Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.Carbon: A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.Ubiquitin-Protein Ligases: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.Sulfur Compounds: Inorganic or organic compounds that contain sulfur as an integral part of the molecule.DNA Ligases: Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).SKP Cullin F-Box Protein Ligases: A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.Sulfur Dioxide: A highly toxic, colorless, nonflammable gas. It is used as a pharmaceutical aid and antioxidant. It is also an environmental air pollutant.Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.Sulfur Isotopes: Stable sulfur atoms that have the same atomic number as the element sulfur, but differ in atomic weight. S-33, 34, and 36 are stable sulfur isotopes.Amino Acids, SulfurCarbon Monoxide: Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)Nanotubes, Carbon: Nanometer-sized tubes composed mainly of CARBON. Such nanotubes are used as probes for high-resolution structural and chemical imaging of biomolecules with ATOMIC FORCE MICROSCOPY.Cullin Proteins: A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.Ubiquitination: The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.Polynucleotide Ligases: Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.Mustard Gas: Severe irritant and vesicant of skin, eyes, and lungs. It may cause blindness and lethal lung edema and was formerly used as a war gas. The substance has been proposed as a cytostatic and for treatment of psoriasis. It has been listed as a known carcinogen in the Fourth Annual Report on Carcinogens (NTP-85-002, 1985) (Merck, 11th ed).Sulfides: Chemical groups containing the covalent sulfur bonds -S-. The sulfur atom can be bound to inorganic or organic moieties.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Thiosulfates: Inorganic salts of thiosulfuric acid possessing the general formula R2S2O3.RING Finger Domains: A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.Carbon Monoxide Poisoning: Toxic asphyxiation due to the displacement of oxygen from oxyhemoglobin by carbon monoxide.Sulfur Oxides: Inorganic oxides of sulfur.Ubiquitin-Conjugating Enzymes: A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.RNA Ligase (ATP): An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.Chlorobi: A phylum of anoxygenic, phototrophic bacteria including the family Chlorobiaceae. They occur in aquatic sediments, sulfur springs, and hot springs and utilize reduced sulfur compounds instead of oxygen.Sulfates: Inorganic salts of sulfuric acid.Carbon Tetrachloride: A solvent for oils, fats, lacquers, varnishes, rubber waxes, and resins, and a starting material in the manufacturing of organic compounds. Poisoning by inhalation, ingestion or skin absorption is possible and may be fatal. (Merck Index, 11th ed)F-Box Proteins: A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Carbon Disulfide: A colorless, flammable, poisonous liquid, CS2. It is used as a solvent, and is a counterirritant and has local anesthetic properties but is not used as such. It is highly toxic with pronounced CNS, hematologic, and dermatologic effects.Carbon Sequestration: Any of several processes for the permanent or long-term artificial or natural capture or removal and storage of carbon dioxide and other forms of carbon, through biological, chemical or physical processes, in a manner that prevents it from being released into the atmosphere.Oxidoreductases Acting on Sulfur Group Donors: Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.Endosomal Sorting Complexes Required for Transport: A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes.Ubiquitins: A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.Sulfur Hexafluoride: Sulfur hexafluoride. An inert gas used mainly as a test gas in respiratory physiology. Other uses include its injection in vitreoretinal surgery to restore the vitreous chamber and as a tracer in monitoring the dispersion and deposition of air pollutants.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Chromatiaceae: A family of phototrophic purple sulfur bacteria that deposit globules of elemental sulfur inside their cells. They are found in diverse aquatic environments.Proteasome Endopeptidase Complex: A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.Chemical Warfare Agents: Chemicals that are used to cause the disturbance, disease, or death of humans during WARFARE.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Sulfurtransferases: Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Peptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Sulfur Acids: Inorganic or organic acids that contain sulfur as an integral part of the molecule.Ubiquitin-Protein Ligase Complexes: Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).Polyubiquitin: An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a second ubiquitin molecule. It is structurally distinct from UBIQUITIN C, which is a single protein containing a tandemly arrayed ubiquitin peptide sequence.Ubiquitin-Activating Enzymes: A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Carbon-Oxygen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.Carbon Tetrachloride PoisoningChlorobium: A genus of phototrophic, obligately anaerobic bacteria in the family Chlorobiaceae. They are found in hydrogen sulfide-containing mud and water environments.Hydrogen Sulfide: A flammable, poisonous gas with a characteristic odor of rotten eggs. It is used in the manufacture of chemicals, in metallurgy, and as an analytical reagent. (From Merck Index, 11th ed)Proto-Oncogene Proteins c-cbl: Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Atmosphere: The gaseous envelope surrounding a planet or similar body. (From Random House Unabridged Dictionary, 2d ed)Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Sulfites: Inorganic salts of sulfurous acid.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Chromatium: A genus of gram-negative, ovoid to rod-shaped bacteria that is phototrophic. All species use ammonia as a nitrogen source. Some strains are found only in sulfide-containing freshwater habitats exposed to light while others may occur in marine, estuarine, and freshwater environments.Bacterial Proteins: Proteins found in any species of bacterium.Proteolysis: Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.S-Phase Kinase-Associated Proteins: A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.Protein Inhibitors of Activated STAT: A family of structurally related proteins that are constitutively expressed and that negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. PIAS proteins inhibit the activity of signal transducers and activators of transcription.Seawater: The salinated water of OCEANS AND SEAS that provides habitat for marine organisms.Acidithiobacillus: A genus of gram-negative rod-shaped bacteria in the class GAMMAPROTEOBACTERIA. They are obligately acidophilic and aerobic, using reduced SULFUR COMPOUNDS to support AUTOTROPHIC GROWTH.Air Pollutants: 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.Sulfonium Compounds: Sulfur compounds in which the sulfur atom is attached to three organic radicals and an electronegative element or radical.SUMO-1 Protein: A 1.5-kDa small ubiquitin-related modifier protein that can covalently bind via an isopeptide link to a number of cellular proteins. It may play a role in intracellular protein transport and a number of other cellular processes.Bacteria: One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Kinetics: The rate dynamics in chemical or physical systems.Small Ubiquitin-Related Modifier Proteins: A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.Sulfur-Reducing Bacteria: A group of gram-negative, anaerobic bacteria that is able to oxidize acetate completely to carbon dioxide using elemental sulfur as the electron acceptor.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Geologic Sediments: 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)Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Carbon Footprint: A measure of the total greenhouse gas emissions produced by an individual, organization, event, or product. It is measured in units of equivalent kilograms of CARBON DIOXIDE generated in a given time frame.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Biodegradation, Environmental: Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.Cysteine Synthase: An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.Anaerobiosis: The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Iron-Sulfur Proteins: A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Autotrophic Processes: 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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Biomass: Total mass of all the organisms of a given type and/or in a given area. (From Concise Dictionary of Biology, 1990) It includes the yield of vegetative mass produced from any given crop.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.RNA, Ribosomal, 16S: Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.Carbon Compounds, Inorganic: Inorganic compounds that contain carbon as an integral part of the molecule but are not derived from hydrocarbons.Sumoylation: A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Thiobacillus: A genus of gram-negative, rod-shaped bacteria that derives energy from the oxidation of one or more reduced sulfur compounds. Many former species have been reclassified to other classes of PROTEOBACTERIA.Sulfhydryl Compounds: Compounds containing the -SH radical.Hydrogensulfite Reductase: An enzyme found primarily in SULFUR-REDUCING BACTERIA where it plays an important role in the anaerobic carbon oxidation pathway.Epsilonproteobacteria: A group of proteobacteria consisting of chemoorganotrophs usually associated with the DIGESTIVE SYSTEM of humans and animals.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Photosynthesis: The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)Phototrophic Processes: Processes by which phototrophic organisms use sunlight as their primary energy source. Contrasts with chemotrophic processes which do not depend on light and function in deriving energy from exogenous chemical sources. Photoautotrophy (or photolithotrophy) is the ability to use sunlight as energy to fix inorganic nutrients to be used for other organic requirements. Photoautotrophs include all GREEN PLANTS; GREEN ALGAE; CYANOBACTERIA; and green and PURPLE SULFUR BACTERIA. Photoheterotrophs or photoorganotrophs require a supply of organic nutrients for their organic requirements but use sunlight as their primary energy source; examples include certain PURPLE NONSULFUR BACTERIA. 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.Gammaproteobacteria: A group of the proteobacteria comprised of facultatively anaerobic and fermentative gram-negative bacteria.Thiosulfate Sulfurtransferase: An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Air Pollution: The presence of contaminants or pollutant substances in the air (AIR POLLUTANTS) that interfere with human health or welfare, or produce other harmful environmental effects. The substances may include GASES; PARTICULATE MATTER; or volatile ORGANIC CHEMICALS.Sulfur Group Transferases: Enzymes that catalyze the transfer of sulfur atoms (2.8.1), sulfur groups (2.8.2) or coenzyme A (2.8.3). EC 2.8.Thiotrichaceae: A family of colorless sulfur bacteria in the order Thiotrichales, class GAMMAPROTEOBACTERIA.Arabidopsis Proteins: 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.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Hydrogen: 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.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Multiprotein Complexes: Macromolecular complexes formed from the association of defined protein subunits.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Cystathionine gamma-Lyase: A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.Water Microbiology: The presence of bacteria, viruses, and fungi in water. This term is not restricted to pathogenic organisms.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Muscular Atrophy: 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.Metabolic Networks and Pathways: Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Lysine: An essential amino acid. It is often added to animal feed.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Iron: A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.DNA, Ribosomal: DNA sequences encoding RIBOSOMAL RNA and the segments of DNA separating the individual ribosomal RNA genes, referred to as RIBOSOMAL SPACER DNA.Cell Cycle Proteins: 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.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Soot: 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.Sulfate Adenylyltransferase: An enzyme that catalyzes the activation of sulfate ions by ATP to form adenosine-5'-phosphosulfate and pyrophosphate. This reaction constitutes the first enzymatic step in sulfate utilization following the uptake of sulfate. EC 2.7.7.4.CarboxyhemoglobinGene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Methane: 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)Molybdenum: A metallic element with the atomic symbol Mo, atomic number 42, and atomic weight 95.94. It is an essential trace element, being a component of the enzymes xanthine oxidase, aldehyde oxidase, and nitrate reductase. (From Dorland, 27th ed)Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Soil: The unconsolidated mineral or organic matter on the surface of the earth that serves as a natural medium for the growth of land plants.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Volcanic Eruptions: The ash, dust, gases, and lava released by volcanic explosion. The gases are volatile matter composed principally of about 90% water vapor, and carbon dioxide, sulfur dioxide, hydrogen, carbon monoxide, and nitrogen. The ash or dust is pyroclastic ejecta and lava is molten extrusive material consisting mainly of magnesium silicate. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Acidianus: A genus of facultatively anaerobic coccoid ARCHAEA, in the family SULFOLOBACEAE. Cells are highly irregular in shape and thermoacidophilic. Lithotrophic growth occurs aerobically via sulfur oxidation in some species. Distribution includes solfataric springs and fields, mudholes, and geothermically heated acidic marine environments.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.DNA-Binding Proteins: 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.Archaea: One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Receptors, Autocrine Motility Factor: 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.Nitrogen Dioxide: Nitrogen oxide (NO2). A highly poisonous gas. Exposure produces inflammation of lungs that may only cause slight pain or pass unnoticed, but resulting edema several days later may cause death. (From Merck, 11th ed) It is a major atmospheric pollutant that is able to absorb UV light that does not reach the earth's surface.Anaphase-Promoting Complex-Cyclosome: 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.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Carbohydrate Metabolism: Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.HeLa Cells: 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.HEK293 Cells: A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.Gases: 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)Oceans and Seas: 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).Ecosystem: A functional system which includes the organisms of a natural community together with their environment. (McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Processing, Post-Translational: 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.Sulfuric Acids: Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Repressor Proteins: 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.Arylsulfatases: Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Environmental Monitoring: 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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Spectrum Analysis: The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Two-Hybrid System Techniques: 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.Soil Microbiology: The presence of bacteria, viruses, and fungi in the soil. This term is not restricted to pathogenic organisms.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Aerobiosis: Life or metabolic reactions occurring in an environment containing oxygen.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Acidithiobacillus thiooxidans: A strictly autotrophic species of bacteria that oxidizes sulfur and thiosulfate to sulfuric acid. It was formerly called Thiobacillus thiooxidans.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Bacteriochlorophylls: Pyrrole containing pigments found in photosynthetic bacteria.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Heterotrophic Processes: 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.Chemoautotrophic Growth: Growth of organisms using AUTOTROPHIC PROCESSES for obtaining nutrients and chemotrophic processes for obtaining a primary energy supply. Chemotrophic processes are involved in deriving a primary energy supply from exogenous chemical sources. Chemotrophic autotrophs (chemoautotrophs) generally use inorganic chemicals as energy sources and as such are called chemolithoautotrophs. Most chemoautotrophs live in hostile environments, such as deep sea vents. They are mostly BACTERIA and ARCHAEA, and are the primary producers for those ecosystems.CystathionineTrees: Woody, usually tall, perennial higher plants (Angiosperms, Gymnosperms, and some Pterophyta) having usually a main stem and numerous branches.Ubiquitin-Specific Proteases: 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.Nuclear Proteins: 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.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Sulfur Radioisotopes: Unstable isotopes of sulfur that decay or disintegrate spontaneously emitting radiation. S 29-31, 35, 37, and 38 are radioactive sulfur isotopes.Adenosine Triphosphate: 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.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Metalloproteins: Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Rhodococcus: A bacterial genus of the order ACTINOMYCETALES.Tetrathionic Acid: A sulfuric acid dimer, formed by disulfide linkage. This compound has been used to prolong coagulation time and as an antidote in cyanide poisoning.

Expression, purification, and characterization of the Mycobacterium tuberculosis acyl carrier protein, AcpM. (1/22)

Mycolic acids are generated in Mycobacterium tuberculosis as a result of the interaction of two fatty acid biosynthetic systems: the multifunctional polypeptide, FASI, in which the acyl carrier protein (ACP) domain forms an integral part of the polypeptide, and the dissociated FASII system, which is composed of monofunctional enzymes and a discrete ACP (AcpM). In order to characterize enzymes of the FASII system, large amounts of AcpM are required to generate substrates such as holo-AcpM, malonyl-AcpM and acyl-AcpM. The M. tuberculosis acpM gene was overexpressed in Escherichia coli and AcpM purified, yielding approximately 15-20 mg/l of culture. Analysis of AcpM by mass spectrometry, N-terminal sequencing, amino acid analysis, and gas chromatography indicated the presence of three species, apo-, holo-, and acyl-AcpM, the former comprising up to 65% of the total pool. The apo-AcpM was purified away from the in vivo generated holo- and acyl-forms, which were inseparable and heterogeneous with respect to acyl chain lengths. Once purified, we were able to convert apo-AcpM into holo- and acyl-forms. These procedures provide the means for the preparation of the large quantities of AcpM and derivatives needed for characterization of the purified enzymes of the mycobacterial FASII system.  (+info)

Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. (2/22)

Acyl carrier protein (ACP) interacts with many different enzymes during the synthesis of fatty acids, phospholipids, and other specialized products in bacteria. To examine the structural and functional roles of amino acids previously implicated in interactions between the ACP polypeptide and fatty acids attached to the phosphopantetheine prosthetic group, recombinant Vibrio harveyi ACP and mutant derivatives of conserved residues Phe-50, Ile-54, Ala-59, and Tyr-71 were prepared from glutathione S-transferase fusion proteins. Circular dichroism revealed that, unlike Escherichia coli ACP, V. harveyi-derived ACPs are unfolded at neutral pH in the absence of divalent cations; all except F50A and I54A recovered native conformation upon addition of MgCl(2). Mutant I54A was not processed to the holo form by ACP synthase. Some mutations significantly decreased catalytic efficiency of ACP fatty acylation by V. harveyi acyl-ACP synthetase relative to recombinant ACP, e.g. F50A (4%), I54L (20%), and I54V (31%), whereas others (V12G, Y71A, and A59G) had less effect. By contrast, all myristoylated ACPs examined were effective substrates for the luminescence-specific V. harveyi myristoyl-ACP thioesterase. Conformationally sensitive gel electrophoresis at pH 9 indicated that fatty acid attachment stabilizes mutant ACPs in a chain length-dependent manner, although stabilization was decreased for mutants F50A and A59G. Our results indicate that (i) residues Ile-54 and Phe-50 are important in maintaining native ACP conformation, (ii) residue Ala-59 may be directly involved in stabilization of ACP structure by acyl chain binding, and (iii) acyl-ACP synthetase requires native ACP conformation and involves interaction with fatty acid binding pocket residues, whereas myristoyl-ACP thioesterase is insensitive to acyl donor structure.  (+info)

Purification and characterization of acyl-acyl carrier protein synthetase from oleaginous yeast and its role in triacylglycerol biosynthesis. (3/22)

Fatty acids are activated in an ATP-dependent manner before they are utilized. We describe here how the 10 S triacylglycerol biosynthetic multienzyme complex from Rhodotorula glutinis is capable of activating non-esterified fatty acids for the synthesis of triacylglycerol. The photolabelling of the complex with [(32)P]azido-ATP showed labelling of a 35 kDa polypeptide. The labelled polypeptide was identified as acyl-acyl carrier protein (ACP) synthetase, which catalyses the ATP-dependent ligation of fatty acid with ACP to form acyl-ACP. The enzyme was purified by successive PAGE separations to apparent homogeneity from the soluble fraction of oleaginous yeast and its apparent molecular mass was 35 kDa under denaturing and reducing conditions. Acyl-ACP synthetase was specific for ATP. The K(m) values for palmitic, stearic, oleic and linoleic acids were found to be 42.9, 30.4, 25.1 and 22.7 microM, respectively. The antibodies to acyl-ACP synthetase cross-reacted with Escherichia coli acyl-ACP synthetase. Anti-ACP antibodies showed no cross-reactivity with the purified acyl-ACP synthetase, indicating no bound ACP with the enzyme. Immunoprecipitations with antibodies to acyl-ACP synthetase revealed that this enzyme is a part of the 10 S triacylglycerol biosynthetic complex. These results demonstrate that the soluble acyl-ACP synthetase plays a novel role in activating fatty acids for triacylglycerol biosynthesis in oleaginous yeast.  (+info)

A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. (4/22)

The formation of S-hydroxymethylglutathione from formaldehyde and glutathione is a central reaction in the consumption of the cytotoxin formaldehyde in some methylotrophic bacteria as well as in many other organisms. We describe here the discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction. The rates of S-hydroxymethylglutathione formation and cleavage were determined under equilibrium conditions via two-dimensional proton exchange NMR spectroscopy. The pseudo first order rate constants k(1)* were estimated from the temperature dependence of the reaction and the signal to noise ratio of the uncatalyzed reaction. At 303 K and pH 6.0 k(1)* was found to be 0.02 s(-1) for the spontaneous reaction. A 10-fold increase of the rate constant was observed upon addition of cell extract from P. denitrificans grown in the presence of methanol corresponding to a specific activity of 35 units mg(-1). Extracts of cells grown in the presence of succinate revealed a lower specific activity of 11 units mg(-1). The enzyme catalyzing the conversion of formaldehyde and glutathione was purified and named glutathione-dependent formaldehyde-activating enzyme (Gfa). The gene gfa is located directly upstream of the gene for glutathione-dependent formaldehyde dehydrogenase, which catalyzes the subsequent oxidation of S-hydroxymethylglutathione. Putative proteins with sequence identity to Gfa from P. denitrificans are present also in Rhodobacter sphaeroides, Sinorhizobium meliloti, and Mesorhizobium loti.  (+info)

Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. (5/22)

Fatty acyl-CoA synthetase (FACS, fatty acid:CoA ligase, AMP forming; EC ) plays a central role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA. In Escherichia coli this enzyme, encoded by the fadD gene, is required for the coupled import and activation of exogenous long-chain fatty acids. The E. coli FACS (FadD) contains two sequence elements, which comprise the ATP/AMP signature motif ((213)YTGGTTGVAKGA(224) and (356)GYGLTE(361)) placing it in the superfamily of adenylate-forming enzymes. A series of site-directed mutations were generated in the fadD gene within the ATP/AMP signature motif site to evaluate the role of this conserved region to enzyme function and to fatty acid transport. This approach revealed two major classes of fadD mutants with depressed enzyme activity: 1) those with 25-45% wild type activity (fadD(G216A), fadD(T217A), fadD(G219A), and fadD(K222A)) and 2) those with 10% or less wild-type activity (fadD(Y213A), fadD(T214A), and fadD(E361A)). Using anti-FadD sera, Western blots demonstrated the different mutant forms of FadD that were present and had localization patterns equivalent to the wild type. The defect in the first class was attributed to a reduced catalytic efficiency although several mutant forms also had a reduced affinity for ATP. The mutations resulting in these biochemical phenotypes reduced or essentially eliminated the transport of exogenous long-chain fatty acids. These data support the hypothesis that the FACS FadD functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters.  (+info)

Isolation and expression pattern of two putative acyl-ACP desaturase cDNAs from Bassia scoparia. (6/22)

The seed lipids of some higher plants contain unusual fatty acids with potentially valuable non-food uses. Seeds of Bassia scoparia contain one such monounsaturated fatty acid, 16:1Delta5. This fatty acid can be used for the production of an insect oviposition pheromone, which is potentially valuable in the control of the mosquito Culex quinquefasciatus, a vector of West Nile virus. Previous work has established that a number of unusual monounsaturated fatty acids are produced by variant forms of the ubiquitous acyl-ACP desaturases. The isolation and initial characterization of two putative acyl-ACP desaturases from B. scoparia, one of which is seed-specific, suggests that such a variant enzyme occurs in this species.  (+info)

A dynamic zinc redox switch. (7/22)

The crystal structures of glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans, which catalyzes the formation of S-hydroxymethylglutathione from formaldehyde and glutathione, and its complex with glutathione (Gfa-GTT) have been determined. Gfa has a new fold with two zinc-sulfur centers, one that is structural (zinc tetracoordinated) and one catalytic (zinc apparently tricoordinated). In Gfa-GTT, the catalytic zinc is displaced due to disulfide bond formation of glutathione with one of the zinc-coordinating cysteines. Soaking crystals of Gfa-GTT with formaldehyde restores the holoenzyme. Accordingly, the displaced zinc forms a complex by scavenging formaldehyde and glutathione. The activation of formaldehyde and of glutathione in this zinc complex favors the final nucleophilic addition, followed by relocation of zinc in the catalytic site. Therefore, the structures of Gfa and Gfa-GTT draw the critical association between a dynamic zinc redox switch and a nucleophilic addition as a new facet of the redox activity of zinc-sulfur sites.  (+info)

Lysophospholipid flipping across the Escherichia coli inner membrane catalyzed by a transporter (LplT) belonging to the major facilitator superfamily. (8/22)

The transfer of phospholipids across membrane bilayers is protein-mediated, and most of the established transporters catalyze the energy-dependent efflux of phospholipids from cells. This work identifies and characterizes a lysophospholipid transporter gene (lplT, formally ygeD) in Escherichia coli that is an integral component in the 2-acylglycerophosphoethanolamine (2-acyl-GPE) metabolic cycle for membrane protein acylation. The lplT gene is adjacent to and in the same operon as the aas gene, which encodes the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-acyl carrier protein synthetase. In some bacteria, acyltransferase/acyl-ACP synthetase (Aas) and LplT homologues are fused in a single polypeptide chain. 2-Acyl-GPE transport to the inside of the cell was assessed by measuring the Aas-dependent formation of phosphatidylethanolamine. The Aas-dependent incorporation of [3H]palmitate into phosphatidylethanolamine was significantly diminished in deltalplT mutants, and the LplT-Aas transport/acylation activity was independent of the proton motive force. The deltalplT mutants accumulated acyl-GPE in vivo and had a diminished capacity to transport exogenous 2-acylglycerophosphocholine into the cell. Spheroplasts prepared from wild-type E. coli transported and acylated fluorescent 2-acyl-GPE with an apparent K(d) of 7.5 microM, whereas this high-affinity process was absent in deltalplT mutants. Thus, LplT catalyzes the transbilayer movement of lysophospholipids and is the first example of a phospholipid flippase that belongs to the major facilitator superfamily.  (+info)

*Phenylacetate-CoA ligase

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 that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\ ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...

*Phytanate-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 ... systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). ...

*Acid-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, an acid-CoA ligase (GDP-forming) (EC 6.2.1.10) is an enzyme that catalyzes the chemical reaction GTP + an acid ... systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase ( ...

*Butyrate-CoA ligase

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 ...

*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 6-carboxyhexanoate-CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction ATP + 6- ... systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6- ...

*Anthranilate-CoA ligase

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 + ... systematic name of this enzyme class is anthranilate:CoA ligase (AMP-forming). Other names in common use include anthraniloyl ...

*Citrate-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 ⇌ {\ ... CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle. Lill U, Schreil A, Eggerer H (1982). " ... systematic name of this enzyme class is citrate:CoA ligase (ADP-forming). Other names in common use include citryl-CoA ...

*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 ... DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid ... In enzymology, a 3alpha,7alpha-dihydroxy-5beta-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997-1004. PMID ...

*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, an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + ... systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ...

*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 propionate-CoA ligase (EC 6.2.1.17) is an enzyme that catalyzes the chemical reaction ATP + propanoate + CoA ... systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA ...

*Trans-feruloyl-CoA synthase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP-hydrolysing). This enzyme is also called trans- ...

*4-chlorobenzoate-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 ...

*4-hydroxybenzoate-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- ... systematic name of this enzyme class is 4-hydroxybenzoate:CoA ligase (AMP-forming). Other names in common use include 4- ...

*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 glutarate-CoA ligase (EC 6.2.1.6) is an enzyme that catalyzes the chemical reaction ATP + glutarate + CoA ⇌ {\ ... systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA ...

*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-luciferin-component ligase (EC 6.2.1.19) is an enzyme that catalyzes the chemical ... systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl- ...

*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 ... In enzymology, a long-chain-fatty-acid-[acyl-carrier-protein] ligase (EC 6.2.1.20) is an enzyme that catalyzes the chemical ... systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in ...

*citrate (pro-3S)-lyase) 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 + ... Antranikian G, Herzberg C, Gottschalk G (1985). "Covalent modification of citrate lyase ligase from Clostridium sphenoides by ...

*Oxalate-CoA ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an oxalate-CoA ligase (EC 6.2.1.8) is an enzyme that catalyzes the chemical reaction ATP + oxalate + CoA ⇌ {\ ... systematic name of this enzyme class is oxalate:CoA ligase (AMP-forming). Other names in common use include oxalyl-CoA ... Organisms with Oxalate-CoA Ligases include: Arabidopsis thalianaSaccharomyces cerevisiae http://www.plantcell.org/content/24/3/ ...

*Arachidonate-CoA ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an arachidonate-CoA ligase (EC 6.2.1.15) is an enzyme that catalyzes the chemical reaction ATP + arachidonate + ... systematic name of this enzyme class is arachidonate:CoA ligase (AMP-forming). This enzyme is also called arachidonoyl-CoA ...

*4-Coumarate-CoA ligase

This enzyme belongs to the family of ligases, to be specific those forming carbon-sulfur bonds as acid-thiol ligases. The ... p-coumaroyl CoA ligase, p-coumaryl coenzyme A synthetase, p-coumaryl-CoA synthetase, p-coumaryl-CoA ligase, feruloyl CoA ligase ... CoA ligase, p-coumaryl-CoA ligase, p-hydroxycinnamic acid:CoA ligase, and 4CL. This enzyme participates in phenylpropanoid ... In enzymology, a 4-coumarate-CoA ligase (EC 6.2.1.12) is an enzyme that catalyzes the chemical reaction ATP + 4-coumarate + CoA ...

*Ligase

... ligases used to form carbon-oxygen bonds EC 6.2 includes ligases used to form carbon-sulfur bonds EC 6.3 includes ligases used ... ligases used to form carbon-carbon bonds EC 6.5 includes ligases used to form phosphoric ester bonds EC 6.6 includes ligases ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... Ligases are classified as EC 6 in the EC number classification of enzymes. Ligases can be further classified into six ...

*Biotin

... which was found to be the iron-sulfur (Fe-S) center contained in the enzyme. D-(+)-Biotin is a cofactor responsible for carbon ... In bacteria, biotin is attached to biotin carboxyl carrier protein (BCCP) by biotin protein ligase (BirA in E. coli). The ... A valeric acid substituent is attached to one of the carbon atoms of the tetrahydrothiophene ring. Biotin is a coenzyme for ... Biotin assists in various metabolic reactions involving the transfer of carbon dioxide. It may also be helpful in maintaining a ...

*List of MeSH codes (D08)

... carbon-carbon double bond isomerases MeSH D08.811.399.475.400.700 --- steroid isomerases MeSH D08.811.399.475.800 --- sulfur- ... tyrosine-tRNA ligase MeSH D08.811.464.263.200.950 --- valine-tRNA ligase MeSH D08.811.464.267.500 --- coenzyme a ligases MeSH ... succinate-coa ligases MeSH D08.811.464.754.600 --- dna ligases MeSH D08.811.464.754.720 --- rna ligase (atp) MeSH D08.811. ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ...

*Acetyl-CoA synthetase

The covalent bond is formed between the sulfur atom in Co-A and the central carbon atom of acetate. The ACS1 form of acetyl-CoA ... Acetyl-CoA synthetase or Acetate-CoA ligase is an enzyme (EC 6.2.1.1) involved in metabolism of acetate. It is in the ligase ... "An acetyl-CoA synthetase not encoded by the facA gene is expressed under carbon starvation in Phycomyces blakesleeanus.", Red ... "Inactivation of Acetyl-CoA Synthase/Carbon Monoxide Dehydrogenase by Copper", J. Am. Chem. Soc., 125 (31): 9316-7, doi:10.1021/ ...

*Methionine gamma-lyase

... specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-methionine methanethiol-lyase ( ... 2-oxobutyrate is ultimately decomposed by acetate-CoA ligase and produces ATP, thus contributing to ATP metabolism. MGL also ... It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols. Because sulfur-containing amino acids play a ... Stipanuk MH (2004). "Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine". Annual ...

*Oxalyl-CoA decarboxylase

A key feature of the cofactor TPP is the relatively acidic proton bound to the carbon atom between the nitrogen and sulfur in ... Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz, A.L. and Allison, M.J. "Purification and ... which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). ... This carbon center ionizes to form a carbanion, which adds to the carbonyl group of oxalyl-CoA. This addition is followed by ...
Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity ...
Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity ...
RN [1] RM 11741920 RT A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. RA Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA. RL J Biol Chem. 2002 Feb 1;277(5):3069-72. DR HAMAP; MF_00723; 13 of ...
The MHC class II gene Aa was disrupted by targeted mutation in embryonic stem (ES) cells derived from C57BL/6 mice to prevent expression of MHC class II molecules. Contrary to previous reports, the effect of the null-mutation on T cell development was investigated in C57BL/6 mice, which provide a defined genetic background. The complete lack of cell surface expression of MHC class II molecules in B6-Aa0/Aa0 homozygous mutant mice was directly demonstrated by cytofluorometric analysis using anti-Ab and anti-Ia specific mAbs. Development of CD4+CD8- T cells in the thymus was largely absent except for a small population of thymocytes expressing high levels of CD4 together with low amounts of CD8. The majority of these cells express the TCR at high density. Although mature CD4+CD8- T cells were undetectable in the thymus, some T cells with a CD4+CD8-TCRhigh phenotype were found in lymph nodes and spleen. Peripheral T cells from the mutant mice can be polyclonally activated in vitro with the mitogen ...
Vip3Aa20 is a mutated form of the vip3Aa19 gene from the Bacillus thuringiensis strain AB88. The mutation occurred by two codon changes within the vip3Aa19 coding sequence when this gene was introduced in the maize event MIR162. One of these was a silent mutation and the other codon change resulted in an amino acid substitution. Therefore, the vip3Aa gene variant present in MIR162 maize has been designated vip3Aa20 ...
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme participates in biotin metabolism.
Pore-forming toxin with nematicidal activity (PubMed:26795495, PubMed:27576487). In infected C.elegans, induces an increase in intracellular Ca(2+) resulting in necrosis of host intestinal cells (PubMed:26795495). Also, induces the expression of aspartic protease asp-1 (PubMed:26795495).
Archives issue of International Journal of Pharma and Bio Sciences which aims to cover the latest outstanding developments in the field of pharmaceutical and biological sciences
ウサギ・ポリクローナル抗体 ab117239 交差種: Hu 適用: WB…ATP citrate lyase抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
15260498] The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units. (Biochemistry. , 2004 ...
2020 Copyright France 24 - All rights reserved. France 24 is not responsible for the content of external websites. Audience ratings certified by ACPM/OJD.. ...
2020 Copyright France 24 - All rights reserved. France 24 is not responsible for the content of external websites. Audience ratings certified by ACPM/OJD.. ...
Accepted name: oleoyl-[acyl-carrier-protein] hydrolase. Reaction: an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate. Other name(s): acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase. Systematic name: oleoyl-[acyl-carrier protein] hydrolase. Comments: Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68009-83-6. References:. 1. Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382-391. [PMID: 30409]. 2. Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of ...
Most studies of biofilms have focused on single species and on genes that control or are regulated by life on a surface. As more information is uncovered by studies of pure cultures, these data can be applied towards understanding the roles of specific genes in multispecies interactions. This chapter focuses mostly on multi-species interactions among oral bacteria in biofilms: a few single-species biofilms are featured to discuss responses to environmental signals, including signals generated by the occupants within the biofilm. Signals involved in cell-to-cell communication among biofilm cells include acyl homoserine lactones, oligopeptides, and autoinducer-2 (AI-2). Importantly, an optimal concentration of 4,5-dihydroxy-2,3-pentanedione (DPD) was critical for maximal biofilm development. One site where natural multispecies biofilms are unusually accessible is the tooth surface in the human oral cavity. We use a retrievable enamel chip model system that permits us to place three pieces of enamel side
Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene classes in higher plants, termed FatA and FatB, whose evolutionary divergence appears to be ancient. FatA encodes the already described 18:1-ACP thioesterase. In contrast, FatB representatives encode thioesterases preferring acyl-ACPs having saturated acyl groups. We unexpectedly obtained a 16:0-ACP thioesterase cDNA from Cuphea hookeriana seed, which accumulate predominantly 8:0 and 10:0. The 16:0 thioesterase transcripts were found in non-seed tissues, and expression in transgenic Brassica napus led to the production of a 16:0-rich oil. We present evidence that this type of FatB gene is ancient and ubiquitous in plants and that specialized plant medium-chain thioesterases have evolved independently from ...
The recent rapid growth in the biofilm field has spawned a number of new strategies for controlling biofilms. Below are descriptions of a few of these emergent strategies.. For some years it has been known that bacteria communicate with each other via diffusible signal molecules in a process termed "quorum sensing." The discovery that quorum sensing regulates biofilm formation opens the door to interdicting normal biofilm development through the use of quorum sensing inhibitors. This strategy of jamming communication is now moving towards application. One example of such inhibitors are the brominated furanones that block quorum sensing by acyl homoserine lactones, signal molecules used by Gram-negative bacteria. These furanones were first isolated from a marine algae and are thought to be part of the plants natural defense against microbial biofouling. Furanone-based quorum sensing inhibitors have been shown to increase antibiotic sensitivity of Pseudomonas aeruginosa biofilms and improve ...
Acyl-acyl carrier protein thioesterases (acyl-ACP TEs) catalyze the hydrolysis of the thioester bond that links the acyl chain to the sulfhydryl group of the phosphopantetheine prosthetic group of ACP. This reaction terminates acyl chain elongation of fatty acid biosynthesis, and in plant seeds it is the biochemical determinant of the fatty acid compositions of storage lipids. To explore acyl-ACP TE diversity and to identify novel acyl ACP-TEs, 31 acyl-ACP TEs from wide-ranging phylogenetic sources were characterized to ascertain their in vivo activities and substrate specificities. These acyl-ACP TEs were chosen by two different approaches: 1) 24 TEs were selected from public databases on the basis of phylogenetic analysis and fatty acid profile knowledge of their source organisms; and 2) seven TEs were molecularly cloned from oil palm (Elaeis guineensis), coconut (Cocos nucifera) and Cuphea viscosissima, organisms that produce medium-chain and short-chain fatty acids in their seeds. The in vivo
The Ramberg-Bäcklund reaction is an organic reaction converting an α-halo sulfone into an alkene in presence of a base with extrusion of sulfur dioxide.[1] The reaction is named after the two Swedish chemists Ludwig Ramberg and Birger Bäcklund. The carbanion formed by deprotonation gives an unstable thiirane dioxide that decomposes with elimination of sulfur dioxide. This elimination step is considered to be a concerted cycloelimination.[citation needed] The overall transformation is the conversion of the carbon-sulfur bonds to a carbon-carbon double bond. The original procedure involved halogenation of a sulfide, followed by oxidation to the sulfone. Recently, the preferred method has reversed the order of the steps. After the oxidation, which is normally done with a peroxy acid, halogenation is done under basic conditions by use of dibromodifluoromethane for the halogen transfer step. [2] This method was used to synthesize 1,8-diphenyl-1,3,5,7-octatetraene. The Ramberg-Bäcklund reaction ...
As the leader for the specialty of Preventive Medicine and physicians dedicated to prevention, ACPM improves the health of individuals and populations through evidence-based health promotion, disease prevention, and systems-based approaches to improving health and health care.
As the leader for the specialty of Preventive Medicine and physicians dedicated to prevention, ACPM improves the health of individuals and populations through evidence-based health promotion, disease prevention, and systems-based approaches to improving health and health care.
The current study reveals several key findings with regard to endogenous cardiac TAG metabolism under both baseline (i.e., normoxia) and I-R conditions. First, increased TAG content and turnover as a result of DGAT1 overexpression do not adversely affect cardiac function, energetics, or the oxidation of exogenous substrates. Second, DGAT1 overexpression significantly increased the incorporation rates of various LCFAs into the TAG pool. Third, our data show that maintaining elevated TAG turnover rates during reperfusion after acute ischemia is cardioprotective, in part, by sequestering fatty acids into the TAG pool and reducing the accumulation of ceramides. Last, we show that when palmitate is the sole source of exogenous fatty acids during the reperfusion period, there are deleterious effects on recovery from ischemia in DGAT1 transgenic hearts. All told, our findings demonstrate an important role of endogenous cardiac TAG metabolism in determining outcomes of cardiac stress. Moreover, they ...
GFA League 2017/2018 - piłkarskie wyniki na żywo, rezultaty końcowe, tabele, podsumowania meczów ze strzelcami bramek, żółte i czerwone kartki, porównania kursów i statystyki H2H.
Acinetobacter calcoaceticus BD413 accumulates wax esters and triacylglycerol under conditions of mineral nutrient limitation. Nitrosoguanidine-induced mutants of strain BD413 were isolated that failed to accumulate wax esters under nitrogen-limited growth conditions. One of the mutants, Wow15 (without wax), accumulated wax when grown in the presence of cis-11-hexadecenal and hexadecanol but not hexadecane or hexadecanoic acid. This suggested that the mutation may have inactivated a gene encoding either an acyl-acyl carrier protein or acyl-coenzyme A (CoA) reductase. The Wow15 mutant was complemented with a cosmid genomic library prepared from wild-type A. calcoaceticus BD413. The complementary region was localized to a single gene (acr1) encoding a protein of 32,468 Da that is 44% identical over a region of 264 amino acids to a product of unknown function encoded by an open reading frame associated with mycolic acid synthesis in Mycobacterium tuberculosis H37Ra. Extracts of Escherichia coli ...
Crassous PA, Cardinaletti C, Carrieri A, Bruni B, Di Vaira M, Gentili F, Ghelfi F, Giannella M, Paris H, Piergentili A, Quaglia W, Schaak S, Vesprini C, Pigini M (August 2007). "Alpha2-adrenoreceptors profile modulation. 3.1 (R)-(+)-m-nitrobiphenyline, a new efficient and alpha2C-subtype selective agonist". Journal of Medicinal Chemistry 50 (16): 3964-8. PMID 17630725. doi:10.1021/jm061487a. Cite uses deprecated parameter ...

Mycobacterium tuberculosis FadD28 protein
     Summary Report | CureHunterMycobacterium tuberculosis FadD28 protein Summary Report | CureHunter

... acyl AMP ligase family member required for biosynthesis of phthiocerol dimycocerosate lipid found in the cell wall of ... a fatty -acyl AMP ligase family member required for biosynthesis of phthiocerol dimycocerosate lipid found in the cell wall of ... Ligases: 2113*Carbon-Sulfur Ligases*Mycobacterium tuberculosis FadD28 protein. CureHunter Inc. provides medical information and ...
more infohttp://www.curehunter.com/public/keywordSummaryC510957-Mycobacterium-tuberculosis-FadD28-protein.do

Phenylacetate-CoA ligase - WikipediaPhenylacetate-CoA ligase - Wikipedia

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 that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\ ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...
more infohttps://en.wikipedia.org/wiki/Phenylacetate%E2%80%94CoA_ligase

Phytanate-CoA ligase - WikipediaPhytanate-CoA ligase - Wikipedia

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 ... systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). ...
more infohttps://en.wikipedia.org/wiki/Phytanate%E2%80%94CoA_ligase

US20170218409A1 - Production of Acrylate in Cells 
      - Google PatentsUS20170218409A1 - Production of Acrylate in Cells - Google Patents

C12Y602/00-Ligases forming carbon-sulfur bonds (6.2) Abstract. A method of producing acrylate in vivo in a genetically modified ... depicts a biosynthetic pathway for 3HP using glucose or other carbon feedstock. The 3HP can then be converted to acrylate using ... The genetically modified bacteria cell produces acrylate from a carbon source which the bacteria can metabolize. ... from the carbon fixation pathway of Chloroflexus aurantiacus (see Mattozzi, M., Ziesack, M., Voges, M. J., Silver, P. A. and ...
more infohttps://patents.google.com/patent/US20170218409A1

Ligase - WikipediaLigase - Wikipedia

EC 6.2 includes ligases used to form carbon-sulfur bonds. *EC 6.3 includes ligases used to form carbon-nitrogen bonds ( ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... DNA ligase. References[edit]. *^ "Synthases and ligases". chem.qmul.ac.uk. Archived from the original on October 15, 2012. ... This article is about general ligases. For DNA specific ligases, see DNA ligase. ...
more infohttps://en.wikipedia.org/wiki/Ligase

Muramyl ligase - WikipediaMuramyl ligase - Wikipedia

6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ... All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each ...
more infohttps://en.wikipedia.org/wiki/Muramyl_ligase

biotin-CoA ligase(EC 6.2.1.11) - Creative Enzymesbiotin-CoA ligase(EC 6.2.1.11) - Creative Enzymes

... specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme participates in biotin metabolism. ... This enzyme belongs to the family of ligases, ... those forming carbon-sulfur bonds as acid-thiol ligases. This ... This enzyme belongs to the family of ligases, specifically ...
more infohttps://www.creative-enzymes.com/product/BiotinCoA-Ligase_15838.html

KEGG ENZYME: 6.2.1.7KEGG ENZYME: 6.2.1.7

Ligases;. Forming carbon-sulfur bonds;. Acid-thiol ligases. Sysname. cholate:CoA ligase (AMP-forming). ... cholate---CoA ligase;. BAL;. bile acid CoA ligase;. bile acid coenzyme A ligase;. choloyl-CoA synthetase;. choloyl coenzyme A ... THCA-CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate---CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta- ... cholic acid:CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase;. 3alpha,7alpha,12alpha- ...
more infohttps://www.genome.jp/dbget-bin/www_bget?enzyme+6.2.1.7

KEGG ENZYME: 6.2.1.28KEGG ENZYME: 6.2.1.28

Ligases;. Forming carbon-sulfur bonds;. Acid-thiol ligases. Sysname. (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate:CoA ... DHCA-CoA ligase;. 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). ... 3alpha,7alpha-dihydroxy-5beta-cholestanate---CoA ligase;. 3alpha,7alpha-dihydroxy-5beta-cholestanoyl coenzyme A synthetase;. ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver. ...
more infohttp://www.genome.jp/dbget-bin/www_bget?ec:6.2.1.28

Acetyl-coenzyme A synthetase 2 (P52910) - Yeast Metabolome DatabaseAcetyl-coenzyme A synthetase 2 (P52910) - Yeast Metabolome Database

ligase activity, forming carbon-sulfur bonds. CoA-ligase activity. AMP binding. acetate-CoA ligase activity. ... Involved in acetate-CoA ligase activity. Specific Function. Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA ... "Anaerobic" isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose ...
more infohttp://www.ymdb.ca/proteins/P52910

EC 6.2.1EC 6.2.1

Forming Carbon Sulfur Bonds. EC 6.2.1 Acid Thiol Ligases. Contents. EC 6.2.1.1 acetate CoA ligase. EC 6.2.1.2 medium-chain acyl ... EC 6.2.1.6 glutarate CoA ligase. EC 6.2.1.7 cholate CoA ligase. EC 6.2.1.8 oxalate CoA ligase. EC 6.2.1.9 malate CoA ligase. EC ... CoA ligase; p-coumaryl-CoA ligase; p-hydroxycinnamic acid:CoA ligase; 4CL Systematic name: 4-coumarate:CoA ligase (AMP-forming) ... EC 6.2.1.22 citrate (pro-3S)-lyase ligase. EC 6.2.1.23 dicarboxylate CoA ligase. EC 6.2.1.24 phytanate CoA ligase. EC 6.2.1.25 ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC6/0201.html

Use of a Chimeric Gene 4-CL Encoding 4-Coumarate:CoA Ligase in Brassicaceae - Patent applicationUse of a Chimeric Gene 4-CL Encoding 4-Coumarate:CoA Ligase in Brassicaceae - Patent application

0023]This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... p-coumaroyl CoA ligase, p-coumaryl coenzyme A synthetase, p-coumaryl-CoA synthetase, p-coumaryl-CoA ligase, feruloyl CoA ligase ... CoA ligase, p-coumaryl-CoA ligase, p-hydroxycinnamic acid:CoA ligase, and 4CL. This enzyme participates in phenylpropanoid ... nucleotide sequence encoding a 4-coumarate-CoA ligase, preferably a 4-coumarate-CoA ligase from plant origin, operably linked ...
more infohttp://www.patentsencyclopedia.com/app/20110072538

ENZYME: 6.2.1.ENZYME: 6.2.1.

Ligases. Forming carbon-sulfur bonds. Acid--thiol ligases. All UniProtKB/Swiss-Prot entries corresponding to class 6.2.1.-.. ... CoA ligase 6.2.1.7 Cholate--CoA ligase 6.2.1.8 Oxalate--CoA ligase 6.2.1.9 Malate--CoA ligase 6.2.1.10 Acid--CoA ligase (GDP- ... CoA ligase 6.2.1.17 Propionate--CoA ligase 6.2.1.18 Citrate--CoA ligase 6.2.1.19 Long-chain-fatty-acid--protein ligase 6.2.1.20 ... CoA ligase 6.2.1.3 Long-chain-fatty-acid--CoA ligase 6.2.1.4 Succinate--CoA ligase (GDP-forming) 6.2.1.5 Succinate--CoA ligase ...
more infohttps://enzyme.expasy.org/EC/6.2.1.-

View source for FF:11684-122I1 - resource browserView source for FF:11684-122I1 - resource browser

... ligase activity, forming carbon-sulfur bonds;0.0135211100688485!GO:0045045;secretory pathway;0.0137519256446866!GO:0030880;RNA ... aminoacyl-tRNA ligase activity;7.29338040255133e-06!GO:0016875;ligase activity, forming carbon-oxygen bonds;7.29338040255133e- ... ligase activity, forming carbon-carbon bonds;0.00310298749495358!GO:0007040;lysosome organization and biogenesis; ... ligase activity, forming carbon-nitrogen bonds;2.11525603869065e-07!GO:0005319;lipid transporter activity;2.19020038963518e-07! ...
more infohttps://fantom.gsc.riken.jp/5/sstar/index.php?title=FF:11684-122I1&action=edit&oldid=3281795

2018  April | mirna array2018 April | mirna array

... phylogenetic finding was a high correlation between iron-sulfur oxidoreductases in combination with carbon nitrogen ligases and ...
more infohttps://mirnaarray.com/2018/04

List of protein families with GO categories currently covered by SVMProtList of protein families with GO categories currently covered by SVMProt

EC6.2 Ligases forming carbon-sulfur bonds. GO:0016877. 79.69. 99.75. 79.69. 99.51. 0.79. 89.5. 98.88. 92.33. 97.66. 0.89. 91.99 ... EC6.4 Ligases forming carbon-carbon bonds. GO:0016885. 63.64. 99.92. 87.5. 99.61. 0.74. 86.73. 98.94. 89.43. 97.79. 0.87. 94.83 ... EC4.4 Carbon-sulfur lyases. GO:0016846. 60.34. 99.86. 83.33. 99.41. 0.71. 83.78. 99.18. 86.84. 98.25. 0.84. 76.99. 98.99. 82.65 ... EC3.7 Acting on carbon-carbon bonds. GO:0016822. 96.48. 99.89. 94.56. 99.82. 0.95. 91.19. 99.91. 95.19. 99.74. 0.93. 84.4. ...
more infohttp://bidd2.nus.edu.sg/html/svmprot/proteinfunc.html

Search Articles | University of Toronto LibrariesSearch Articles | University of Toronto Libraries

Carbon-Sulfur Ligases - isolation & purification , Carbon-Sulfur Ligases - chemistry , Electrophoresis, Polyacrylamide Gel , ... Coenzyme A Ligases - isolation & purification , Mutation , Binding Sites , Carbon-Sulfur Ligases - metabolism , Fatty Acids - ... Carbon-Carbon Lyases - isolation & purification , Carbon-Carbon Lyases - metabolism , Mutation , Bacterial Proteins - isolation ... Carbon-Sulfur Ligases - metabolism , Ligases , Fatty acids ... Coenzyme A Ligases - metabolism , Carbon-Carbon Lyases - ...
more infohttps://query.library.utoronto.ca/index.php/search/q?kw=SubjectTerms:Coenzyme%20A%20Ligases%20-%20isolation%20&%20purification

Difference between revisions of FF:10008-101B6 - resource browserDifference between revisions of "FF:10008-101B6" - resource browser

... ligase activity, forming carbon-sulfur bonds;0.0221351274010242!GO:0008026;ATP-dependent helicase activity;0.0222210577092456! ... aminoacyl-tRNA ligase activity;0.0126076737411523!GO:0016875;ligase activity, forming carbon-oxygen bonds;0.0126076737411523!GO ... ligase activity, forming carbon-nitrogen bonds;1.30346325492069e-05!GO:0044270;nitrogen compound catabolic process; ... acting on sulfur group of donors;0.0358685778543418!GO:0006892;post-Golgi vesicle-mediated transport;0.0361995400095021!GO: ...
more infohttp://fantom.gsc.riken.jp/5/sstar/index.php?title=FF:10008-101B6&diff=1839697&oldid=1829072

ENZYME search by enzyme classENZYME search by enzyme class

Cyclo-ligases. 6. 2. -.- Forming carbon-sulfur bonds. 6. 2. 1.- Acid--thiol ligases. 6. 3. -.- Forming carbon-nitrogen bonds. 6 ... Acting on carbon-sulfur bonds. 3.13. 1.- Acting on carbon-sulfur bonds. 4. -. -.- Lyases. 4. 1. -.- Carbon-carbon lyases. 4. 1 ... 4. 3.99.- Other carbon-nitrogen lyases. 4. 4. -.- Carbon-sulfur lyases. 4. 4. 1.- Carbon-sulfur lyases. 4. 5. -.- Carbon-halide ... 1.- Acting on carbon-phosphorus bonds. 3.12. -.- Acting on sulfur-sulfur bonds. 3.12. 1.- Acting on sulfur-sulfur bonds. 3.13 ...
more infohttps://enzyme.expasy.org/enzyme-byclass.html

Impaired metabolomics of sulfur-containing substances in rats acutely treated with carbon tetrachloride<...Impaired metabolomics of sulfur-containing substances in rats acutely treated with carbon tetrachloride<...

... in liver was elevated in 4̃8 h and then returned to normal in accordance with the changes in glutamate cysteine ligase activity ... Impaired metabolomics of sulfur-containing substances in rats acutely treated with carbon tetrachloride. / Kim, Sun Ju; Kwon, ... Impaired metabolomics of sulfur-containing substances in rats acutely treated with carbon tetrachloride. Toxicological Research ... Impaired metabolomics of sulfur-containing substances in rats acutely treated with carbon tetrachloride. In: Toxicological ...
more infohttps://koreauniv.pure.elsevier.com/en/publications/impaired-metabolomics-of-sulfur-containing-substances-in-rats-acu

COLLAGEN AND FIBRIN MICROTHREADS IN A DISCRETE THREAD MODEL OF IN VITRO ACL SCAFFOLD REGENERATION - Patent applicationCOLLAGEN AND FIBRIN MICROTHREADS IN A DISCRETE THREAD MODEL OF IN VITRO ACL SCAFFOLD REGENERATION - Patent application

... wherein the ligase generates a carbon-oxygen bond, a carbon-sulfur bond, a carbon-nitrogen bond, or a carbon-carbon bond ... wherein the ligase generates a carbon-oxygen bond, a carbon-sulfur bond, a carbon-nitrogen bond, or a carbon-carbon bond ... carbon-oxygen bond, a carbon-sulfur bond, a carbon-nitrogen bond, or a carbon-carbon bond between the therapeutic agent and the ... Air dried fibrin threads were mounted on aluminum stubs (Ted Pella, Inc., Redding, Calif.) coated with double-sided carbon tape ...
more infohttp://www.patentsencyclopedia.com/app/20110034388

Proteogenomics Reveals Novel Reductive Dehalogenases and Methyltransferases Expressed during Anaerobic Dichloromethane...Proteogenomics Reveals Novel Reductive Dehalogenases and Methyltransferases Expressed during Anaerobic Dichloromethane...

... methylated corrinoid/iron-sulfur protein; CH3CO-SCoA, acetyl-CoA; CO, carbon monoxide; CH3CO-PO4, acetyl phosphate; CH3COO−, ... Formyl-THF ligase. Syntrophobotulus glycolicus. 85. Membrane. Yes. 00605. fchA. Methenyl-THF cyclohydrolase. Desulfosporosinus ... Carbon monoxide dehydrogenase. Dehalobacter sp. FTH1. 93. Cytoplasm. Yes. 00220. cooS. Carbon monoxide dehydrogenase catalytic ... B) The RDase subunit A genes encode twin-arginine translocation (Tat) pathway signals and iron-sulfur binding domains. The ...
more infohttps://aem.asm.org/content/85/6/e02768-18/figures-only

Structure of a Bmi-1-Ring1B Polycomb Group Ubiquitin Ligase… - 道客巴巴Structure of a Bmi-1-Ring1B Polycomb Group Ubiquitin Ligase… - 道客巴巴

The residues involved are shown in a stick model (carbon: green for Bmi-1 and yellow for Ring1B; nitrogen: blue; oxygen: red; ... sulfur: orange) superimposed with the Ca chains (cyan = Bmi-1 and orange = Ring1B). A salt bridge involving Asp72 of Bmi-1 and ... The catalytic subunit of the PRC1 E3 ligase complex is Ring1B. The E3 ligase activity has been shown to be important for the ... while Bmi-1 displays no detectable ubiquitin ligase activity, the binding of Bmi-1 greatly stimulates the E3 ligase activity of ...
more infohttp://maixius.com/q-1324509144914.iunm

List of enzymes - WikipediaList of enzymes - Wikipedia

Category:EC 6.2 (form carbon-sulfur bonds)Edit. *EC 6.2.1.1: Acetate--CoA ligase ... Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ... Category:EC 4.4 (carbon-sulfur lyases)Edit. *Category:EC 4.4.1 *Cystathionine gamma-lyase ...
more infohttps://en.m.wikipedia.org/wiki/List_of_enzymes

Frontiers | Bacterial Catabolism of Dimethylsulfoniopropionate (DMSP) | MicrobiologyFrontiers | Bacterial Catabolism of Dimethylsulfoniopropionate (DMSP) | Microbiology

... review will focus on the recent discoveries in the biochemical pathways that mineralize and assimilate DMSP carbon and sulfur, ... a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. The activity of these ... a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. The activity of these ... pathways control the natural flux of sulfur released to the atmosphere. Although these biochemical pathways and the factors ...
more infohttps://www.frontiersin.org/articles/10.3389/fmicb.2011.00172/full
  • In enzymology, a phenylacetate-CoA ligase is an enzyme that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + phenylacetyl-CoA The 3 substrates of this enzyme are ATP, phenylacetate, and CoA, whereas its 3 products are AMP, diphosphate, and phenylacetyl-CoA. (wikipedia.org)
  • The systematic name of this enzyme class is phenylacetate:CoA ligase (AMP-forming). (wikipedia.org)
  • Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver. (genome.jp)
  • Glutathione (GSH) concentration in liver was elevated in 4̃8 h and then returned to normal in accordance with the changes in glutamate cysteine ligase activity. (elsevier.com)
  • The physiological significance of the change in the metabolomics of sulfur-containing substances and its role in the induction of liver injury need to be explored in future studies. (elsevier.com)
  • 1. A method of increasing the resistance against fungal disease or of increasing the lodging resistance in a Brassica plant comprising introducing a chimeric gene into cells of said Brassica plant, said chimeric gene comprising a nucleotide sequence encoding a 4-coumarate-CoA ligase operably linked to a heterologous plant-expressible promoter, a transcription termination and a polyadenylation region. (patentsencyclopedia.com)
  • 6. The method of claim 1, wherein said nucleotide sequence encoding a 4-coumarate-CoA ligase comprises the nucleotide sequence of SEQ ID No.: 1 from the nucleotide at position 11 to the nucleotide at position 1621, or comprises the sequence of SEQ ID No. (patentsencyclopedia.com)
  • 9. A chimeric DNA comprising a nucleotide sequence encoding a 4-coumarate-CoA ligase, operably linked to a heterologous plant-expressible promoter, a transcription termination, and a polyadenylation region. (patentsencyclopedia.com)
  • Ligase can join two complementary fragments of nucleic acid and repair single stranded breaks that arise in double stranded DNA during replication. (wikipedia.org)
  • These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso- diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP- N-acetylmuramic acid . (wikipedia.org)
  • C. autoethanogenum can grow on CO as the sole carbon and energy source, forming mainly ethanol and acetic acid but also 2,3-butanediol, lactic acid, and some H 2 as fermentation products ( 6 , 10 ). (asm.org)
  • Using this metabolic map, the analysis of genetic potential for functioning of tricarboxylic acid cycle replenishment pathways was carried out for seven strains of purple non-sulfur bacterium Rhodopseudomonas palustris . (springer.com)
  • Berg IA, Kockelkorn D, Buckel W, Fuchs G (2007) A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in archaea. (springer.com)
  • strain Rue61a is an isolate from sewage sludge able to utilize quinaldine (2-methylquinoline) as sole carbon and energy source. (biomedcentral.com)
  • Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. (wikipedia.org)
  • This review will focus on the recent discoveries in the biochemical pathways that mineralize and assimilate DMSP carbon and sulfur, as well as the areas for which a comprehensive understanding is still lacking. (frontiersin.org)
  • The two regions of interaction have a synergistic effect on the E3 ligase activity. (maixius.com)
  • The E3 ligase activity has been shown to be important for the involvement of PRC1 in X-chromosome inactivation and the control of Hox gene expression (16-19). (maixius.com)
  • The use of a lignin monomer synthetic gene 4-CL encoding 4-coumarate: CoA ligase from Populus tomentosa in increasing Sclerotinia resistance and lodging resistance. (patentsencyclopedia.com)
  • This family includes UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). (wikipedia.org)
  • An alternative demethylation/demethiolation pathway results in the eventual release of methanethiol, a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. (frontiersin.org)
  • Adessi A, Corneli E, De Philippis R (2017) Photosynthetic purple non sulfur bacteria in hydrogen producing systems: new approaches in the use of well-known and innovative substrates. (springer.com)