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.
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.
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.
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).
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.
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.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
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)
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.
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.
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.
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.
Inorganic compounds that contain nitrogen as an integral part of the molecule.
Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.
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 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.
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.
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)
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
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.
Toxic asphyxiation due to the displacement of oxygen from oxyhemoglobin by carbon monoxide.
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.
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.
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.
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.
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.
Inorganic oxides that contain nitrogen.
A family of signal transducing adaptor proteins that control the METABOLISM of NITROGEN. They are primarily found in prokaryotes.
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)
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.
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.
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.
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.
Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.
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.
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.
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.
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.
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.
The unconsolidated mineral or organic matter on the surface of the earth that serves as a natural medium for the growth of land plants.
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.
Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.
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.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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).
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An 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.
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.
Proteins found in any species of bacterium.
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.
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.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.
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.
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 that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.
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.
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.
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.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
The gaseous envelope surrounding a planet or similar body. (From Random House Unabridged Dictionary, 2d ed)
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)
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.
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)
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.
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.
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)
The relationships of groups of organisms as reflected by their genetic makeup.
An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1.
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.
The rate dynamics in chemical or physical systems.
A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.
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.
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)
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).
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.
Woody, usually tall, perennial higher plants (Angiosperms, Gymnosperms, and some Pterophyta) having usually a main stem and numerous branches.
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.
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)
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.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
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.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).
Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.
The presence of bacteria, viruses, and fungi in the soil. This term is not restricted to pathogenic organisms.
An essential amino acid. It is often added to animal feed.
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.
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.
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.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
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.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
A 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.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
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.
Purified Recombinant Human MTHFS Protein, GST-tagged from Creative Biomart. Recombinant Human MTHFS Protein, GST-tagged can be used for research.
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 ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
CTPS2 antibody LS-C167137 is an unconjugated rabbit polyclonal antibody to human CTPS2 (CTP Synthetase 2) (aa77-105). Validated for Flow and WB.
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
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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.
Lionel Ballut, Sebastien Violot, Santosh Shivakumaraswamy, Lakshmi Prasoona Thota, Manu Sathya, Jyothirmai Kunala, Bauke W. Dijkstra, Raphael Terreux, Richard Haser, Hemalatha Balaram and Nushin Aghajari, Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation, Nature Communications 6, (2015 ...
The protein encoded by this gene catalyzes the formation of CTP from UTP with the concomitant deamination of glutamine to glutamate. This protein is the rate-limiting enzyme in the synthesis of cytosine nucleotides, which play an important role in various metabolic processes and provide the precursors necessary for the synthesis of RNA and DNA. Cancer cells that exhibit increased cell proliferation also exhibit an increased activity of this encoded protein. Thus, this protein is an attractive target for selective chemotherapy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013] ...
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 ...
TY - JOUR. T1 - Selective inhibition of biotin protein ligase from Staphylococcus aureus. AU - Soares Da Costa, Tatiana P.. AU - Tieu, William. AU - Yap, Min Y.. AU - Pendini, Nicole R.. AU - Polyak, Steven W.. AU - Pedersen, Daniel Sejer. AU - Morona, Renato. AU - Turnidge, John D.. AU - Wallace, John C.. AU - Wilce, Matthew C J. AU - Booker, Grant W.. AU - Abell, Andrew D.. N1 - Copyright: Copyright 2013 Elsevier B.V., All rights reserved.. PY - 2012/5/18. Y1 - 2012/5/18. N2 - There is a well documented need to replenish the antibiotic pipeline with new agents to combat the rise of drug resistant bacteria. One strategy to combat resistance is to discover new chemical classes immune to current resistance mechanisms that inhibit essential metabolic enzymes. Many of the obvious drug targets that have no homologous isozyme in the human host have now been investigated. Bacterial drug targets that have a closely related human homologue represent a new frontier in antibiotic discovery. However, to ...
Looking for biotin carboxylase? Find out information about biotin carboxylase. An enzyme which condenses bicarbonate with biotin to form carboxybiotin Explanation of biotin carboxylase
TY - JOUR. T1 - Inhibition of escherichia coil dethiobiotin synthetase by stable phosphorous analogs of the carbamate intermediate. AU - Taylor, W.. AU - Rendina, A.. AU - Rayner, D.. AU - Lockett, B.. AU - Kraals, K.. AU - Marsilli, E.. AU - Chii, H.. AU - Wawrzak, Z.. AU - Calabrese, J.. AU - Huang, W.. AU - Jia, J.. AU - Schneider, G.. AU - Lindqvist, Y.. PY - 1997/12/1. Y1 - 1997/12/1. N2 - A series of phosphoric, phosphonic and phosphinic acid mimics of the N7DAPA-carbamate were prepared and analyzed as inhibitors and alternate substrates for DTBS. Extension of the phosphorous moiety by a methylene spacer resulted in weaker inhibition at high ATP levels suggesting that the phosphorous group was overlapping with the 7 -phosphate of ATP rather than the carbamate carboxyt site. This was confirmed by the crystal structure of 7-( 1-hydroxyethyl)-9-phosphonononanoic acid (KU843) complexed with the enzyme. In general, phosphorous-containing inhibitors that were dianionic showed weaker inhibition ...
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 ...
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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 ...
What are the characters Mendel selected for his experiments on pea plant? MTHFS is the first identified 10-formylTHF tight-binding protein. 2, the WT GBS strain, A909 is prototrophic for both purine and pyrimidine biosynthesis and reach an optical density at 600 nm (OD 600) of 0.8-0.9 (3-5 × 10 9 cfu ml −1) in dCDM, similar to growth in cCDM (Fig. Control by purines occurs through PurR-mediated repression ( 4 , 84 ), and nitrogen control involves the Ntr system acting through the nitrogen assimilation control protein NAC ( 4 , 119 ). Pyrimidine biosynthesis Unlike in purine biosynthesis, the pyrimidine ring is synthesized before it is conjugated to PRPP. Thus, the behavior of liver CTP synthetase activity is tightly linked with that of the CTP pool. the reaction catalysed by the enzyme aspartate transcarbamoylase. 2. iii. the reaction catalysed by the enzyme aspartate transcarbamoylase. CTP. Here we review progress in molecular aspects and recent studies on the regulation and manipulation of ...
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 ...
Eukaryotic complex phototrophs exhibit a colorful evolutionary history. At least three independent endosymbiotic events accompanied by the gene transfer from the endosymbiont to host assembled a complex genomic mosaic. Resulting patchwork may give rise to unique metabolic capabilities; on the other hand, it can also blur the reconstruction of phylogenetic relationships. The ornithine-urea cycle (OUC) belongs to the cornerstone of the metabolism of metazoans and, as found recently, also photosynthetic stramenopiles. We have analyzed the distribution and phylogenetic positions of genes encoding enzymes of the urea synthesis pathway in eukaryotes. We show here that metazoan and stramenopile OUC enzymes share common origins and that enzymes of the OUC found in primary algae (including plants) display different origins. The impact of this fact on the evolution of stramenopiles is discussed here.. ...
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.
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Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_2081 (SAUSA300_RS11455); symbol: pyrG; product: CTP synthetase
Cell therapy products (CTPs) need quantitative, validated, and robust assays to support informed decision making during their development, manufacturing, and re
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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.. ...
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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 ...
In the EC scheme, such carboxylases are classed under EC 6.3.4, "Other Carbon-Nitrogen Ligases". Another example is the ... Braunstein, Pierre; Matt, Dominique; Nobel, Dominique (August 1988). "Reactions of Carbon Dioxide with Carbon-Carbon Bond ... Carbon-based life originates from carboxylation that couples atmospheric carbon dioxide to a sugar. The process is usually ... Carboxylation is a chemical reaction in which a carboxylic acid group is produced by treating a substrate with carbon dioxide. ...
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 ( ... "Synthases and Ligases". IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN), and Nomenclature Commission of IUB (NC- ... Li H, Xu H, Graham DE, White RH (Aug 2003). "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic ... Galperin MY, Koonin EV (1997). "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". ...
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 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 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 deamido-NAD+:L-glutamine amido-ligase (AMP-forming). Other names in common use ...
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 hydrogenobyrinic-acid:L-glutamine amido-ligase (AMP-forming). This enzyme is also ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... L-glutamine amido-ligase (ADP-forming). Other names in common use include CobQ, cobyric acid synthase, 5'-deoxy-5'- ... adenosylcobyrinic-acid-a,c-diamide:L-glutamine, amido-ligase, and Ado-cobyric acid synthase [glutamine hydrolyzing]. This ...
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 ...
... carbon-nitrogen ligases with glutamine as amide-n-donor MeSH D08.811.464.259.400.300 - carbamoyl-phosphate synthase (glutamine- ... valine-tRNA ligase MeSH D08.811.464.267.500 - coenzyme a ligases MeSH D08.811.464.267.500.200 - acetate-coa ligase MeSH D08.811 ... 500.600 - succinate-coa ligases MeSH D08.811.464.754.600 - dna ligases MeSH D08.811.464.754.720 - rna ligase (atp) MeSH D08.811 ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ...
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 ...
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... This enzyme participates in one carbon pool by folate. As of late 2007, 5 structures have been solved for this class of enzymes ... In enzymology, a 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) is an enzyme that catalyzes the chemical reaction ATP + 5- ... name of this enzyme class is 5-formyltetrahydrofolate cyclo-ligase (ADP-forming). Other names in common use include 5,10- ...
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... Other names in common use include L-amino acid alpha-ligase, bacilysin synthetase, YwfE, and L-amino acid ligase. Tabata K, ... In enzymology, an L-amino-acid alpha-ligase (EC 6.3.2.28) is an enzyme that catalyzes the chemical reaction ATP + an L-amino ... Ikeda H, Hashimoto S (2005). "ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase". J. Bacteriol. 187 (15 ...
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. ...
Thalidomide has been shown to bind to cereblon, inhibiting the activity of the E3 ubiquitin ligase, resulting in accumulation ... The substances that had nitrogen salts as the R group showed good activity. The improved angiogenesis inhibitory activity could ... such as cyclopentoxy at the 3-position carbon (X3). However the thalidomide PDE4 inhibitory analogs do not follow the SAR of ... It acts as a component of the E3 ubiquitin ligase, regulating various developmental processes, including embryogenesis, ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ... An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically ...
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 ...
... , though, binds better than N-methylephedrine, which has an additional methyl group at the nitrogen atom. Also the ... Benzaldehyde reacts with pyruvic acid to attach a 2 carbon unit. This product then undergoes transamination and methylation to ... proposed suggests that phenylalanine first forms cinnamoyl-CoA via the enzymes phenylalanine ammonia-lyase and acyl CoA ligase. ...
N-Acetyl-L-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold ... Ubiquitin ligases transfer ubiquitin to its pendant, proteins, and caspases, which engage in proteolysis in the apoptotic cycle ... In the newer R/S system of designating chirality, based on the atomic numbers of atoms near the asymmetric carbon, cysteine ( ... selenium) as a second neighbor to the asymmetric carbon. The remaining chiral amino acids, having lighter atoms in that ...
... carbon = white, oxygen = red, nitrogen = blue) based on the PDB: 1HS6​ structure. ...
Some plants have coevolved with nitrogen fixing bacteria, making plants an important part of the nitrogen cycle. Plant roots ... Waterworth, W.M.; Masnavi, G.; Bhardwaj, R.M.; Jiang, Q.; Bray, C.M.; West, C.E. (2010). "A plant DNA ligase is an important ... Through the process of photosynthesis, most plants use the energy in sunlight to convert carbon dioxide from the atmosphere, ... Plants usually rely on soil primarily for support and water (in quantitative terms), but they also obtain compounds of nitrogen ...
... of the two-carbon acetate residue from acetyl coenzyme A and a molecule of four-carbon oxaloacetate to form the six-carbon ... These experiments have revealed that this single site alternates between two forms, which participate in ligase and hydrolase ... the epsilon nitrogen lone pair of electrons on His-274 formed in the last step abstracts the hydroxyl enol proton to reform an ... One of the oxygen's lone pairs nucleophilically attacks the carbonyl carbon of citroyl−CoA. This forms a tetrahedral ...
Note the traceable carbon and nitrogen ring framework of quinoline in this structure. ... Third- and fourth-generation fluoroquinolones are more selective for the topoisomerase IV ligase domain, and thus have enhanced ... the nitrogen (N)-containing pyridine ring is now on the left, and the N-1 atom and C-6 carbonyl are at 12 o'clock and 6 o'clock ... and add a fluorine atom to the all-carbon containing ring, typically at the C-6 or C-7 positions. ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ... Glutamine synthetase (GS) (EC 6.3.1.2)[3] is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ... strain PCC 6803 is differently regulated in response to nitrogen availability". Journal of Bacteriology. 179 (8): 2678-89. doi: ...
Of these amino acids, aspartate and glutamine are used, together with carbon and nitrogen atoms from other sources, to form the ... Most organisms utilize EC 6.2.1.5, succinate-CoA ligase (ADP-forming) (despite its name, the enzyme operates in the pathway in ... The citric acid cycle begins with the transfer of a two-carbon acetyl group from acetyl-CoA to the four-carbon acceptor ... into two molecules each of carbon dioxide and water. Through catabolism of sugars, fats, and proteins, the two-carbon organic ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ...
The aspartate is hydrogen bonded to the histidine, increasing the pKa of its imidazole nitrogen from 7 to around 12. This ... The lone pair of electrons present on the oxygen or sulfur attacks the electropositive carbonyl carbon.[3] The 20 naturally ... 1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183 ... First, the activated nucleophile attacks the carbonyl carbon and forces the carbonyl oxygen to accept an electron, leading to a ...
Enzymes called DNA ligases can rejoin cut or broken DNA strands.[120] Ligases are particularly important in lagging strand DNA ... carbon-carbon bond formation, and etc. DNAzymes can enhance catalytic rate of chemical reactions up to 100,000,000,000-fold ... Each nucleotide is composed of one of four nitrogen-containing nucleobases (cytosine [C], guanine [G], adenine [A] or thymine [ ... Nucleases and ligases. Nucleases are enzymes that cut DNA strands by catalyzing the hydrolysis of the phosphodiester bonds. ...
Bacterial and fungal proteases are particularly important to the global carbon and nitrogen cycles in the recycling of proteins ... Sims GK, Wander MM (2002). "Proteolytic activity under nitrogen or sulfur limitation". Appl. Soil Ecol. 568: 1-5.. ... "Nitrogen Starvation Promotes Biodegradation of N-Heterocyclic Compounds in Soil". Soil Biology & Biochemistry. 38 (8): 2478- ... present in soil can be observed at the overall microbial community level as proteins are broken down in response to carbon, ...
... and adding two methyl groups at the para-hydroxyl and the meta carbon position. This modified tyrosine reacts with the original ... biosynthesis of trabectedin in Candidatus Endoecteinascidia frumentensis starts with a fatty acid loading onto the acyl-ligase ... Nitrogen mustards: Mechlorethamine. *Cyclophosphamide# (Ifosfamide#. *Trofosfamide). *Chlorambucil# (Melphalan. *Prednimustine) ... adding several functional groups and making a sulfide bridge between the original cysteine residue and the beta-carbon of the ...
The liver's crucial role in controlling blood sugar concentrations by breaking down glucose into carbon dioxide and glycogen is ... These target proteins become substrates for particular E3 ubiquitin ligases only when they are phosphorylated. ... and some lower eukaryotes histidine's nitrogen act as a nucleophile and binds to a phosphate group.[38] Once histidine is ... The cascade effect of phosphorylation eventually causes instability and allows enzymes to open the carbon bonds in glucose. ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ... E3 ligase activity[edit]. The E3 ubiquitin ligase MDM2 is a negative regulator of the p53 tumor suppressor protein. MDM2 binds ... ubiquitin protein ligase activity. • NEDD8 ligase activity. • disordered domain specific binding. • protein domain specific ... The RING domain of Mdm2 confers E3 ubiquitin ligase activity and is sufficient for E3 ligase activity in Mdm2 RING ...
one-carbon metabolic process. • axon regeneration. • regulation of transcription involved in G1/S transition of mitotic cell ... The acidity of the targeted nitrogen on the substrate is important in the binding of the substrate to the enzyme's binding site ... which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR ...
2-carbon groups, α cleavage. Bacteria, archaea and eukaryotes NAD+ and NADP+ [31]. Niacin (B3). ADP. Electrons. Bacteria, ... Other organisms require additional metals as enzyme cofactors, such as vanadium in the nitrogenase of the nitrogen-fixing ...
6.3: Carbon-Nitrogen. *Glutamine synthetase. *Ubiquitin ligase *Cullin. *Von Hippel-Lindau tumor suppressor ... L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction ... Boehlein SK, Richards NG, Schuster SM (March 1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine ...
... and the second hydrogen atom transferred to the C4 carbon atom opposite this nitrogen. The midpoint potential of the NAD+/NADH ... Other NAD-dependent enzymes include bacterial DNA ligases, which join two DNA ends by using NAD+ as a substrate to donate an ... Since the C4 carbon that accepts the hydrogen is prochiral, this can be exploited in enzyme kinetics to give information about ... The nucleosides each contain a ribose ring, one with adenine attached to the first carbon atom (the 1' position) and the other ...
Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... Category:EC 3.5 (act on carbon-nitrogen bonds, other than peptide bonds)Edit. *Category:EC 3.5.1 (In linear amides) *Urease (EC ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ... Category:EC 4.3 (carbon-nitrogen lyases)Edit. *Category:EC 4.3.1 *Phenylalanine ammonia-lyase (EC 4.3.1.24) ...
"butyrate-CoA ligase. BRENDA. Technische Universität Braunschweig.. *^ "Substrate/Product". glycine N-acyltransferase. BRENDA. ... reactive nitrogen species (RNS), and damage-associated molecular pattern molecules (DAMPs), the dysregulation of glutamate ... phenylacetone is reacted with two equivalents of N-methylformamide to produce the formyl amide of methamphetamine plus carbon ... CYP2D6, dopamine β-hydroxylase, flavin-containing monooxygenase 3, butyrate-CoA ligase, and glycine N-acyltransferase are the ...
Hydrolases: carbon-nitrogen non-peptide (EC 3.5). 3.5.1: Linear amides /. Amidohydrolases. *Asparaginase ...
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. ...
Pyruvate Carboxylase Genes and a PutativeEscherichia coli-Type Bifunctional Biotin Protein Ligase Gene (bpl/birA) Exhibit a ...
Forming carbon-nitrogen bonds [6.3] <5>. (59,78). (58,59,38). 0: Other carbon--nitrogen ligases [6.3.4] <24>. (28,31). (27,28, ... Enzyme Commission (EC): Other carbon--nitrogen ligases. (show info) Phenotype Ontology. Like Gene Ontology (GO), phenotypy ... Phosphoribosylamine--glycine ligase [6.3.4.13]. (6,6). (6,6,6). - 1: Ribose-5-phosphate--ammonia ligase [6.3.4.7]. (0,0). (0,0, ... ligase ,, Biotin--[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase ,, Biotin--[biotin carboxyl-carrier protein] ligase. ...
ligase activity, forming carbon-nitrogen bonds. id: GO:0016879. name: ligase activity, forming carbon-nitrogen bonds. namespace ... Description: Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, ... acid-amino acid ligase activity. GO:0016882. cyclo-ligase activity. GO:0016884. carbon-nitrogen ligase activity, with glutamine ... acid-ammonia (or amide) ligase activity. GO:0016881. ... citrate-L-glutamate ligase activity. Parent Functions. id. name ...
ligase activity, forming carbon-nitrogen bonds Source: InterPro. *magnesium ion binding Source: UniProtKB-UniRule ... Belongs to the Pup ligase/Pup deamidase family. Pup-conjugating enzyme subfamily.UniRule annotation. Manual assertion according ... sp,D2ATU8,PAFA_STRRD Pup--protein ligase OS=Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) OX= ...
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, ...
ligase activity, forming carbon-nitrogen bonds. acid-amino acid ligase activity. ubiquitin-protein ligase activity. ... E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N ... Kume K, Iizumi Y, Shimada M, Ito Y, Kishi T, Yamaguchi Y, Handa H: Role of N-end rule ubiquitin ligases UBR1 and UBR2 in ... Showing Protein E3 ubiquitin-protein ligase UBR2 (HMDBP09274). IdentificationBiological propertiesGene propertiesProtein ...
ligase activity. ligase activity, forming carbon-nitrogen bonds. acid-amino acid ligase activity. ... May also act as a E3 ubiquitin- protein ligase which accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of ... Involved in acid-amino acid ligase activity. Specific Function. Involved in membrane trafficking via some guanine nucleotide ... Showing Protein Probable E3 ubiquitin-protein ligase HERC1 (HMDBP08447). IdentificationBiological propertiesGene properties ...
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, ...
Carbon-Nitrogen Ligases / chemistry * Carbon-Nitrogen Ligases / genetics * Carbon-Nitrogen Ligases / metabolism* ...
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 ...
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 - ...
ligase activity, forming carbon-nitrogen bonds Source: UniProtKB-UniRule. Complete GO annotation on QuickGO ... ...
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. ...
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- ...
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 ...
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. ...
Ligases;. Forming carbon-nitrogen bonds;. Other carbon-nitrogen ligases. BRITE hierarchy. Sysname. hydrogencarbonate:ammonia ... carbon-dioxide---ammonia ligase;. carbamoylphosphate synthase;. carbamylphosphate synthetase;. carbamoylphosphate synthase ( ...
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 / ...
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 (C)] and nitrogen (N), is important for the regulation of plant metabolism and development. In addition to independent ... carbon and nitrogen metabolic enzymes and signaling proteins such as protein kinases and transcription factors. Further ... carbon and nitrogen metabolic enzymes and signaling proteins such as protein kinases and transcription factors. Further ... and nitrogen (N), is important for the regulation of plant metabolism and development. In addition to independent utilization ...
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 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)] ...
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 ...
  • Nutrient availability, in particular the availability of sugar [carbon (C)] and nitrogen (N), is important for the regulation of plant metabolism and development. (frontiersin.org)
  • these processes include cell wall organization, carbohydrate metabolism, nitrogen compound transport, and the regulation of proteolysis. (frontiersin.org)
  • Expression of Formate-Tetrahydrofolate Ligase Did Not Improve Growth but Interferes With Nitrogen and Carbon Metabolism ofSynechocystissp. (mpg.de)
  • This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism. (creative-enzymes.com)
  • Although these factors have been explored separately, they all involve one-carbon (C1) metabolism. (isharonline.org)
  • Maternal one-carbon (1-C) metabolism provides methylgroups for fetal development and programing by DNA methylation as one of the underlying epigenetic mechanisms. (isharonline.org)
  • Comparative transcriptomics profiling revealed that a set of genes, related to the ribosome, ribosome biogenesis, proteasome, and nitrogen metabolism, were significantly up- or down-regulated under nitrogen sufficient conditions, which could be regulated by the TOR signaling pathway. (biomedcentral.com)
  • This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. (wikipedia.org)
  • It is also said that a synthase is a lyase (a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure) and does not require any energy, whereas a synthetase is a ligase (a ligase is an enzyme that binds two chemicals or compounds) and thus requires energy. (wikipedia.org)
  • This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). (wikipedia.org)
  • New covalent bonds between two molecules are created by the enzyme called ligase. (biospace.com)
  • Carbon-nitrogen bonds are formed by the action of the same enzyme as peptide synthetases and amide synthetases. (biospace.com)
  • Ligases are used in catalysis where two substrates are ligated and the formation of carbon-carbon, carbon-sulfide, carbon-nitrogen, and carbon-oxygen bonds due to condensation reactions. (wikibooks.org)
  • Urea carboxylase (EC 6.3.4.6) is an enzyme that belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. (worldofchemicals.com)
  • Other common names for ligases include the word "synthetase", because they are used to synthesize new molecules. (wikipedia.org)
  • The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales. (wikipedia.org)
  • A ligase is also known as a Synthetase. (biospace.com)
  • Holocarboxylase synthetase (HCS, human) and BirA (Escherichia coli) are biotin protein ligases that catalyze the ATP-dependent attachment of biotin to apocarboxylases. (ox.ac.uk)
  • 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 [2]. (genome.jp)
  • Unlike ligases, lyases bring about synthase reactions without the participation of energy-rich (macroergic) compounds. (thefreedictionary.com)
  • 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)
  • The systematic name of this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). (wikipedia.org)
  • Lyases are classified as carbon-carbon lyases (some of these are called synthases), carbon-nitrogen, carbon-oxygen, and so forth. (thefreedictionary.com)
  • Awakening a latent carbon fixation cycle in Escherichia coli. (mpg.de)
  • 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)
  • These enzymes are grouped into six classes: hydrolases (including proteases, amylases and lipases that break down the main nutrients - fats, carbohydrates and proteins), isomerases, ligases, lyases , oxidoreductases and transferases. (thefreedictionary.com)
  • This study suggests that the thumb loop found in bacterial carboxylases interferes with optimal interaction with the mammalian biotin protein ligase. (ox.ac.uk)
  • A ubiquitin ligase complex found in the nucleus. (leibniz-fli.de)
  • A ubiquitin ligase complex found in the ER. (leibniz-fli.de)
  • 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 formate:dihydrofolate ligase (ADP-forming). (wikipedia.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 4-methylene-L-glutamate:ammonia ligase (AMP-forming). (wikipedia.org)
  • The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). (wikibooks.org)
  • The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming) . (wikidoc.org)
  • DNA ligase has the function of forming a bond between the end of an 'acceptor' nucleotide and at the end of a 'donor' nucleotide. (biospace.com)
  • In enzymology, a 4-methyleneglutamate-ammonia ligase (EC 6.3.1.7) is an enzyme that catalyzes the chemical reaction ATP + 4-methylene-L-glutamate + NH3 ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + 4-methylene-L-glutamine The 3 substrates of this enzyme are ATP, 4-methylene-L-glutamate, and NH3, whereas its 3 products are AMP, diphosphate, and 4-methylene-L-glutamine. (wikipedia.org)
  • In the first step, an amino group given by glutamine is attached at carbon 1 of PRPP. (wikibooks.org)
  • GO annotations related to this gene include hydrolase activity and carbon-nitrogen ligase activity, with glutamine as amido-N-donor . (genecards.org)
  • FAAH2 has several biochemical functions, for example, carbon-nitrogen ligase activity, with glutamine as amido-N-donor, hydrolase activity. (creativebiomart.net)
  • Glutamine plays a role in a variety of biochemical functions including protein synthesis, cellular energy, as a source, next to glucose, 2) Nitrogen donation for many anabolic processes and 3) Carbon donation, as a source, refilling the citric acid cycle. (ymdb.ca)
  • 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)
  • The dependence of the enzyme on pyridoxal 5′-phosphate and the production of 3H4P with the release of ammonia indicate that it is a carbon-nitrogen lyase. (plantphysiol.org)
  • 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)
  • 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)
  • Some ligases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix , [2] for example certain ubiquitin ligase related proteins. (wikipedia.org)
  • Phosphoproteomics under conditions of C/N-nutrient stress showed a global change in the phosphorylation status of proteins, including plasma membrane H + -ATPase, carbon and nitrogen metabolic enzymes and signaling proteins such as protein kinases and transcription factors. (frontiersin.org)
  • Same as all enzymes, ligases are embedded with proteins that have a target molecule identification site. (biospace.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)
  • Aminoacyl tRNA-synthetases is included in ligases that join amino acids to the relative tRNA, which promotes the DNA ligases to bring the two pieces of DNA together. (biospace.com)
  • Any process that stops, prevents or reduces the frequency, rate or extent of isoleucine-tRNA ligase activity. (semanticscholar.org)
  • A reaction of ligase catalyzing the formation of a carbon-oxygen bond between an amino acid and transfer RNA leads to the formation of the amino acid-RNA ligase bond. (biospace.com)
  • A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. (leibniz-fli.de)
  • 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)
  • Doping-induced enhancement of crystallinity in polymeric carbon nitride nanosheets to improve their visible-light photocatalytic activity. (bioportfolio.com)
  • The catalytic subunit of the PRC1 E3 ligase complex is Ring1B. (maixius.com)
  • Glutamate-Cysteine Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • 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)
  • 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)
  • RN [2] RM PMID:22910360 RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. (jcvi.org)
  • The most distinct phylogenetic finding was a high correlation between iron-sulfur oxidoreductases in combination with carbon nitrogen ligases and Chlorobium. (mirnaarray.com)
  • In terms of application, the global ligases enzyme market can be divided into polymerase chain reaction, mutation detection, cloning, drug target, and next generation sequencing. (biospace.com)
  • An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. (healthmatics.info)
  • 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)
  • Seed development and nitrogen (N) storage depend on delivery of amino acids to seed sinks. (plantcell.org)
  • Nitrogen (N) and carbon (C) are two of the most important nutrients for plant growth, and in the majority of plant species, they are transported in the phloem to sink organs in the form of amino acids and sucrose, respectively. (plantcell.org)
  • These are alpha amino acids which have the L-configuration of the alpha-carbon atom. (ymdb.ca)
  • Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. (systemsbiology.net)
  • Ligases catalyze the addition of two molecules, deriving the needed energy from the cleavage of an energy-rich phosphate bond. (biospace.com)
  • Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. (bvsalud.org)