (April 2007). "An NAD(P)H-nicotine blue oxidoreductase is part of ... NADP+ 11-oxidoreductase. This enzyme catalyses the following chemical reaction 3,3'-bipyridine-2,2',5,5',6,6'-hexol + NAD(P ...

https://en.wikipedia.org/wiki/Nicotine_blue_oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Tersteegen A, Linder D, Thauer RK, Hedderich R (1997). "Structures and functions of four anabolic 2-oxoacid oxidoreductases in ... In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction ( ... The systematic name of this enzyme class is 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole- ...

https://en.wikipedia.org/wiki/Indolepyruvate_ferredoxin_oxidoreductase

The systematic name of this enzyme class is D-glucose:D-fructose oxidoreductase. As of late 2007, 7 structures have been solved ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... In enzymology, a glucose-fructose oxidoreductase (EC 1.1.99.28) is an enzyme that catalyzes the chemical reaction D-glucose + D ... Hardman MJ, Scopes RK (1988). "The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis". Eur. J. Biochem. 173 (1 ...

https://en.wikipedia.org/wiki/Glucose-fructose_oxidoreductase

The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. A representative list ... TCDB: 5.A.1 The Disulfide Bond Oxidoreductase D (DsbD) Family Portal: Biology (Protein pages needing a picture, Protein ... Oxidoreductase Redox Disulfide DsbA Transporter Classification Database Tsu BV, Saier MH (2015-01-01). "The LysE Superfamily of ...

https://en.wikipedia.org/wiki/Disulfide_oxidoreductase_D

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur ... The systematic name of this enzyme class is (3Z)-phycoerythrobilin:ferredoxin oxidoreductase. This enzyme is also called PebB. ... In enzymology, a phycoerythrobilin:ferredoxin oxidoreductase (EC 1.3.7.3) is an enzyme that catalyzes the chemical reaction (3Z ...

https://en.wikipedia.org/wiki/Phycoerythrobilin:ferredoxin_oxidoreductase

Other names in common use include hydrogen-ubiquinone oxidoreductase, hydrogen:menaquinone oxidoreductase, membrane-bound ... This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a quinone or similar ... In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction H2 + quinone ... Portal: Biology v t e (EC 1.12.5, Enzymes of unknown structure, All stub articles, Oxidoreductase stubs). ...

https://en.wikipedia.org/wiki/Hydrogen:quinone_oxidoreductase

... may stand for NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...

https://en.wikipedia.org/wiki/NADH:ubiquinone_oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... VII Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme". Biol. Chem. Hoppe-Seyler. 371 (12): 1137 ... The systematic name of this enzyme class is quinoline:acceptor 2-oxidoreductase (hydroxylating). As of late 2007, only one ... In enzymology, a quinoline 2-oxidoreductase (EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction quinoline + ...

https://en.wikipedia.org/wiki/Quinoline_2-oxidoreductase

... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...

https://en.wikipedia.org/wiki/NADH-ubiquinone_oxidoreductase

... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme This ...

https://en.wikipedia.org/wiki/NADH-Q6_oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... In enzymology, a quinaldate 4-oxidoreductase (EC 1.3.99.18) is an enzyme that catalyzes the chemical reaction quinaldate + ... The systematic name of this enzyme class is quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating). This enzyme is ... XVIII Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia ...

https://en.wikipedia.org/wiki/Quinaldate_4-oxidoreductase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... In enzymology, an isoquinoline 1-oxidoreductase (EC 1.3.99.16) is an enzyme that catalyzes the chemical reaction isoquinoline ... Lehmann M, Tshisuaka B, Fetzner S, Lingens F (1995). "Molecular cloning of the isoquinoline 1-oxidoreductase genes from ... The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating). Lehmann M, Tshisuaka B, ...

https://en.wikipedia.org/wiki/Isoquinoline_1-oxidoreductase

This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase ( ... which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase. AOR ... With formaldehyde ferredoxin oxidoreductase, Glu308 and Tyr 416 would be involved while Glu313 and His448 is shown to be ... The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a ...

https://en.wikipedia.org/wiki/Aldehyde_ferredoxin_oxidoreductase

... may refer to: 4-hydroxyphenylpyruvate dioxygenase 4-hydroxymandelate synthase ...

https://en.wikipedia.org/wiki/4-Hydroxyphenylpyruvate:oxygen_oxidoreductase

The oxidoreductase FAD-binding domain is an evolutionary conserved protein domain. To date, the 3D-structures of the ...

https://en.wikipedia.org/wiki/Oxidoreductase_FAD-binding_domain

... (PORD) is a rare disease and inborn error of metabolism caused by deficiency of ... "P450 Oxidoreductase deficiency: Analysis of mutations and polymorphisms". The Journal of Steroid Biochemistry and Molecular ... "Human P450 Oxidoreductase Deficiency", in Huhtaniemi, Ilpo; Martini, Luciano (eds.), Encyclopedia of Endocrine Diseases (Second ... "NADPH P450 oxidoreductase: structure, function, and pathology of diseases". Pharmacology & Therapeutics. 138 (2): 229-254. doi: ...

https://en.wikipedia.org/wiki/Cytochrome_P450_oxidoreductase_deficiency

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. doi: 10.1007/ ...

https://medlineplus.gov/genetics/condition/cytochrome-p450-oxidoreductase-deficiency/

... Proc Natl Acad Sci U S A. 2017 Nov ... We have tentatively named the flavoprotein "DDOR" (diflavin-linked disulfide oxidoreductase) and propose that its activity is ... These findings expand the structural and mechanistic repertoire of flavoenzymes with oxidoreductase activity and pave the way ...

https://pubmed.ncbi.nlm.nih.gov/29133410/

thiol-disulfide oxidoreductase. A, B, C, D. 148. Bacteroides fragilis NCTC 9343. Mutation(s): 0 Gene Names: BF9343_4170, ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343. Duke, N.E.C., Freeman, L., Tesar, C., Joachimiak, A.. To be ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343. *PDB DOI: 10.2210/pdb3FKF/pdb ... thiol-disulfide oxidoreductase from Bacteroides fragilis NCTC 9343 ...

https://www.rcsb.org/structure/3fkf

More info for Superfamily c.1.4: FMN-linked oxidoreductases. Timeline for Superfamily c.1.4: FMN-linked oxidoreductases: * ... Superfamily c.1.4: FMN-linked oxidoreductases appears in SCOP 1.65. *Superfamily c.1.4: FMN-linked oxidoreductases appears in ... Lineage for Superfamily c.1.4: FMN-linked oxidoreductases. *Root: SCOP 1.67 *. Class c: Alpha and beta proteins (a/b) [51349] ( ... Superfamily c.1.4: FMN-linked oxidoreductases first appeared (with stable ids) in SCOP 1.55. * ...

http://scop.berkeley.edu/sunid=51395&ver=1.67

Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes ... Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance ... Functional expression of the quinoline 2-oxidoreductase genes (qorMSL) in Pseudomonas putida KT2440 pUF1 and in P. putida 86-1 ... X. The molybdopterin cofactors of quinoline oxidoreductases from Pseudomonas putida 86 and Rhodococcus B1 and of xanthine ...

https://brenda-enzymes.org/all_enzymes.php?ecno=1.3.99.17&table=Reference

... hydroxysteroid oxidoreductase. It was interesting to note that ipsilateral administration of allopregnanolone reversed a clear ... hydroxysteroid oxidoreductase, the enzyme that catalyzes progesterone to its active metabolite allopregnanolone. Coherently, we ... The second one is mediated by the enzyme 3α-hydroxysteroid oxidoreductase (3α-HSOR) that catalyzes reduction of ... α-Hydroxysteroid Oxidoreductase and Allopregnanolone as Suggestive of Receptors Involvement. Roberto Yunes. ,1,2Sebastián Casas ...

https://www.hindawi.com/journals/pd/2015/431690/

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https://www.axonmedchem.com/products/enzymes/oxidoreductases/reductases/gsnor

Among these, we focused on GmcA, a putative glucose-methanol-choline oxidoreductase which is upregulated in a ΔflbB background ... GmcA Is a Putative Glucose-Methanol-Choline Oxidoreductase Required for the Induction of Asexual Development in Aspergillus ...

https://addi.ehu.es/handle/10810/9307?locale-attribute=en

... similar to other ferredoxin oxidoreductases. In the present study, the native enzyme was purified from this strain and ... 2-ketoisovalerate ferredoxin oxidoreductase (VOR) is a key enzyme in hyperthermophiles catalyzing the coenzyme A-dependent ... 2-ketoglutarate ferredoxin oxidoreductase (KGOR) [8] and 2-ketoisovalerate ferredoxin oxidoreductase (VOR) [9] are relatively ... Pyruvate ferredoxin oxidoreductase (PFOR) is one of the well-characterized members of the ferredoxin-dependent enzyme family [3 ...

https://file.scirp.org/Html/3-2880056_59459.htm

Tag Archives: NAD(P)H:quinone oxidoreductase 1 NQ01 - a new target for cancer therapy NQO1 [NAD(P)H:quinone oxidoreductase 1 ... quinone oxidoreductase 1, NQ01, oncogene on December 21, 2016. by Joseph Gulfo. ...

http://blogs.shu.edu/cancer/tag/nadphquinone-oxidoreductase-1/

NADPH-cytochrome P450 oxidoreductase (CYPOR) was shown to undergo large conformational rearrangements in its functional cycle. ... NADPH-cytochrome P450 oxidoreductase (CYPOR) was shown to undergo large conformational rearrangements in its functional cycle. ... Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast ... "Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast ...

https://epublications.marquette.edu/chem_fac/533/

Engineering of fungal oxidoreductases and thin-film electrodes for improvement of membraneless biofuel cells and carbohydrate ...

https://portal.research.lu.se/en/publications/improving-the-biocatalyst-engineering-of-fungal-oxidoreductases-a/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Fsystematicreview&ordering=type&descending=false

Keywords: xanthine oxidoreductase, breast cancer, NKG2D ligand, uric acid, MAP kinase. Received: January 19, 2016 Accepted: ... Xanthine oxidoreductase is required for genotoxic stress-induced NKG2D ligand expression and gemcitabine-mediated antitumor ... Here, we report that inhibition of xanthine oxidoreductase (XOR) activity by allopurinol or inhibition of XOR expression by ...

https://www.oncotarget.com/article/11042/

EC 1 - Oxidoreductases EC 1.1 - Acting on the CH-OH group of donors EC 1.1.1 - With NAD+ or NADP+ as acceptor ...

https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.1.1.350

Amino Acid Oxidoreductases* / isolation & purification * Ammonia-Lyases * Carbon Isotopes * Carboxylic Acids * Centrifugation, ...

https://pubmed.ncbi.nlm.nih.gov/4399881/?dopt=Abstract

View mouse Ints14 Chr9:64868187-64894260 with: sequences, polymorphisms, proteins, references, function, expression

https://www.informatics.jax.org/marker/MGI:1917132

The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is ...

https://www.cdek.liu.edu/mesh/D010088/

Superfamily c.1.4: FMN-linked oxidoreductases [51395] (1 family) *. Family c.1.4.1: FMN-linked oxidoreductases [51396] (15 ... Timeline for Protein Old yellow enzyme (OYE) from c.1.4.1: FMN-linked oxidoreductases: *Protein Old yellow enzyme (OYE) from c. ... Protein Old yellow enzyme (OYE) from c.1.4.1: FMN-linked oxidoreductases appears in SCOP 1.65. *Protein Old yellow enzyme (OYE ... Protein Old yellow enzyme (OYE) from c.1.4.1: FMN-linked oxidoreductases appears in the current release, SCOPe 2.08. ...

http://scop.berkeley.edu/sunid=51401&ver=1.67

We assayed, by PCR-RFLP, for a polymorphism in an enzyme that detoxifies quinones, NAD(P)H:quinone oxidoreductase (NQO1), in a ... We assayed, by PCR-RFLP, for a polymorphism in an enzyme that detoxifies quinones, NAD(P)H:quinone oxidoreductase (NQO1), in a ... A lack of a functional NAD(P)H:quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL ... A lack of a functional NAD(P)H:quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL ...

https://www.well.ox.ac.uk/publications/991674

Dataset: prot-a- ...

https://gwas.mrcieu.ac.uk/datasets/prot-a-1389/

sulfide:quinone oxidoreductase ...

http://rails.biochem.susx.ac.uk/gos/3261

Oxidoreductases Acting on Aldehyde or Oxo Group Donors*Oxidoreductases Acting on Aldehyde or Oxo Group Donors ... "Oxidoreductases Acting on Aldehyde or Oxo Group Donors" is a descriptor in the National Library of Medicines controlled ... A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in ... This graph shows the total number of publications written about "Oxidoreductases Acting on Aldehyde or Oxo Group Donors" by ...

https://researchers.childrensmercy.org/display/25837

Follow Flavin-containing amine oxidoreductase to get latest updates from Flavin-containing amine oxidoreductase ... Flavin-containing amine oxidoreductase is on Rediff pages, , ... Flavin-containing amine oxidoreductases are a family of various ... to get instant updates about Flavin-Containing Amine Oxidoreductase on your MyPage. Meet other similar minded people. Its ...

http://pages.rediff.com/flavin-containing-amine-oxidoreductase/1653502

The NADP-dependent oxidoreductase L4BD family has 2 members , canSAR.ai ...

https://cansar.ai/protein-family/NADP-dependent%20oxidoreductase%20L4BD%20family

Oxidoreductase. katE. DM42_4492. DM42_7100. annotation not available. Catalase family protein; Serves to protect cells from the ... Oxidoreductase. polA. DM42_4492. DM42_4183. annotation not available. In addition to polymerase activity, this DNA polymerase ... Oxidoreductase. ahpC. DM42_4492. DM42_3874. annotation not available. Nadh-dependent peroxiredoxin subunit c; Thiol-specific ... Oxidoreductase. ahpC_3. DM42_4492. DM42_1017. annotation not available. Thioredoxin-dependent peroxiredoxin; Peroxidase; C- ...

https://string-db.org/network/292.DM42_4492

The mission of CDCs Public Health Genomics is to integrate advances in human genetics into public health research, policy, and programs

https://www.cdc.gov/genomics/resources/books/huge/tables/chap09_tables.htm

NADH:ubiquinone oxidoreductase subunit A6. 0.5610. 77. ATP5MC1. ATP synthase membrane subunit c locus 1. 0.5506. 18. ...

http://www.proteinatlas.org/ENSG00000091483-FH/single+cell+type

Phylogenetic analysis of Pyruvate and other 2-ketoacid oxidoreductases from hyperthermophiles.. In: Biochemistry and physiology ...

https://tubiblio.ulb.tu-darmstadt.de/50553/

Cytochrome P450 oxidoreductase deficiency is a disorder of hormone production. (medlineplus.gov)
The hormonal changes associated with cytochrome P450 oxidoreductase deficiency can affect the development of the reproductive system, skeleton, and other parts of the body. (medlineplus.gov)
The signs and symptoms of cytochrome P450 oxidoreductase deficiency vary from mild to severe. (medlineplus.gov)
People with moderate cytochrome P450 oxidoreductase deficiency usually do not have skeletal abnormalities. (medlineplus.gov)
The severe form of cytochrome P450 oxidoreductase deficiency is sometimes called Antley-Bixler syndrome with genital anomalies and disordered steroidogenesis. (medlineplus.gov)
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. (medlineplus.gov)
The prevalence of cytochrome P450 oxidoreductase deficiency is unknown. (medlineplus.gov)
Researchers suspect that cytochrome P450 oxidoreductase deficiency is underdiagnosed and that mild cases of this disorder may be relatively common. (medlineplus.gov)
Because the signs and symptoms can be difficult to detect, people with mild cytochrome P450 oxidoreductase deficiency may never come to medical attention. (medlineplus.gov)
Cytochrome P450 oxidoreductase deficiency is caused by mutations in the POR gene. (medlineplus.gov)
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. (medlineplus.gov)
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. (medlineplus.gov)

This gene provides instructions for making the enzyme cytochrome P450 oxidoreductase, which plays a critical role in the formation of steroid hormones . (medlineplus.gov)
Also, in order to find potential explanatory mechanisms, we studied expression and activity of nigrostriatal 3 α -hydroxysteroid oxidoreductase, the enzyme that catalyzes progesterone to its active metabolite allopregnanolone. (hindawi.com)
The second one is mediated by the enzyme 3 α -hydroxysteroid oxidoreductase (3 α -HSOR) that catalyzes reduction of dihydroprogesterone to ALLO [ 16 - 18 ]. (hindawi.com)
2-ketoisovalerate ferredoxin oxidoreductase (VOR) is a key enzyme in hyperthermophiles catalyzing the coenzyme A-dependent oxidative decarboxylation of aliphatic amino acid-derived 2-keto acids. (scirp.org)
The enzyme purified under anaerobic conditions from a hyperthermophilic archaeon, Thermococcus profundus, is a hetero-octamer (αβγδ) 2 consisting of four different subunits, α = 45 kDa, β = 31 kDa, γ = 22 kDa and δ = 13 kDa, respectively, and it has three [4Fe-4S] clusters per αβγδ-protomer, similar to other ferredoxin oxidoreductases. (scirp.org)
We assayed, by PCR-RFLP, for a polymorphism in an enzyme that detoxifies quinones, NAD(P)H:quinone oxidoreductase (NQO1), in a series (n = 36) of infant leukemias with MLL rearrangements versus unselected cord blood controls (n = 100). (ox.ac.uk)
For example, polymorphisms of NAD(P)H:quinone oxidoreductase (NQO1), an enzyme that metabolizes benzene derivatives, are associated with an increased risk of AML. (medscape.com)
Incubation o f these pchlide con- taining PLB-like tubules under red light with N A D PH : pchlide oxidoreductase led to a specific association of the enzyme protein to the tubules. (mpg.de)
Complex II (Succinate-ubiquinone oxidoreductase) is an importnat enzyme complex for the tricarboxylic acid cycle and the aerobic respiratory chain of motochondria and procaryotic organisms (12, 24). (bvsalud.org)

NQO1 [NAD(P)H:quinone oxidoreductase 1 over-expression has been shown to confer a poor prognosis for patients with cancer of the breast, colon, cervix, lung and pancreas. (shu.edu)
We analyzed the signaling pathway for induction of detoxification gene NAD (P)H:quinone oxidoreductase (Nqo1) by As. (cdc.gov)

NADPH-cytochrome P450 oxidoreductase (CYPOR) was shown to undergo large conformational rearrangements in its functional cycle. (marquette.edu)
To develop a whole-cell oxidoreductase system without the practical limitation of substrate/product transport, easy preparation, stability of enzymes, and low expression levels, we here report the development of a whole cell biocatalyst displaying rat NADPH-cytochrome P450 oxidoreductase (CPR, 77-kDa) on the surface of Escherichia coli by using ice-nucleation protein from Pseudomonas syringae. (kribb.re.kr)

Among these, we focused on GmcA, a putative glucose-methanol-choline oxidoreductase which is upregulated in a ΔflbB background. (ehu.es)

Flavin-containing amine oxidoreductases are a family of various amine oxidases , including maize polyamine oxidase (PAO), L- amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). (rediff.com)

We have tentatively named the flavoprotein "DDOR" (diflavin-linked disulfide oxidoreductase) and propose that its activity is linked to a thiol-based transfer of reducing equivalents in bacterial membranes. (nih.gov)
Many secreted proteins require addition of disulfide bonds by the DsbA disulfide oxidoreductase for activity or stability. (umassmed.edu)

Cytochrome P450 oxidoreductase (POR) deficiency is a rare autosomal recessive disorder caused by mutations in the POR gene encoding an electron donor for all microsomal P450 enzymes. (e-apem.org)
Cytochrome P450 oxidoreductase (POR) deficiency (OMIM #613571) is a rare autosomal recessively-inherited form of congenital adrenal hyperplasia that was first reported in 1985 [ 1 ]. (e-apem.org)

These findings expand the structural and mechanistic repertoire of flavoenzymes with oxidoreductase activity and pave the way to explore new protein engineering approaches aimed at designing redox-active proteins for diverse biotechnological applications. (nih.gov)
A Disulfide-bond-A Oxidoreductase-like Protein (DsbA-L) Regulates Adiponectin MultimeriZation. (unm.edu)
Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. (silverchair.com)
Alteration of pulmonary xenobiotic pathways was determined by monitoring the protein levels and activities of P-450 isozymes (CYP1A1 and CYP2B1), glutathioneS-transferase (GST), and NADPH:quinone oxidoreductase (QR). (cdc.gov)

Oxidoreductases Acting on Aldehyde or Oxo Group Donors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (childrensmercy.org)

The 2-ketoisovalerate ferredoxin oxidoreductase (VOR) catalyzes a reaction to produce acetyl CoA in the presence of coenzyme A from these 2-keto acids through oxidative decarboxylation. (scirp.org)

Here, we report that inhibition of xanthine oxidoreductase (XOR) activity by allopurinol or inhibition of XOR expression by gene knockdown abrogated genotoxic stress-induced expression of MICA/B and Rae I in three tumor cell lines. (oncotarget.com)

This graph shows the total number of publications written about "Oxidoreductases Acting on Aldehyde or Oxo Group Donors" by people in this website by year, and whether "Oxidoreductases Acting on Aldehyde or Oxo Group Donors" was a major or minor topic of these publications. (childrensmercy.org)
Below are the most recent publications written about "Oxidoreductases Acting on Aldehyde or Oxo Group Donors" by people in Profiles. (childrensmercy.org)

Oxidoreductases are a large class of enzymes that use unpaired electrons to facilitate redox reactions with other chemical species and are involved in nearly all aspects of life. (nature.com)

The systematic name is based on donor:acceptor oxidoreductase. (liu.edu)

A set of genes with higher basal expression in both H471 and P28 compared with HHZ were functionally enriched in oxidoreductase and lyase activities, implying their positive role in intrinsic DT. (biomedcentral.com)

Mutations in the POR gene reduce the activity of cytochrome P450 oxidoreductase, which disrupts the production of steroid hormones. (medlineplus.gov)
We found that progesterone, in addition to an apparent neuroprotective effect, also increased ipsilateral expression and activity of 3 α -hydroxysteroid oxidoreductase. (hindawi.com)

All enzymes that can catalyze the oxidation-reduction reaction of a substrate are called oxidoreductases. (articlesfactory.com)

Identification of a gene encoding a novel thiosulfate:quinone oxidoreductase in marine Acidithiobacillus sp. (elsevier.com)

Human manganese superoxide dismutase is a critical oxidoreductase found in the mitochondrial matrix. (nature.com)

Isolation and characterization of the quinoline oxidoreductase from Rhodococcus sp. (brenda-enzymes.org)

Organización molecular del complejo II y su rol en la anaerobiosis. (bvsalud.org)

A novel thiosulfate:quinone oxidoreductase from strain SH (SH-TQO) has been purified from its solubilized membrane fraction. (elsevier.com)

A lack of a functional NAD(P)H:quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL fusions. (ox.ac.uk)

This system will allow us to select and develop oxidoreductases, containing bulky and complex prosthetic groups of FAD and FMN, into practically useful whole-cell biocatalysts for broad biological and biotechnological applications including the selective synthesis of new chemicals and pharmaceuticals, bioconversion, bioremediation, and bio-chip development. (kribb.re.kr)
Arsenic induces NAD (P)H-quinone oxidoreductase I by disrupting the Nrf2·Keap1·Cul3 complex and recruiting Nrf2·Maf to the antioxidant response element enhancer. (cdc.gov)

ROS levels are central to programmed cell death and abnormal regulation by these oxidoreductases play significant roles in cancer and cardiovascular diseases 5 . (nature.com)

Anatomy5

Organisms13

Chemicals and Drugs76

Analytical, Diagnostic and Therapeutic Techniques and Equipment18

Phenomena and Processes45

Information Science4

Health Care1

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

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

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)

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

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

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

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

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

Oxidoreductases

Protein Disulfide Reductase (Glutathione)

Pyruvate Synthase

NADH, NADPH Oxidoreductases

Alcohol Oxidoreductases

Ketone Oxidoreductases

Glutaredoxins

NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases

Protein Disulfide-Isomerases

Oxidoreductases Acting on Sulfur Group Donors

Oxidation-Reduction

Thioredoxins

Flavoproteins

Quinone Reductases

Oxidoreductases Acting on Aldehyde or Oxo Group Donors

Electron Transport Complex II

Nanoarchaeota

Wolinella

Amino Acid Sequence

Molecular Sequence Data

Thioredoxin-Disulfide Reductase

Succinate Dehydrogenase

Disulfides

Ecological and Environmental Processes

Glucose Oxidase

Electron Transport

Oxidoreductases Acting on CH-CH Group Donors

Ferredoxin-NADP Reductase

Electron Transport Complex I

NAD(P)H Dehydrogenase (Quinone)

15-Oxoprostaglandin 13-Reductase

Aldehyde Oxidoreductases

NADP

Pleurotus

Flavin-Adenine Dinucleotide

NAD

Sequence Homology, Amino Acid

Coenzymes

Iron-Sulfur Proteins

Flavins

Escherichia coli

Oxidoreductases Acting on CH-NH2 Group Donors

Prokaryotic Cells

Catalysis

Protochlorophyllide

Sequence Alignment

Cysteine

Substrate Specificity

FMN Reductase

Electrons

Periplasm

Glucose 1-Dehydrogenase

Isomerases

Flavodoxin

Rhodobacter capsulatus

Multienzyme Complexes

Glutathione Reductase

Protein Folding

Bacterial Proteins

Models, Molecular

Hydroxysteroid Dehydrogenases

PQQ Cofactor

Binding Sites

Sulfhydryl Compounds

Periplasmic Proteins

Xanthine Dehydrogenase

Oxidoreductases, O-Demethylating

Archaea

Succinic Acid

Sugar Alcohol Dehydrogenases

Fumarates

Mutation

Malate Dehydrogenase

Ferredoxins

Cloning, Molecular

Base Sequence

Selenocysteine

Dihydrolipoamide Dehydrogenase

Kinetics

Multigene Family