Carbon carbon ligases. Medical search

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.

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.

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.

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.

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 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.

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.

Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.

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.

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.

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.

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.

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.

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.

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.

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 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.

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.

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 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.

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.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.

A dark powdery deposit of unburned fuel residues, composed mainly of amorphous CARBON and some HYDROCARBONS, that accumulates in chimneys, automobile mufflers and other surfaces exposed to smoke. It is the product of incomplete combustion of carbon-rich organic fuels in low oxygen conditions. It is sometimes called lampblack or carbon black and is used in INK, in rubber tires, and to prepare CARBON NANOTUBES.

The gaseous envelope surrounding a planet or similar body. (From Random House Unabridged Dictionary, 2d ed)

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).

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.

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.

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.

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.

Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.

The unconsolidated mineral or organic matter on the surface of the earth that serves as a natural medium for the growth of land plants.

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.

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.

Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.

An allotropic form of carbon that is used in pencils, as a lubricant, and in matches and explosives. It is obtained by mining and its dust can cause lung irritation.

Inorganic compounds that contain carbon as an integral part of the molecule but are not derived from hydrocarbons.

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 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.

Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.

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.

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.

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.

The rate dynamics in chemical or physical systems.

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 facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

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 degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.

The relationships of groups of organisms as reflected by their genetic makeup.

Woody, usually tall, perennial higher plants (Angiosperms, Gymnosperms, and some Pterophyta) having usually a main stem and numerous branches.

Electric conductors through which electric currents enter or leave a medium, whether it be an electrolytic solution, solid, molten mass, gas, or vacuum.

Proteins found in any species of bacterium.

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 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 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).

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 simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)

The processes by which organisms use simple inorganic substances such as gaseous or dissolved carbon dioxide and inorganic nitrogen as nutrient sources. Contrasts with heterotrophic processes which make use of organic materials as the nutrient supply source. Autotrophs can be either chemoautotrophs (or chemolithotrophs), largely ARCHAEA and BACTERIA, which also use simple inorganic substances for their metabolic energy reguirements; or photoautotrophs (or photolithotrophs), such as PLANTS and CYANOBACTERIA, which derive their energy from light. Depending on environmental conditions some organisms can switch between different nutritional modes (autotrophy; HETEROTROPHY; chemotrophy; or PHOTOTROPHY) to utilize different sources to meet their nutrient and energy requirements.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

A functional system which includes the organisms of a natural community together with their environment. (McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).

A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).

Transport proteins that carry specific substances in the blood or across cell membranes.

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.

One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.

A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 1.14.99.3.

Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The generic name for the group of aliphatic hydrocarbons Cn-H2n+2. They are denoted by the suffix -ane. (Grant & Hackh's Chemical Dictionary, 5th ed)

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The salinated water of OCEANS AND SEAS that provides habitat for marine organisms.

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.

Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

The presence of bacteria, viruses, and fungi in the soil. This term is not restricted to pathogenic organisms.

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.

A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.

The pressure that would be exerted by one component of a mixture of gases if it were present alone in a container. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

A mass of organic or inorganic solid fragmented material, or the solid fragment itself, that comes from the weathering of rock and is carried by, suspended in, or dropped by air, water, or ice. It refers also to a mass that is accumulated by any other natural agent and that forms in layers on the earth's surface, such as sand, gravel, silt, mud, fill, or loess. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1689)

Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation.

The effect of GLOBAL WARMING and the resulting increase in world temperatures. The predicted health effects of such long-term climatic change include increased incidence of respiratory, water-borne, and vector-borne diseases.

An essential amino acid. It is often added to animal feed.

Macromolecular complexes formed from the association of defined protein subunits.

Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.

Established cell cultures that have the potential to propagate indefinitely.

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.

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.

The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.

Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.

Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.

Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.

The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

Elements of limited time intervals, contributing to particular results or situations.

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)

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.

Salts or ions of the theoretical carbonic acid, containing the radical CO2(3-). Carbonates are readily decomposed by acids. The carbonates of the alkali metals are water-soluble; all others are insoluble. (From Grant & Hackh's Chemical Dictionary, 5th ed)

Life or metabolic reactions occurring in an environment containing oxygen.

Oxidoreductases that are specific for ALDEHYDES.

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)

A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.

A broad class of substances containing carbon and its derivatives. Many of these chemicals will frequently contain hydrogen with or without oxygen, nitrogen, sulfur, phosphorus, and other elements. They exist in either carbon chain or carbon ring form.

A great expanse of continuous bodies of salt water which together cover more than 70 percent of the earth's surface. Seas may be partially or entirely enclosed by land, and are smaller than the five oceans (Atlantic, Pacific, Indian, Arctic, and Antarctic).

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.

The processes by which organisms utilize organic substances as their nutrient sources. Contrasts with AUTOTROPHIC PROCESSES which make use of simple inorganic substances as the nutrient supply source. Heterotrophs can be either chemoheterotrophs (or chemoorganotrophs) which also require organic substances such as glucose for their primary metabolic energy requirements, or photoheterotrophs (or photoorganotrophs) which derive their primary energy requirements from light. Depending on environmental conditions some organisms can switch between different nutritional modes (AUTOTROPHY; heterotrophy; chemotrophy; or PHOTOTROPHY) to utilize different sources to meet their nutrients and energy requirements.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

Cell surface receptors for AUTOCRINE MOTILITY FACTOR, which is the secreted form of GLUCOSE-6-PHOSPHATE ISOMERASE. The receptor has an unusual composition in that it shares some structural similarities with G-PROTEIN-COUPLED RECEPTORS and functions as an ubiquitin protein ligase when internalized.

The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.

The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.

An E3 ubiquitin ligase primarily involved in regulation of the metaphase-to-anaphase transition during MITOSIS through ubiquitination of specific CELL CYCLE PROTEINS. Enzyme activity is tightly regulated through subunits and cofactors, which modulate activation, inhibition, and substrate specificity. The anaphase-promoting complex, or APC-C, is also involved in tissue differentiation in the PLACENTA, CRYSTALLINE LENS, and SKELETAL MUSCLE, and in regulation of postmitotic NEURONAL PLASTICITY and excitability.

A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.

The use of a heavy ion particle beam for radiotherapy, such as the HEAVY IONS of CARBON.

A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

The utilization of an electrical current to measure, analyze, or alter chemicals or chemical reactions in solution, cells, or tissues.

The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.

An amorphous form of carbon prepared from the incomplete combustion of animal or vegetable matter, e.g., wood. The activated form of charcoal is used in the treatment of poisoning. (Grant & Hackh's Chemical Dictionary, 5th ed)

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.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.

A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.

Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.

The vapor state of matter; nonelastic fluids in which the molecules are in free movement and their mean positions far apart. Gases tend to expand indefinitely, to diffuse and mix readily with other gases, to have definite relations of volume, temperature, and pressure, and to condense or liquefy at low temperatures or under sufficient pressure. (Grant & Hackh's Chemical Dictionary, 5th ed)

The act of blowing a powder, vapor, or gas into any body cavity for experimental, diagnostic, or therapeutic purposes.

A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)

Deoxyribonucleic acid that makes up the genetic material of bacteria.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.

Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.

The amount of a gas taken up, by the pulmonary capillary blood from the alveolar gas, per minute per unit of average pressure of the gradient of the gas across the BLOOD-AIR BARRIER.

Proteins prepared by recombinant DNA technology.

An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.

A polyhedral CARBON structure composed of around 60-80 carbon atoms in pentagon and hexagon configuration. They are named after Buckminster Fuller because of structural resemblance to geodesic domes. Fullerenes can be made in high temperature such as arc discharge in an inert atmosphere.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.

The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

Proteins found in any species of fungus.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

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)

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.

Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.

The presence of bacteria, viruses, and fungi in water. This term is not restricted to pathogenic organisms.

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

The monitoring of the level of toxins, chemical pollutants, microbial contaminants, or other harmful substances in the environment (soil, air, and water), workplace, or in the bodies of people and animals present in that environment.

A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

The act of breathing with the LUNGS, consisting of INHALATION, or the taking into the lungs of the ambient air, and of EXHALATION, or the expelling of the modified air which contains more CARBON DIOXIDE than the air taken in (Blakiston's Gould Medical Dictionary, 4th ed.). This does not include tissue respiration (= OXYGEN CONSUMPTION) or cell respiration (= CELL RESPIRATION).

The characteristic three-dimensional shape of a molecule.

The exchange of OXYGEN and CARBON DIOXIDE between alveolar air and pulmonary capillary blood that occurs across the BLOOD-AIR BARRIER.

Any substance in the air which could, if present in high enough concentration, harm humans, animals, vegetation or material. Substances include GASES; PARTICULATE MATTER; and volatile ORGANIC CHEMICALS.

The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

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.

The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.

The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.

The science of developing, caring for, or cultivating forests.

The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.

A product of hard secondary xylem composed of CELLULOSE, hemicellulose, and LIGNANS, that is under the bark of trees and shrubs. It is used in construction and as a source of CHARCOAL and many other products.

Product of the oxidation of ethanol and of the destructive distillation of wood. It is used locally, occasionally internally, as a counterirritant and also as a reagent. (Stedman, 26th ed)

A climate which is typical of equatorial and tropical regions, i.e., one with continually high temperatures with considerable precipitation, at least during part of the year. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

The adhesion of gases, liquids, or dissolved solids onto a surface. It includes adsorptive phenomena of bacteria and viruses onto surfaces as well. ABSORPTION into the substance may follow but not necessarily.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

Organic compounds containing the carboxy group (-COOH). This group of compounds includes amino acids and fatty acids. Carboxylic acids can be saturated, unsaturated, or aromatic.

Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.

The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.

An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Free-floating minute organisms that are photosynthetic. The term is non-taxonomic and refers to a lifestyle (energy utilization and motility), rather than a particular type of organism. Most, but not all, are unicellular algae. Important groups include DIATOMS; DINOFLAGELLATES; CYANOBACTERIA; CHLOROPHYTA; HAPTOPHYTA; CRYPTOMONADS; and silicoflagellates.

Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)

Relating to the size of solids.

A microanalytical technique combining mass spectrometry and gas chromatography for the qualitative as well as quantitative determinations of compounds.

The development and use of techniques to study physical phenomena and construct structures in the nanoscale size range or smaller.

The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase. (1/225)

The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the modification of specific glutamates in a number of proteins required for blood coagulation and associated with bone and calcium homeostasis. All known vitamin K-dependent proteins possess a conserved eighteen-amino acid propeptide sequence that is the primary binding site for the carboxylase. We compared the relative affinities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibition constants (Ki) toward a factor IX propeptide/gamma-carboxyglutamic acid domain substrate. The Ki values for six of the propeptides (factor X, matrix Gla protein, factor VII, factor IX, PRGP1, and protein S) were between 2-35 nM, with the factor X propeptide having the tightest affinity. In contrast, the inhibition constants for the propeptides of prothrombin and protein C are approximately 100-fold weaker than the factor X propeptide. The propeptide of bone Gla protein demonstrates severely impaired carboxylase binding with an inhibition constant of at least 200,000-fold weaker than the factor X propeptide. This study demonstrates that the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable range; this may have important physiological consequences in the levels of vitamin K-dependent proteins and the biochemical mechanism by which these substrates are modified by the carboxylase. (+info)

Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. (2/225)

Vitamin K-dependent proteins contain a propeptide that is required for recognition by the enzyme gamma-glutamylcarboxylase. Substrates used in vitro for carboxylation studies lacking a prosequence are characterized by Km values in the millimolar range, whereas the Km for peptides containing a prosequence is three or four orders of magnitude smaller. Here we report that descarboxy-osteocalcin is an exception in this respect. With descarboxy-osteocalcin in purified propeptide-free recombinant carboxylase, the Km was 1.8 microM. Furthermore, osteocalcin was an inhibitor of descarboxy-osteocalcin carboxylation with a Ki of 76 microM. In contrast with the other vitamin K-dependent proteins, free propeptides do not inhibit descarboxy-osteocalcin carboxylation. Moreover, propeptide-containing substrates were inhibited neither by osteocalcin nor by its propeptide. From our studies we conclude that descarboxy-osteocalcin must have an internal recognition sequence that binds to gamma-glutamylcarboxylase at a site different from the propeptide-recognition site. (+info)

Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (3/225)

Two genes, accA1 and accA2, with nearly identical nucleotide sequences were cloned from Streptomyces coelicolor A3(2). The deduced amino acid sequences of the product of these two genes showed high similarity to BcpA2 of Saccharopolyspora erythraea and other biotin-containing proteins from different organisms assumed to be the alpha subunit of a propionyl-CoA carboxylase. A gene, pccB, encoding the carboxyl transferase subunit of this enzyme complex was also characterized. Strains disrupted in accA1 did not show any change in acetyl- or propionyl-CoA carboxylase activity, whilst cell-free extracts of a pccB mutant strain contained a reduced level of propionyl-CoA carboxylase. No mutants in accA2 could be isolated, suggesting that the gene may be essential. Heterologous expression of accA1, accA2 and pccB in Escherichia col and in vitro reconstitution of enzyme activity confirmed that PccB is the beta subunit of a propionyl-CoA carboxylase and that either AccA1 or AccA2 could act as the alpha component of this enzyme complex. The fact that accA2 mutants appear to be inviable suggests that this gene encodes a biotinylated protein that might be shared with other carboxyl transferases essential for the growth of S. coelicolor. (+info)

Molecular characterization of the non-biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase. (4/225)

The biotin enzyme, 3-methylcrotonyl-CoA carboxylase (MCCase) (3-methylcrotonyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1. 4), catalyzes a pivotal reaction required for both leucine catabolism and isoprenoid metabolism. MCCase is a heteromeric enzyme composed of biotin-containing (MCC-A) and non-biotin-containing (MCC-B) subunits. Although the sequence of the MCC-A subunit was previously determined, the primary structure of the MCC-B subunit is unknown. Based upon sequences of biotin enzymes that use substrates structurally related to 3-methylcrotonyl-CoA, we isolated the MCC-B cDNA and gene of Arabidopsis. Antibodies directed against the bacterially produced recombinant protein encoded by the MCC-B cDNA react solely with the MCC-B subunit of the purified MCCase and inhibit MCCase activity. The primary structure of the MCC-B subunit shows the highest similarity to carboxyltransferase domains of biotin enzymes that use methyl-branched thiol esters as substrate or products. The single copy MCC-B gene of Arabidopsis is interrupted by nine introns. MCC-A and MCC-B mRNAs accumulate in all cell types and organs, with the highest accumulation occurring in rapidly growing and metabolically active tissues. In addition, these two mRNAs accumulate coordinately in an approximately equal molar ratio, and they each account for between 0.01 and 0.1 mol % of cellular mRNA. The sequence of the Arabidopsis MCC-B gene has enabled the identification of animal paralogous MCC-B cDNAs and genes, which may have an impact on the molecular understanding of the lethal inherited metabolic disorder methylcrotonylglyciuria. (+info)

Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase. (5/225)

Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase. Previously, the gastropod Conus was the only known invertebrate with a demonstrated vitamin K-dependent carboxylase. We report here the discovery of a gamma-glutamyl carboxylase in Drosophila. This Drosophila enzyme is remarkably similar in amino acid sequence to the known mammalian carboxylases; it has 33% sequence identity and 45% sequence similarity to human gamma-glutamyl carboxylase. The Drosophila carboxylase is vitamin K-dependent, and it has a K(m) toward a model pentapeptide substrate, FLEEL, of about 4 mm. However, unlike the human gamma-glutamyl carboxylase, it is not stimulated by human blood coagulation factor IX propeptides. We found the mRNA for Drosophila gamma-glutamyl carboxylase in virtually every embryonic and adult stage that we investigated, with the highest concentration evident in the adult head. (+info)

An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230. (6/225)

Analysis of a region of chromosomal DNA lying between jadR1 and jadI in the gene cluster for jadomycin biosynthesis in Streptomyces venezuelae ISP5230 detected an ORF encoding 584 amino acids similar in sequence to the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) components of acyl-coenzyme A carboxylases. Multiple sequence alignments of the deduced Jad protein with acyl-coenzyme A carboxylases from various sources located the BC and BCCP components in the N- and C-terminal regions, respectively, of the deduced polypeptides. The organization and amino acid sequence of the deduced polypeptide most closely resembled those in other Gram-positive bacteria broadly classified as actinomycetes. Disrupting the gene, designated jadJ, severely reduced but did not eliminate jadomycin production. The disruption had no effect on growth or morphology of the organism, implying that the product of jadJ is not essential for fatty acid biosynthesis. It is concluded that jadJ supplies malonyl-coenzyme A for biosynthesis of the polyketide intermediate that is eventually processed to form the antibiotic jadomycin B. (+info)

A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla. (7/225)

The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the posttranslational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to the function of the vitamin K-dependent blood coagulation proteins. Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a marine invertebrate, we hypothesized that structurally conserved regions would identify sequences critical to this common functionality. Furthermore, we examined the diversity of animal species that maintain vitamin K-dependent carboxylation to generate gamma-carboxyglutamic acid. We have cloned carboxylase homologs in full-length or partial form from the beluga whale (Delphinapterus leucas), toadfish (Opsanus tau), chicken (Gallus gallus), hagfish (Myxine glutinosa), horseshoe crab (Limulus polyphemus), and cone snail (Conus textile) to compare these structures to the known bovine, human, rat, and mouse cDNA sequences. Comparison of the predicted amino acid sequences identified a nearly perfectly conserved 38-amino acid residue region in all of these putative carboxylases. In addition, this amino acid motif is also present in the Drosophila genome and identified a Drosophila homolog of the gamma-carboxylase. Assay of hagfish liver demonstrated vitamin K-dependent carboxylase activity in this hemichordate. These results demonstrate the broad distribution of the vitamin K-dependent carboxylase gene, including a highly conserved motif that is likely critical for enzyme function. The vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid appears to be a highly conserved function in the animal kingdom. (+info)

A topological study of the human gamma-glutamyl carboxylase. (8/225)

gamma-Glutamyl carboxylase (GC), a polytopic membrane protein found in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of glutamate to gamma-carboxyl glutamate. In an attempt to delineate the structure of this important enzyme, in vitro translation and in vivo mapping were used to study its membrane topology. Using terminus-tagged full-length carboxylase, expressed in 293 cells, it was demonstrated that the amino-terminus of the GC is on the cytoplasmic side of the ER, while the carboxyl-terminus is on the lumenal side. In addition, a series of fusions were made to encode each predicted transmembrane domain (TMD) followed by a leader peptidase (Lep) reporter tag, as analyzed by the computer algorithm TOPPRED II. Following in vitro translation of each fusion in the presence of canine microsomes, the topological orientation of the Lep tag was determined by proteinase K digestion and endoglycosidase H (Endo H) cleavage. From the topological orientation of the Lep tag in each fusion, the GC spans the ER membrane at least 5 times, with its N-terminus in the cytoplasm and its C-terminus in the lumen. (+info)

List of Penicillium species MycoBank Straininfo of Penicillium emmonsii Q. Ashton Acton, PhD (2012). Carbon-Carbon Ligases: ...

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

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 ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). This enzyme participates in purine metabolism. Reem GH ( ...

https://en.wikipedia.org/wiki/Ribose-5-phosphate—ammonia_ligase

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 + ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is formate:dihydrofolate ligase (ADP-forming). Drake JC, Baram J, Allegra CJ (1990). "Isolation and ...

https://en.wikipedia.org/wiki/Formate—dihydrofolate_ligase

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a biotin-[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming). This enzyme participates ...

https://en.wikipedia.org/wiki/Biotin—(methylmalonyl-CoA-carboxytransferase)_ligase

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... In enzymology, an imidazoleacetate-phosphoribosyldiphosphate ligase (EC 6.3.4.8) is an enzyme that catalyzes a chemical ... this enzyme class is imidazoleacetate:5-phosphoribosyl-diphosphate ligase (ADP- and diphosphate-forming). This enzyme is also ...

https://en.wikipedia.org/wiki/Imidazoleacetate—phosphoribosyldiphosphate_ligase

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a glutamate-methylamine ligase (EC 6.3.4.12) is an enzyme that catalyzes the chemical reaction ATP + L-glutamate ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is L-glutamate:methylamine ligase (ADP-forming). This enzyme is also called gamma-glutamylmethylamide ...

https://en.wikipedia.org/wiki/Glutamate—methylamine_ligase

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. In bacteria, GARS is a ... In addition to similar structure across species, GARS as a whole has a very similar structure to D-alanine:D-alanine ligase, ... Phosphoribosylamine-glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), (EC 6.3.4.13) is an enzyme that ... The systematic name of this enzyme class is 5-phospho-D-ribosylamine:glycine ligase (ADP-forming). Other names in common use ...

https://en.wikipedia.org/wiki/Phosphoribosylamine—glycine_ligase

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme ... The systematic name of this enzyme class is formate:tetrahydrofolate ligase (ADP-forming). Other names in common use include: ... In enzymology, a formate-tetrahydrofolate ligase (EC 6.3.4.3) is an enzyme that catalyzes the chemical reaction ATP + formate ... Human genes encoding formate-tetrahydrofolate ligases include: MTHFD1 - cytoplasmic MTHFD1L - mitochondrial As of late 2007, 3 ...

https://en.wikipedia.org/wiki/Formate–tetrahydrofolate_ligase

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- ...

https://en.wikipedia.org/wiki/5-formyltetrahydrofolate_cyclo-ligase

The systematic name is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase. Krakower GR, Kim KH (March ...

https://en.wikipedia.org/wiki/(acetyl-CoA_carboxylase)-phosphatase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). This ... In enzymology, a phenylacetate-CoA ligase is an enzyme (EC 6.2.1.30) that catalyzes the chemical reaction ATP + phenylacetate ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...

https://en.wikipedia.org/wiki/Phenylacetate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... This enzyme is also called phytanoyl-CoA ligase. Muralidharan FN, Muralidharan VB (1986). "Phytanoyl-CoA ligase activity in rat ... In enzymology, a phytanate-CoA ligase (EC 6.2.1.24) is an enzyme that catalyzes the chemical reaction ATP + phytanate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

https://en.wikipedia.org/wiki/Phytanate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acid-CoA ligase (GDP-forming) (EC 6.2.1.10) is an enzyme that catalyzes the chemical reaction GTP + an acid ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase ( ...

https://en.wikipedia.org/wiki/Acid—CoA_ligase_(GDP-forming)

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme ... Butyrate-CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme (EC 6.2.1.2) that ... 3-hydroxybutyryl CoA ligase, xenobiotic/medium-chain fatty acid ligase, and short-chain acyl-CoA synthetase. ACSM1 ACSM2A ... This reaction is catalyzed by the HXM-A and HXM-B medium-chain acid:CoA ligases and requires energy in the form of ATP. ... The ...

https://en.wikipedia.org/wiki/Butyrate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 6-carboxyhexanoate-CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction ATP + 6- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6- ...

https://en.wikipedia.org/wiki/6-carboxyhexanoate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (ADP-forming). Other names in common use include succinyl-CoA ...

https://en.wikipedia.org/wiki/Succinate—CoA_ligase_(ADP-forming)

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 2-aminobenzoate-CoA ligase, 2-aminobenzoate-coenzyme A ligase, and 2-aminobenzoate coenzyme A ligase. This enzyme participates ... In enzymology, an anthranilate-CoA ligase (EC 6.2.1.32) is an enzyme that catalyzes the chemical reaction ATP + anthranilate + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, Anthranilates, All stub articles, Ligase stubs). ...

https://en.wikipedia.org/wiki/Anthranilate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a citrate-CoA ligase (EC 6.2.1.18) is an enzyme that catalyzes the chemical reaction ATP + citrate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle. Lill U, Schreil A, Eggerer H (1982). " ...

https://en.wikipedia.org/wiki/Citrate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid ... In enzymology, a 3α,7α-dihydroxy-5β-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical reaction ATP ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997-1004. PMID ...

https://en.wikipedia.org/wiki/3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ...

https://en.wikipedia.org/wiki/Acetate—CoA_ligase_(ADP-forming)

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a propionate-CoA ligase (EC 6.2.1.17) is an enzyme that catalyzes the chemical reaction ATP + propanoate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA ...

https://en.wikipedia.org/wiki/Propionate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 4-chlorobenzoate-CoA ligase (EC 6.2.1.33) is an enzyme that catalyzes the chemical reaction 4-chlorobenzoate ... Loffler F, Muller R, Lingens F (1992). "Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. ... systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate ...

https://en.wikipedia.org/wiki/4-chlorobenzoate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 4-hydroxybenzoate-coenzyme A ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A synthetase, and 4-hydroxybenzoyl-CoA ligase. ... In enzymology, a 4-hydroxybenzoate-CoA ligase (EC 6.2.1.27) is an enzyme that catalyzes the chemical reaction ATP + 4- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

https://en.wikipedia.org/wiki/4-hydroxybenzoate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) is an enzyme that catalyzes the chemical reaction GTP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (GDP-forming). Other names in common use include succinyl-CoA ...

https://en.wikipedia.org/wiki/Succinate—CoA_ligase_(GDP-forming)

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a glutarate-CoA ligase (EC 6.2.1.6) is an enzyme that catalyzes the chemical reaction ATP + glutarate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA ...

https://en.wikipedia.org/wiki/Glutarate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is malate:CoA ligase (ADP-forming). Other names in common use include malyl-CoA synthetase ...

https://en.wikipedia.org/wiki/Malate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a dicarboxylate-CoA ligase (EC 6.2.1.23) is an enzyme that catalyzes the chemical reaction ATP + an alphaomega- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include ...

https://en.wikipedia.org/wiki/Dicarboxylate—CoA_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-luciferin-component ligase (EC 6.2.1.19) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl- ...

https://en.wikipedia.org/wiki/Long-chain-fatty-acid—luciferin-component_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-[acyl-carrier-protein] ligase (EC 6.2.1.20) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in ...

https://en.wikipedia.org/wiki/Long-chain-fatty-acid—(acyl-carrier-protein)_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... HS-citrate lyase ligase, and acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming). This enzyme participates in two- ... In enzymology, a [citrate (pro-3S)-lyase] ligase (EC 6.2.1.22) is an enzyme that catalyzes the chemical reaction ATP + acetate ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

https://en.wikipedia.org/wiki/(citrate_(pro-3S)-lyase)_ligase

"Carbon-Oxygen Ligases" by people in UAMS Profiles by year, and whether "Carbon-Oxygen Ligases" was a major or minor topic of ... "Carbon-Oxygen Ligases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Carbon-Oxygen Ligases" by people in Profiles over the past ten years. ... Below are MeSH descriptors whose meaning is more general than "Carbon-Oxygen Ligases". ...

https://uams-triprofiles.uams.edu/profiles/display/114077

Carbon carbon ligase. Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are ...

https://www.chemwatch.net/resource-center/carbon-carbon-ligase-2/

propanoyl-CoA:carbon dioxide ligase beta subunit. *propionyl CoA carboxylase, beta polypeptide ...

https://medlineplus.gov/genetics/gene/pccb/

6.4 Forming carbon-carbon bonds. 6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date). 6.4.1.2 ... 6. Ligases. 6.3 Forming carbon-nitrogen bonds. 6.3.4 Other carbon-nitrogen ligases. 6.3.4.14 biotin carboxylase. CLAFUR5_06324 ... 2.1 Transferring one-carbon groups. 2.1.3 Carboxy- and carbamoyltransferases. 2.1.3.15 acetyl-CoA carboxytransferase. CLAFUR5_ ...

https://www.kegg.jp/entry/ffu:CLAFUR5_06324

6. Ligases. 6.3 Forming carbon-nitrogen bonds. 6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases). 6.3.1.15 8- ... Ligases;. Forming carbon-nitrogen bonds;. Acid-D-ammonia (or amine) ligases (amide synthases). BRITE hierarchy. ... novobiocin ligase;. novobiocic acid synthetase (misleading);. 8-desmethyl-novobiocic acid synthetase;. 8-demethylnovobiocic ... 3-dimethylallyl-4-hydroxybenzoate:3-amino-4,7-dihydroxycoumarin ligase (AMP-forming). ...

https://www.genome.jp/entry/K12709+6.3.1.15+R10453

Expression of Formate-Tetrahydrofolate Ligase Did Not Improve Growth but Interferes With Nitrogen and Carbon Metabolism of ... Awakening a latent carbon fixation cycle in Escherichia coli. Nature Communications 11 (1), 5812 (2020) ...

https://www.mpimp-golm.mpg.de/publication-search/2138865?person=%2Fpersons%2Fresource%2Fpersons196387

nucleotide binding (GO:0000166), ligase activity, forming carbon-nitrogen bonds (GO:0016879), ATP binding (GO:0005524). ... The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate ... nucleophilically attacksthe C2 carbon from the rear. Escherichia coli TilS (called MesJ) has anadditional CTD, which may ... adenylationof C34 and lysine attack on the C2 carbon. Conserved amino acid residuesare clustered around the NTD central hole. ...

http://smart.embl.de/smart/do_annotation.pl?DOMAIN=TilS_C&BLAST=DUMMY

Carbon-dioxide ligase (ADP-forming). Hardie, D. G., Guy, P. S. & Cohen, P., 1 Jan 1981, In: Methods in Enzymology. 71, C, p. 26 ... Metabolism of carbon tetrachloride in hepatic microsomes and reconstituted monooxygenase systems and its relationship to lipid ...

https://discovery.dundee.ac.uk/en/publications/?showAdvanced=false&allConcepts=true&inferConcepts=true&publicationYear=2012&publicationYear=2014&publicationYear=2015&publicationYear=2017&publicationYear=2019&format=&nofollow=true&ordering=publicationYearThenTitle&descending=false&page=2

accC (gene name); biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). ... biotin carboxyl-carrier protein]-biotin-N6-L-lysine:hydrogencarbonate ligase (ADP-forming). ... ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. ...

https://www.enzyme-database.org/query.php?ec=6.3.4.14

ligase activity, forming carbon-oxygen bonds. IEP. Neighborhood. MF. GO:0017076. purine nucleotide binding. IEP. Neighborhood. ...

https://evorepro.sbs.ntu.edu.sg/sequence/view/365548

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases and ... The 2.0 A crystal structure of D-alanine--D-alanine ligase from Bacillus anthracis complexed with ATP revealed a dimer with ... Crystal Structure of D-alanine--D-Alanine Ligase from Bacillus anthracis complexed with ATP. (tree view) ...

https://csgid.org/deposits/view/3R5X

ligase activity. ligase activity, forming carbon-nitrogen bonds. carbon-nitrogen ligase activity, with glutamine as amido-N- ...

http://www.ymdb.ca/proteins/P38625

Carbon-Oxygen Ligases - Preferred Concept UI. M0029291. Scope note. Enzymes that catalyze the joining of two molecules by the ... Carbono-Oxigênio Ligases Descriptor French: Carbon-oxygen ligases Entry term(s):. Carbon Oxygen Ligases. Ligases, Carbon-Oxygen ... do not confuse with CARBON-OXYGEN LYASES. Allowable Qualifiers:. AD administration & dosage. AE adverse effects. AI antagonists ... Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.. ...

https://decs.bvsalud.org/en/ths/resource/?id=33444

carbon-nitrogen ligase activity, with glutamine as amido-N-donor. IEP. Enrichment. ...

https://bacteria.sbs.ntu.edu.sg/sequence/view/58407

1 Carbon-Oxygen Ligases. *1 Catheterization --adverse effects. *1 Child, Preschool. *1 Clindamycin --pharmacology ...

https://imsear.searo.who.int/handle/123456789/1/simple-search?query=&sort_by=score&order=desc&rpp=10&filter_field_1=subject&filter_type_1=equals&filter_value_1=Humans&filter_field_2=dateIssued&filter_type_2=equals&filter_value_2=%5B2000+TO+2009%5D&filter_field_3=dateIssued&filter_type_3=equals&filter_value_3=2006&filter_field_4=subject&filter_type_4=equals&filter_value_4=India&etal=0&filtername=author&filterquery=Mohanty%2C+Srujana&filtertype=equals

EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor Show first 5 Terms ... Any EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor that interferes with the action of NAD(+) ... EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor ... deamido-NAD(+):L-glutamine amido-ligase (AMP-forming) inhibitor. *deamido-NAD(+):L-glutamine amido-ligase (AMP-forming) ...

http://zfin.org/action/ontology/term-detail/CHEBI:138953

Carbon-Carbon Ligases. 1. + 46. Acyl-CoA Dehydrogenases. 1. + 47. Adenosine Deaminase. 1. + ...

https://lookfordiagnosis.com/results.php?symptoms=protein+deficiency&lang=1&parent=%2F&mode=F&therapy_ap=1

6.3 Forming carbon-nitrogen bonds. 6.3.4 Other carbon-nitrogen ligases. 6.3.4.9 biotin-[methylmalonyl-CoA-carboxytransferase] ... ligase (AMP-forming), Biotin-[methylmalonyl-CoA-carboxyltransferase] ligase ... 6.3.4.9: biotin-[methylmalonyl-CoA-carboxytransferase] ligase. This is an abbreviated version!. For detailed information about ... methylmalonyl-CoA-pyruvate apocarboxyltransferase ligase (AMP), Biotin-apotranscarboxylase synthetase, biotin:apo[methylmalonyl ...

https://brenda-enzymes.org/all_enzymes.php?ecno=6.3.4.9&table=Storage_Stability

D08.811.464 Ligases .. D08.811.464.259 Carbon-Nitrogen Ligases .. D08.811.464.259.200 Amide Synthases .. HP4 Materia Medica .. ... Acid-Amide Ligases .. Acid-Ammonia Ligases .. Acid Amide Ligases .. Acid Ammonia Ligases .. Ligases, Acid-Amide .. Ligases, ...

http://trigramas.bireme.br/cgi-bin/mx/[email protected]?collection=DeCSi&lang=p&minsim=0.30&maxrel=10&text=Aqua%20Ammoniae

Ligases are used in catalysis where two substrates are litigated and the formation of carbon-carbon, carbon-sulfide, carbon- ... Ligases Catalyze bond formation coupled with ATP hydrolysis. Citric acid synthetase Lyases Catalyze a group elimination in ... The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. Then the carbonic acid becomes a ... 2. Carbonic Anhydrase (metalloenzymes) These enzymes catalyzes the rapid interconversion of carbon dioxide and water to ...

https://en.wikibooks.org/wiki/Structural_Biochemistry/Enzyme

ligase activity, forming carbon-oxygen bonds. IEP. Enrichment. MF. GO:0017111. nucleoside-triphosphatase activity. IEP. ...

https://protists.sbs.ntu.edu.sg/sequence/view/62713

ligase activity, forming carbon-sulfur bonds. IEP. Enrichment. MF. GO:0016878. acid-thiol ligase activity. IEP. Enrichment. ...

https://bacteria.sbs.ntu.edu.sg/sequence/view/20404

ligase activity, forming carbon-oxygen bonds. IEP. Neighborhood. MF. GO:0016891. endoribonuclease activity, producing 5- ...

https://evorepro.sbs.ntu.edu.sg/sequence/view/282732

carbon nitrogen ligase; 3. glucan [group of polysaccharides composed of repeating glucose units; they can consist of branched ... It causes the carbon dioxide produced during dough fermentation to be retained by the dough in a manner which provides the ... 49. glutamate ammonia ligase [An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and ... biosynthesis of glucose from 3-carbon precursors, including aminoacids (this is the basis of protein breakdown during ...

http://www.medindex.am/glossary/index.php/list/UMLS.+CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM/,G,L,U.xhtml

... carbon monoxide; food intake; gastric acid; glutamate-cysteine ligase; heme oxygenase (biliverdin-producing); iron; quinones; ... glutamate-cysteine ligase, and NAD(P)H quinone dehydrogenase 1, among which HO-1 is an enzyme catalyzing the degradation of ... heme.producing biliverdin, ferrous iron, and carbon monoxide. In the s .... DOI:. 10.1016/j.abb.2020.108466. https://doi.org/ ...

https://pubag.nal.usda.gov/?f%5Bsubject_facet%5D%5B%5D=basic-leucine+zipper+transcription+factors&f%5Bsubject_term%5D%5B%5D=basic-leucine+zipper+transcription+factors&per_page=50&sort=title

fig,[email protected]~Central [email protected]^Central metabolism - no [email protected]^EC 6.4.1.- Ligases that form carbon-carbon ... fig,[email protected]~Central [email protected]^Central metabolism - no [email protected]^EC 6.4.1.- Ligases that form carbon-carbon ... Ligases that form carbon-carbon [email protected]^Acetyl-coenzyme A carboxyl transferase beta chain (EC 6.4.1.2)@^fig,[email protected]~ ... Ligases that form carbon-carbon [email protected]^Acetyl-coenzyme A carboxyl transferase alpha chain (EC 6.4.1.2)@^fig,[email protected]~ ...

https://pubseed.theseed.org/FIG/seedviewer.cgi?page=Organism&organism=216591.1

RM01859Name: Propanoyl-CoA:carbon-dioxide ligase (ADP-forming). Type: Regular. Location: Mitochondria. KEGG ID: R01859. click ...

http://wormflux.umassmed.edu/Rxns/RM01859.html

carbon-nitrogen ligase activity GO:0016884 * protein O-GlcNAc transferase activity GO:0097363 ...

https://bio2vec.cbrc.kaust.edu.sa/bio2vec/details/1?iri=GO:0000030

Curated sequence Q3J4E3: Propionyl-CoA carboxylase beta chain; PCCase; Propanoyl-CoA:carbon dioxide ligase; EC 6.4.1.3. ... Curated sequence P53003: Propionyl-CoA carboxylase beta chain; PCCase; Propanoyl-CoA:carbon dioxide ligase; EC 6.4.1.3 ... carbon dioxide ligase subunit beta; EC 6.4.1.3. propionyl-CoA carboxylase β chain, mitochondrial (EC 6.4.1.3) ... carbon dioxide ligase subunit beta; EC 6.4.1.3. propionyl-CoA carboxylase (EC 6.4.1.3) ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__PV4&path=valine&step=pccB

DVU2557 Bifunctional ligase/repressor BirA Details for DVU2557 - Bifunctional ligase/repressor BirA GO Terms: GO:0004077, GO: ...

http://networks.systemsbiology.net/syntrophy/modules/bicluster_0148

carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor that interferes with the action of NAD(+) synthase (glutamine-hydrolysing) (EC 6.3.5.1). (zfin.org)

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases and participates in d-alanine metabolism and peptidoglycan biosynthesis. (csgid.org)
Ligases, Forming carbon-nitrogen bonds, Acid--D-amino-acid ligases (peptide synthases). (uma.es)

For example, the protein molecules that control the functions of all living organisms are held together by amide bonds, which form a link between the carbon and nitrogen atoms of amino acid building blocks. (indiaeducationdiary.in)
The ligase enzymes provide a cleaner more efficient and rapid way to construct amide bonds. (indiaeducationdiary.in)
Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups. (bvsalud.org)

Our work identified a novel mammalian prenyltransferase which we named GGtase3 that modifies FBXL2, an E3 ligase subunit, with geranylgeranylation (a 20-carbon lipid PTM) for localization to membrane compartments. (kuchaylab.org)

Often substrate degradation via ubiquitin ligases is regulated for precision and fine control. (kuchaylab.org)
We are currently involved in functional characterization of GGtase3 and extending our studies for functional characterization of PTMs involving membrane bound E3 ubiquitin ligases. (kuchaylab.org)
We seek to elucidate the spatiotemporal mechanistic understating for the specificity of the ubiquitylation reaction by E3 ubiquitin ligases. (kuchaylab.org)
In cells, PROTAC molecules can recognize and selectively bind target proteins, recruit specific E3 ubiquitin ligases, and form a "target protein-PROTAC-E3 ubiquitin ligase" ternary complex. (cd-bioparticles.net)

Expression of Formate-Tetrahydrofolate Ligase Did Not Improve Growth but Interferes With Nitrogen and Carbon Metabolism of Synechocystissp. (mpg.de)
All these processes are tightly regulated by proteins and microRNA in response to both external and internal nitrogen levels, carbon status of the plant and hormones. (scirp.org)
Among macro nutrients, nitrogen is next to carbon in importance to plants. (scirp.org)
Flux Balance Analysis (FBA) of the model resulted in balanced carbon, nitrogen, proton, energy and redox states under both light and dark conditions. (biomedcentral.com)
The subsequent accumulation of TAG under nitrogen deprivation was a consequence of the reallocation of carbon, nitrogen sources, and lipids, rather than an up-regulation of TAG biosynthesis genes. (biomedcentral.com)
on the other hand, nitrogen deprivation induced the up-regulation of cell autophagy and ubiquitin-mediated protein proteolysis which resulted in a recycling of preformed protein nitrogen and carbon. (biomedcentral.com)
One of the most important protection mechanisms is the reallocation of limited carbon, nitrogen, and energy resources to optimize growth and metabolism [ 7 ]. (biomedcentral.com)

This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15 , biotin-[biotin carboxyl-carrier protein] ligase. (enzyme-database.org)
For detailed information about biotin-[methylmalonyl-CoA-carboxytransferase] ligase, go to the full flat file . (brenda-enzymes.org)

Starch is a repository of carbon which is later used during the dark phase as the primary carbon source for biomass formation [ 2 ] and fuelling of sucrose biosynthesis and its transport. (biomedcentral.com)
For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code . (lbl.gov)

A pyridoxal-phosphate protein that catalyzes the alpha-decarboxylation of L-glutamic acid to form gamma-aminobutyric acid and carbon dioxide. (medindex.am)
Ubiquitin--protein ligase. (uma.es)
In a recent article in the Journal of Biological Chemistry , Hanjie Jiang and collaborators at Brigham and Women's Hospital describe using protein microarray technology as a platform to identify WWP2 substrates using an activated version of this ligase. (asbmb.org)
Several physio-molecular processes are initiated during this phase, including protein synthesis and the resumption of respiratory activities , observed by a significant increase in oxygen consumption and carbon dioxide release. (globalplantcouncil.org)
PROTAC is a bifunctional molecule composed of three parts: one end is the target protein binding ligand, the other end is the E3 ubiquitin ligase ligand, and the middle is the linker chain. (cd-bioparticles.net)
Afterwards, E3 ubiquitin ligase and E2 ubiquitin conjugating enzyme work together to ubiquitinate the target protein. (cd-bioparticles.net)
After PROTAC completes the ubiquitination labeling of a target protein, it can be separated from the target protein and E3 ubiquitin ligase and continue to label the next protein. (cd-bioparticles.net)
Degradation of CIC protein following lack of ATXN1L was as an alternative noticed to be mediated by the E3 ubiquitin ligase TRIM25 which was additional validated utilizing glioma-derived cell traces and the TCGA breast carcinoma and liver hepatocellular carcinoma cohorts. (ataxin.com)

The tricarboxylic acid, or TCA, cycle is essential to carbon metabolism. (asbmb.org)
Furthermore, the structured metabolic model should take into account major pathways of primary metabolism such as sugar metabolism, central carbon metabolisms, photosynthesis, photorespiration, energy and redox metabolism, proton turnover, sucrose translocation from source to sink tissues and biomass growth. (biomedcentral.com)
In future, we will use the model to recognize cause-effect relationships and describe regulatory processes in carbon metabolism and transport. (biomedcentral.com)

Identifying new substrates for a ubiquitin ligase. (asbmb.org)
Although, PTMs on substrates are well studied, PTMs on E3 ligases and how they regulate the UPS have not been established. (kuchaylab.org)
The new findings have demonstrated that the ligase enzymes can accept many substrates, but in some cases proved too unstable for practical use. (indiaeducationdiary.in)

One Cohesive-End Ligation Unit (CEU) is defined as the amount of enzyme required to give 50 % ligation of Hin d III fragments of λ DNA (5' DNA termini concentration of 0.12 μM, 300 μg/ml) in a total reaction volume of 20 μl in 30 minutes at 16 °C in 1x T4 DNA Ligase Reaction Buffer. (jenabioscience.com)
However, when they used X-ray crystallography to determine the structure of one of the ligase enzymes, they realised that the enzyme active site was relatively open and could accommodate a much wider range of substrate building blocks for production of pharmaceuticals. (indiaeducationdiary.in)

In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain. (embl.de)

Awakening a latent carbon fixation cycle in Escherichia coli. (mpg.de)
The origin of carbon fixation is a fundamental question in astrobiology. (researchgate.net)
While the Calvin cycle is the most active on the modern Earth, the reductive TCA cycle (rTCA) pathway for carbon fixation has been proposed to have played an important role in early evolution. (researchgate.net)
Fundamental to astrobiology is origin of autotrophy with reductive TCA cycle (rTCA) being often proposed as a primordial carbon fixation pathway. (researchgate.net)
Design and analysis of synthetic carbon fixation pathways. (southcoastbiosciencesdtp.ac.uk)

They found a family of ligase enzymes that bacteria use to make amide containing toxins that kill plants. (indiaeducationdiary.in)
For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. (lbl.gov)

The HECT E3 ligase WWP2 targets lysine residues for ubiquitination in a broad range of proteins involved in different physiological processes. (asbmb.org)

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5' phosphate and 3'-hydroxyl termini in duplex DNA or RNA. (jenabioscience.com)

The production of fuels and commodities as well as fine chemicals by bacterial C 1 -assimilation (CO 2 -valorization) will compete with lignin valorization and plastics upcycling in a future circular carbon economy. (southcoastbiosciencesdtp.ac.uk)

Residual gas diffuses away, whereas free carbon atoms dissolve into the nanoparticles and then segregate to the catalyst surface to form nanotubes [44]. (a-inhibitor.com)

The authors deleted mqo from Mycobacterium smegmatis, an environmental saprophyte - that is, it feeds on decaying matter - that lacks Mdh in its genome and found that Mqo is essential for growth on nonfermentable carbon sources. (asbmb.org)
Complementation experiments with a heterologous Mdh from Mycobacterium tuberculosis shortened the delayed growth on fermentable carbon sources and restored growth on nonfermentable carbon sources at a reduced growth rate. (asbmb.org)

In growing plants, sucrose is the most widespread sugar used to supply both carbon and energy from 'source' tissues (e.g. autotrophic mesophyll) to 'sink' tissues (e.g. heterotrophic roots, growing shoots or reproductive organs) to build up a biomass [ 1 ]. (biomedcentral.com)
Woody biomass can also be utilized as a sustainable and carbon-neutral resource for bioenergy [1]. (researchsquare.com)

Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. (uams.edu)

DNA ligase, activated following imbibition, is involved to bind together broken pieces of DNA. (globalplantcouncil.org)

One potential novel T. brucei drug target is RNA editing ligase 1 ( Tb REL1), a critical component of a unique mitochondrial RNA-editing complex called the editosome [ 5 ]. (biomedcentral.com)

New research published today, in Nature , describes a new family of enzymes (ligases) which can assemble the key chemical building blocks required for pharmaceutical production. (indiaeducationdiary.in)

The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. (wikibooks.org)

For example, we are investigating FBXL2, an E3 ligase complex that regulates critical signaling networks operating from membrane compartments. (kuchaylab.org)

This paper describes the recent progress at Nottingham towards the exploitation of the unique properties of scCO 2 (supercritical carbon dioxide) for the preparation of polymeric scaffolds for tissue engineering applications and new devices for controlled drug delivery, as well as the synthesis of novel block copolymers by the combination of eROP (enzymatic ring opening polymerization) and controlled polymerization methods for the potential use as drug carriers. (portlandpress.com)

The authors also determined that mqo mutants grew more slowly on fermentable carbon sources. (asbmb.org)

The 2.0 A crystal structure of D-alanine--D-alanine ligase from Bacillus anthracis complexed with ATP revealed a dimer with each monomer consisting of three alpha-beta domains. (csgid.org)

Anatomy7

Organisms13

Diseases6

Chemicals and Drugs114

Analytical, Diagnostic and Therapeutic Techniques and Equipment28

Phenomena and Processes79

Disciplines and Occupations4

Technology, Industry, Agriculture7

Information Science4

Health Care16

Geographicals1

The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase. (1/225)

Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. (2/225)

Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (3/225)

Molecular characterization of the non-biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase. (4/225)

Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase. (5/225)

An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230. (6/225)

A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla. (7/225)

A topological study of the human gamma-glutamyl carboxylase. (8/225)

Carbon

Ubiquitin-Protein Ligases

Carbon Dioxide

Carbon Monoxide

Nanotubes, Carbon

DNA Ligases

SKP Cullin F-Box Protein Ligases

Carbon Monoxide Poisoning

Carbon Isotopes

Cullin Proteins

Ubiquitination

Carbon Tetrachloride

Carbon Sequestration

Polynucleotide Ligases

Ubiquitin

Carbon Disulfide

Coenzyme A Ligases

RING Finger Domains

Ubiquitin-Conjugating Enzymes

Carbon Tetrachloride Poisoning

RNA Ligase (ATP)

Molecular Sequence Data

Carbon Footprint

F-Box Proteins

Endosomal Sorting Complexes Required for Transport

Carbon Radioisotopes

Amino Acid Sequence

Ubiquitins

Nitrogen

Proteasome Endopeptidase Complex

Biomass

Substrate Specificity

Peptide Synthases

Soot

Carboxyhemoglobin

Atmosphere

Ubiquitin-Protein Ligase Complexes

Polyubiquitin

Protein Structure, Tertiary

Protein Binding

Mutation

Ubiquitin-Activating Enzymes

Carbon-Oxygen Ligases

Biodegradation, Environmental

Soil

Proto-Oncogene Proteins c-cbl

Culture Media

Proteolysis

Acetates

Graphite

Carbon Compounds, Inorganic

Photosynthesis

Saccharomyces cerevisiae

Carbohydrate Metabolism

S-Phase Kinase-Associated Proteins

Protein Inhibitors of Activated STAT

Models, Biological

Glucose

Kinetics

Oxygen

Catalysis

SUMO-1 Protein

Sequence Homology, Amino Acid

Small Ubiquitin-Related Modifier Proteins

Phylogeny

Trees

Electrodes

Bacterial Proteins

Saccharomyces cerevisiae Proteins

Temperature

Oxidation-Reduction

Escherichia coli

Methane

Autotrophic Processes

Hydrogen-Ion Concentration

Ecosystem

Models, Molecular

Magnetic Resonance Spectroscopy

Sumoylation

Carrier Proteins