Carbon: A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.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.Ubiquitin-Protein Ligases: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.DNA Ligases: Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).SKP Cullin F-Box Protein Ligases: A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.Nitrogen Fixation: The process in certain BACTERIA; FUNGI; and CYANOBACTERIA converting free atmospheric NITROGEN to biologically usable forms of nitrogen, such as AMMONIA; NITRATES; and amino compounds.Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.Carbon Monoxide: Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)Nanotubes, Carbon: Nanometer-sized tubes composed mainly of CARBON. Such nanotubes are used as probes for high-resolution structural and chemical imaging of biomolecules with ATOMIC FORCE MICROSCOPY.Cullin Proteins: A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.Ubiquitination: The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.Nitrogen Isotopes: Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.Nitrogen Compounds: Inorganic compounds that contain nitrogen as an integral part of the molecule.Polynucleotide Ligases: Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.Nitrogen Cycle: The circulation of nitrogen in nature, consisting of a cycle of biochemical reactions in which atmospheric nitrogen is compounded, dissolved in rain, and deposited in the soil, where it is assimilated and metabolized by bacteria and plants, eventually returning to the atmosphere by bacterial decomposition of organic matter.Nitrogen Dioxide: Nitrogen oxide (NO2). A highly poisonous gas. Exposure produces inflammation of lungs that may only cause slight pain or pass unnoticed, but resulting edema several days later may cause death. (From Merck, 11th ed) It is a major atmospheric pollutant that is able to absorb UV light that does not reach the earth's surface.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.Blood Urea Nitrogen: The urea concentration of the blood stated in terms of nitrogen content. Serum (plasma) urea nitrogen is approximately 12% higher than blood urea nitrogen concentration because of the greater protein content of red blood cells. Increases in blood or serum urea nitrogen are referred to as azotemia and may have prerenal, renal, or postrenal causes. (From Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology, 1984)Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.RING Finger Domains: A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.Carbon Monoxide Poisoning: Toxic asphyxiation due to the displacement of oxygen from oxyhemoglobin by carbon monoxide.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Ubiquitin-Conjugating Enzymes: A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.Reactive Nitrogen Species: Nitrogenous products of NITRIC OXIDE synthases, ranging from NITRIC OXIDE to NITRATES. These reactive nitrogen intermediates also include the inorganic PEROXYNITROUS ACID and the organic S-NITROSOTHIOLS.RNA Ligase (ATP): An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.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.Nitrogen Oxides: Inorganic oxides that contain nitrogen.PII Nitrogen Regulatory Proteins: A family of signal transducing adaptor proteins that control the METABOLISM of NITROGEN. They are primarily found in prokaryotes.Carbon Tetrachloride: A solvent for oils, fats, lacquers, varnishes, rubber waxes, and resins, and a starting material in the manufacturing of organic compounds. Poisoning by inhalation, ingestion or skin absorption is possible and may be fatal. (Merck Index, 11th ed)Carbon Sequestration: Any of several processes for the permanent or long-term artificial or natural capture or removal and storage of carbon dioxide and other forms of carbon, through biological, chemical or physical processes, in a manner that prevents it from being released into the atmosphere.F-Box Proteins: A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.Endosomal Sorting Complexes Required for Transport: A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes.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.Nitrates: Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.Ammonia: A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.Carbon Disulfide: A colorless, flammable, poisonous liquid, CS2. It is used as a solvent, and is a counterirritant and has local anesthetic properties but is not used as such. It is highly toxic with pronounced CNS, hematologic, and dermatologic effects.Biomass: Total mass of all the organisms of a given type and/or in a given area. (From Concise Dictionary of Biology, 1990) It includes the yield of vegetative mass produced from any given crop.Fertilizers: Substances or mixtures that are added to the soil to supply nutrients or to make available nutrients already present in the soil, in order to increase plant growth and productivity.Ubiquitins: A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.Soil: The unconsolidated mineral or organic matter on the surface of the earth that serves as a natural medium for the growth of land plants.Proteasome Endopeptidase Complex: A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.Peptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Quaternary Ammonium Compounds: Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Ubiquitin-Protein Ligase Complexes: Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).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.Polyubiquitin: An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a second ubiquitin molecule. It is structurally distinct from UBIQUITIN C, which is a single protein containing a tandemly arrayed ubiquitin peptide 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.Bacterial Proteins: Proteins found in any species of bacterium.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.Ubiquitin-Activating Enzymes: A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.Carbon-Oxygen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.Carbon Tetrachloride PoisoningGlutamate-Ammonia Ligase: An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.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.Proto-Oncogene Proteins c-cbl: Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Proteolysis: Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.Urea: A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.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.Symbiosis: The relationship between two different species of organisms that are interdependent; each gains benefits from the other or a relationship between different species where both of the organisms in question benefit from the presence of the other.Atmosphere: The gaseous envelope surrounding a planet or similar body. (From Random House Unabridged Dictionary, 2d ed)Plant Roots: The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)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.Photosynthesis: The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)S-Phase Kinase-Associated Proteins: A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.Protein Inhibitors of Activated STAT: A family of structurally related proteins that are constitutively expressed and that negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. PIAS proteins inhibit the activity of signal transducers and activators of transcription.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Nitrogenase: An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1.SUMO-1 Protein: A 1.5-kDa small ubiquitin-related modifier protein that can covalently bind via an isopeptide link to a number of cellular proteins. It may play a role in intracellular protein transport and a number of other cellular processes.Kinetics: The rate dynamics in chemical or physical systems.Small Ubiquitin-Related Modifier Proteins: A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.Nitrogen Mustard Compounds: A group of alkylating agents derived from mustard gas, with the sulfur replaced by nitrogen. They were formerly used as toxicants and vesicants, but now function as antineoplastic agents. These compounds are also powerful mutagens, teratogens, immunosuppressants, and carcinogens.Ecosystem: A functional system which includes the organisms of a natural community together with their environment. (McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)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).Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Carbon Footprint: A measure of the total greenhouse gas emissions produced by an individual, organization, event, or product. It is measured in units of equivalent kilograms of CARBON DIOXIDE generated in a given time frame.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Biodegradation, Environmental: Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.Trees: Woody, usually tall, perennial higher plants (Angiosperms, Gymnosperms, and some Pterophyta) having usually a main stem and numerous branches.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.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)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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.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.Glutamine: 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.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.AcetyleneSumoylation: A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Soil Microbiology: The presence of bacteria, viruses, and fungi in the soil. This term is not restricted to pathogenic organisms.Lysine: An essential amino acid. It is often added to animal feed.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.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.Carbohydrate Metabolism: Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.Fermentation: Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.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.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.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.

Molecular biology of biotin attachment to proteins. (1/456)

Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins.  (+info)

A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. (2/456)

The Escherichia coli biotin holoenzyme synthetase, BirA, catalyzes transfer of biotin to the epsilon amino group of a specific lysine residue of the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase. Sequences of naturally biotinylated substrates are highly conserved across evolutionary boundaries, and cross-species biotinylation has been demonstrated in several systems. To define the minimal substrate requirements in BirA-catalyzed biotinylation, we have measured the kinetics of modification of a 23-residue peptide previously identified by combinatorial methods. Although the sequence of the peptide bears little resemblance to the biotinylated sequence in BCCP, it is enzymatically biotinylated in vivo. Rates of biotin transfer to the 23-residue peptide are similar to those determined for BCCP. To further elucidate the sequence requirements for biotinylation, transient kinetic measurements were performed on a series of amino- and carboxy-terminal truncations of the 23-mer. The results, determined by stopped-flow fluorescence, allowed identification of a 14-residue peptide as the minimum required sequence. Additional support was obtained using matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometric analysis of peptides that had been incubated with an excess of biotinyl-5'-adenylate intermediate and catalytic amounts of BirA. Results of these measurements indicate that while kinetically inactive truncations showed no significant shift in molecular mass to the values expected for biotinylated species, kinetically active truncations exhibited 100% biotinylation. The specificity constant (k(cat)/Km) governing BirA-catalyzed biotinylation of the 14-mer minimal substrate is similar to that determined for the natural substrate, BCCP. We conclude that the 14-mer peptide efficiently mimics the biotin acceptor function of the much larger protein domain normally recognized by BirA.  (+info)

Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component. (3/456)

Plastidic acetyl-CoA carboxylase (ACCase; EC 6.4.1.2), which catalyses the synthesis of malonyl-CoA and is the regulatory enzyme of fatty acid synthesis, is activated by light, presumably under redox regulation. To obtain evidence of redox regulation in vivo, the activity of ACCase was examined in pea chloroplasts isolated from plants kept in darkness (dark-ACCase) or after exposure to light for 1 h (light-ACCase) in the presence or absence of a thiol-reducing agent, dithiothreitol (DTT). The protein level was similar for light-ACCase and dark-ACCase, but the activity of light-ACCase in the absence of DTT was approx. 3-fold that of dark-ACCase. The light-ACCase and dark-ACCase were activated approx. 2-fold and 6-fold by DTT respectively, indicating that light-ACCase was in a much more reduced, active form than the dark-ACCase. This is the first demonstration of the light-dependent reduction of ACCase in vivo. Measurement of the activities of ACCase, carboxyltransferase and biotin carboxylase in the presence and absence of DTT, and the thiol-oxidizing agent, 5, 5'-dithiobis-(2-nitrobenzoic) acid, revealed that the carboxyltransferase reaction, but not the biotin carboxylase reaction, was redox-regulated. The cysteine residue(s) responsible for redox regulation probably reside on the carboxyltransferase component. Measurement of the pH dependence of biotin carboxylase and carboxyltransferase activities in the ACCase suggested that both components affect the activity of ACCase in vivo at a physiological pH range. These results suggest that the activation of ACCase by light is caused partly by the pH-dependent activation of two components and by the reductive activation of carboxyltransferase.  (+info)

Rickettsia prowazekii transports UMP and GMP, but not CMP, as building blocks for RNA synthesis. (4/456)

Rickettsia prowazekii, the etiological agent of epidemic typhus, is an obligate intracellular bacterium and is apparently unable to synthesize ribonucleotides de novo. Here, we show that as an alternative, isolated, purified R. prowazekii organisms transported exogenous uridyl- and guanylribonucleotides and incorporated these labeled precursors into their RNA in a rifampin-sensitive manner. Transport systems for nucleotides, which we have shown previously and show here are present in rickettsiae, have never been reported in free-living bacteria, and the usual nucleobase and nucleoside transport systems are absent in rickettsiae. There was a clear preference for the monophosphate form of ribonucleotides as the transported substrate. In contrast, rickettsiae did not transport cytidylribonucleotides. The source of rickettsial CTP appears to be the transport of UMP followed by its phosphorylation and the amination of intrarickettsial UTP to CTP by CTP synthetase. A complete schema of nucleotide metabolism in rickettsiae is presented that is based on a combination of biochemical, physiological, and genetic information.  (+info)

X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. (5/456)

BACKGROUND: The purine biosynthetic pathway in procaryotes enlists eleven enzymes, six of which use ATP. Enzymes 5 and 6 of this pathway, formylglycinamide ribonucleotide (FGAR) amidotransferase (PurL) and aminoimidazole ribonucleotide (AIR) synthetase (PurM) utilize ATP to activate the oxygen of an amide within their substrate toward nucleophilic attack by a nitrogen. AIR synthetase uses the product of PurL, formylglycinamidine ribonucleotide (FGAM) and ATP to make AIR, ADP and P(i). RESULTS: The structure of a hexahistidine-tagged PurM has been solved by multiwavelength anomalous diffraction phasing techniques using protein containing 28 selenomethionines per asymmetric unit. The final model of PurM consists of two crystallographically independent dimers and four sulfates. The overall R factor at 2.5 A resolution is 19.2%, with an R(free) of 26.4%. The active site, identified in part by conserved residues, is proposed to be a long groove generated by the interaction of two monomers. A search of the sequence databases suggests that the ATP-binding sites between PurM and PurL may be structurally conserved. CONCLUSIONS: The first structure of a new class of ATP-binding enzyme, PurM, has been solved and a model for the active site has been proposed. The structure is unprecedented, with an extensive and unusual sheet-mediated intersubunit interaction defining the active-site grooves. Sequence searches suggest that two successive enzymes in the purine biosynthetic pathway, proposed to use similar chemistries, will have similar ATP-binding domains.  (+info)

The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin. (6/456)

Acetyl-CoA carboxylase catalyzes the first committed step in the biosynthesis of long-chain fatty acids. The Escherichia coli form of the enzyme consists of a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase activity. The C-terminal 87 amino acids of the biotin carboxyl carrier protein (BCCP87) form a domain that can be independently expressed, biotinylated, and purified (Chapman-Smith, A., Turner, D. L., Cronan, J. E., Morris, T. W., and Wallace, J. C. (1994) Biochem. J. 302, 881-887). The ability of the biotinylated form of this 87-residue protein (holoBCCP87) to act as a substrate for biotin carboxylase and carboxyltransferase was assessed and compared with the results with free biotin. In the case of biotin carboxylase holoBCCP87 was an excellent substrate with a K(m) of 0.16 +/- 0.05 mM and V(max) of 1000.8 +/- 182.0 min(-1). The V/K or catalytic efficiency of biotin carboxylase with holoBCCP87 as substrate was 8000-fold greater than with biotin as substrate. Stimulation of the ATP synthesis reaction of biotin carboxylase where carbamyl phosphate reacted with ADP by holoBCCP87 was 5-fold greater than with an equivalent amount of biotin. The interaction of holoBCCP87 with carboxyltransferase was characterized in the reverse direction where malonyl-CoA reacted with holoBCCP87 to form acetyl-CoA and carboxyholoBCCP87. The K(m) for holoBCCP87 was 0.45 +/- 0.07 mM while the V(max) was 2031.8 +/- 231.0 min(-1). The V/K or catalytic efficiency of carboxyltransferase with holoBCCP87 as substrate is 2000-fold greater than with biotin as substrate.  (+info)

Biotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity. (7/456)

Catalytically active biotin protein ligase from Saccharomyces cerevisiae (EC 6.3.4.15) was overexpressed in Escherichia coli and purified to near homogeneity in three steps. Kinetic analysis demonstrated that the substrates ATP, biotin, and the biotin-accepting protein bind in an ordered manner in the reaction mechanism. Treatment with any of three proteases of differing specificity in vitro revealed that the sequence between residues 240 and 260 was extremely sensitive to proteolysis, suggesting that it forms an exposed linker between an N-terminal 27-kDa domain and the C-terminal 50-kDa domain containing the active site. The protease susceptibility of this linker region was considerably reduced in the presence of ATP and biotin. A second protease-sensitive sequence, located in the presumptive catalytic site, was protected against digestion by the substrates. Expression of N-terminally truncated variants of the yeast enzyme failed to complement E. coli strains defective in biotin protein ligase activity. In vitro assays performed with purified N-terminally truncated enzyme revealed that removal of the N-terminal domain reduced BPL activity by greater than 3500-fold. Our data indicate that both the N-terminal domain and the C-terminal domain containing the active site are necessary for complete catalytic function.  (+info)

Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. (8/456)

The gene thiI encodes a protein (ThiI) that plays a role in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine, but the reaction catalyzed by ThiI remains undetermined. Based upon sequence alignments, ThiI shares a unique "P-loop" motif with the PPi synthetase family, four enzymes that catalyze adenylation and subsequent substitution of carbonyl oxygens. To test whether or not this motif is critical for ThiI function, the Asp in the motif was converted to Ala (D189A), and a screen for in vivo 4-thiouridine production revealed the altered enzyme to be inactive. Further scrutiny of sequence data and the crystal structures of two members of the PPi synthetase family implicated Lys321 in the proposed adenylation function of ThiI, and the critical nature of Lys321 has been demonstrated by site-directed mutagenesis and genetic screening. Our results, then, indicate that ThiI catalyzes the adenylation of a substrate at the expense of ATP, a narrowing of possible reactions that provides a strong new basis for deducing the early steps in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine.  (+info)

CTP synthase catalyses the ATP-dependent formation of CTP from UTP using either NH3 or l-glutamine as the nitrogen source. GTP is required as an allosteric effector to promote glutamine hydrolysis. In an attempt to identify nucleotide-binding sites, scanning alanine mutagenesis was conducted on a highly conserved region of amino acid sequence (residues 102-118) within the synthase domain of Escherichia coli CTP synthase. Mutant K102A CTP synthase exhibited wild-type activity with respect to NH3 and glutamine; however, the R105A, D107A, L109A and G110A enzymes exhibited wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation. The E103A, R104A and H118A enzymes exhibited no glutamine-dependent activity and were only partially active with NH3. Although these observations were compatible with impaired activation by GTP, the apparent affinity of the D107A, L109A and G110A enzymes for GTP was reduced only 2-4-fold, suggesting that these residues do ...
Plasmid pSKB3.MPN348 from Dr. Sung-Hou Kims lab contains the insert methenyltetrahydrofolate synthetase and is published in Proteins. 2004 Sep 1. 56(4):839-43. This plasmid is available through Addgene.
The enzyme systems associated with the synthesis and degradation of pyrimidine nucleotides in rat liver after the repeated administration of phenobarbital were studied. The incorporation of [2-14C]orotic acid into uridine components of the free nucleotide pool remains unchanged, whereas incorporation into cytidine components is decreased. The cytidine triphosphate synthetase, UTPase, and CTPase activities of cytosol are increased. The activities of 5-nucleotidases of the cytosol and microsomal fraction as well as UTPase and CTPase of the microsomal fraction are decreased. The activities of nucleoside, nucleoside monophosphate, and diphosphate kinases of uridine and cytidine components and the activity of cytosol uridine phosphorylase are not affected. Deamination of cytidine in the presence of the whole homogenate, the microsomal fraction, and the cytosol is not altered. Finally, the ATPase activity of the cytosol is not affected, while that of the microsomal fraction is decreased.. ...
Recombinant protein of human holocarboxylase synthetase (biotin-(proprionyl-Coenzyme A-carboxylase (ATP-hydrolysing)) ligase) (HLCS), 20 ug available for purchase from OriGene - Your Gene Company.
Complete information for ST20-MTHFS gene (Protein Coding), ST20-MTHFS Readthrough, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Mycobacterium tuberculosis (Mtb), a dreaded pathogen, has a unique cell envelope composed of high fatty acid content that plays a crucial role in its pathogenesis. Acetyl Coenzyme A Carboxylase (ACC), an important enzyme that catalyzes the first reaction of fatty acid biosynthesis, is biotinylated by biotin acetyl-CoA carboxylase ligase (BirA). The ligand-binding loops in all known apo BirAs to date are disordered and attain an ordered structure only after undergoing a conformational change upon ligand-binding. Here, we report that dehydration of Mtb-BirA crystals traps both the apo and active conformations in its asymmetric unit, and for the first time provides structural evidence of such transformation. Recombinant Mtb-BirA was crystallized at room temperature, and diffraction data was collected at 295 K as well as at 120 K. Transfer of crystals to paraffin and paratone-N oil (cryoprotectants) prior to flash-freezing induced lattice shrinkage and enhancement in the resolution of the X-ray ...
CTPS2 Peptides and Proteins available through Novus Biologicals. Browse our CTPS2 Peptides and Proteins all backed by our Guarantee+.
Ctps2 - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN303974G1|/strong|, Ctps2 gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
MetabolismFatty acid and phospholipid metabolismBiosynthesisacetyl-CoA carboxylase, biotin carboxylase subunit (TIGR00514; EC 6.3.4.14; HMM-score: 11.1) ...
Background Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. Description CTPS2...
1B6S: Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.
biotinyl-AMP synthetase: the first of two reactions catalyzed by holocarboxylase synthetases; forms biotinyl-5-AMP from biotin + ATP
Gentaur molecular products has all kinds of products like :search , GenWay \ Phosphate Acceptor Peptide - \ 06-271-83419 for more molecular products just contact us
Bachem offers H-6098 Biotinyl-S6 Phosphate Acceptor Peptide for your research. Find all specific details here. Find product specific information including available pack sizes, CAS, detailed description and references here.
Whatever the assay you have in mind, you need the right technologies for your target. We can custom conjugate your antibody or biomolecule to any bead, or biotinylate or DIG-label your targets, so you can develop the assay you need. If you prefer, we can even perform the assay development for you.
Biotin Carboxyl Carrier Protein is on Rediff pages, ,Follow Biotin Carboxyl Carrier Protein to get latest updates from Biotin Carboxyl Carrier Protein
Holocarboxylase synthetase (HCS, human) and BirA (Escherichia coli) are biotin protein ligases that catalyze the ATP-dependent attachment of biotin to apocarboxylases. Biotin attachment occurs on a highly conserved lysine residue within a consensus sequence (Ala/Val-Met-Lys-Met) that is found in carboxylases in most organisms. Numerous studies have indicated that HCS and BirA, as well as biotin protein ligases from other organisms, can attach biotin to apocarboxylases from different organisms, indicating that the mechanism of biotin attachment is well conserved. In this study, we examined the cross-reactivity of biotin attachment between human and bacterial biotin ligases by comparing biotinylation of p-67 and BCCP87, the biotin-attachment domain fragments from human propionyl-CoA carboxylase and E. coli acetyl-CoA carboxylase, respectively. While BirA has similar biotinylation activity toward the two substrates, HCS has reduced activity toward bacterial BCCP87 relative to its native substrate, p-67.
Biotin protein ligase of is the 35. or that the presence of the reaction intermediate impedes access of subtilisin to the cleavage site. The disordered loop containing residues 115C123 lies close to the biotin binding site, and residues 115C118 become ordered in the crystal structure when biotinyl-lysine occupies the active site. Because of the similarity to nucleotide-binding sequences in protein buy 118876-58-7 kinases, the sequence 115GRGRRG120 within this loop had been thought to function in ATP binding (Buoncristiani et al. 1986; Wilson et al. 1992). However, a recent mutational analysis shows that this sequence has a role in biotin binding (Kwon and Beckett 2000). No function has been identified previously for the C-terminal domain comprising residues 274C321, which shows structural similarity to the Src homology 3 domains (Noble et al. 1993). However, recent evidence of safety by biotinyl-5-AMP buy 118876-58-7 against hydroxyl radical cleavage from the BirA backbone at a number of sites ...
Looking for biotin carboxylase? Find out information about biotin carboxylase. An enzyme which condenses bicarbonate with biotin to form carboxybiotin Explanation of biotin carboxylase
GT:ID BAD56666.1 GT:GENE bioD GT:PRODUCT putative dethiobiotin synthetase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 1987153..1987884 GB:FROM 1987153 GB:TO 1987884 GB:DIRECTION + GB:GENE bioD GB:PRODUCT putative dethiobiotin synthetase GB:PROTEIN_ID BAD56666.1 LENGTH 243 SQ:AASEQ MNTLLVTGTSTDVGKTVVTAALTALARAEALPVAVCKPAQTGVAPGEPGDLAEVRRLAGPVPTLELARYPEPLAPDTAARRCGAPLLTLDETATAVRGLDAELTVVEGAGGLLVRIGEFTLLDLARELDAPVLVVAAAGLGTLNHTELTIRALDAAGVRCAGVVIGAWPAEPDLASVCNREDLPRLTGVPIVGAVPAGVGAWDHDRFTAAVPGWFAPGWSPRLPFNSDSPPSTWGFDTSQSGT GT:EXON 1,1-243:0, SW:ID BIOD_NOCFA SW:DE RecName: Full=Dethiobiotin synthetase; EC=6.3.3.3;AltName: Full=Dethiobiotin synthase;AltName: Full=DTB synthetase; Short=DTBS; SW:GN Name=bioD; OrderedLocusNames=NFA_18200; SW:KW ATP-binding; Biotin biosynthesis; Complete proteome; Ligase;Magnesium; Nucleotide-binding. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1-,243,BIOD_NOCFA,e-114,100.0,243/243, GO:SWS:NREP 4 GO:SWS GO:0005524,GO:ATP ...
K11263 bccA; acetyl-CoA/propionyl-CoA carboxylase, biotin carboxylase, biotin carboxyl carrier protein [EC:6.4.1.2 6.4.1.3 6.3.4.14 ...
1DAM: Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis.
During mid‐oogenesis, a massive supply of nucleotides is required for the synthesis of cellular DNA and RNA. Nurse cells in egg chambers of stages 2-10 undergo 10-12 cycles of endoreplication of nuclear DNA [21] producing an approximately 1,000‐fold increase in their DNA content. Endoreplication is essential to support increased transcription and protein production for deposition into developing oocytes [22]. Likewise, RNA production, particularly ribosomal RNA, is strikingly upregulated in nurse cells from these same stages in parallel with increases in ribosomal gene copy number [23]. The presence of CTPS filaments in Drosophila ovarian germ cells at stages with a high demand for CTP, together with the observation that reduced CTPS expression is associated with defects in oogenesis, suggests that CTPS filaments are assembled to promote CTP biosynthesis and support endoreplication. Consistent with this model, the diameters of DAck86 nurse cell nuclei were significantly smaller than ...
putative acetyl-CoA carboxylase biotin carboxylase subunit [PokAC2] GTGTTCCGCACCGTCCTCGTCGCCAACCGGGGCGAGATCGCCCTGCGTGTCGCGCGCGCC TGCCGTGAACTGGGGATCAGGGTCGCCGTCGTGTACTCCACCGAGGACACCGACAGCGAG GTCGTGCGGTACGCCGACGAGGCGGTCCGCATCGGCCCGGGGTCGGCGCAGGCGAGCTAC CTCAGCATCCCCGCCGTCATCGAGGCCGCCCGGCGCGTCGGCGCGGACGCGATCCACCCC GGGTACGGATTCCTCTCCGAGAACGCCGACTTCGCCGAGGTGTGCGCGGCCGAGGGCATC ACCTTCATCGGCCCGCCCCCGGAGGTGATGGAGGCGCTGGGCGACAAGTCCACCTGCCGC GGCCTCATGGCCGACGCGGGGCTGCCCCTGCTGCCCGGCACGCTGGACCCCGTGTCGTCG CCGCGCGAGGCCGAGGCGTTCGCCGCCGAGATCGGCTACCCGGTGGTGGTGAAGGCGGTG GCCGGGGGCGGCGGCCGCGGGATCGGAGTGGCGCACTCGGCCGACGAGTTCCCCGCCGTC TACCGGGAGACGCGACGCCACGCCGCCGCCGTGTTCGGGGACGGCAGGGTCTATCTGGAG CGCTATCTGCAGTCCGCACGGCACGTGGAGATCCAGATACTCGCCGACCGCTTCGGCAAT GTGATCCATCTCGGCGAGCGCGACTGCTCGGTGCAGCGCCGCCATCAGAAGCTCATCGAG GAGACCCCGGCTCCCGGGCTGGACCGCGATGTGCTCGCCGCGATGGCGGAACACGCCGTG CAGGGAGCCAAGGCCGCCGGATACGTCGGCGCGGGGACCTTCGAGTTCCTGTACGACGAC AGCGGACGCTTCTACTTCATGGAGGTCAACTGCCGTATCCAGGTCGAGCATCCGGTCACA ...
am1a04d AJ229366 409 Homolog to proteins of other species than S. cerevisiae (see table 2) am1a07d AJ229367 307 am1a12d AJ229368 234 am1b02d AJ229369 236 am1b03d AJ229370 123 am1b04d AJ229371 314 7.0 E-41 YFL036w RPO41 DNA-directed RNA pol., mitochondrial am1b06d AJ229372 410 4.7 E-41 YGR208w SER2 phosphoserine phosphatase am1b11d AJ229373 327 2.1 E-42 YDL213c RNA recognition domain in the N-terminal region am1b12d AJ229374 280 am1c01d AJ229375 489 3.0 E-100 YMR229c RRP5 processing of pre-ribosomal RNA am1c05d AJ229376 275 am1c08d AJ229377 288 1.5 E-56 YDL102w CDC2 DNA-directed DNA pol. delta, catalytic 125 KD subunit am1c11d AJ229378 157 am1c12d AJ229379 145 am1d02d AJ229380 322 am1d05d AJ229381 195 repeats or mito am1d06d AJ229382 302 5.1 E-55 YBR208c DUR1,2 urea amidolyase am1d08d AJ229383 241 am1d12d AJ229384 174 am1e05r AJ229385 220 6.6 E-15 YMR287c MSU1 3-5 exonuclease for RNA 3 ss-tail, mitochondrial am1e06d AJ229386 290 am1e09r AJ229387 241 am1e10r AJ229388 138 1.7 E-06 YDL153c SAS10 ...
HCS antibody (holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase)) for IHC-P, WB. Anti-HCS pAb (GTX109815) is tested in Human samples. 100% Ab-Assurance.
Bachem offers H-3204 Biotinyl-(Leu⁸,D-Trp²²,Tyr²⁵)-Somatostatin-28 for your research. Find all specific details here. Find product specific information including available pack sizes, CAS, detailed description and references here.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Pay less for domain names. Register your .com, .net and .org domains from $6.99/yr. Bulk pricing and private domain name registration options. Transfer domain names risk-free from $6.99.
Pay less for domain names. Register your .com, .net and .org domains from $6.99/yr. Bulk pricing and private domain name registration options. Transfer domain names risk-free from $6.99.
Magazin online ce contine produse naturiste Calivita, vitamine calivita, minerale calivita, sanatate calivita, produse bio calivita.
We,China P-METHYL BENZOYL CHLORIDE 874-60-2 Suppliers and China P-METHYL BENZOYL CHLORIDE 874-60-2 Manufacturers, provide P-METHYL BENZOYL CHLORIDE 874-60-2 product and the products related with China P-METHYL BENZOYL CHLORIDE 874-60-2 - panoxi
Fig. 7.2.2.05. Granulocytic leukocytes (G) from a rabbit brain granuloma containing phagocytosed Nosema protozoa (arrows). Scale = 2 µm. (Rabbit, neocortex.) Download the high resolution image.. ...
THANKS to the ongoing support of viewers like you, EWTN is able to work day and night to bring you the best in quality Catholic programming whether its on EWTN television, EWTN Radio, or streaming on our ever-expanding, interactive website, EWTN.com.. Make a Donation. ...
As the spread of antibiotic resistant bacteria steadily increases, there is an urgent need for new antibacterial agents. Because fatty acid synthesis is only used for membrane biogenesis in bacteria, the enzymes in this pathway are attractive targets for antibacterial agent development. Acetyl-CoA carboxylase catalyzes the committed and regulated step in fatty acid synthesis. In bacteria, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. Fragment-based screening revealed that amino-oxazole inhibits biotin carboxylase activity and also exhibits antibacterial activity against Gram-negative organisms. In this report, we redesigned previously identified lead inhibitors to expand the spectrum of bacteria sensitive to the amino-oxazole derivatives by including Gram-positive species. Using 9,411 small organic building blocks, we constructed a diverse combinatorial library of 1.2 × 108 amino-oxazole derivatives. A subset
Approach and Results-Using both rat balloon injury and mouse wire injury models, we identified CTP synthase 1 (CTPS1) as one of the potential targets that may be used for developing therapeutics for treating neointima-related disorders. CTPS1 was induced in proliferative SMCs in vitro and neointima SMCs in vivo. Blockade of CTPS1 expression by small hairpin RNA or activity by cyclopentenyl cytosine suppressed SMC proliferation and neointima formation. Surprisingly, cyclopentenyl cytosine had much less effect on EC proliferation. Of importance, blockade of CTPS1 in vivo sustained the re-endothelialization as a result of induction of CTP synthesis salvage pathway enzymes nucleoside-diphosphate kinase A and B in ECs. Diphosphate kinase B seemed to preserve EC proliferation via use of extracellular cytidine to synthesize CTP. Indeed, blockade of both CTPS1 and diphosphate kinase B suppressed EC proliferation in vitro and the re-endothelialization in vivo.. ...
Vaccinia virus thymidylate kinase, although similar in sequence to human TMP kinase, has broader substrate specificity and phosphorylates (E)-5-(2-bromovinyl)-dUMP and dGMP. Modified guanines such as glyoxal-dG, 8-oxo-dG, O(6)-methyl-dG, N(2)-ethyl-dG and N(7)-methyl-dG were found present in cancer cell DNA. Alkylated and oxidized dGMP analogs were examined as potential substrates for vaccinia TMP kinase and also for human TMP and GMP kinases. Molecular models obtained from structure-based docking rationalized the enzymatic data. All tested nucleotides are found surprisingly substrates of vaccinia TMP kinase and also of human GMP kinase. Interestingly, O(6)-methyl-dGMP is the only analog specific for the vaccinia enzyme. Thus, O(6)-Me-dGMP could be useful for designing new compounds of medical interest either in antipoxvirus therapy or in experimental combined gene/chemotherapy of cancer. These results also provide new insights regarding dGMP analog reaction with human GMP kinase and their slow ...
Biotin is required for enzymatic activity of several important carboxylases (Table 28.10). Biotin is first attached to a lysine residue of biotin carboxyl carrier protein (BCCP) by biotin- [propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase (holocarboxylase [HCS], EC 6.3.4.10), which forms the biotinyl domain of the enzyme or separate subunit. The N1 position is subsequently carboxylated to form carboxy-biotin (Fig. 28.40), which is then able to transfer the carboxyl group to other substrates. The source of the carboxyl is either bicarbonate or decarboxylation of another substrate as is seen in transcarboxylation reactions.196 A typical carboxylation reaction mediated by biotin-BCCP is shown in Figure 28.41. The source of the carboxyl is bicarbonate with ATP supplying energy for the reaction. This is followed by the subsequent transfer of the carboxyl to the substrate with regeneration of the biotin-BCCP complex.. An interesting recent development is the finding that biotin is also attached to ...
BirA biotin ligase was expressed as maltose-binding protein (MBP) fusion in an E. coli cells. The dual 6xHis-MBP tag at the N-terminus is useful for removal of BirA after biotinylation through either Ni-NTA or amylose resin columns. Catalog number: MBBL-301 Expression host: Escherichia coli (E. coli). Expressed Region
ID C7QJ90_CATAD Unreviewed; 417 AA. AC C7QJ90; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256,HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000256,HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000256,HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256,HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256,HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000256,HAMAP-Rule:MF_00138}; GN OrderedLocusNames=Caci_0279 {ECO:0000313,EMBL:ACU69232.1}; OS Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC OS 102108 / JCM 14897). OC Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae; OC Catenulispora. OX NCBI_TaxID=479433 {ECO:0000313,EMBL:ACU69232.1, ECO:0000313,Proteomes:UP000000851}; RN [1] {ECO:0000313,EMBL:ACU69232.1, ECO:0000313,Proteomes:UP000000851} RP NUCLEOTIDE SEQUENCE ...
Urea Amidolyase; Contains Both Urea Carboxylase And Allophanate Hydrolase Activities, Degrades Urea To CO2 And NH3; Expression Sensitive To Nitrogen Catabolite Repression And Induced By Allophanate, An Intermediate In Allantoin Degradation; Protein Abundance Increases In Response To DNA Replication Stress
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Norcoclaurine HCl (Norcoline TM ) Effective as a stimulant or not? Ive been seeing it a bit more in Supplements, wondering its effectiveness, if any
To develop, implement and improve these variety and seed regulations, the Ministry of Agriculture relies on an Advisory Committee: the Permanent Technical Committee for the Selection of Cultivated Plants (CTPS).. One of the primary missions of the CTPS is to assist and guide genetic progress by developing the technical rules for variety registration. These rules aim to ensure the best possible match between the objectives of variety users, civil society, public authorities, and the scientific and technical capacities of breeders, in order to meet the needs of sustainable and diverse agriculture. The CTPS proposes the listing and de-listing of plant varieties in the Official French Catalogue.. In France, the Ministry delegates seed production controls to various bodies: the Official Control Service (GNIS / SOC) for agricultural and vegetable plants, the Interprofessional Technical Centre for Fruits and Vegetables (CTIFL) for fruit trees, FranceAgriMer for Vine plants.. Post-marketing controls are ...
Sir Rateb Rabie, President/CEO of HCEF commented: The beauty of the project is that it is a joint effort of three partners (HCEF, CRS, and HLCS) who brought their respective expertise and resources to serve Palestinian craftsmen in order to make them efficient workers with high quality production. This program could not exist without the joint support of all partners.. For 15 years, HCEF has been involved with helping handicraft workers improve productivity and marketability of their crafts. In the past, HCEF worked to open new markets for artisans products and advised workshops about the need for quality control and improved packaging.. ...
rs6495446, an intronic SNP in the MTHFS gene, was associated with increased risk for chronic kidney disease based on a study associated with the Framingham Heart Study of ~1,000 Caucasian individuals. The odds ratio rs6495446(C) allele was 1.24 (CI: 1.09-1.41, p=0.001).news 23andMe reports this same information with a different emphasis since the T allele is the minor allele in both European and Asian populations: each T allele lowers the odds of chronic kidney disease by 0.8 times. [PMID 18522750 ...
Shop L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase ELISA Kit, Recombinant Protein and L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Cytidine triphosphate, labeled on the alpha phosphate group with 35S, is typically used in reactions involving enzymes that will incorporate the ribonucleoside monophosphate (base, sugar, and alpha-labeled phosphate) into a chain of RNA. The advantage of 35S, when compared to other short-lived isotopes, is its relatively low signal (which contributes to a sharp band width), as well as longer shelf life.. Common applications include:. ...
Biotinylated histone H3 peptide acetylated methylated phosphorylated for use in enzyme assays, histone binding and pulldown experiments
... enable isolation, separation, concentration and further downstream processing or analysis of biomolecules.
Equilife Biotin Plus Small Animal Formulation. Biotin Plus is a small animal formulation of concentrated biotin that improves skin and coat health of all your small
Biotin helps your body produce energy from carbohydrate, proteins, and fats. Learn about food sources of biotin & problems associated with deficiency
I had been skeptical After i to start with commenced utilizing Biotin, and soon became a believer within the efficacy with the product provided by Bulk Provides. As time goes on, And that i use the biotin I am gaining power, in a position to move way more freely, have energy to previous throughout the day, and am over the verge of beginning a toughness routine that I havent been ready to do in above ten years. ;)* On 12/21/2015 Robert claimed ...
I had been skeptical After i very first began using Biotin, and shortly turned a believer in the efficacy of the products supplied by Bulk Materials. As time goes on, and I use the biotin I am gaining strength, equipped to maneuver way more freely, have energy to final each day, and am within the verge of commencing a Full Article energy regimen that I have not been capable of do in Learn More Here above ten years. ;)* On twelve/21/2015 Robert explained ...
I was skeptical After i 1st started using Biotin, and shortly turned a believer in the efficacy with the product provided by Bulk Materials. As time goes on, And that i use the biotin I am attaining power, equipped to move way more freely, have Vitality to final each day, and am within the verge of starting a power plan that I have not been ready to do in in excess of a decade. ;)* On 12/21/2015 Robert stated ...
I had been skeptical when I very first commenced utilizing Biotin, and shortly became a believer while in the efficacy of your item provided by Bulk Provides. As time goes on, And that i utilize the biotin Im getting energy, equipped to move a great deal more freely, have energy to very last learn the facts here now throughout the day, and am to the verge of starting a strength schedule that I have not been capable to do in about a decade. ;)* On 12/21/2015 Robert stated ...
Biotin 0.2% Fuso is a medicine available in a number of countries worldwide. A list of US medications equivalent to Biotin 0.2% Fuso is available on the Drugs.com website.
전세계 고객의 Biotin, 비오틴등급을 인증 한 한국 최대 소스. 오늘 방문하여 Biotin, 비오틴부작용, 혜택 등에 대해 알아보십시오.
国内在庫あります!Biotin標識済みマウス・モノクローナル抗体 ab28107 交差種: Hu 適用: Flow Cyt…CD45抗体一覧 一次抗体にBiotinを直接標識し、操作時間の短縮と低いバックグラウンドを実現。
抗马Biotin (ab6920)经WB, ELISA, IHC-P, IHC-Fr, IM, Dot, ICC/IF实验严格验证。被多篇发表文献引用。其他多种Biotin偶联二抗可供选择。品质保证,中国80%以上现货。
Biotin偶联Cpn10抗体(ab106171)可与人样本反应并经WB, ELISA, RIA实验严格验证,实验条件参看说明书。Abcam对所有产品均提供质保服务和专属技术支持,中国75%以上现货。
Gentaur molecular products has all kinds of products like :search , Jena Bio \ Dibenzylcyclooctyne-PEG4-Biotin Conjugate, 100 mg pack \ CLK-A105P4-100 for more molecular products just contact us
Buy our Synthetic Mouse MCP1 protein (Biotin) (Animal Free). Ab176032 is a protein fragment produced syntheticaly (animal free) and has been validated in HPLC…
well just looked out of the lounge window today to find that the whole street is being dug up. cant park outside my house, cant get on my drive, and...
... Ingrediente: 100% coacaze negre pudra* *din agricultura ecologica Amestecati pudra de coacaze negre in sucuri, smoothies, in salate de fructe, in inghetate, prajituri, preparate...
Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase, pyruvate carboxylase (PC), and...
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5-adenylate (BirA-bio- 5-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon (319 aa ...
Biotin (vitamin H or vitamin B7) is the essential cofactor of biotin-dependent carboxylases, such as pyruvate carboxylase and acetyl-CoA carboxylase. Mammals cannot synthesize biotin, while in bacteria, fungi, and plants it is synthesized from pimelate thioester through different pathways. In E. coli and many organisms, pimelate thioester is derived from malonyl-ACP. The pathway starts with the methylation to malonyl-ACP methyl ester, followed by the fatty acid chain elongation cycle to form pimeloyl-ACP methyl ester, which is then demethylated to form pimeloyl-ACP [MD:M00572]. Pimeloyl-ACP is converted to biotin through the final four steps in the biotin bicyclic ring assembly, which are conserved among biotin-producing organisms [MD:M00123]. In B. subtilis, biotin is derived from pimeloyl-ACP formed by oxidative cleavage of long-chain acyl-ACPs [MD:M00573]. Some bacteria synthesize biotin from pimeloyl-CoA derived from pimelate [MD:M00577]. Biotin is covalently attached to biotin-dependent ...
The following proteins are candidates for maintaining biotin homeostasis in humans: the biotin transporters sodium-dependent multivitamin transporter (SMVT) and monocarboxylate transporter 1, the biotinyl-protein ligase holocarboxylase synthetase (HC
1b) ATP + XMP + NH3 = AMP + diphosphate + GMP. For diagram of reaction click here.. Glossary: XMP = xanthosine 5-phosphate. Other name(s): GMP synthetase (glutamine-hydrolysing); guanylate synthetase (glutamine-hydrolyzing); guanosine monophosphate synthetase (glutamine-hydrolyzing); xanthosine 5-phosphate amidotransferase; guanosine 5-monophosphate synthetase. Systematic name: xanthosine-5-phosphate:L-glutamine amido-ligase (AMP-forming). Comments: Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37318-71-1. References:. 1. Lagerkvist, U. Biosynthesis of guanosine 5-phosphate. II. Amination of xanthosine 5-phosphate by purified enzyme from pigeon liver. J. ...
Since its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications
Since its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Plays an important role in the regulation of phospholipid synthesis.
I wish to immobilise a peptide on a column. I think the easiest way to do this would be to biotinylate the peptide at the C-terminus and link it to streptavidin-agarose. a) Is this true? b) What is the easiest way to biotinylate specifically on the C-terminus of a peptide - do I link through a cysteine? c) How do I get rid of free biotin from a small peptide (approx. 2kD ...
5 mos soon after beginning to choose three hundred mg Biotin on a daily basis, I recognized the slightly blurred vision I have had learn this here now on and off For many years, fully stopped. Admit when I started getting 300mg Biotin/day, I had my doubts which id see any reversal of any of my MS signs and symptoms immediately after dwelling with PPMS for 25 yrs. To double Check out that my outcomes were not just in my head, Ive not taken the Biotin dose a few days inside a row. Every time I ended the Biotin, the blurry vision returned to The purpose I was not ready to generate ...
5 mos soon after starting to take three hundred mg Biotin daily, I noticed The marginally blurred vision Ive had on and off For several years, fully stopped. Confess when I started using 300mg Biotin/working day, Id my doubts which id discover any reversal of any of my MS signs and symptoms right after living with PPMS for 25 yrs. To double check that my success werent just in my head, I have not taken the Biotin dose a couple of days in a row. Each time I finished the Biotin, the blurry vision returned to the point I was not capable to generate ...
five mos just after beginning to consider three hundred mg Biotin daily, find out I found the slightly blurred vision I have experienced on and off For many years, wholly stopped. Admit when I began using 300mg Biotin/working day, I had my doubts which id discover any reversal of any of my MS signs or symptoms soon after residing with PPMS for twenty five yrs. To double Test that my final results werent just in my head, Ive not taken the Biotin dose a few days in a very row. Every time I finished the Biotin, the blurry vision returned to the point my site I was not able to travel. ...
View Notes - VitaminMineralHO from SMHM 1450 at North Texas. Nutrient Short List NUTRIENT NAME, DESCRIPTION, SOURCES Nutrient Biotin Description with Sources Biotin is a coenzyme required for
Biotin - Get up-to-date information on Biotin side effects, uses, dosage, overdose, pregnancy, alcohol and more. Learn more about Biotin
Solgar Biotin 300 ug - Biotin has an essential role in helping the body metabolise proteins, carbohydrates and fats. It is such a beneficial vitamin that it should not be ignored.
Solgar Biotin 300 ug - Biotin has an essential role in helping the body metabolise proteins, carbohydrates and fats. It is such a beneficial vitamin that it should not be ignored.
Need Us Pharmaceutical Division/McKesson Corp Biotin Supplement? Cascade Healthcare has Us Pharmaceutical Division/McKesson Corp Biotin Supplement - 2583797BT
国内在庫あります!Biotin標識済みシープ・ポリクローナル抗体 ab2284 適用: IP,ELISA,IHC-FoFr,IHC-P,IHC-Fr,ICC/IF…BrdU抗体一覧 一次抗体にBiotinを直接標識し、操作時間の短縮と低いバックグラウンドを実現。
Abcam provides specific protocols for Endogenous Avidin + Biotin Blocking System (ab3387) : Endogenous Avidin + Biotin Blocking System
Product Page for Biotin 5000 mcg 60 Vcaps made by natural-factors offering price, ingredients and full item description from betterlife
Product Page for Biotin 8000 mcg 60 Vcaps made by natures-life offering price, ingredients and full item description from betterlife
Cumpara rapid si simplu Sante Luciu BIO de buze shiny cassis. Sante Luciu BIO de buze shiny cassis confera stralucire pentru buze senzuale, pline de volum.
Known proteins associated with the cell-adhesion protein E-cadherin include catenins and proteins involved in signaling, trafficking and actin organization. However, the list of identified adherens junction proteins is likely to be incomplete, limiting investigation into this critical cell structure. To expand the inventory of potentially relevant proteins, we expressed E-cadherin fused to biotin ligase in MDCK epithelial cells, and identified by mass spectrometry neighboring proteins which were biotinylated. The most abundant of the 303 proteins identified were catenins and nearly 40 others that had been previously reported to influence cadherin function. Many others could be rationalized as novel candidates for regulating the adherens junction, cytoskeleton, trafficking or signaling. We further characterized lipoma preferred partner (LPP), which is present at both cell-contacts and focal adhesions. Knockdown of LPP demonstrated its requirement for E-cadherin dependent adhesion and suggested it ...
Propionyl-CoA metabolism: propionyl-CoA is an intermediate in the catabolism of a number of amino acids, as well as in the breakdown of odd-chain fatty acids. Propionyl-CoA (3-C) enters the TCA Cycle at succinyl-CoA (4-C), thus another carbon must be added to bring it into mainstream metabolism. A biotin-dependent carboxylase adds carbon dioxide at the cost of one ATP to give D-methylmalonyl-CoA. D-methylmalonyl-CoA is then racemized to L-methylmalonyl-CoA. Methylmalonyl-CoA is a branched-chain, whereas succinyl-CoA is straight-chain: the carboxyl group and a hydrogen must be exchanged. This exchange requires C-C bond-breaking and making, a process apparently involving a Co-C bond intermediate. The cobalamin cofactor derived from Vit B12 is used in catalyzing this reaction. ...
NAD+ synthase (EC 6.3.5.1) catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide and is induced by stress factors such as heat shock and glucose limitation. The three-dimensional structure of NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and in complex with ATP shows that the enzyme consists of a tight homodimer with alpha/beta subunit topology [(PUBMED:8895556)]. This domain is also found in guanosine 5-monophosphate (GMP) synthetase. GMP synthase catalyses the synthesis of GMP from XMP. The protein is a homodimer, but in some archaea it is a heterodimer composed of a glutamine amidotransferase subunit and a ATP pyrophosphatase subunit. In eucaryotes, bacteria, and some archaea the two catalytic units are encoded by a single gene, producing a two-domain-type GMP, with a GATase domain in the N-terminal half and a ATP-PPase domain in the C-terminal half. This entry represents the ATP pyrophosphatase domain. ...
TY - JOUR. T1 - High-throughput immunoblotting identifies biotin-dependent signaling proteins in HepG2 hepatocarcinoma cells. AU - Rodriguez-Melendez, Rocio. AU - Griffin, Jacob B.. AU - Sarath, Gautam. AU - Zempleni, Janos. PY - 2005/7/1. Y1 - 2005/7/1. N2 - Biotin affects the abundance of mRNA coding for ∼10% of genes expressed in human-derived hepatocarcinoma (HepG2) cells. Here, we determined whether effects of biotin on gene expression are associated with changes in the abundance of distinct proteins in cell signaling and structure. HepG2 cells were cultured in media containing the following concentrations of biotin: 0.025 nmol/L (denoted "deficient"), 0.25 nmol/L ("physiological" = control), and 10 nmol/L ("pharmacological") for 10 d before harvesting. The abundance of 1009 proteins from whole-cell extracts was quantified by using high-throughput immunoblots. The abundance of 44 proteins changed by at least 25% in biotin-deficient and biotin-supplemented cells compared with physiological ...
If you want to get the best signal to background ratio you should go for biotinylation of your protein so you can do stringent washes. Tagging your protein with biotin ligase recognition peptide and coepressing with biotin ligase will result in the biotinylation of your protein. You can get a very good signal to background ratio this way ...
This domain is found in carbamoyl dehydratase HypE, which is involved in the maturation of NifE hydrogenase; AIR synthase (PurM) and FGAM synthase (PurL), which are involved in de novo purine biosynthesis; and selenide, water dikinase, an enzyme which synthesizes selenophosphate from selenide and ATP.. In PurM this domain, which has an alpha-beta-type fold, is found at the C terminus of the protein [(PUBMED:10508786)].. ...
This unit describes a system for expression of biotinylated proteins in mammalian cells in vivo, and its application to chromatin immunoprecipitation (ChIP)
Alfa Chemistry is the worlds leading provider for special chemicals. We offer qualified products for 111317-91-0(Glycinamide,L-cysteinyl-L-phenylalanyl-L-isoleucyl-L-arginyl-L-asparaginyl-L-cysteinyl-L-prolyl-L-lysyl-,cyclic (1®6)-disulfide),please inquire us for 111317-91-0(Glycinamide,L-cysteinyl-L-phenylalanyl-L-isoleucyl-L-arginyl-L-asparaginyl-L-cysteinyl-L-prolyl-L-lysyl-,cyclic (1®6)-disulfide).
Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
Biotinylated histone H2A peptide acetylated methylated phosphorylated for use in enzyme assays, histone binding and pulldown experiments
TY - JOUR. T1 - Epigenetic regulation of chromatin structure and gene function by biotin. AU - Hassan, Yousef I.. AU - Zempleni, Janos. PY - 2006/7/6. Y1 - 2006/7/6. N2 - Covalent modifications of histones are a crucial component of epigenetic events that regulate chromatin structures and gene function. Evidence exists that distinct lysine residues in histones are modified by covalent attachment of the vitamin biotin, catalyzed by biotinidase and holocarboxylase synthetase. Biotinylation of histones appears to be conserved across species. The following biotinylation sites were identified using both MS and enzymatic biotinylation of synthetic peptides: K9, K13, K125, K127, and K129 in histone H2A; K4, K9, and K18 in histone H3; and K8 and K12 in histone H4. Evidence was provided that biotinylated histone H4 is enriched in pericentromeric heterochromatin, and that biotinylation of histone H4 participates in gene silencing, mitotic condensation of chromatin, and the cellular response to DNA damage. ...
Psychiatry healthcare professionals gain a thorough knowledge base of psychiatric disorder information to offer the best patient care. Get our FREE app now.
The purinosome is a putative multi-enzyme complex that carries out de novo purine biosynthesis within the cell. It is postulated to include all six of the human enzymes identified as direct participants in this ten-step biosynthetic pathway converting phosphoribosyl pyrophosphate to inosine monophosphate: The enzymes of the multi-step de novo purine biosynthesis pathway have been postulated to form a multi-enzyme complex to facilitate substrate channeling between each enzyme of the pathway. Slight variations of the pathway exists between phyla; however, there are 13 enzymes that can be considered part of this biosynthetic pathway. Several individual enzymatic functions have consolidated onto single bifunctional or trifunctional polypeptide chains in higher organisms, suggesting stable physical interactions exist between enzymes. The functional consolidation of steps 2,3, and 5 of the pathway into a single enzyme in higher organisms such as humans suggests physical local proximity of the enzyme ...
Introduction: Brachytherapy is one of the most common treatment modalities for gynecological cancer. The GZP6 brachytherapy system is one of the devices utilized in Iran. It has been considered particularly due to its low cost compared to other more complete and established systems. This system has some deficiencies including lack of a treatment planning software for non-predefined treatments, inability to change the gradually changeable dosimetric variables and using a point source estimation in dose calculation. This report presents a complementary treatment planning software (CTPS) to the systems own dedicated program. Material and Methods: First, the dosimetric characteristics of three GZP6 sources were calculated based on the TG-43 protocol using the MCNP4C Monte Carlo code. Then, the calculated dose distribution around the implanted applicators, based on the selected dwell positions and dwell times, was shown in a graphical user interface (GUI) written using the MATLAB software. Results: The
Higenamine is a tetrahydroisoquinoline present in several plants that has β-adrenergic receptor agonist activity. Study of the biosynthesis of higenamine has shown the participation of norcoclaurine synthase, which controls the stereochemistry to construct the (S)-isomer. However, when isolated from nature, higenamine is found as the racemate, or even the (R)-isomer. We recently reported the isolation of higenamine 4′-O-β-d-glucoside. Herein, its (R)- and (S)-isomers were synthesized and compared to precisely determine the stereochemistry of the isolate. Owing to their similar spectral properties, determination of the stereochemistry based on NMR data was considered inappropriate. Therefore, a high-performance liquid chromatography method was established to separate the isomers, and natural higenamine 4′-O-β-d-glucoside was determined to be a mixture of isomers.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... carbon-dioxide ligase (ADP-forming). This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase). This ...
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... this enzyme class is 5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) . Other names in ...
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... carbon-dioxide ligase (ADP-forming). Other names in common use include urease (ATP-hydrolysing), urea carboxylase (hydrolysing ...
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... carbon-dioxide ligase (ADP-forming). Other names in common use include N5-CAIR synthetase, N5-carboxyaminoimidazole ...
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... carbon-dioxide cyclo-ligase (ADP-forming). This enzyme is also called desthiobiotin synthase. This enzyme participates in ...
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... arginine cyclo-ligase (AMP-forming). This enzyme participates in clavulanic acid biosynthesis. Miller, M. T.; Bachmann, B. O.; ... name of this enzyme class is L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme is also called L-2-N-(2- ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... The gene encoding the Carnosine synthase is ATPGD1, a member of the "ATP-grasp family" of ligases. Because of its involvement ... peptide synthases). The systematic name of this enzyme class is 'L-histidine:beta-alanine ligase (AMP-forming)' (incorrect on ...
Its C-terminal domain is a synthetase and has an ATP-grasp family fold that is usually found in carbon-nitrogen ligases. The N- ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is glutathionylspermidine:glutathione ligase (ADP-forming ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... L-glutamate gamma-ligase (ADP-forming), tetrahydropteroyl-[gamma-Glu]n:L-glutamate gamma-ligase, and (ADP-forming). This enzyme ... Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437-52. doi:10.1016 ... L-glutamate gamma-ligase (ADP-forming). Other names in common use include folylpolyglutamate synthase, folate polyglutamate ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming). ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming). ... This enzyme is also called citrate:6-N-acetyl-6-N-hydroxy-L-lysine ligase (ADP-forming). This enzyme participates in lysine ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... L-lysine ligase (ADP-forming). Glass NL, Kosuge T (1986). "Cloning of the gene for indoleacetic acid-lysine synthetase from ... peptide synthases). The systematic name of this enzyme class is (indol-3-yl)acetate:L-lysine ligase (ADP-forming). This enzyme ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437-52. doi:10.1016 ... L-glutamate ligase (ADP-forming), and DHFS. This enzyme participates in folate biosynthesis. As of late 2007, 3 structures have ... peptide synthases). The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is L-glutamate:histamine ligase. Other names in common use include ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Other names in common use ... include Asp-AdT, Asp-tRNAAsn amidotransferase, aspartyl-tRNAAsn amidotransferase, and Asn-tRNAAsn:L-glutamine amido-ligase (ADP ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase ( ... spermidine ligase (ADP-forming). This enzyme participates in glutathione metabolism. It employs one cofactor, magnesium. As of ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming). Other ... amido-ligase, and Ado-cobyric acid synthase [glutamine hydrolyzing]. This enzyme participates in porphyrin and chlorophyll ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... L-glutamine amido-ligase, (ADP-forming), 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine, and amido-ligase (ADP- ... The systematic name of this enzyme class is N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names ... This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism. As of late 2007, 11 structures have ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming). Other names in common use ... include Glu-AdT, Glu-tRNAGln amidotransferase, glutamyl-tRNAGln amidotransferase, and Glu-tRNAGln:L-glutamine amido-ligase (ADP ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). Other names in ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is hydrogenobyrinic-acid:L-glutamine amido-ligase (AMP-forming). This enzyme is also ...
This enzyme belongs to the family of ligases, to be specific those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... L-aspartate ligase (ADP-forming). This enzyme participates in purine metabolism. This particular protein family is of huge ... phosphate and carbon dioxide". J. Biol. Chem. 234 (7): 1799-805. PMID 13672967. Parker J (1984). "Identification of the purC ...
... specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name ... and glutamate This enzyme belongs to the family of ligases, ... of this enzyme class is deamido-NAD+:L-glutamine amido-ligase ( ...
... carbon-nitrogen ligases with glutamine as amide-n-donor MeSH D08.811.464.259.400.300 --- carbamoyl-phosphate synthase ( ... tyrosine-tRNA ligase MeSH D08.811.464.263.200.950 --- valine-tRNA ligase MeSH D08.811.464.267.500 --- coenzyme a ligases MeSH ... succinate-coa ligases MeSH D08.811.464.754.600 --- dna ligases MeSH D08.811.464.754.720 --- rna ligase (atp) MeSH D08.811. ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ...
This enzyme belongs to the family of ligases, to be specific those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... The E3 ligases are classified into four families: HECT, RING-finger, U-box, and PHD-finger. The RING-finger E3 ligases are the ... A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has ... Quips article describing E3 Ligase function at PDBe Ubiquitin-Protein Ligases at the US National Library of Medicine Medical ...
The bortezomib molecule is in the center colored by atom type (carbon = pink, nitrogen = blue, oxygen = red, boron = yellow), ... Once a protein is tagged with a single ubiquitin molecule, this is a signal to other ligases to attach additional ubiquitin ... Bashir T, Dorrello NV, Amador V, Guardavaccaro D, Pagano M (March 2004). "Control of the SCF(Skp2-Cks1) ubiquitin ligase by the ... The tagging reaction is catalyzed by enzymes called ubiquitin ligases. ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... n ligase (ADP-forming). Other names in common use include Aslfm, UDP-MurNAc-pentapeptide:D-aspartate ligase, and D-aspartic ... In enzymology, a D-aspartate ligase (EC 6.3.1.12) is an enzyme that catalyzes the chemical reaction ATP + D-aspartate + [beta- ... Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL (2006). "Aslfm, the D-aspartate ligase responsible for the addition of ...
Pyruvate Carboxylase Genes and a PutativeEscherichia coli-Type Bifunctional Biotin Protein Ligase Gene (bpl/birA) Exhibit a ...
Glutamate-Cysteine Ligase: One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma- ... Ligases: 2113*Carbon-Nitrogen Ligases*Peptide Synthases: 6*Glutamate-Cysteine Ligase: 110*human glutamate-cysteine ligase ... Glutamate-Cysteine Ligase. Subscribe to New Research on Glutamate-Cysteine Ligase One of the enzymes active in the gamma- ... Glutamylcysteine Synthetase; Glutamate Cysteine Ligase; Ligase, Glutamate-Cysteine; Synthetase, Glutamylcysteine; Synthetase, ...
EC 6.2 includes ligases used to form carbon-sulfur bonds. *EC 6.3 includes ligases used to form carbon-nitrogen bonds ( ... EC 6.5 includes ligases used to form phosphoric ester bonds. *EC 6.6 includes ligases used to form nitrogen-metal bonds, as in ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... EC 6.4 includes ligases used to form carbon-carbon bonds. * ... DNA ligase. References[edit]. *^ "Synthases and ligases". chem. ...
ligase activity, forming carbon-nitrogen bonds. down. 2.30E-09. acid-amino acid ligase activity ... Decrease in ligase activity was ranked at the top (Table 3). Subsequently, decreases in response to oxidative stress and ... ubiquitin-protein ligase activity were included. Next, pathway analysis was also performed, by IPA. As in GO analysis, protein ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ... All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each ...
Carbon-Nitrogen Ligases* * Conserved Sequence / genetics * Crystallography, X-Ray * DNA-Binding Proteins / chemistry ...
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule. DR GO; GO:0006400; P:tRNA ... Ligase {ECO:0000256,HAMAP-Rule:MF_01161, ECO:0000256,SAAS:SAAS00054817, KW ECO:0000313,EMBL:CAL99742.1}; KW Nucleotide-binding ...
Ligases: 2113*Carbon-Nitrogen Ligases*biotinyl-AMP synthetase: 1. Related Diseases. 1. Holocarboxylase Synthetase Deficiency 08 ...
GO:0016879: ligase activity, forming carbon-nitrogen bonds molecular_function. GO:0019941: modification-dependent protein ... Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a ... Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady- ... RN [2] RM PMID:22910360 RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification ...
Monoclonal Antibody Carbon-Nitrogen Ligase Activity Monoclonal Antibody Carbon-Nitrogen Ligase Activity: Monoclonal Antibody - ...
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a ribose-5-phosphate-ammonia ligase (EC 6.3.4.7) is an enzyme that catalyzes the chemical reaction ATP + ribose ... this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). Other names in common use include 5-phosphoribosylamine ...
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a formate-dihydrofolate ligase (EC 6.3.4.17) is an enzyme that catalyzes the chemical reaction ATP + formate + ... this enzyme class is formate:dihydrofolate ligase (ADP-forming). Other names in common use include formyltransferase, ...
6. Ligases. 6.3 Forming carbon-nitrogen bonds. 6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor. 6.3.5.4 ...
Carbon-Nitrogen Ligases. Papers overview. Semantic Scholar uses AI to extract papers important to this topic. ...
LIGASE_ACTIVITY_FORMING_CARBON_NITROGEN_BONDS , GO_CARBOHYDRATE_PHOSPHATASE_ACTIVITY ## GO_LIPASE_ACTIVITY , GO_PEPTIDE_ ... Nitrogen metabolism ## Tyrosine metabolism , Systemic lupus erythematosus ## ## ** Comparison analysis ** ## Collecting duct ...
Carbon-nitrogen ligase activity, with glutamine as amido-n-donor. Specific Function. Not Available. Gene Name. pam. Uniprot ID ... Organic nitrogen compound / Carbonyl group / Aldehyde / Organic oxygen compound / Organopnictogen compound / Organic oxide / ...
Journal Article] The Arabidopsis ubiquitin ligases ATL31 and ATL6 control the defense response as well as the carbon/nitrogen ... Journal Article] Carbon and nitrogen metabolism regulated by ubiquitin-proteasome system2011. *. Author(s). Takeo Sato ... Journal Article] The carbon/nitrogen regulator ARABIDOPSIS TOXICOS EN LEVADURA31 controls papilla formation in response to ... Ubiquitin ligase ATL31 functions in leaf senescence in response to the balance between atmospheric CO2 and nitrogen ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is 4-methylene-L-glutamate:ammonia ligase (AMP-forming). ... In enzymology, a 4-methyleneglutamate-ammonia ligase (EC 6.3.1.7) is an enzyme that catalyzes the chemical reaction ATP + 4- ...
GO:0016874 [ligase activity]. GO:0016884 [carbon-nitrogen ligase activity, with glutamine as amido-N-donor]. GO:0030956 [ ... GO:0016874 [ligase activity]. GO:0016884 [carbon-nitrogen ligase activity, with glutamine as amido-N-donor]. GO:0030956 [ ... GO:0016874 [ligase activity]. GO:0016884 [carbon-nitrogen ligase activity, with glutamine as amido-N-donor]. ... GO:0016874 [ligase activity]. GO:0016884 [carbon-nitrogen ligase activity, with glutamine as amido-N-donor]. ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is xanthosine-5-phosphate:L-glutamine amido-ligase (AMP-forming). Other names in ... an amino group given by glutamine is attached at carbon 1 of PRPP. The resulting molecule is 5-phosphoribosylamine, which is ...
6.3.- Forming carbon-nitrogen bonds 6.4 Forming carbon-carbon bonds 6.4.1 Ligases that form carbon-carbon bonds (only sub- ... 6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor ... 6.3.4 Other carbon-nitrogen ligases 6.3.4.2 CTP synthase ( ... 6.3.4.9 biotin---[methylmalonyl-CoA-carboxytransferase] ligase 6.3.4.10 biotin---[propionyl-CoA-carboxylase (ATP-hydrolysing)] ...
Ligases;. Forming carbon-nitrogen bonds;. Acid-D-amino-acid ligases (peptide synthases). ... which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store [2]. Both enzymes ...
Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor. Specific function:. Degrades bioactive fatty acid ... Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor. Specific function:. Degrades bioactive fatty acid ...
Carbon-Nitrogen Ligases/chemistry/genetics/metabolism*. *Cytidine Triphosphate/biosynthesis*. *Escherichia coli/chemistry/ ...
2012). The Arabidopsis ubiquitin ligases ATL31 and ATL6 control the defense response as well as the carbon-nitrogen response. ... Carbon/Nitrogen Insensitive1, also known as ATL31), and AT3G05200 (ATL6) have been linked previously to both fungal (Libault et ... Interestingly, a family of RING type ubiquitin ligases is also present in the network (HOM03D000017). Both AT5G27420, which ... Identification of 118 Arabidopsis transcription factor and 30 ubiquitin-ligase genes responding to chitin, a plant-defense ...
  • Both this enzyme and EC 6.3.2.29 , cyanophycin synthase (L-aspartate-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store . (genome.jp)
  • In this review, we will first describe the many uses of glutamine and its products in proliferating cells, including its role in supplying carbon and nitrogen atoms for construction of a variety of macromolecular precursors, as well as its significance as a regulator of biosynthesis and bioenergetics, anti‐oxidative defense, and gene expression. (cloudfront.net)
  • In this study, the effects of different nitrogen concentration on cell growth and PMA biosynthesis were investigated via comparative transcriptomics and proteomics analyses, and a related signaling pathway was also evaluated. (biomedcentral.com)
  • The level of nitrogen could regulate cell growth and PMA biosynthesis. (biomedcentral.com)
  • Low concentration of nitrogen was beneficial for PMA biosynthesis, which could upregulate the expression of key genes involved in the PMA biosynthesis pathway. (biomedcentral.com)
  • Cell growth and PMA biosynthesis might be mediated by the TOR signaling pathway in response to nitrogen. (biomedcentral.com)
  • Here, the transcription levels of key genes involved in PHA biosynthesis were tracked in Pseudomonas putida strain A514 grown on vanillic acid as the sole carbon source under different levels of nutrient availability. (asm.org)
  • Second, much higher expression levels of 3-hydroxyacyl-acyl carrier protein (ACP) thioesterase (encoded by phaG ) and long-chain fatty acid-CoA ligase (encoded by alkK ) under both high and low nitrogen (N) led to the hypothesis that they likely not only have a role in PHA biosynthesis but are also essential to cell growth. (asm.org)
  • In this study, we traced and compared transcription levels of key genes involved in PHA biosynthesis pathways in Pseudomonas putida A514 under different nitrogen concentrations to unveil the unusual features of PHA synthesis. (asm.org)
  • In biochemistry , a ligase is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond , usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. (wikipedia.org)
  • The systematic name of this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). (wikipedia.org)
  • In enzymology, a ribose-5-phosphate-ammonia ligase (EC 6.3.4.7) is an enzyme that catalyzes the chemical reaction ATP + ribose 5-phosphate + NH3 ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + 5-phosphoribosylamine The 3 substrates of this enzyme are ATP, ribose 5-phosphate, and NH3, whereas its 3 products are ADP, phosphate, and 5-phosphoribosylamine. (wikipedia.org)
  • Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady-state levels of certain proteasome targets in Mycobacterium tuberculosis. (jcvi.org)
  • This study suggests that the thumb loop found in bacterial carboxylases interferes with optimal interaction with the mammalian biotin protein ligase. (ox.ac.uk)
  • Numerous studies have indicated that HCS and BirA, as well as biotin protein ligases from other organisms, can attach biotin to apocarboxylases from different organisms, indicating that the mechanism of biotin attachment is well conserved. (ox.ac.uk)
  • In this study, we examined the cross-reactivity of biotin attachment between human and bacterial biotin ligases by comparing biotinylation of p-67 and BCCP87, the biotin-attachment domain fragments from human propionyl-CoA carboxylase and E. coli acetyl-CoA carboxylase, respectively. (ox.ac.uk)
  • Urease functionally, belong to the superfamily of amidohydrolases and phosphotriestreases.It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia.In 1926, James B. Sumner, an assistant professor at Cornell University, showed that urease is a protein by examining its crystallized form.Urease is produced by numerous taxonomically diverse bacterial species, including normal flora and nonpathogens. (worldofchemicals.com)
  • DNA Ligase: Catalyzes the joining together of Okazaki fragments. (rpi.edu)
  • Carbon atoms in the graphitic carbon skeleton can be replaced by heteroatoms with different electronegative from that of the carbon atom (i.e., heteroatom doping) to modulate the charge distribution o. (bioportfolio.com)
  • The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. (maixius.com)
  • The two regions of interaction have a synergistic effect on the E3 ligase activity. (maixius.com)
  • The E3 ligase activity has been shown to be important for the involvement of PRC1 in X-chromosome inactivation and the control of Hox gene expression (16-19). (maixius.com)
  • It was shown that Bmi-1, a Drosophila Psc homolog that was originally discovered through its ability to collaborate with Myc in lymphomagenesis (20-22), plays a central role in the assembly of the PRC1 complex and, while Bmi-1 displays no detectable ubiquitin ligase activity, the binding of Bmi-1 greatly stimulates the E3 ligase activity of Ring1B (15,19). (maixius.com)
  • Doping-induced enhancement of crystallinity in polymeric carbon nitride nanosheets to improve their visible-light photocatalytic activity. (bioportfolio.com)
  • The protein encoded by this gene is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. (wikidoc.org)
  • The main action of the VHL protein is thought to be its E3 ubiquitin ligase activity that results in specific target proteins being 'marked' for degradation. (wikidoc.org)
  • On the other hand, the fungus expressed to high levels effectors and pathogenicity-related genes in plants under high nitrogen regime. (frontiersin.org)
  • Moreover, some rice genes implicated in nitrogen recycling were highly induced during NIS. (frontiersin.org)
  • qRT-PCR further confirmed that the expression levels of key genes involved in the PMA biosynthetic pathway ( GLK, CS, FUM, DAT , and MCL ) and the TOR signaling pathway ( GS , TOR1 , Tap42, and Gat1 ) were upregulated due to nitrogen limitation. (biomedcentral.com)
  • For example, DNA ligases are used with restriction enzymes to insert DNA fragments, often genes, into plasmids. (chemeurope.com)
  • Some ligases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix , for example certain ubiquitin ligase related proteins. (wikipedia.org)
  • A recent study revealed that a human PRC1 complex composed of Bmi-1, HPH2, PC3 and Ring proteins (Ring1A & Ring1B), which are homologs of Drosophila Psc, Ph, Pc and dRing, respectively, is an E3 ubiquitin ligase complex that mono-ubiquitinates lysine 119 of nucleosomal histone H2A (15). (maixius.com)
  • The systematic name of this enzyme class is urea:carbon-dioxide ligase. (worldofchemicals.com)
  • Also, urease has been demonstrated as a potent virulence factor for some species.Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea into 2 molecules of ammonia and 1 of carbon dioxide.Urease is a highly efficient catalyst for the hydrolysis of urea with a rate approximately 10 14 times the rate of the noncatalyzed reaction. (worldofchemicals.com)
  • Carbonic anhydrase, which removes carbon dioxide from the blood by binding it to water, has a turnover rate of 10 6 . (thefreedictionary.com)
  • That means that one molecule of the enzyme can cause a million molecules of carbon dioxide to react in one second. (thefreedictionary.com)
  • Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a Lys side-chain to direct the target to the proteasome. (jcvi.org)
  • The common names of ligases often include the word "ligase", such as DNA ligase , an enzyme commonly used in molecular biology laboratories to join together DNA fragments. (wikipedia.org)
  • The interaction between Magnaporthe oryzae and rice was used as a model for analyzing the molecular mechanisms underlying Nitrogen-Induced Susceptibility (NIS). (frontiersin.org)
  • In molecular biology, DNA ligase is a particular type of ligase ( EC 6.5.1.1) that can link together DNA strands that have double-strand breaks (a break in both complementary strands of DNA). (chemeurope.com)
  • In addition, DNA ligase has extensive use in molecular biology laboratories for Genetic recombination experiments (see Applications in molecular biology research ). (chemeurope.com)
  • DNA ligases have become an indispensable tool in modern molecular biology research for generating recombinant DNA sequences. (chemeurope.com)
  • Crawford NM, Forde BG (2002) Molecular and developmental biology of inorganic nitrogen nutrition. (springer.com)
  • On the one hand, we show that enhanced susceptibility was visible despite an over-induction of defense gene expression by infection under high nitrogen regime. (frontiersin.org)
  • A high final PMA titer of 44.00 ± 3.65 g/L (49.9 ± 4.14 g/L of malic acid after hydrolysis) was achieved in a 5-L fermentor under low nitrogen concentration (2 g/L of NH 4 NO 3 ), which was 18.3 % higher yield than that obtained under high nitrogen concentration (10 g/L of NH 4 NO 3 ). (biomedcentral.com)
  • The most distinct phylogenetic finding was a high correlation between iron-sulfur oxidoreductases in combination with carbon nitrogen ligases and Chlorobium. (mirnaarray.com)
  • Template free synthesis of lithium doped three-dimensional macroporous graphitic carbon nitride for photocatalytic N fixation: the effect of Li-N active sites. (bioportfolio.com)
  • DNA ligase I: ligates Okazaki fragments during lagging strand DNA replication and some recombinant fragments. (chemeurope.com)
  • First, enoyl-coenzyme A (CoA) hydratase (encoded by phaJ4 ) is stress induced and likely to contribute to PHA synthesis under nitrogen starvation conditions. (asm.org)
  • In this study, TaMIR2275, a miRNA family member of wheat ( T. aestivum ), was subjected to functional characterization in mediation of the nitrogen (N) starvation response. (springer.com)
  • Transport of dicarboxylates across the chloroplast envelope plays an important role in transferring carbon skeletons to the nitrogen assimilation pathway and exporting reducing equivalent to the cytosol to prevent photo-inhibition (the malate valve). (semanticscholar.org)
  • RN RM PMID:22910360 RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. (jcvi.org)
  • Nanorod carbon nitride as a carbo catalyst for selective oxidation of hydrogen sulfide to sulfur. (bioportfolio.com)
  • Total fatty acid production (22 mg/L) could be increased up to 2.5-fold by knocking out PHB synthesis, a major sink for acetyl-CoA, or by knocking out the acyl-CoA ligase fadD3 , an entry point for fatty acids into β -oxidation. (peerj.com)
  • DNA ligase III: complexes with DNA repair protein XRCC1 to aid in sealing base excision mutations and recombinant fragments. (chemeurope.com)
  • As Δ fadD3 mutants still consumed laurate, and because the R. eutropha genome is predicted to encode over 50 acyl-CoA ligases, we employed RNA-Seq to identify acyl-CoA ligases upregulated during growth on laurate. (peerj.com)
  • Doping-induced Hydrogen-Bond Engineering in Polymeric Carbon Nitride to Significantly Boost the Photocatalytic H2 Evolution Performance. (bioportfolio.com)
  • Knockouts of the three most highly upregulated acyl-CoA ligases increased fatty acid yield significantly, with one strain (Δ A2794 ) producing up to 62 mg/L free fatty acid. (peerj.com)