Amino Acid Oxidoreductases: A class of enzymes that catalyze oxidation-reduction reactions of amino acids.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Protein Disulfide Reductase (Glutathione): An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Pyruvate Synthase: A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.NADH, NADPH Oxidoreductases: A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.Glutaredoxins: A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.NAD (+) and NADP (+) Dependent Alcohol OxidoreductasesSequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Protein Disulfide-Isomerases: Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Oxidoreductases Acting on Sulfur Group Donors: Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Thioredoxins: 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.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.FlavoproteinsMutation: 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.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Quinone Reductases: NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.Oxidoreductases Acting on Aldehyde or Oxo Group Donors: A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.Bacterial Proteins: Proteins found in any species of bacterium.Kinetics: The rate dynamics in chemical or physical systems.Electron Transport Complex II: A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Nanoarchaeota: A kingdom of hyperthermophilic ARCHAEA found in diverse environments.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Wolinella: A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Thioredoxin-Disulfide Reductase: A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5Succinate Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.Genes, Bacterial: The functional hereditary units of BACTERIA.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Structure-Activity Relationship: 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.Amino Acids, Aromatic: Amino acids containing an aromatic side chain.Electron Transport: The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)Oxidoreductases Acting on CH-CH Group Donors: A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.Molecular Weight: The sum of the weight of all the atoms in a molecule.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Amino Acids, SulfurEcological and Environmental Processes: Ecosystem and environmental activities, functions, or events.Glucose Oxidase: An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Leucine: An essential branched-chain amino acid important for hemoglobin formation.NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Ferredoxin-NADP Reductase: An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Flavin-Adenine Dinucleotide: A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Proteins: 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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Electron Transport Complex I: A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.NAD(P)H Dehydrogenase (Quinone): A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.Plasmids: 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.Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Pleurotus: A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)15-Oxoprostaglandin 13-Reductase: (5Z)-(15S)-11 alpha-Hydroxy-9,15-dioxoprostanoate:NAD(P)+ delta(13)-oxidoreductase. An enzyme active in prostaglandin E and F catabolism. It catalyzes the reduction of the double bond at the 13-14 position of the 15-ketoprostaglandins and uses NADPH as cofactor. EC 1.3.1.48.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Iron-Sulfur Proteins: A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Flavins: Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.Prokaryotic Cells: Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Open Reading Frames: 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).Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Isomerases: A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Oxidoreductases Acting on CH-NH2 Group Donors: Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Sequence Homology: The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.Membrane Proteins: 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.Protochlorophyllide: A photo-active pigment localized in prolamellar bodies occurring within the proplastids of dark-grown bean leaves. In the process of photoconversion, the highly fluorescent protochlorophyllide is converted to chlorophyll.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Electrons: Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Sulfhydryl Compounds: Compounds containing the -SH radical.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).FMN Reductase: An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.Periplasm: The space between the inner and outer membranes of a cell that is shared with the cell wall.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Isoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Rhodobacter capsulatus: Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.Flavodoxin: A low-molecular-weight (16,000) iron-free flavoprotein containing one molecule of flavin mononucleotide (FMN) and isolated from bacteria grown on an iron-deficient medium. It can replace ferredoxin in all the electron-transfer functions in which the latter is known to serve in bacterial cells.Amino Acids, Basic: Amino acids with side chains that are positively charged at physiological pH.Fungal Proteins: Proteins found in any species of fungus.Lysine: An essential amino acid. It is often added to animal feed.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Genetic Complementation Test: 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.Species Specificity: The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Glutathione Reductase: Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.Archaea: One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)PQQ Cofactor: A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Cyanogen Bromide: Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Ferredoxins: Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Periplasmic Proteins: Proteins found in the PERIPLASM of organisms with cell walls.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Amino Acids, DiaminoGlutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Bacteria: One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Circular Dichroism: 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)Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Excitatory Amino Acids: Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Arginine: An essential amino acid that is physiologically active in the L-form.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Gene Library: A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Xanthine Dehydrogenase: An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Oxidoreductases, O-Demethylating: Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Succinic Acid: A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Amino Acid Transport System A: A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.Amino Acids, Neutral: Amino acids with uncharged R groups or side chains.Sugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Selenocysteine: A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.Tryptophan: An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Fumarates: Compounds based on fumaric acid.Mutagenesis, Insertional: 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.Clostridium: A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Operon: 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.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Selenoproteins: Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.Anaerobiosis: The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Metalloproteins: Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Viral Proteins: Proteins found in any species of virus.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Electron Transport Complex III: A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Receptors, Amino Acid: Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Epitopes: Sites on an antigen that interact with specific antibodies.Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.Quinones: Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.

NADH-glutamate synthase in alfalfa root nodules. Genetic regulation and cellular expression. (1/1399)

NADH-dependent glutamate synthase (NADH-GOGAT; EC 1.4.1.14) is a key enzyme in primary nitrogen assimilation in alfalfa (Medicago sativa L.) root nodules. Here we report that in alfalfa, a single gene, probably with multiple alleles, encodes for NADH-GOGAT. In situ hybridizations were performed to assess the location of NADH-GOGAT transcript in alfalfa root nodules. In wild-type cv Saranac nodules the NADH-GOGAT gene is predominantly expressed in infected cells. Nodules devoid of bacteroids (empty) induced by Sinorhizobium meliloti 7154 had no NADH-GOGAT transcript detectable by in situ hybridization, suggesting that the presence of the bacteroid may be important for NADH-GOGAT expression. The pattern of expression of NADH-GOGAT shifted during root nodule development. Until d 9 after planting, all infected cells appeared to express NADH-GOGAT. By d 19, a gradient of expression from high in the early symbiotic zone to low in the late symbiotic zone was observed. In 33-d-old nodules expression was seen in only a few cell layers in the early symbiotic zone. This pattern of expression was also observed for the nifH transcript but not for leghemoglobin. The promoter of NADH-GOGAT was evaluated in transgenic alfalfa plants carrying chimeric beta-glucuronidase promoter fusions. The results suggest that there are at least four regulatory elements. The region responsible for expression in the infected cell zone contains an 88-bp direct repeat.  (+info)

The mechanism of rhythmic ethylene production in sorghum. The role of phytochrome B and simulated shading. (2/1399)

Mutant sorghum (Sorghum bicolor [L.] Moench) deficient in functional phytochrome B exhibits reduced photoperiodic sensitivity and constitutively expresses a shade-avoidance phenotype. Under relatively bright, high red:far-red light, ethylene production by seedlings of wild-type and phytochrome B-mutant cultivars progresses through cycles in a circadian rhythm; however, the phytochrome B mutant produces ethylene peaks with approximately 10 times the amplitude of the wild type. Time-course northern blots show that the mutant's abundance of the 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase mRNA SbACO2 is cyclic and is commensurate with ethylene production, and that ACC oxidase activity follows the same pattern. Both SbACO2 abundance and ACC oxidase activity in the wild-type plant are very low under this regimen. ACC levels in the two cultivars did not demonstrate fluctuations coincident with the ethylene produced. Simulated shading caused the wild-type plant to mimic the phenotype of the mutant and to produce high amplitude rhythms of ethylene evolution. The circadian feature of the ethylene cycle is conditionally present in the mutant and absent in the wild-type plant under simulated shading. SbACO2 abundance in both cultivars demonstrates a high-amplitude diurnal cycle under these conditions; however, ACC oxidase activity, although elevated, does not exhibit a clear rhythm correlated with ethylene production. ACC levels in both cultivars show fluctuations corresponding to the ethylene rhythm previously observed. It appears that at least two separate mechanisms may be involved in generating high-amplitude ethylene rhythms in sorghum, one in response to the loss of phytochrome B function and another in response to shading.  (+info)

Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein. (3/1399)

Highly active D-proline reductase was obtained from Clostridium sticklandii by a modified purification scheme. The cytoplasmic enzyme had a molecular mass of about 870 kDa and was composed of three subunits with molecular masses of 23, 26, and 45 kDa. The 23-kDa subunit contained a carbonyl group at its N terminus, which could either be labeled with fluorescein thiosemicarbazide or removed by o-phenylenediamine; thus, N-terminal sequencing became feasible for this subunit. L-[14C]proline was covalently bound to the 23-kDa subunit if proline racemase and NaBH4 were added. Selenocysteine was detected in the 26-kDa subunit, which correlated with an observed selenium content of 10.6 g-atoms in D-proline reductase. No other non-proteinaceous cofactor was identified in the enzyme. A 4.8-kilobase pair (kb) EcoRI fragment was isolated and sequenced containing the two genes prdA and prdB. prdA coding for a 68-kDa protein was most likely translated as a proprotein that was posttranslationally cleaved at a threonine-cysteine site to give the 45-kDa subunit and most probably a pyruvoyl-containing 23-kDa subunit. The gene prdB encoded the 26-kDa subunit and contained an in frame UGA codon for selenocysteine insertion. prdA and prdB were transcribed together on a transcript of 4.5 kb; prdB was additionally transcribed as indicated by a 0.8-kb mRNA species.  (+info)

Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis. (4/1399)

The substrate-specific selenoprotein B of glycine reductase (PBglycine) from Eubacterium acidaminophilum was purified and characterized. The enzyme consisted of three different subunits with molecular masses of about 22 (alpha), 25 (beta) and 47 kDa (gamma), probably in an alpha 2 beta 2 gamma 2 composition. PBglycine purified from cells grown in the presence of [75Se]selenite was labeled in the 47-kDa subunit. The 22-kDa and 47-kDa subunits both reacted with fluorescein thiosemicarbazide, indicating the presence of a carbonyl compound. This carbonyl residue prevented N-terminal sequencing of the 22-kDa (alpha) subunit, but it could be removed for Edman degradation by incubation with o-phenylenediamine. A DNA fragment was isolated and sequenced which encoded beta and alpha subunits of PBglycine (grdE), followed by a gene encoding selenoprotein A (grdA2) and the gamma subunit of PBglycine (grdB2). The cloned DNA fragment represented a second GrdB-encoding gene slightly different from a previously identified partial grdBl-containing fragment. Both grdB genes contained an in-frame UGA codon which confirmed the observed selenium content of the 47-kDa (gamma) subunit. Peptide sequence analyses suggest that grdE encodes a proprotein which is cleaved into the previously sequenced N-terminal 25-kDa (beta) subunit and a 22-kDa (alpha) subunit of PBglycine. Cleavage most probably occurred at an -Asn-Cys- site concomitantly with the generation of the blocking carbonyl moiety from cysteine at the alpha subunit.  (+info)

Oxygen depletion-induced dormancy in Mycobacterium bovis BCG. (5/1399)

Gradual depletion of oxygen causes the shift-down of aerobic growing Mycobacterium bovis BCG to an anaerobic synchronized state of nonreplicating persistence. The persistent culture shows induction of glycine dehydrogenase and alpha-crystallin-like protein and is sensitive to metronidazole.  (+info)

Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. (6/1399)

l-Aspartate oxidase is the first enzyme in the de novo biosynthesis of pyridinic coenzymes in facultative aerobic organisms. The enzyme is FAD dependent and it shares common features with both the oxidase and the fumarate reductase classes of flavoproteins. In this report we focused our attention on the supersecondary structure of the molecule by means of limited proteolysis studies. Moreover the polymerization state of the protein at different pH and the interactions with NAD and its analogues are described. The results suggest that l-aspartate oxidase is a monomer at pH values lower than 4.5 and a dimer at pH values higher than 6.5. The protein is organized in two major domains connected by a flexible loop located in the 120-140 region. The data obtained by limited proteolysis of the holo and the apo form in the presence and in the absence of substrates (fumarate and menadione), inhibitors (succinate) and NAD allows the proposition that both domains are involved in the binding of the flavin coenzyme. Moreover the data reported in this manuscript suggest that NAD inhibits l-aspartate oxidase activity by competing with the flavin for the binding to the enzyme.  (+info)

Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5'-CTTCTT-3' motif. (7/1399)

Expression of yeast genes involved in one-carbon metabolism is controlled by glycine, by L-methionine, and by nitrogen sources. Here we report a novel control element containing a core CTTCTT motif mediating the glycine response, demonstrating that a protein binds this element, that binding is modulated by tetrahydrofolate, and that folate is required for the in vivo glycine response. In an heterologous CYC1 promoter the region needed for the glycine response of GCV2 (encoding the P-subunit of glycine decarboxylase) mediated repression that was relieved by glycine. It was also responsible for L-methionine control but not nitrogen repression. GCV1 and GCV3 have an homologous region in their promoters. The GCV1 region conferred a glycine response on an heterologous promoter acting as a repressor or activator depending on promoter context. A protein was identified that bound to the glycine regulatory regions of GCV1 and GCV2 only if the CTTCTT motif was intact. This protein protected a 17-base pair CATCN7CTTCTT region of GCV2 that is conserved between GCV1 and GCV2. Protein binding was increased by tetrahydrofolate, and use of a fol1 deletion mutant indicated the involvement of a folate in the in vivo glycine response. Tetrahydrofolate or a derivative may act as a ligand for the transcription factor controlling expression of one-carbon metabolism genes.  (+info)

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors. (8/1399)

The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli. A purification procedure, faster than the one used for the enzyme from the natural source (bDASPO), has been set up yielding about 2 mg of pure recombinant protein (rDASPO) per each gram of wet E. coli paste. rDASPO has been shown to possess the same general biochemical properties of bDASPO, except that the former contains only FAD, while the latter is a mixture of two forms, one active containing FAD and one inactive containing 6-OH-FAD (9-20% depending on the preparation). This results in a slightly higher specific activity (about 15%) for rDASPO compared to bDASPO and in facilitated procedures for apoprotein preparation and reconstitution. Redox potentials of -97 mV and -157 mV were determined for free and l-(+)-tartrate complexed DASPO, respectively, in 0.1 M KPi, pH 7.0, 25 degrees C. The large positive shift in the redox potential of the coenzyme compared to free FAD (-207 mV) is in agreement with similar results obtained with other flavooxidases. rDASPO has been used to assess a possible oxidative activity of the enzyme towards a number of compounds used as agonists or antagonists of neurotransmitters, including d-aspartatic acid, d-glutamic acid, N-methyl-d-aspartic acid, d,l-cysteic acid, d-homocysteic acid, d, l-2-amino-3-phosphonopropanoic acid, d-alpha-aminoadipic acid, d-aspartic acid-beta-hydroxamate, glycyl-d-aspartic acid and cis-2, 3-piperidine dicarboxylic acid. Kinetic parameters for each substrate in 50 mM KPi, pH 7.4, 25 degrees C are reported.  (+info)

*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 ...

*List of MeSH codes (D08)

... amino acid oxidoreductases MeSH D08.811.682.664.500.062 --- alanine dehydrogenase MeSH D08.811.682.664.500.125 --- d-amino-acid ... l-amino acid oxidase MeSH D08.811.682.664.500.724 --- leucine dehydrogenase MeSH D08.811.682.664.500.772 --- nitric oxide ... aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224.125.100.500 --- dopa decarboxylase MeSH D08.811.520.224.125.250 --- ... amino acid naphthylamidases MeSH D08.811.277.656.350.100.150.400 --- leucyl-beta-naphthylamidase MeSH D08.811.277.656.350.100. ...

*L-amino-acid dehydrogenase

The systematic name of this enzyme class is L-amino-acid:NAD+ oxidoreductase (deaminating). Nisman, B; Mager, J (9 February ... In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction an L-amino acid + ... H+ The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+. ... "Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes ...

*N-methyl-L-amino-acid oxidase

The systematic name of this enzyme class is N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating). Other names in common ... an L-amino acid + formaldehyde + H2O2 The 3 substrates of this enzyme are N-methyl-L-amino acid, H2O, and O2, whereas its 3 ... a N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the chemical reaction an N-methyl-L-amino acid + H2O ... products are L-amino acid, formaldehyde, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those ...

*D-amino acid dehydrogenase (quinone)

... (EC 1.4.5.1, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase ( ... Amino Acids. 38: 247-255. doi:10.1007/s00726-009-0240-0. PMID 19212808. D-amino acid dehydrogenase (quinone) at the US National ... Olsiewski, P.J.; Kaczorowski, G.J.; Walsh, C. (1980). "Purification and properties of D-amino acid dehydrogenase, an inducible ... This enzyme catalyses the following chemical reaction D-amino acid + H2O + quinone ⇌ {\displaystyle \rightleftharpoons } 2-oxo ...

*Aldehyde ferredoxin oxidoreductase

... they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. AOR is homodimeric. Each 67kDa ... For example, acetaldehyde reaches its kcat/KM value up to 22.0 μM-1s-1. Some bacteria in fact only makes use of amino acids as ... Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. Aldehyde Ferredoxin ... However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated ...

*L-amino-acid oxidase

The systematic name of this enzyme class is L-amino-acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio- ... In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction an L-amino acid + ... Snake venom Oxidoreductase Oxidative deamination D-amino acid oxidase Molecular and Cellular Biology portal. ... The mechanism proceeds via oxidative deamination of the L-amino acid, which affords an imino acid intermediate. Following ...

*NAD(P)H dehydrogenase (quinone 1)

"Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase". FEBS J. 281 ( ... is leading to an amino acid exchange on position 139 from arginine to tryptophane. Furthermore, an alternative RNA splicing ... Yang FY, Guan QK, Cui YH, Zhao ZQ, Rao W, Xi Z (Sep 2012). "NAD(P)H quinone oxidoreductase 1 (NQO1) genetic C609T polymorphism ... ISBN 978-0-12-374113-4. Ross D, Kepa JK, Winski SL, Beall HD, Anwar A, Siegel D (Dec 2000). "NAD(P)H:quinone oxidoreductase 1 ( ...

*Flavin-containing amine oxidoreductase

Tsugeno Y, Ito A (1997). "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B". J. Biol. Chem. ... L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin ... Flavin-containing amine oxidoreductases are a family of various amine oxidases, including maize polyamine oxidase (PAO), ...

*MT-ND6

... replaces the amino acid alanine with the amino acid valine at protein position 72 in the NADH-ubiquinone oxidoreductase chain 6 ... The encoded protein is 18 kDa and composed of 172 amino acids. MT-ND6 is one of seven mitochondrially-encoded subunits of the ... This mutation changes a single amino acid in the NADH dehydrogenase 6 protein at position 64, from methionine to valine. The ... NADH-ubiquinone oxidoreductase chain 6 is a protein that in humans is encoded by the mitochondrial MT-ND6 gene. The ND6 protein ...

*FAD dependent oxidoreductase family

DAO D-amino-acid dehydrogenase D-amino acid oxidase D-aspartate oxidase Glycerol-3-phosphate dehydrogenase Sarcosine oxidase ... D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-amino acid oxidase EC 1.4.3.3 (DAMOX or DAO) is an ... FAD flavoenzyme that catalyses the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have ... In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members ...

*Oxidoreductase

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 ... EC 1.12 includes oxidoreductases that act on hydrogen as donors EC 1.13 includes oxidoreductases that act on single donors with ...

*Chloroflexi (class)

In particular, a four-amino-acid insert in the protein pyruvate flavodoxin/ferredoxin oxidoreductase, a protein which plays ... dephlogisticated muriatic acid air) which was confirmed as such in 1810 by Sir Humphry Davy and named after its pale green ... and fatty acid profiles that are consistently absent in the other suborder. In addition to demarcating taxonomic ranks, CSIs ... Nucleic Acids Research. 18 (7): 1929. doi:10.1093/nar/18.7.1929. PMC 330654 . PMID 1692410. Khadka B, Adeolu M, Blankenship RE ...

*D-amino acid oxidase

This enzyme belongs to the FAD dependent oxidoreductase family, and acts on the CH-NH2 group of D-amino acid donors with oxygen ... DAO DAOA-AS1 D-amino acid dehydrogenase D-amino acid oxidase activator D-aspartate oxidase Diamine oxidase D-Amino-Acid Oxidase ... The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids. DAAO is a candidate ... It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino ...

*Tetrahydrocannabinolic acid synthase

FAD is also bound by hydrogen bonds with neighboring amino acid main chains and side chains. The co-crystallization of THCA ... and aclacinomycin oxidoreductase (AknOx). The FAD moiety is the location of enzymatic activity and is covalently bound to ... THCA synthase is a 60 kDa (~500 amino acids) monomeric enzyme with the isoelectric point at 6.4. Post-translational N-linked ... Enzymes that share similar amino acid sequences include the flavoproteins berberine bridge enzyme (BBE), glucooligosaccharide ...

*ETFB

... fatty acid and amino acid catabolism and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. The gene ... 1991). "RsaI RFLP for electron transport flavoprotein-beta(ETFB)". Nucleic Acids Res. 19 (14): 4021. doi:10.1093/nar/19.14.4021 ...

*Cannabidiolic acid synthase

Its amino acid sequence is partly (40-50%) homologous to several other oxidoreductases, such as berberine bridge enzyme in ... oxygen oxidoreductase (cyclizing, cannabidiolate-forming). It is an oxidoreductase found in Cannabis sativa that catalyses the ... Biochemical analysis of a novel enzyme that catalyzes the oxidocyclization of cannabigerolic acid to cannabidiolic acid". J. ... Cannabidiolic acid synthase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...

*R,R)-butanediol dehydrogenase

1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism. ... D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ ... 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 (R,R)-butane-2,3-diol:NAD+ oxidoreductase. Other names in common use include ...

*Ferrochelatase

Human ferrochelatase is a homodimer composed of two 359 amino acid polypeptide chains. It has a total molecular weight of 85.07 ... Furthermore, heme B is found in cytochrome b, a key component in Q-cytochrome c oxidoreductase (complex III) in oxidative ...

*NAD(P)H dehydrogenase, quinone 2

"Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone ... Strassburg A, Strassburg CP, Manns MP, Tukey RH (2002). "Differential gene expression of NAD(P)H:quinone oxidoreductase and NRH ... Kwiek JJ, Haystead TA, Rudolph J (2004). "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial ... Wang W, Jaiswal AK (2005). "Sp3 repression of polymorphic human NRH:quinone oxidoreductase 2 gene promoter". Free Radic. Biol. ...

*Leghemoglobin reductase

The amino acid sequence of soybean FLbR is highly related to that of the flavin-nucleotide disulfide oxidoreductases, ... The amino acid sequence of soybean FLbR contains a 30-residue signal peptide for translocation into the mitochondria as well as ... The amino acid sequence of soybean FLbR2 has considerable homology with soybean FLbR1 and pea leaf mitochondria DLDH and ... This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as ...

*ALOX12

Leukocyte-type 12-lipoxygenase in these animal species shares 73-86% amino acid identity with human ALOX15 but only 57-66% ... Other systematic names for ALOX12 include platelet-type 12-lipoxygenase, arachidonate:oxygen 12-oxidoreductase, Delta12- ... It metabolizes the omega-3 fatty acid, docosahexaenoic acid (DHA i.e., 4(Z),7(Z),10(Z),13(Z),16(Z),19(Z)-docosahexaenoic acid ... ALOX12 is 75 kilodalton protein composed of 663 amino acids. ... The enzyme participates in arachidonic acid metabolism by ...

*Aldo-keto reductase

cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547-51. PMID 2498333 ... This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. Some proteins of this family contain a potassium ... these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, ... channel beta chain regulatory domain; these are reported to have oxidoreductase activity. AKR1 Steroidogenic enzyme Bohren KM, ...

*Cholesterol 7 alpha-hydroxylase

It is an oxidoreductase. CYP7A1 is located in the endoplasmic reticulum (ER) and is important for the synthesis of bile acid ... Cholesterol 7 alpha hydroxylase consists of 491 amino acids, which on folding forms 23 alpha helices and 26 beta sheets. ... Substrates identified to date include saturated and unsaturated fatty acids, eicosanoids, sterols and steroids, bile acids, ... Bile acids have powerful toxic properties like membrane disruption and there are a wide range of mechanisms to restrict their ...

*Nicotinamide adenine dinucleotide

In organisms, NAD can be synthesized from simple building-blocks (de novo) from the amino acids tryptophan or aspartic acid. In ... Class A oxidoreductases transfer the atom from above; class B enzymes transfer it from below. Since the C4 carbon that accepts ... from an amino acid-either tryptophan (Trp) in animals and some bacteria, or aspartic acid (Asp) in some bacteria and plants. ... For instance, in the active site of NADP-dependent enzymes, an ionic bond is formed between a basic amino acid side-chain and ...

*Mugineic-acid 3-dioxygenase

... deoxymugineic acid + succinate + CO2 Mugineic-acid 3-dioxygenase contains iron(II). Mugineic acid is an amino acid excreted by ... oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction (1) mugineic acid + 2- ... 3-hydroxymugineic acid, 2'-deoxymugineic acid, avenic acid, and distichonic acid. The effectiveness of mugineic acid under iron ... Mugineic-acid 3-dioxygenase (EC 1.14.11.25, IDS2) is an enzyme with systematic name mugineic acid,2-oxoglutarate: ...
Fructosyl amino acid oxidase products available through Novus Biologicals. Browse our Fructosyl amino acid oxidase product catalog backed by our Guarantee+.
The invention provides enzymatic methods for direct determination of percentage of glycated hemoglobin in blood samples without the need of a separated measurement of total hemoglobin content in blood samples. The methods utilizes one or two different types of oxidizing agents which selectively oxidize low-molecular weight reducing substances and high-molecular weight (mainly hemoglobin) reducing substances in blood samples, coupled with enzymatic reactions catalyzed by proteases, fructosyl amino acid oxidase, and peroxidase. The invention provides kits for performing the methods of the invention.
A new use for HMG-CoA reductase inhibitors is provided. In the instant invention, HMG-CoA reductase inhibitors are found to upregulate endothelial cell Nitric Oxide Synthase activity through a mechanism other than preventing the formation of oxidative-LDL. As a result, HMG-CoA reductase inhibitors are useful in treating or preventing conditions that result from the abnormally low expression and/or activity of endothelial cell Nitric Oxide Synthase. Such conditions include pulmonary hypertension, ischemic stroke, impotence, heart failure, hypoxia-induced conditions, insulin deficiency, progressive renal disease, gastric or esophageal motility syndrome, etc. Subjects thought to benefit mostly from such treatments include nonhyperlipidemics and nonhypercholesterolemics, but not necessarily exclude hyperlipidemics and hypercholesterolemics.
A use for rho GTPase function inhibitors is provided. In the instant invention, rho GTPase function inhibitors are found to upregulate endothelial cell Nitric Oxide Synthase activity. As a result, rho GTPase function inhibitors are useful in treating or preventing conditions that result from the abnormally low expression and/or activity of endothelial cell Nitric Oxide Synthase. Such conditions include pulmonary hypertension, ischemic stroke, impotence, heart failure, hypoxia-induced conditions, insulin deficiency, progressive renal disease, gastric or esophageal motility syndrome, etc. Subjects thought to benefit mostly from such treatments include nonhyperlipidemics and nonhypercholesterolemics, but do not necessarily exclude hyperlipidemics and hypercholesterolemics.
References for Abcams Anti-D Amino Acid Oxidase antibody (ab123524). Please let us know if you have used this product in your publication
Gentaur molecular products has all kinds of products like :search , BioBasic \ L_Amino acid oxidase >4 U_mg \ ALS002764 for more molecular products just contact us
购买我们的重组人D Amino Acid Oxidase蛋白。Ab117193为全长蛋白,在大肠杆菌中生产并经过SDS-PAGE实验验证。Abcam提供免费的实验方案,操作技巧及专业的支持。
To evaluate the association profiles of the lysyl oxidase-like 1 gene polymorphisms with pseudoexfoliation syndrome in the Korean population, peripheral blood sampling will be done from the patients with pseudoexfoliation.. And genotypes of the three single nucleotide polymorphisms of lysyl oxidase-like 1 gene , rs1048661, rs3825942, rs2165241 were analyzed by direct sequencing. ...
The active site and substrate-binding mode of MD-ACO1 (Malus domestica Borkh. 1-aminocyclopropane-1-carboxylate oxidase) have been determined using site-directed mutagenesis and comparative modelling methods. The MD-ACO1 protein folds into a compact jelly-roll motif comprised of eight α-helices, 12 β-strands and several long loops. The active site is well defined as a wide cleft near the C-terminus. The co-substrate ascorbate is located in cofactor Fe2+-binding pocket, the so-called 2-His-1-carboxylate facial triad. In addition, our results reveal that Arg244 and Ser246 are involved in generating the reaction product during enzyme catalysis. The structure agrees well with the biochemical and site-directed mutagenesis results. The three-dimensional structure together with the steady-state kinetics of both the wild-type and mutant MD-ACO1 proteins reveal how the substrate specificity of MD-ACO1 is involved in the catalytic mechanism, providing insights into understanding the fruit ripening ...
From: Dave Chinner ,[email protected], In preparation for verifying dir2 block format buffers, factor the read operations out of the block operations (lookup, addname, getdents) and some of the additional logic to make it easier to understand an dmodify the code. Signed-off-by: Dave Chinner ,[email protected], --- fs/xfs/xfs_dir2_block.c , 386 +++++++++++++++++++++++++---------------------- 1 file changed, 209 insertions(+), 177 deletions(-) diff --git a/fs/xfs/xfs_dir2_block.c b/fs/xfs/xfs_dir2_block.c index 53666ca..25ce409 100644 --- a/fs/xfs/xfs_dir2_block.c +++ b/fs/xfs/xfs_dir2_block.c @@ -56,6 +56,178 @@ xfs_dir_startup(void) xfs_dir_hash_dotdot = xfs_da_hashname((unsigned char *).., 2); } +static int +xfs_dir2_block_read( + struct xfs_trans *tp, + struct xfs_inode *dp, + struct xfs_buf **bpp) +{ + struct xfs_mount *mp = dp-,i_mount; + + return xfs_da_read_buf(tp, dp, mp-,m_dirdatablk, -1, bpp, + XFS_DATA_FORK, NULL); +} + +static void +xfs_dir2_block_need_space( + struct ...
A dual-cell device has been designed as an oxidase-like mimic with the oxidation of 3,3′,5,5′-tetramethylbenzidine as a model reaction. This dual-cell device could be also used to study oxidase-like nanozymes. It was found that only the catalytic sites for oxygen reduction are essential and necessary for oxidase-li
Video created by University of Manchester for the course Industrial Biotechnology. This module looks at the production of pharmaceuticals and fine chemicals using biocatalysis. Specifically, we will look at isolated biocatalytic ...
L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA ...
The inode allocator enables random sparse inode chunk allocations in DEBUG mode to facilitate testing. Sparse inode allocations are not always possible, however, depending on the fs geometry. For example, there is no possibility for a sparse inode allocation on filesystems where the block size is large enough to fit one or more inode chunks within a single block. Fix up the DEBUG mode sparse inode allocation logic to trigger random sparse allocations only when the geometry of the fs allows it. Signed-off-by: Brian Foster ,[email protected], --- fs/xfs/libxfs/xfs_ialloc.c , 15 ++++++++------- 1 file changed, 8 insertions(+), 7 deletions(-) diff --git a/fs/xfs/libxfs/xfs_ialloc.c b/fs/xfs/libxfs/xfs_ialloc.c index a18bc75..66efc70 100644 --- a/fs/xfs/libxfs/xfs_ialloc.c +++ b/fs/xfs/libxfs/xfs_ialloc.c @@ -606,20 +606,20 @@ xfs_ialloc_ag_alloc( uint16_t allocmask = (uint16_t) -1; /* init. to full chunk */ struct xfs_inobt_rec_incore rec; struct xfs_perag *pag; - int do_sparse = 0; -#ifdef DEBUG - ...
Buy our Recombinant human D Amino Acid Oxidase protein. Ab86700 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam…
Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ1.: D-Aspartate oxidase (EC 1.4.3.1), which is highly specific to D-aspartate,
Glycine Oxidase H244K, Bacillus subtilis recombinant protein, Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO validated in (PBV11404r-250), Abgent
Basal-like breast carcinoma is characterized by the expression of basal/myoepithelial markers, undifferentiated phenotype, highly aggressive behaviour and frequent triple negative status (ESR-, PR-, Her2neu-). We have previously shown that epithelial-mesenchymal transition (EMT) occurs in basal-like breast tumours and identified Lysyl-oxidase-like 2 (LOXL2) as an EMT player and poor prognosis marker in squamous cell carcinomas. We now show that LOXL2 mRNA is overexpressed in basal-like human breast carcinomas. Breast carcinoma cell lines with basal-like phenotype show a specific cytoplasmic/perinuclear LOXL2 expression, and this subcellular distribution is significantly associated with distant metastatic incidence in basal-like breast carcinomas. LOXL2 silencing in basal-like carcinoma cells induces a mesenchymal-epithelial transition (MET) associated with a decrease of tumourigenicity and suppression of metastatic potential. Mechanistic studies indicate that LOXL2 maintains the mesenchymal ...
In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ↔ 4-methyl-2-oxopentanoate + NH3 + NADH +
Scleroderma is a chronic skin-hardening disease. There are two types of scleroderma. The first type is called limited cutaneous scleroderma, where disrupted blood flow causes skin discoloration and sometimes patients experience high blood pressure in their arteries. The second type is called diffuse cutaneous scleroderma and it is much more aggressive, affecting a larger area of skin causing organ damage. This study will determine if the disease is associated with an elevated expression of LOXL2 levels in tissue samples from patients ...
The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli. A purification procedure, faster than the one used for the enzyme from the natural source (bDASPO), has been set up yielding about 2
Ray, S. S., Sengupta, R., Tiso, M., Haque, M. M., Sahoo, R., Konas, D. W., Aulak, K., Regulski, M. R., Tully, T., Stuehr, D. J., Ghosh, S. (2007) Reductase Domain of Drosophila melanogaster Nitric-Oxide Synthase: Redox Transformations, Regulation, and Similarity to Mammalian Homologues. Biochemistry, 46 (42). pp. 11865-11873. ISSN 0006-2960 (Print) Ray, S. S., Tejero, J., Wang, Z. Q., Dutta, T., Bhattacharjee, A., Regulski, M. R., Tully, T., Ghosh, S., Stuehr, D. J. (2007) Oxygenase Domain of Drosophila melanogaster Nitric Oxide Synthase: Unique Kinetic Parameters Enable a More Efficient NO Release. Biochemistry, 46 (42). pp. 11857-11864. ISSN 0006-2960 (Print) Regulski, M., Stasiv, Y., Tully, T., Enikolopov, G. (2004) Essential function of nitric oxide synthase in Drosophila. Current Biology, 14 (20). R881-R882. ISSN 0960-9822 Regulski, M., Tully, T. (1995) Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase. Proc Natl Acad Sci U S A, ...
3VPX: A psychrophilic leucine dehydrogenase from Sporosarcina psychrophila: Purification, characterization, gene sequencing and crystal structure analysis
1OMO: Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin.
Glycine dehydrogenase (aminomethyl-transferring)Glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2 ...
This SNP, located in an intron of the LOXL1 gene, was initially reported to be associated with exfoliation glaucoma. However, it was shown in the same study to no longer be significant once two other SNPs, which cause actual changes in the LOXL1 protein, were identified. More specifically, the risk allele rs2165241(T) was found to be associated with glaucoma only because it effectively predicted (with 90% probability) the actual high-risk haplotype consisting of rs1048661(G) and rs3825942(C), as oriented with respect to their entries in dbSNP. [PMID 17690259] However, a meta-analysis published in 2010 concluded that its likely that SNPs rs1048661 and rs2165241 are not directly implicated in the pathogenesis of glaucoma; only the nearby rs3825942 seemed to be the disease-associated SNP.[PMID 20142848 ...
Re: [PATCH v3] xfstests: xfs mount option sanity test 2020-01-18 17:23 ` Darrick J. Wong @ 2020-01-19 7:23 ` Zorro Lang 0 siblings, 0 replies; 3+ messages in thread From: Zorro Lang @ 2020-01-19 7:23 UTC (permalink / raw) To: Darrick J. Wong; +Cc: fstests, linux-xfs On Sat, Jan 18, 2020 at 09:23:30AM -0800, Darrick J. Wong wrote: , On Wed, Jan 15, 2020 at 04:11:32PM +0800, Zorro Lang wrote: , , XFS is changing to suit the new mount API, so add this case to make , , sure the changing wont bring in regression issue on xfs mount option , , parse phase, and wont change some default behaviors either. , , , , Signed-off-by: Zorro Lang ,[email protected], , , --- , , , , Hi, , , , , Thanks the suggestions from Darrick, v3 did below changes: , , 1) Add more debug info output in do_mkfs and do_test. , , 2) A new function filter_loop. , , 3) Update .out file content , , , , Ive simply run this case on RHEL-7, RHEL-8 and upstream 5.5-rc4 kernel, , , all passed. , , Something else I noticed -- if for ...
Purified Recombinant Human LOXL2 Protein, His-tagged from Creative Biomart. Recombinant Human LOXL2 Protein, His-tagged can be used for research.
Eubacterium acidaminophilum GrdD protein: Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum; GenBank L04500
Prevalence and Associations of Pseudoexfoliation Glaucoma in a Group of Tertiary Eye Care Facilities in Southwest Nigeria. . 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.
[Purification and isolation of isoenzymes of L-amino acid oxidase from the venom of Bothrops asper].: L-amino acid oxidase (E.C. 1.4.3.2) was purified from the
An NAD-dependent enzyme that catalyzes the reversible Deamination of L-Alanine to PYRUVATE and Ammonia. The enzyme is needed for Growth when Alanine is the sole Carbon or Nitrogen source. It may also play a Role in Cell Wall synthesis because L-Alanine is an important constituent of the PEPTIDOGLYCAN layer ...
Publications Somrutai Winichayakul, Anton Pernthaner, Sam Livingston, Ruth Cookson, Richard Scott, Nick Roberts (2012) Production of active single-chain antibodies in seeds using trimeric polyoleosin fusion. Journal of Biotechnology 161: 407‑413. Scott RW, Yoo SD, Hunter DA, Gong D, Chen B, Leung S and McManus MT (2010) Regulation of 1-aminocyclopropane-1-carboxylate oxidase gene expression during leaf ontogeny in white clover. Plant Growth Regulation 62: 31‑41. Scott RW, Winichayakul S, Roldan M, Cookson R, Willingham M, Castle M, Pueschel R, Peng C-C, Tzen JTC and Roberts NJ (2010) Elevation of oil body integrity and emulsion stability by polyoleosins, multiple oleosin units joined in tandem head to tail fusions. Plant Biotechnology Journal 8: 912‑927. ...
Mixed transition-metal oxides (MTMOs) have attracted much research interest because of their promising applications in artificial enzymes. In this work, uniform hollow MnCo2O4 nanofibers have been fabricated via an electrospinning technique followed by a calcination process, which can be used as efficient oxidase m
La D-aspartato ossidasi è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: D-aspartato + H2O + O2 ⇄ ossalacetato + NH3 + H2O2 È una flavoproteina (FAD). Dixon, M. and Kenworthy, P., D-Aspartate oxidase of kidney, in Biochim. Biophys. Acta, vol. 146, 1967, pp. 54-76, Entrez PubMed 6060479. Still, J.L., Buell, M.V., Knox, W.E. and Green, D.E., Studies on the cyclophorase system. VII. D-Aspartic oxidase, in J. Biol. Chem., vol. 179, 1949, pp. 831-837. Still, J.L. and Sperling, E., On the prosthetic group of the D-aspartic oxidase, in J. Biol. Chem., vol. 182, 1950, pp. 585-589 ...
retitle 336993 initramfs done by yaird with XFS severity 336993 serious thanks I use XFS on a production system and surely I am not alone in that case, so IMHO, it is a dead serious bug. It seems the initramfs implementation is sensitive to cruft at the end of the cpio.gz file. Also, it seems like yaboot might be loading extra data and appending them to the end of the image causing the kernel to fail to unpack the image. Most probably, the issue is located in the xfs_read code of yaboot. We will investigate that... Cheers, -- ((__,--,__)) Aurélien GÉRÔME .---. `--)~ ~(--` Free Software Developer / \ .-( )`-. Unix Sys & Net Admin \[email protected]@./ `~~`@) (@`~~` /`\_/`\ , , .`. // _ \\ , , : : : , \ ),_ (8___8) `. `` /`\_`, ,_/ \ `---` `- \__/---\__/ BOFH excuse #320: Youve been infected by the Telescoping Hubble virus ...
XFS filesystem is fragmented into subgroups. These groups are something like smaller partitions in a bigger one. This allows kernel to use paralellism - it can write to several parts of filesystem at the same time. Offcourse, disk head will still write data in one place after another, because disks have only one head - so this technology gives benefits before data is sent to a disk. If you have too much a. groups, your FS will be divided in many sections, and then its very likely files will get fragmented in between two or even three section. Next bad thing is that when you fill up your FS, itll start to use too much CPU. Those things slows things down dramaticly... It has been tought that at least 1 a. group is needed per 4GB, but some XFS developers denied that information, and marked it as obsolete on LKML recently. So, what to choose here? Depends on how much parallelism do you really need. This thing has its benefits in server usage, but for desktop, 2 allocation groups per one CPU seems ...
In the conceptualization and planning stages of this feature we were certain it was going to be among the best coverage we have offered in regards to exfoliation. Indeed I think the information in this feature as well as the supporting articles is very informative and well written. What I know now that I didnt know before we began the process of talking to potential writers, is how difficult it would be to find four people who were willing to contribute to this feature, primarily because of the title. I can only imagine what they would have said if they had seen the cover and opening art for this feature. Their reaction might have been similar to your own and even ours when we first looked at these images - a bit shocked and taken aback. But lets stay focused, and I will get back to the art in a minute. ...
... refers to the process in which information carried by extracellular messenger molecules is translated into changes that occur inside a cell.
How is Nitric Oxide Synthase Inhibitor NG-Monomethyl-L-Arginine abbreviated? L-NMMA stands for Nitric Oxide Synthase Inhibitor NG-Monomethyl-L-Arginine. L-NMMA is defined as Nitric Oxide Synthase Inhibitor NG-Monomethyl-L-Arginine rarely.
Glycine decarboxylase is a mitochondrial enzyme complex, which is the site of photorespiratory CO2 and NH3 release. Although the proteins that constitute the complex are located within the mitochondria, because of their intimate association with photosynthesis their expression is controlled by light. Comparisons of the kinetics of mRNA accumulation between the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and the H-protein of glycine decarboxylase during the greening of etiolated Arabidopsis thaliana suggest that their expression is controlled in parallel. A genomic clone for the H-protein (gdcH) was isolated from Arabidopsis and sequenced. The upstream region from -856 to +62 was fused to the β-glucuronidase (GUS) reporter gene, and this construct was transformed into tobacco. This 5′ upstream regulatory region appears to control GUS expression in a manner very similar to that of the endogenous H-protein gene. Constructs with deletions in the 5′ upstream region were ...
Purpose.: We examined the association between caffeine and caffeinated beverage consumption in relation to the risk of exfoliation glaucoma or exfoliation glaucoma suspect (EG/EGS). Methods.: We followed 78,977 women from the Nurses Health Study (NHS) and 41,202 men from the Health Professionals Follow-up Study (HPFS) who were at least 40 years of age, did not have glaucoma, and reported undergoing eye examinations from 1980 (NHS) or 1986 (HPFS) to 2008. Information on consumption of caffeine-containing beverages and potential confounders were repeatedly ascertained in validated follow-up questionnaires. Confirmation with medical record review revealed 360 incident EG/EGS cases. Multivariate rate ratios (RRs) for EG/EGS were calculated in each cohort and then pooled using meta-analytic techniques. Results.: Compared with participants whose cumulatively updated total caffeine consumption was ,125 mg/day, participants who consumed ≥500 mg/day had a trend toward increased risk of EG/EGS that was ...
1.Nitric oxide is a potent vasodilator which plays a major role in the control of blood pressure. The hyperdynamic circulation of cirrhosis has been linked to nitric oxide.. 2.We measured neutrophil nitric oxide synthase activity in relation to the level of hepatic dysfunction in patients with liver disease of varying aetiology and severity.. 3.Neutrophils were isolated from 21 patients (7 Child-Pugh score A, 6 grade B and 8 grade C) aged 28-76 (median 49) years. Nitric oxide synthase activity was measured using the conversion of oxyhaemoglobin to methaemoglobin by nitric oxide and expressed in terms of cell protein. Blood pressure and biochemical indices were recorded. Data were assessed using Kruskal-Wallis one-way analysis of variance, Mann-Whitney U-test or Pearson correlation as appropriate.. 4.Systolic, mean arterial and diastolic blood pressures decreased with increasing hepatic damage (P = 0.031, P = 0.01 and P = 0.038 respectively). Nitric oxide synthase activity increased with the ...
HONG, TAN NGET (2009) Snake venom L-amino acid oxidase. In: CRC Handbook of Venoms and Toxins of Reptiles. Taylor and Francis / CRC Press, pp. 219-234. ...
91368PRTRhodococcus qingshengii 1Met Ser Ile Asp Asp Glu Leu Arg Trp Asp Gly Glu Leu Thr Val Thr1 5 10 15Arg His Asp Arg Glu Thr Gly Thr Thr Phe Val Ile Arg Ile Asp Ser 20 25 30Thr Arg Leu Gly Pro Ala Ser Gly Gly Thr Arg Ala Ala His Tyr Pro 35 40 45Ser Ile Gly His Ala Leu Ala Asp Ala Gly Lys Leu Ala Gly Ala Met 50 55 60Thr Leu Lys Met Ala Val Ser Asp Leu Pro Met Gly Gly Gly Lys Ser65 70 75 80Val Ile Ala Leu Pro Ala Pro Arg Asn Gln Ile Asp Ala Ala Thr Trp 85 90 95Ser Arg Ile Leu Gly Ile His Ala Glu Asn Ile Asp Lys Leu Glu Gly 100 105 110Asn Tyr Trp Thr Gly Pro Asp Val Asn Thr Asn Ser Ser Asp Met Asp 115 120 125Gln Leu Ser Arg Thr Thr Arg Tyr Val Phe Gly Arg Ser Val Asp Lys 130 135 140Gly Gly Ala Gly Ser Ser Ala His Ala Thr Ala Leu Gly Val Phe Glu145 150 155 160Ala Met Lys Ala Thr Ala Arg Arg Arg Gly Leu Gly Thr Leu Asp Gly 165 170 175Arg Thr Val Leu Val Gln Gly Leu Gly Ala Val Gly Gly Asp Val Val 180 185 190Arg Leu Ala Ala Gln Ala Gly Ala Arg Leu Leu Val Ala Asp Thr Asp 195 200 205Pro Gln Arg Leu ...
H Subunit Of The Mitochondrial Glycine Decarboxylase Complex; Glycine Decarboxylase Is Required For The Catabolism Of Glycine To 5,10-methylene-THF; Also Required For All Protein Lipoylation; Expression Is Regulated By Levels Of 5,10-methylene-THF
Affiliation:助手, Research Field:応用微生物学・応用生物化学, Keywords:Arthrobacter sp.,Phenylalanine dehydrogenase,Peptide,Opine dehydrogenase,Enzymatic synthesis,Bacillus sphaericus,D-Aminopeptidase,Organic solvent, # of Research Projects:2, # of Research Products:0
Is Skin Exfoliation a common side effect of Tildiem? View Skin Exfoliation Tildiem side effect risks. Female, 60 years of age, was diagnosed with lung abscess and took Tildiem 60 Mg Qd Po. Patient was hospitalized.
The transcriptional activator IFN regulatory factor 1 (IRF-1) and its antagonistic repressor IRF-2 are regulators of the IFN system. IRF-1 also manifests tumor suppressive activity, and its inactivation could contribute to the development of human hematopoietic malignancies. Here, we report the identification of the lysyl oxidase gene as a target gene of IRF-1. An IRF response element was identified in the lysyl oxidase gene promoter. We also demonstrate that the transformed phenotype of ras-expressing embryonic fibroblasts with a null mutation in the IRF-1 allele could be suppressed by the expression of the lysyl oxidase cDNA, implicating its potential role in tumor suppression. Thus, the regulation of the lysyl oxidase gene by IRF-1 could contribute to the multistep process of malignant transformation.. ...
All Natural Facial Peels to achieve the best results of skin exfoliation and help with the skins natural anti-aging process - Jadiences Spa Collection
DAX) provides, as a Technology Preview on the ext4 and XFS file systems, a means for an application to directly map persistent memory into its address space. To use DAX, a system must have some form of persistent memory available, usually in the form of one or more Non-Volatile Dual In-line Memory Modules (NVDIMMs), and a file system that supports DAX must be created on the NVDIMM(s). Also, the file system must be mounted with the ...
Callstack: at Proteins/NESGC/1xfs at Template:Protein at template MindTouch.Deki.Script.Runtime.DekiScriptUndefinedNameException: reference to undefined name note Exception of type MindTouch.Deki.Script.Runtime.DekiScriptUndefinedNameException was thrown. at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Visit (MindTouch.Deki.Script.Expr.DekiScriptVar expr, DekiScriptExpressionEvaluationState state) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Expr.DekiScriptVar.VisitWith[DekiScriptExpressionEvaluationState,Range] (IDekiScriptExpressionVisitor`2 visitor, DekiScriptExpressionEvaluationState state) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Evaluate (MindTouch.Deki.Script.Expr.DekiScriptAccess expr, DekiScriptExpressionEvaluationState state, Boolean evaluateProperties) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Visit ...
This reaction, and by extension the glycine cleavage system, is required for photorespiration in C3 plants. The glycine cleavage system takes glycine, which is created from an unwanted byproduct of the Calvin cycle, and converts it to serine which can reenter the cycle. The ammonia generated by the glycine cleavage system, is assimilated by the Glutamine synthetase-Glutamine oxoglutarate aminotransferase cycle but costs the cell one ATP and one NADPH. The upside is that one CO2 is produced for every two O2 that are mistakenly taken up by the cell, generating some value in an otherwise energy depleting cycle. Together the proteins involved in these reactions comprise about half the proteins in mitochondria from spinach and pea leaves.[3] The glycine cleavage system is constantly present in the leaves of plants, but in small amounts until they are exposed to light. During peak photosynthesis, the concentration of the glycine cleavage system increases ten-fold.[7] In the anaerobic bacteria, ...
Curcumin inhibits nitric oxide synthase gene expression. Curcumin is a naturally occurring, dietary polyphenolic phytochemical that has been shown to inhibit cancer among other things. With respect to inflammation, it inhibits the activation of free radical activated transcription factors, and reduces the production of proinflammatory cytokines such as tumor necrosis factor-alpha (TNF), interleukin-1 and interleukin-8). Upon inflammation, an enzyme is induced (nitric oxide synthase) that catalyzes the production of nitric oxide (NO), a molecule that may lead to carcinogenesis. In this study in mouse immune cells curcumin reduced the production of nitric oxide in a concentration-dependent manner. Furthermore, curcumin reduced nitric oxide expression in the livers of mice by 50-70%. Investigators were able to obtain potency at nanomoles per gram of body weight, even though it is believed that curcumin needs to be given at dosages that are unattainable through diet to produce an in vivo effect. ...
Pseudoexfoliation syndrome, often abbreviated as PEX and sometimes as PES or PXS, is an aging-related systemic disease manifesting itself primarily in the eyes which is characterized by the accumulation of microscopic granular amyloid-like protein fibers. Its cause is unknown, although there is speculation that there may be a genetic basis. It is more prevalent in women than men, and in persons past the age of seventy. Its prevalence in different human populations varies; for example, it is prevalent in Scandinavia. The buildup of protein clumps can block normal drainage of the eye fluid called the aqueous humor and can cause, in turn, a buildup of pressure leading to glaucoma and loss of vision (pseudoexfoliation glaucoma, exfoliation glaucoma). As worldwide populations become older because of shifts in demography, PEX may become a matter of greater concern. Patients may have no specific symptoms. In some cases, patients may complain of lessened visual acuity or changes in their perceived ...
Abstract. King cobra (Ophiophagus hannah) venom L-amino acid oxidase (OH-LAAO), a heat stable enzyme, has been shown to exhibit very potent anti-proliferative activity against human breast and lung tumorigenic cells but not in their non-tumorigenic counterparts. We further examine its in vitro and in vivo anti-tumor activity in a human prostate adenocarcinoma (PC-3) model. OH-LAAO demonstrated potent cytotoxicity against PC-3 cells with IC50 of 0.05 µg/mL after 72 h incubation in vitro. It induced apoptosis as evidenced with an increase in caspase-3/7 cleavages and an increase in annexin V-stained cells. To examine its in vivo anti-tumor activity, we treated PC-3 tumor xenograft implanted subcutaneously in immunodeficient NU/NU (nude) mice with 1 µg/g OH-LAAO given intraperitoneally (i.p.). After 8 weeks of treatment, OH-LAAO treated PC-3 tumors were markedly inhibited, when compared to the control group (P ,0.05). TUNEL staining analysis on the tumor sections showed a significantly increase ...
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As described in Chapter 42, niric oxide (NO) is synthesized from the amino acid l-arginine by the actions of a family of enymes, the NO synthases (NOS), each isoform of which is encoded by a separate gene. Two NOS isoforms are calcium-dependent and constitutively expressed and produce low levels of NO: NOS1 (neuronal NOS or nNOS), which is found mostly in neurons and skeletal muscle, and NOS3 (endothelial NOS or eNOS), which is found mostly in endothelial cells. NOS1 is critical for neurotransmission and learning, and NOS3 regulates vascular tone and adhesion of circulating cells. Inducible NOS (iNOS or NOS2) is transcriptionally induced by proinflammatory cytokines (such as tumor necrosis factor-α [TNF-α] and interferon-γ [IFN-γ]) and microbial products (e.g., lipoplysaccharide [LPS]). iNOS is calciumindependent, expressed by many cell types (especially mononuclear phagocytes, hepatocytes, chondrocytes and smooth muscle cells) and is responsible for high output NO production (1-3). While ...
Purpose: Exfoliation syndrome (XFS) is an age-related disease, manifesting primarily in the eyes. XFS is a very common and recognizable cause of secondary glaucoma world-wide. We sought to better understand the overall disease process of XFS. To this end, we thus conducted a genome-wide association study (GWAS) on ~1500 patients with XFS matched to ~1200 controls from Japan.. Methods: Genome-wide genotyping was performed using the Illumina OmniExpress beadchip, which assesses ,700,000 single nucleotide polymorphisms (SNPs) throughout the human genome. The association between each genetic marker and susceptibility to XFS was measured using logistic regression, contrasting each SNP genotype between XFS patients and controls. The analysis was performed with additional compensation for the top 6 principal components of genetic stratification. We followed up the most significantly associated genetic markers (surpassing P , 1 x 10-4 on primary association analysis) on a further ~7,000 patients and ...
Animal, Base-Sequence, Chromosome-Mapping, Crosses-Genetic, Enzyme-Induction, Genes-Structural, Human, Hybridization, Mice: ge, Mice-Inbred-C57BL, Mice-Inbred-NOD: ge, Molecular-Sequence-Data, Muridae: ge, Rats, Rats-Wistar, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S. ...
PURPOSE: To investigate the outcome of trabeculectomy with or without adjunctive intracameral bevacizumab. MATERIALS AND METHODS: In this prospective, double-blind, randomized clinical trial, 71 patients with primary open-angle or pseudoexfoliation glaucoma were randomly assigned to receive either 1.25 mg intracameral bevacizumab (n=36) or balanced salt solution as placebo (n=35) at the end of trabeculectomy. Success was defined as at least a 30% drop in intraocular pressure (IOP) compared with baseline values and an IOP between 6 and 21 mm Hg at the last postoperative visit with (qualified) or without (complete) glaucoma medications ...
The present invention relates to a novel lysyl oxidase genes, termed EER-7. The invention relates to the protein and nucleic acids encoding the protein. The invention further relates to an assay system to identify compounds that selectively modulate EER-7 protein activity by interaction with estrogen receptors.
Summary of Facts and Submissions. I. The opponent (appellant) filed an appeal against the interlocutory decision of the opposition division dated 26 August 2008 whereby the European patent no. 1 254 957 was maintained in amended form (Article 101(3)(a) EPC). II. The opposition division, finding that the main request before it, claims 1 to 7 as granted, did not meet the requirements of Article 54 EPC, decided that auxiliary request 1, claims 1 to 6 filed on 27 May 2008, met all requirements of the EPC.. Claim 1 of auxiliary request 1 read as follows:. A method for producing an L-amino acid utilizing a microorganism and comprising culturing the microorganism in a medium to produce and accumulate the L-amino acid in the medium and collecting the L-amino acid from the culture, wherein the microorganism is a mutant or recombinant strain of a microorganism in which maltose assimilation is controlled by an interaction between IIA**(Glc) protein of glucose PTS and Malk protein, and the interaction ...
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1. Glycine decarboxylase and glycine-bicarbonate exchange activities were detected in extracts of Rhodopseudomonas spheroides and in rat liver mitochondria and their properties were studied. 2. The glycine decarboxylase activity from both sources is stimulated when glyoxylate is added to the assay system. 3. Several proteins participate in these reactions and a heat-stable low-molecular-weight protein was purified from both sources. 4. These enzyme activities increase markedly when R. spheroides is grown in the presence of glycine, glyoxylate, glycollate, oxalate or serine. 5. All the enzymes required to catalyse the conversion of glycine into acetyl-CoA via serine and pyruvate were detected in extracts of R. spheroides; of these glycine decarboxylase has the lowest activity. 6. The increase in the activity of glycine decarboxylase on illumination of R. spheroides in a medium containing glycine, and the greater increase when ATP is also present in the medium, probably accounts for the increased ...
Victoria blight of oats is caused by the fungus Cochhobolus victoriae. This fungus is pathogenic due to its ability to produce the host-selective toxin victorin. Previously, a 100-kD protein that binds victorin in vivo only in susceptible genotypes was identified as the P protein of the glycine decarboxylase complex (GDC). Victorin is a potent in vivo inhibitor of GDC. Leaf slices pretreated with victorin displayed an effective Victorin inhibited the concentration for 50% inhibition (EC₅₀) of 81 μM for GDA. glycine-bicarbonate exchange reaction in vitro with an EC₅₀ of 23 μM. We also identified a 15-kD mitochondrial protein in susceptible and resistant genotypes that hound victorin. Amino acid sequence analysis indicated this protein is the H protein component of the GDC. Thus, victorin specifically binds to two components of the GDC. Victorin had no detectable effect on GDC in isolated mitochondria, apparently due to the inability of isolated mitochondria to import victorin. The ...
Glycine is a simple amino acid. The glycine cleavage enzyme system comprises four proteins: P-, T-, H- and L-proteins (EC 1.4.4.2, EC 2.1.2.10 and EC 1.8.1.4 for P-, T- and L-proteins). The glycine cleavage system catalyses the oxidative conversion of glycine into carbon dioxide and ammonia, with the remaining one-carbon unit transferred to folate as methylenetetrahydrofolate. It is the main catabolic pathway for glycine and it also contributes to one-carbon metabolism ...
Does the Inhibitory Action of Asymmetric Dimethylarginine (ADMA) on the Endothelial Nitric Oxide Synthase Activity Explain Its Importance in the Cardiovascular System? The ADMA Paradox
Sigma-Aldrich offers abstracts and full-text articles by [Rubén Darío Castro-Torres, Verónica Chaparro-Huerta, Mario Eduardo Flores-Soto, Luis Jave-Suárez, Antoni Camins, Juan Armendáriz-Borunda, Carlos Beas-Zárate, Salvador Mena-Munguía].
The protocol I have seen and used calls for cryostat or sliding microtome/frozen sections of paraformaldehyde-fixed material. Mount sections on slides, I dont think I ever did free-floating sections. Dehydration and/or embedding kills the enzyme. Geoff Sharon Cooperman wrote: > Im going to try do some NADPH diaphorase on brain sections. I assume > you cant do the technique on formalin fixed, paraffin embedded > tissue, but I found a protocol in Current Protocols in Neuroscience > which says you can do the technique on tissue fixed in > paraformaldehyde which has been put on a slide prior to staining. Does > anyone know if this would work (if not should I use floating > sections?) and am I correct in assuming that paraffin embedded tissue > wont work? > > Thanks, > Sharon -- -- ********************************************** Geoff McAuliffe, Ph.D. Neuroscience and Cell Biology Robert Wood Johnson Medical School 675 Hoes Lane, Piscataway, NJ 08854 voice: (732)-235-4583; fax: -4029 ...
The deCODE team discovered the variants by first analyzing more than 300,000 SNPs in Icelandic and Swedish glaucoma patients and control subjects, utilizing the Illumina Hap300 SNP chip. One SNP was strongly linked to exfoliation syndrome, in which fibrous deposits begin to accumulate in the front of the eye but have not yet begun to impair vision. Analysis of additional SNPs in public databases and which were not included on the chip led to the identification of the two risk variants - allele G of rs1048661 and allele G of rs3825942 - strongly linked to XFG in Icelandic and Swedish case-control cohorts. A combined total of some 16,000 patients and control subjects participated in the study. Glaucoma is one of the most common causes of blindness worldwide. There are various types of glaucoma, all of which lead to damage in the optic nerve and progressive loss of vision. Exfoliation glaucoma is caused by the buildup of fibrous deposits on the surfaces on the front of the eye. Between 10-20% of ...
NADH-GOGAT is a minor form of GOGAT species and little has been known concerning its cellular and subcellular localization, gene structure and expression, or function in higher plants. In 1992, a specific antibody for NADH-GOGAT from rice cell cultures was prepared as the first instance to crossreact NADH-GOGAT protein in rice plants.19 Antibody for NADH-GOGAT in alfalfa root nodules had been obtained prior to the rice, but the antibody hardly recognized NADH-GOGAT in plant organs other than nodules.20 Using the antibody for rice NADH-GOGAT, immunochemical and immunocyto-logical experiments have been performed. A high abundance of NADH-GOGAT protein was detected in the non-green, developing leaf blade14 and in the developing grains.21 Immunocytological results showed that the NADH-GOGAT protein was present in vascular parenchyma cells and mestome sheath cells of vascular bundles of the developing leaf blade, as well as in vascular parenchyma cells, nucellar projection, and nucellar epidermis of ...
The Glaucoma Genetics Lab joined Tin Aung, CC Khor, and our colleagues around the world in conducting a genome-wide association study (GWAS) of exfoliation syndrome and glaucoma. This huge multi-center study of 13,620 patients and 109,837 control subjects identified five new genetic risk factors for exfoliation syndrome: POMP, TMEM136, AGPAT1, RBMS3, and SEMA6A. Read more about this discovery here (11.8 MB).. ...
Principal Investigator:KUBOTA Toshiaki, Project Period (FY):1996 - 1998, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Ophthalmology
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What exactly is the difference between between being insulin resistant and having diabetes. And apparently from reading the post you can have both. An
1. This study examined the effects of the COX inhibitors, ketorolac and ibuprofen, and the NOS inhibitor L-NAME for their potential to both inhibit the development and reverse tolerance to the antinociceptive action of morphine. 2. Repeated administration of intrathecal morphine (15 micrograms), once daily, resulted in a progressive decline of antinociceptive effect and an increase in the ED50 value in the tailflick and paw pressure tests. Co-administration of ketorolac (30 and 45 micrograms) or S(+) ibuprofen (10 micrograms) with morphine (15 micrograms) prevented the decline of antinociceptive effect and increase in ED50 value. Similar treatment with L-NAME (100 micrograms) exerted weaker effects. Administration of S(+) but not R(-) ibuprofen (10 mg kg-1) had similar effects on systemic administration of morphine (15 mg kg-1). 3. Intrathecal or systemic administration of the COX or NOS inhibitors did not alter the baseline responses in either tests. Acute keterolac or S(+) ibuprofen also did not
There are several mechanisms by which statins might exhibit anti-inflammatory effects in the eye [28]. Statins are known to inhibit the activation of Rho guanosine triphosphatase (GTPase), a key molecule in the endothelial ICAM-1-mediated pathway that facilitates lymphocyte migration [29-31]. Statins thus inhibit interactions between leukocytes and endothelial cells, preventing leukocyte transmigration from the vasculature, across the blood-retinal barrier [29, 32-34]. Endothelial cell nitric oxide synthase expression is up-regulated in the presence of statins, leading to higher levels of nitric oxide, which has protective effects on endothelial cells [35]. Statins also inhibit the formation of oxygen free radicals by endothelial cells [36, 37]. Thus, statins may act to stabilize the blood-ocular and blood-retinal barrier, transgression across which enables inflammatory mediators and immune activator cells to enter the anterior chamber, vitreous cavity, and retinal tissues. In addition, statins ...
Swedish University dissertations (essays) about CONSTITUTIVE NITRIC OXIDE SYNTHASE CNOS. Search and download thousands of Swedish university dissertations. Full text. Free.
Alanine dehydrogenase catalyses the NAD-dependent reversible reductive amination of pyruvate into alanine. Pyridine nucleotide transhydrogenase catalyses the reduction of NADP+ to NADPH with the concomitant oxidation of NADH to NAD+. This enzyme is located in the plasma membrane of prokaryotes and in the inner membrane of the mitochondria of eukaryotes. The transhydrogenation between NADH and NADP is coupled with the translocation of a proton across the membrane. In prokaryotes the enzyme is composed of two different subunits, an alpha chain (gene pntA) and a beta chain (gene pntB), while in eukaryotes it is a single chain protein.. The sequence of alanine dehydrogenase from several bacterial species is related with that of the alpha subunit of bacterial pyridine nucleotide transhydrogenase and the N-terminal half of the eukaryotic enzyme. The two most conserved regions correspond respectively to the N-terminal domain of these proteins, and to a central glycine-rich region which is part of the ...
Read "Isoforms of TGF-β in the aqueous humor of patients with pseudoexfoliation syndrome and a possible association with the long-term stability of the capsular bag after cataract surgery, Graefe
Nitric oxide synthase inhibition improves contractile economy in rat hindlimb muscles perfused in situ at matched convective oxygen ...
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Mutations in the GLDC gene account for about 80 percent of all cases of glycine encephalopathy. More than 40 mutations have been identified in affected individuals. Many of these genetic changes alter single amino acids in glycine dehydrogenase. For example, the most common GLDC mutation in the Finnish population replaces the amino acid serine with the amino acid isoleucine at position 564 in the enzyme (also written as Ser564Ile or S564I). Other mutations insert or delete genetic material in the GLDC gene, or disrupt how genetic information from the gene is spliced together to make a blueprint for producing glycine dehydrogenase.. Some GLDC mutations lead to the production of a nonfunctional version of glycine dehydrogenase, while other mutations reduce but do not eliminate the enzymes activity. When an altered version of this enzyme is incorporated into the glycine cleavage enzyme complex, it prevents the complex from breaking down glycine properly. As a result, excess glycine can build up to ...
Ethylene synthesis regulated by biphasic induction of 1-aminocyclopropane-1-carboxylic Acid synthase and 1-aminocyclopropane-1-carboxylic Acid oxidase genes is required for hydrogen peroxide accumulation and cell death in ozone-exposed tomato ...
Razor, is a simple, elegant high-throughput, peptide cleavage system from CEM that produces higher purity peptides while protecting synthesis instrument...
How is Neuronal Type Nitric Oxide Synthase abbreviated? N-NOS stands for Neuronal Type Nitric Oxide Synthase. N-NOS is defined as Neuronal Type Nitric Oxide Synthase rarely.
Epithelial Nitric Oxide Synthase (eNOS)Nitric Oxide (NO) produced in the endothelial cells is involved in vasorelaxation, platelet aggregation, and mechanisms of cardiovascular homeostasis. Endothelial nitric oxide synthase (eNOS, cNOS, Type III) is constitutively expressed in endothelial and other Slideshow 978890 by larissa
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The long range goal of this project is to study structure-function relationships in nitric oxide synthase (NOS) and to develop isoform selective NOS inhibitors...
Updated Features/Annotations ============= SCCDC48 X56956 6485bp DNA PLN 14-NOV-1996 S. cerevisiae CDC48 gene for cell cycle protein CDC48p. cell divisionCDC48 gene; CDC48p protein; cell cycle control; HNT1; CDC48; CDC48p; CLN4, PCL2. SCCHA4 Z49975 2561bp DNA PLN 14-NOV-1996 S.cerevisiae DNA for CHA4 gene encoding DNA-binding activator. DNA-binding activator; CHA4. SCU20641 U20641 3984bp DNA PLN 15-NOV-1996 Saccharomyces cerevisiae glycine decarboxylase (GCV2) gene, complete cds, and c-HIS5 homolog gene, partial cds. Glycine decarboxylase; glycine cleavage; glycine synthase; GCV2; c-HIS5; glycine decarboxylase. SCU51431 U51431 2760bp DNA PLN 14-NOV-1996 Saccharomyces cerevisiae FLO8 gene, complete cds. FLO8; Flo8p. SCYNL173C Z71449 1989bp DNA PLN 15-NOV-1996 S.cerevisiae chromosome XIV reading frame ORF YNL173c. YSCRLM1 D63340 4421bp DNA PLN 12-NOV-1996 Bakers yeast DNA for Rlm1, complete cds. Rlm1. Please note that new sequences take about a week to appear in SGD. To obtain any of the yeast ...
Dihydrolipoyl dehydrogenase 1; Lipoamide dehydrogenase is a component of the glycine decarboxylase (GDC) or glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. LPD1 is probably the protein most often associated with the glycine decarboxylase complex while LPD2 is probably incorporated into alpha-ketoacid dehydrogenase complexes (507 aa ...

The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in...The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in...

The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase. Identification of SDH3P amino acid residues involved in ... Characterization of human SDHC gene encoding one of the integral membrane proteins of succinate-quinone oxidoreductase in ...
more infohttps://www.deepdyve.com/lp/springer_journal/the-four-subunits-of-mitochondrial-respiratory-complex-ii-are-encoded-xB9jOFFlgi

Amino acid oxidoreductases - Biology-Online Dictionary | Biology-Online DictionaryAmino acid oxidoreductases - Biology-Online Dictionary | Biology-Online Dictionary

Science: enzyme) a class of enzymes that catalyze oxidation-reduction reactions of amino acids. ... Retrieved from "https://www.biology-online.org/dictionary/index.php?title=Amino_acid_oxidoreductases&oldid=54296" ... Amino acid oxidoreductases ( ... Amino acid oxidoreductases. From Biology-Online Dictionary , ...
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Amino acid oxidoreductases - WikipediaAmino acid oxidoreductases - Wikipedia

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 ...
more infohttps://en.wikipedia.org/wiki/Amino_acid_oxidoreductases

Preliminary report of NAD+-dependent amino acid dehydrogenase producing bacteria isolated from soil.Preliminary report of NAD+-dependent amino acid dehydrogenase producing bacteria isolated from soil.

L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the ... reversible oxidative deamination of an amino acid to its keto acid and ammonia with ... BACKGROUND: Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider ... Amino Acid Oxidoreductases / isolation & purification, metabolism*. Amino Acids / metabolism. Bacteria / enzymology*, isolation ...
more infohttp://www.biomedsearch.com/nih/Preliminary-report-NAD-dependent-amino/18051956.html

MEDLINE - Resultado p gina 1
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0 (Antifungal Agents); 0 (Plant Extracts); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.1.- (aspartate dehydrogenase); EC 3.1 ... While these substances all contain tannins, testing to possible constituents tannic acid and gallic acid was negative.. ... thereby affecting amino acid biosynthesis. CONCLUSION: Thus, this study confirms the anti-candidal potential of L. inermis and ... Amino cido Oxirredutases/metabolismo. Antif ngicos/farmacologia. Candida albicans/efeitos dos f rmacos. Medicina Herb ria. ...
more infohttp://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=B01.650.940.800.575.912.250.665.437

KEGG SSDB Best Search Result: rpx:Rpdx1 4819KEGG SSDB Best Search Result: rpx:Rpdx1 4819

blas:BSY18_2027 FAD dependent oxidoreductase family pro K00285 409 100 ( -) 29 0.322 59 -, 1 cbw:RR42_m0907 D-amino acid ... abab:BJAB0715_00144 Glycine/D-amino acid oxidases (deam K00285 421 120 ( -) 33 0.349 83 -, 1 abad:ABD1_00970 D-amino acid ... abc:ACICU_00123 Glycine/D-amino acid oxidase (deaminati K00285 427 120 ( -) 33 0.349 83 -, 1 abd:ABTW07_0123 D-amino acid ... abz:ABZJ_00124 glycine/D-amino acid oxidase (deaminatin K00285 427 120 ( -) 33 0.349 83 -, 1 acb:A1S_0095 D-amino acid ...
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KEGG SSDB Best Search Result: app:CAP2UW1 0825KEGG SSDB Best Search Result: app:CAP2UW1 0825

bpa:BPP3800 putative amino acid oxidoreductase K00285 422 108 ( -) 30 0.318 110 -, 1 bpar:BN117_3852 amino acid oxidoreductase ... pami:JCM7686_3162 D-amino acid dehydrogenase, small sub K00285 434 108 ( -) 30 0.405 42 -, 1 pse:NH8B_0655 D-amino-acid ... pnr:AT302_18325 amino acid dehydrogenase K00285 424 129 ( 24) 35 0.333 78 -, 2 pspu:NA29_14590 amino acid dehydrogenase K00285 ... xfa:XF_0851 D-amino acid dehydrogenase subunit K00285 435 109 ( -) 31 0.318 66 -, 1 xfh:XFHB_11080 amino acid dehydrogenase ...
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Search Articles | University of Toronto LibrariesSearch Articles | University of Toronto Libraries

Amino Acid Oxidoreductases - metabolism , Cell Adhesion , Smad4 Protein - metabolism , Case-Control Studies , Collagen - ... Ribonucleic acid--RNA , Pathology , Molecular modelling , Overexpression , Lungs , MicroRNAs , Cell lines , Stem cells , In ... Pyruvic acid , Hepatocellular carcinoma , Metastasis , Glucose , Kinases , Stomach cancer , Metastases , Liver cancer , ... TRANS-RETINOIC ACID , REGULATORY T , DIFFERENTIATION , RECEPTORS , CANCER , T-CELLS , Hypoxia-inducible factors , Hypoxia- ...
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The α-aminoadipate pathway for lysine biosynthesis in fungi | SpringerLinkThe α-aminoadipate pathway for lysine biosynthesis in fungi | SpringerLink

... α-aminoadipate reductase saccharopine reductase saccharopine dehydrogenase pyridine nucleotide-linked amino acid oxidoreductase ... Comparative amino acid sequence analysis of the C6 zinc cluster family of transcriptional regulators. Nucleic Acids Res. 24, ... Umbargar, H. E. (1978) Amino acid biosynthesis and its regulation. Annu. Rev. Biochem. 47, 533-606.Google Scholar ... Jones, E. W. and Fink, G. R. (1982) Regulation of amino acid and nucleotide synthesis in yeast, in Molecular Biology of the ...
more infohttps://link.springer.com/article/10.1385/CBB:46:1:43

IJMS | Free Full-Text | Overexpression of Arachis hypogaea AREB1 Gene Enhances Drought Tolerance by Modulating ROS Scavenging...IJMS | Free Full-Text | Overexpression of Arachis hypogaea AREB1 Gene Enhances Drought Tolerance by Modulating ROS Scavenging...

Previously, we found that expression of AhAREB1 was specifically induced by abscisic acid (ABA), dehydration and drought. To ... abscisic acid-insensitive 5). Constitutive expression of AhAREB1 confers water stress tolerance and is highly sensitive to ... Arachis hypogaea Abscisic-acid Response Element Binding Protein 1) is a member of the basic domain leucine zipper (bZIP)-type ... Reconstructing a Flavodoxin Oxidoreductase with Early Amino Acids. Previous Article in Journal. Putative Genes Involved in ...
more infohttp://mdpi.com/1422-0067/14/6/12827

IJMS  | Free Full-Text | Overexpression of Arachis hypogaea AREB1 Gene Enhances Drought Tolerance by Modulating ROS Scavenging...IJMS | Free Full-Text | Overexpression of Arachis hypogaea AREB1 Gene Enhances Drought Tolerance by Modulating ROS Scavenging...

Previously, we found that expression of AhAREB1 was specifically induced by abscisic acid (ABA), dehydration and drought. To ... abscisic acid-insensitive 5). Constitutive expression of AhAREB1 confers water stress tolerance and is highly sensitive to ... Arachis hypogaea Abscisic-acid Response Element Binding Protein 1) is a member of the basic domain leucine zipper (bZIP)-type ... Reconstructing a Flavodoxin Oxidoreductase with Early Amino Acids. Previous Article in Journal. Putative Genes Involved in ...
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Amino Acid Oxidoreductases, antagonists & inhibitors, Animals, Arginine, analogs & derivatives, pharmacology, Dizocilpine ... Antinociception induced by 3-((+-)-2-carboxypiperazin-4-yl)-propyl-1- phosphonic acid (CPP), an N-methyl-D-aspartate (NMDA) ...
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NAVER Academic > Search...NAVER Academic > Search...

Amino Acid Oxidoreductases, antagonists & inhibitors, Animals, Arginine, analogs & derivatives, pharmacology, therapeutic use, ... Presynaptic gamma-hydroxybutyric acid (GHB) and gamma-aminobutyric acidB (GABAB) receptor-mediated release of GABA and ... Animals, Arachidonic Acids, chemistry, metabolism, Behavior, Animal, drug effects, Cannabinoids, Cyclohexanols, ... Inhibitors of phosphodiesterase IV (PDE IV) increase acid secretion in rabbit isolated gastric glands: correlation between ...
more infohttps://academic.naver.com/search.naver?field=3&query=JOURNAL+OF+PHARMACOLOGY+AND+EXPERIMENTAL+THERAPEUTICS+273%EA%B6%8C+3%ED%98%B8

Calzyme -
Manufacturers of Enzymes , Proteins , Coenzymes , Substrates and Related BiochemicalsCalzyme - Manufacturers of Enzymes , Proteins , Coenzymes , Substrates and Related Biochemicals

D-Amino Acid Oxidase (DAAO). (D-Amino acid: oxygen oxidoreductase (deaminating); EC 1.4.3.3) D-Amino acid oxidase catalyzes the ... amino acid isomers from a racemic mixture and in the preparation of keto acids. The usefulness and application of D-amino acid ... D-Amino acid oxidase has several possible applications such as the determination of D-amino acids, the separation of natural L ... D-Amino acid oxidase solution. Dilute in buffer to give a concentration of 0.1-0.5 U/ml. Must be prepared fresh prior to assay ...
more infohttp://calzyme.com/commerce/catalog/spcategory.jsp?category_id=1043

List of MeSH codes (D08) - WikipediaList of MeSH codes (D08) - Wikipedia

... amino acid oxidoreductases MeSH D08.811.682.664.500.062 --- alanine dehydrogenase MeSH D08.811.682.664.500.125 --- d-amino-acid ... l-amino acid oxidase MeSH D08.811.682.664.500.724 --- leucine dehydrogenase MeSH D08.811.682.664.500.772 --- nitric oxide ... aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224.125.100.500 --- dopa decarboxylase MeSH D08.811.520.224.125.250 --- ... amino acid naphthylamidases MeSH D08.811.277.656.350.100.150.400 --- leucyl-beta-naphthylamidase MeSH D08.811.277.656.350.100. ...
more infohttps://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

Frontiers | Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita nelsonii Reveals Genomic Plasticity |...Frontiers | Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita nelsonii Reveals Genomic Plasticity |...

Supplementary Material 3. Amino acid alignment of arsenite oxidoreductase subunit A.. Supplementary Material 4. Spreadsheet of ... A total of 46 tRNA genes are present and cover the 20 standard amino acids, except as in BOGUAY, tRNA-Arg-TCT and tRNA-Leu-TAA ... Le, S. Q., and Gascuel, O. (2008). An improved general amino acid replacement matrix. Mol. Biol. Evol. 25, 1307-1320. doi: ... For maximum likelihood analysis, the LG amino acid substitution model (Le and Gascuel, 2008) with proportions of invariant ...
more infohttps://www.frontiersin.org/articles/10.3389/fmicb.2016.00603/full

The P450 Monooxygenase BcABA1 Is Essential for Abscisic Acid Biosynthesis in Botrytis cinerea | Applied and Environmental...The P450 Monooxygenase BcABA1 Is Essential for Abscisic Acid Biosynthesis in Botrytis cinerea | Applied and Environmental...

Cladogram of fungal cytochrome P450 oxidoreductases based on amino acid sequences. The accession numbers are as follows: ... R-OH-α-ionylideneacetic acid (structure 4), (1′R)-4′S-OH-α-ionylideneacetic acid (structure 5), 1′-OH-α-ionylideneacetic acid ( ... As expected from the EST data, the derived amino acid sequence of bcaba1 showed significant homology to fungal P450 ... A linear gradient of H2O (containing 10 mM ammonium acetate and 20 mM formic acid) and CH3CN (containing 20 mM formic acid) was ...
more infohttps://aem.asm.org/content/70/7/3868?ijkey=51455cc196056e8ef24b160a3f406366441392a1&keytype2=tf_ipsecsha

Plus itPlus it

This variant amino acid is located in an oxidoreductase domain; whether it represents a rare polymorphism or a missense ... involves a G to A transition at nucleotide 547 and results in an aspartic acid to asparagine substitution at amino acid 183 ( ... WW Domain Containing Oxidoreductase Gene Expression Is Altered in Non-Small Cell Lung Cancer. Sai Yendamuri, Tamotsu Kuroki, ... 4 The abbreviations used are: NSCLC, non-small cell lung cancer; WWOX, WW domain containing oxidoreductase gene; LOH, loss of ...
more infohttp://cancerres.aacrjournals.org/content/63/4/878

Glutaraldehyde cross-linked glutamate oxidase coated microelectrode arrays: selectivity and resting levels of glutamate in the...Glutaraldehyde cross-linked glutamate oxidase coated microelectrode arrays: selectivity and resting levels of glutamate in the...

Amino Acid Oxidoreductases/drug effects*. *Amino Acid Oxidoreductases/physiology. *Biosensing Techniques. *Cross-Linking ... Amino acids with measurable responses at glutamate sites showed similar responses at the sentinel sites. These amino acids are ... while the remaining amino acids yielded no detectable responses. Electroactive amino acids were effectively blocked with a m- ... Averages of 10 working (glutamate) and 10 control (sentinel) site responses from the MEAs for each of the 23 amino acids tested ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/23650904

Molecular cloning and characterization of human endothelial nitric oxide synthase.  - PubMed - NCBIMolecular cloning and characterization of human endothelial nitric oxide synthase. - PubMed - NCBI

Amino Acid Oxidoreductases/genetics*. *Amino Acid Oxidoreductases/metabolism. *Amino Acid Sequence. *Animals ... Complementary DNA clones predict a protein of 1,203 amino acids sharing 94% identity with the bovine endothelial protein, but ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/1379542?dopt=Abstract

Frontiers | The Structure and Biological Function of CREG | Cell and Developmental BiologyFrontiers | The Structure and Biological Function of CREG | Cell and Developmental Biology

... is a 220 amino acid glycoprotein structurally similar to oxidoreductases. However, CREG does not have enzymatic activities ... is a 220 amino acid glycoprotein structurally similar to oxidoreductases. However, CREG does not have enzymatic activities ... The cellular repressor of E1A-stimulated genes (CREG) is a 220 amino acid glycoprotein structurally similar to oxidoreductases ... amino acids 1-31 in human and mice, 1-23 amino acids in Drosophila) and one or more N-glycosylation sites (three in human, N160 ...
more infohttps://www.frontiersin.org/articles/10.3389/fcell.2018.00136/full

Angiogenesis | Proteasome Inhibition Results in TRAIL Sensitization of Primary KeratinocytesAngiogenesis | Proteasome Inhibition Results in TRAIL Sensitization of Primary Keratinocytes

... from the nucleosome core particle.28 Interestingly Hst4 represses genes which get excited about amino-acid oxidoreductase and ... due to the presence of glucuronic acid.9 Although we notice that the term GalXM is inadequate for this polysaccharide we ...
more infohttp://laserpienteamarilla.com/category/angiogenesis/

Eubacterium acidaminophilum GrdD protein
     Summary Report | CureHunterEubacterium acidaminophilum GrdD protein Summary Report | CureHunter

Oxidoreductases: 9264*Oxidoreductases Acting on CH-NH2 Group Donors*Amino Acid Oxidoreductases*Eubacterium acidaminophilum GrdD ...
more infohttp://www.curehunter.com/public/keywordSummaryC443819-Eubacterium-acidaminophilum-GrdD-protein.do

The Propanediol Utilization (pdu) Operon ofSalmonella enterica Serovar Typhimurium LT2 Includes Genes Necessary for Formation...The Propanediol Utilization (pdu) Operon ofSalmonella enterica Serovar Typhimurium LT2 Includes Genes Necessary for Formation...

The PduS protein is a possibility, since it is related in amino acid sequence to several membrane-bound oxidoreductases. In ... over 611 amino acids, to the DdrA proteinK. oxytoca, and the PduH protein is 87% identical in sequence (99 of 124 amino acids) ... The edited alignment consisted of sequences 85 amino acids in length that aligned to the following PduA amino acids: ... for tree construction consisted of a group of sequences 77 amino acids in length that aligned to the following PduN amino acid ...
more infohttps://jb.asm.org/content/181/19/5967?ijkey=f00465dfbededdedf6ba863f3e13ac3d1b8cdb07&keytype2=tf_ipsecsha

The Propanediol Utilization (pdu) Operon ofSalmonella enterica Serovar Typhimurium LT2 Includes Genes Necessary for Formation...The Propanediol Utilization (pdu) Operon ofSalmonella enterica Serovar Typhimurium LT2 Includes Genes Necessary for Formation...

The PduS protein is a possibility, since it is related in amino acid sequence to several membrane-bound oxidoreductases. In ... over 611 amino acids, to the DdrA proteinK. oxytoca, and the PduH protein is 87% identical in sequence (99 of 124 amino acids) ... The edited alignment consisted of sequences 85 amino acids in length that aligned to the following PduA amino acids: ... for tree construction consisted of a group of sequences 77 amino acids in length that aligned to the following PduN amino acid ...
more infohttps://jb.asm.org/content/181/19/5967?ijkey=a0a5f9cd9abde864d91a7bc1ededbe927a3bb8d6&keytype2=tf_ipsecsha