Coenzyme a ligases. Medical search

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.

Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.

Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).

A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.

Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.

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.

A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.

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.

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

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

A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.

A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.

A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.

Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.

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.

Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.

A sulfhydryl compound used to prevent urothelial toxicity by inactivating metabolites from ANTINEOPLASTIC AGENTS, such as IFOSFAMIDE or CYCLOPHOSPHAMIDE.

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.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

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

A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.

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

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.

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

A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.

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.

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.

The rate dynamics in chemical or physical systems.

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.

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.

Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).

An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a second ubiquitin molecule. It is structurally distinct from UBIQUITIN C, which is a single protein containing a tandemly arrayed ubiquitin peptide sequence.

A phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.

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.

An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.

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

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

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

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.

A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.

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.

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.

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.

Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

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.

Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.

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.

An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.

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.

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

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

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.

A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.

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

A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.

A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.

A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.

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.

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.

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.

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

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

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.

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.

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)

This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).

Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.

An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.

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

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

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

Proteins prepared by recombinant DNA technology.

Established cell cultures that have the potential to propagate indefinitely.

Proteins found in any species of bacterium.

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.

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.

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.

Enzymes that catalyze the first step leading to the oxidation of succinic acid by the reversible formation of succinyl-CoA from succinate and CoA with the concomitant cleavage of ATP to ADP (EC 6.2.1.5) or GTP to GDP (EC 6.2.1.4) and orthophosphate. Itaconate can act instead of succinate and ITP instead of GTP.EC 6.2.1.-.

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).

Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.

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

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).

Macromolecular complexes formed from the association of defined protein subunits.

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)

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.

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

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.

Cyclic TETRAPYRROLES based on the corrin skeleton.

A derivative of LOVASTATIN and potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It may also interfere with steroid hormone production. Due to the induction of hepatic LDL RECEPTORS, it increases breakdown of LDL CHOLESTEROL.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.

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.

An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.

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.

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.

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.

A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

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

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

Oxidoreductases that are specific for ALDEHYDES.

Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.

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.

An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. This enzyme was formerly listed as EC 4.1.3.5.

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

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)

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.

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.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

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.

An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.

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.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.

A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.

Proteins found in any species of archaeon.

A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.

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.

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.

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

The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.

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

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

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

The sum of the weight of all the atoms in a molecule.

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

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

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

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

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

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

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

The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.

An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.

A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.

A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.

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

A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.

A class of enzymes that transfers nucleotidyl residues. EC 2.7.7.

A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

An E3 UBIQUITIN LIGASE that interacts with and inhibits TUMOR SUPPRESSOR PROTEIN P53. Its ability to ubiquitinate p53 is regulated by TUMOR SUPPRESSOR PROTEIN P14ARF.

Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.

A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.

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

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

7-carbon saturated monocarboxylic acids.

Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.

Virulent bacteriophage and type species of the genus T4-like phages, in the family MYOVIRIDAE. It infects E. coli and is the best known of the T-even phages. Its virion contains linear double-stranded DNA, terminally redundant and circularly permuted.

A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.

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.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A degradation process whereby incorrectly folded proteins are selectively transported out of the ENDOPLASMIC RETICULUM and into the CYTOSOL. The misfolded proteins are subsequently ubiquitinated and degraded by the PROTEASOME.

A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.

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

Steroids with a hydroxyl group at C-3 and most of the skeleton of cholestane. Additional carbon atoms may be present in the side chain. (IUPAC Steroid Nomenclature, 1987)

Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.

Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

Biological catalysts and their cofactors.

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.

Methyl, propyl, butyl, and ethyl esters of p-hydroxybenzoic acid. They have been approved by the FDA as antimicrobial agents for foods and pharmaceuticals. (From Hawley's Condensed Chemical Dictionary, 11th ed, p872)

Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.

Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.

A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.

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

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Compounds based on 2-amino-4-hydroxypteridine.

An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.

The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.

A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)

Together with the Apc2 subunit, forms the catalytic core of the E3 ubiquitin ligase, anaphase-promoting complex-cyclosome. It has a RING H2 domain which interacts with the cullin domain of Apc2. Apc11 also interacts with the E2 ubiquitin ligases involved in APC-C ubiquitination reactions.

The 4-aminomethyl form of VITAMIN B 6. During transamination of amino acids, PYRIDOXAL PHOSPHATE is transiently converted into pyridoxamine phosphate.

Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.

Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.

The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

An order of stalked, sessile, single-celled EUKARYOTES. They are considered the transitional link between the flagellated protozoa and the SPONGES, the most primitive metazoans.

The characteristic three-dimensional shape of a molecule.

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).

Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.

Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.

A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.

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

An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.

Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. (1/783)

Epidermal growth factor (EGF) has been reported to stimulate carbohydrate, amino acid, and electrolyte transport in the small intestine, but its effects on lipid transport are poorly documented. This study aimed to investigate EGF effects on fatty acid uptake and esterification in a human enterocyte cell line (Caco-2). EGF inhibited cell uptake of [14C]palmitate and markedly reduced its incorporation into triglycerides. In contrast, the incorporation in phospholipids was enhanced. To elucidate the mechanisms involved, key steps of lipid synthesis were investigated. The amount of intestinal fatty acid-binding protein (I-FABP), which is thought to be important for fatty acid absorption, and the activity of diacylglycerol acyltransferase (DGAT), an enzyme at the branch point of diacylglycerol utilization, were reduced. EGF effects on DGAT and on palmitate esterification occurred at 2-10 ng/ml, whereas effects on I-FABP and palmitate uptake occurred only at 10 ng/ml. This suggests that EGF inhibited palmitate uptake by reducing the I-FABP level and shifted its utilization from triglycerides to phospholipids by inhibiting DGAT. This increase in phospholipid synthesis might play a role in the restoration of enterocyte absorption function after intestinal mucosa injury. (+info)

The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat. (2/783)

1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids. (+info)

Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane. (3/783)

Long-chain fatty acyl-CoA synthetase (FACS) catalyzes esterification of long-chain fatty acids (LCFAs) with coenzyme A (CoA), the first step in fatty acid metabolism. FACS has been shown to play a role in LCFA import into bacteria and implicated to function in mammalian cell LCFA import. In the present study, we demonstrate that FACS overexpression in fibroblasts increases LCFA uptake, and overexpression of both FACS and the fatty acid transport protein (FATP) have synergistic effects on LCFA uptake. To explore how FACS contributes to LCFA import, we examined the subcellular location of this enzyme in 3T3-L1 adipocytes which natively express this protein and which efficiently take up LCFAs. We demonstrate for the first time that FACS is an integral membrane protein. Subcellular fractionation of adipocytes by differential density centrifugation reveals immunoreactive and enzymatically active FACS in several membrane fractions, including the plasma membrane. Immunofluorescence studies on adipocyte plasma membrane lawns confirm that FACS resides at the plasma membrane of adipocytes, where it co-distributes with FATP. Taken together, our data support a model in which imported LCFAs are immediately esterified at the plasma membrane upon uptake, and in which FATP and FACS function coordinately to facilitate LCFA movement across the plasma membrane of mammalian cells. (+info)

Development and initial evaluation of a novel method for assessing tissue-specific plasma free fatty acid utilization in vivo using (R)-2-bromopalmitate tracer. (4/783)

We describe a method for assessing tissue-specific plasma free fatty acid (FFA) utilization in vivo using a non-beta-oxidizable FFA analog, [9,10-3H]-(R)-2-bromopalmitate (3H-R-BrP). Ideally 3H-R-BrP would be transported in plasma, taken up by tissues and activated by the enzyme acyl-CoA synthetase (ACS) like native FFA, but then 3H-labeled metabolites would be trapped. In vitro we found that 2-bromopalmitate and palmitate compete equivalently for the same ligand binding sites on albumin and intestinal fatty acid binding protein, and activation by ACS was stereoselective for the R-isomer. In vivo, oxidative and non-oxidative FFA metabolism was assessed in anesthetized Wistar rats by infusing, over 4 min, a mixture of 3H-R-BrP and [U-14C] palmitate (14C-palmitate). Indices of total FFA utilization (R*f) and incorporation into storage products (Rfs') were defined, based on tissue concentrations of 3H and 14C, respectively, 16 min after the start of tracer infusion. R*f, but not Rfs', was substantially increased in contracting (sciatic nerve stimulated) hindlimb muscles compared with contralateral non-contracting muscles. The contraction-induced increases in R*f were completely prevented by blockade of beta-oxidation with etomoxir. These results verify that 3H-R-BrP traces local total FFA utilization, including oxidative and non-oxidative metabolism. Separate estimates of the rates of loss of 3H activity indicated effective 3H metabolite retention in most tissues over a 16-min period, but appeared less effective in liver and heart. In conclusion, simultaneous use of 3H-R-BrP and [14C]palmitate tracers provides a new useful tool for in vivo studies of tissue-specific FFA transport, utilization and metabolic fate, especially in skeletal muscle and adipose tissue. (+info)

Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35. (5/783)

A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia coli to yield an active enzyme. The purified enzyme had a pH optimum of approximately 8.0, Km values of 0.49 mM for pimelic acid, 0.18 mM for CoA and 0.72 mM for ATP, a subunit Mr of approximately 80000 as determined by SDS/PAGE, and was found to be a tetramer by gel-filtration chromatography. The specific activity of the purified enzyme was 77.3 units/mg of protein. The enzyme was not absolutely specific for pimelic acid. The relative activity for adipic acid (C6) was 72% and for azaleic acid (C9) was 18% of that for pimelic acid (C7). The N-terminal amino acid was blocked to amino acid sequencing, but controlled proteolysis resulted in three peptide fragments for which amino acid sequences were obtained. An oligonucleotide gene probe corresponding to one of the amino acid sequences was synthesized and used to isolate the gene (pauA, pimelic acid-utilizing A) coding for pimeloyl-CoA synthetase. The pauA gene, which codes for a protein with a theoretical Mr of 74643, was then sequenced. The deduced amino acid sequence of the enzyme showed similarity to hypothetical proteins from Archaeoglobus fulgidus, Methanococcus jannaschii, Pyrococcus horikoshii, E. coli and Streptomyces coelicolor, and some limited similarity to microbial succinyl-CoA synthetases. The similarity with the protein from A. fulgidus was especially strong, thus indicating a function for this unidentified protein. The pauA gene was cloned into E. coli, where it was expressed and resulted in an active enzyme. (+info)

Preventing neurodegeneration in the Drosophila mutant bubblegum. (6/783)

The Drosophila melanogaster recessive mutant bubblegum (bgm) exhibits adult neurodegeneration, with marked dilation of photoreceptor axons. The bubblegum mutant shows elevated levels of very long chain fatty acids (VLCFAs), as seen in the human disease adrenoleukodystrophy (ALD). In ALD, the excess can be lowered by dietary treatment with "Lorenzo's oil," a mixture of unsaturated fatty acids. Feeding the fly mutant one of the components, glyceryl trioleate oil, blocked the accumulation of excess VLCFAs as well as development of the pathology. Mutant flies thus provide a potential model system for studying mechanisms of neurodegenerative disease and screening drugs for treatment. (+info)

The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. (7/783)

Biochemical and genetic evidence is presented to demonstrate that the prpE gene of Salmonella typhimurium encodes propionyl-CoA synthetase, an enzyme required for the catabolism of propionate in this bacterium. While prpE mutants used propionate as carbon and energy source, prpE mutants that lacked acetyl-CoA synthetase (encoded by acs) did not, indicating that Acs can compensate for the lack of PrpE in prpE mutants. Cell-free extracts enriched for PrpE catalysed the formation of propionyl-CoA in a propionate-, ATP-, Mg2+- and HS-CoA dependent manner. Acetate substituted for propionate in the reaction at 48% the rate of propionate; butyrate was not a substrate for PrpE. The propionyl-CoA synthetase activity of PrpE was specific for ATP. GTP, ITP, CTP and TTP were not used as substrates by the enzyme. UV-visible spectrophotometry, HPLC and MS data demonstrated that propionyl-CoA was the product of the reaction catalysed by PrpE. (+info)

Biosynthesis of 1,2-dieicosapentaenoyl-sn-glycero-3-phosphocholine in Caenorhabditis elegans. (8/783)

Previously, we showed that lowering the growth temperature increased the level of eicosapentaenoic acid (EPA) in the phosphatidylcholine (PtdCho) of Caenorhabditis elegans. In this study, we investigated the molecular species composition of PtdCho of C. elegans, with an emphasis on EPA-containing species. C. elegans contained a substantial amount of 1,2-dipolyunsaturated fatty acid-containing PtdCho (1,2-diPUFA-PtdCho) species, such as arachidonic acid/EPA and EPA/EPA, which are unusual phospholipids in higher animals. The EPA/EPA-PtdCho content was significantly increased in C. elegans grown at a low temperature. To examine the possibility that the acyltransferase activity involved in the remodeling of phospholipids accounts for the production of 1,2-diPUFA-PtdCho, we investigated the substrate specificity of this enzyme in C. elegans and found that it did not exhibit a preference for saturated fatty acid for acylation to the sn-1 position of PtdCho. The efficacy of the esterification of EPA to the sn-1 position was almost equal to that of stearic acid. The lack of preference for a saturated fatty acid for acylation to the sn-1 position of PtdCho is thought to result in the existence of the unusual 1,2-diEPA-PtdCho in C. elegans. (+info)

There are several types of muscular atrophy, including:

1. Disuse atrophy: This type of atrophy occurs when a muscle is not used for a long period, leading to its degeneration.
2. Neurogenic atrophy: This type of atrophy occurs due to damage to the nerves that control muscles.
3. Dystrophic atrophy: This type of atrophy occurs due to inherited genetic disorders that affect muscle fibers.
4. Atrophy due to aging: As people age, their muscles can degenerate and lose mass and strength.
5. Atrophy due to disease: Certain diseases such as cancer, HIV/AIDS, and muscular dystrophy can cause muscular atrophy.
6. Atrophy due to infection: Infections such as polio and tetanus can cause muscular atrophy.
7. Atrophy due to trauma: Traumatic injuries can cause muscular atrophy, especially if the injury is severe and leads to prolonged immobilization.

Muscular atrophy can lead to a range of symptoms depending on the type and severity of the condition. Some common symptoms include muscle weakness, loss of motor function, muscle wasting, and difficulty performing everyday activities. Treatment for muscular atrophy depends on the underlying cause and may include physical therapy, medication, and lifestyle changes such as exercise and dietary modifications. In severe cases, surgery may be necessary to restore muscle function.

There are several methods for diagnosing myringosclerosis, including:

1. Otoscopy: an examination of the outer ear and eardrum using a specialized instrument called an otoscope.
2. Tympanometry: a test that measures the movement of the eardrum and the reflexes of the middle ear muscles.
3. Acoustic reflectometry: a test that uses sound waves to measure the stiffness of the eardrum.
4. Auditory brainstem response (ABR) testing: a test that measures the electrical activity of the hearing nerve in response to sound.

There is no cure for myringosclerosis, but there are several treatment options available, including:

1. Hearing aids: devices that amplify sound and can help improve hearing.
2. Cochlear implants: devices that bypass the damaged part of the ear and directly stimulate the auditory nerve.
3. Surgery: in some cases, surgery may be necessary to remove the affected portion of the eardrum.
4. Medications: certain medications, such as corticosteroids, may be prescribed to help reduce inflammation and improve hearing.

It is important to seek medical attention if you experience any symptoms of myringosclerosis, as early diagnosis and treatment can help improve outcomes.

There are several types of genomic instability, including:

1. Chromosomal instability (CIN): This refers to changes in the number or structure of chromosomes, such as aneuploidy (having an abnormal number of chromosomes) or translocations (the movement of genetic material between chromosomes).
2. Point mutations: These are changes in a single base pair in the DNA sequence.
3. Insertions and deletions: These are changes in the number of base pairs in the DNA sequence, resulting in the insertion or deletion of one or more base pairs.
4. Genomic rearrangements: These are changes in the structure of the genome, such as chromosomal breaks and reunions, or the movement of genetic material between chromosomes.

Genomic instability can arise from a variety of sources, including environmental factors, errors during DNA replication and repair, and genetic mutations. It is often associated with cancer, as cancer cells have high levels of genomic instability, which can lead to the development of resistance to chemotherapy and radiation therapy.

Research into genomic instability has led to a greater understanding of the mechanisms underlying cancer and other diseases, and has also spurred the development of new therapeutic strategies, such as targeted therapies and immunotherapies.

In summary, genomic instability is a key feature of cancer cells and is associated with various diseases, including cancer, neurodegenerative disorders, and aging. It can arise from a variety of sources and is the subject of ongoing research in the field of molecular biology.

PKAN typically presents in children during the first few years of life, and is characterized by progressive loss of motor skills, cognitive decline, and vision loss. Affected individuals may also experience seizures, difficulty with speech and communication, and changes in behavior. The disorder is often diagnosed based on a combination of clinical features, genetic testing, and imaging studies such as magnetic resonance imaging (MRI) or positron emission tomography (PET).

The underlying pathology of PKAN involves the accumulation of a toxic protein called aggregated pantothenate kinase, which disrupts normal cellular function and leads to progressive degeneration of brain cells. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression. This may include medications to control seizures and muscle spasticity, physical therapy to maintain mobility and strength, and supportive care to address cognitive and behavioral changes.

PKAN is a rare disorder, and the prevalence is not well-defined. However, it is estimated to affect approximately 1 in 200,000 individuals worldwide. The progression of PKAN can be variable, with some individuals experiencing a rapid decline in cognitive and motor functions, while others may have a more gradual course.

In summary, pantothenate kinase-associated neurodegeneration (PKAN) is a rare genetic disorder that affects the brain and spinal cord, causing progressive loss of motor skills, cognitive decline, and vision loss. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression.

Neoplasm refers to an abnormal growth of cells that can be benign (non-cancerous) or malignant (cancerous). Neoplasms can occur in any part of the body and can affect various organs and tissues. The term "neoplasm" is often used interchangeably with "tumor," but while all tumors are neoplasms, not all neoplasms are tumors.

Types of Neoplasms

There are many different types of neoplasms, including:

1. Carcinomas: These are malignant tumors that arise in the epithelial cells lining organs and glands. Examples include breast cancer, lung cancer, and colon cancer.
2. Sarcomas: These are malignant tumors that arise in connective tissue, such as bone, cartilage, and fat. Examples include osteosarcoma (bone cancer) and soft tissue sarcoma.
3. Lymphomas: These are cancers of the immune system, specifically affecting the lymph nodes and other lymphoid tissues. Examples include Hodgkin lymphoma and non-Hodgkin lymphoma.
4. Leukemias: These are cancers of the blood and bone marrow that affect the white blood cells. Examples include acute myeloid leukemia (AML) and chronic lymphocytic leukemia (CLL).
5. Melanomas: These are malignant tumors that arise in the pigment-producing cells called melanocytes. Examples include skin melanoma and eye melanoma.

Causes and Risk Factors of Neoplasms

The exact causes of neoplasms are not fully understood, but there are several known risk factors that can increase the likelihood of developing a neoplasm. These include:

1. Genetic predisposition: Some people may be born with genetic mutations that increase their risk of developing certain types of neoplasms.
2. Environmental factors: Exposure to certain environmental toxins, such as radiation and certain chemicals, can increase the risk of developing a neoplasm.
3. Infection: Some neoplasms are caused by viruses or bacteria. For example, human papillomavirus (HPV) is a common cause of cervical cancer.
4. Lifestyle factors: Factors such as smoking, excessive alcohol consumption, and a poor diet can increase the risk of developing certain types of neoplasms.
5. Family history: A person's risk of developing a neoplasm may be higher if they have a family history of the condition.

Signs and Symptoms of Neoplasms

The signs and symptoms of neoplasms can vary depending on the type of cancer and where it is located in the body. Some common signs and symptoms include:

1. Unusual lumps or swelling
2. Pain
3. Fatigue
4. Weight loss
5. Change in bowel or bladder habits
6. Unexplained bleeding
7. Coughing up blood
8. Hoarseness or a persistent cough
9. Changes in appetite or digestion
10. Skin changes, such as a new mole or a change in the size or color of an existing mole.

Diagnosis and Treatment of Neoplasms

The diagnosis of a neoplasm usually involves a combination of physical examination, imaging tests (such as X-rays, CT scans, or MRI scans), and biopsy. A biopsy involves removing a small sample of tissue from the suspected tumor and examining it under a microscope for cancer cells.

The treatment of neoplasms depends on the type, size, location, and stage of the cancer, as well as the patient's overall health. Some common treatments include:

1. Surgery: Removing the tumor and surrounding tissue can be an effective way to treat many types of cancer.
2. Chemotherapy: Using drugs to kill cancer cells can be effective for some types of cancer, especially if the cancer has spread to other parts of the body.
3. Radiation therapy: Using high-energy radiation to kill cancer cells can be effective for some types of cancer, especially if the cancer is located in a specific area of the body.
4. Immunotherapy: Boosting the body's immune system to fight cancer can be an effective treatment for some types of cancer.
5. Targeted therapy: Using drugs or other substances to target specific molecules on cancer cells can be an effective treatment for some types of cancer.

Prevention of Neoplasms

While it is not always possible to prevent neoplasms, there are several steps that can reduce the risk of developing cancer. These include:

1. Avoiding exposure to known carcinogens (such as tobacco smoke and radiation)
2. Maintaining a healthy diet and lifestyle
3. Getting regular exercise
4. Not smoking or using tobacco products
5. Limiting alcohol consumption
6. Getting vaccinated against certain viruses that are associated with cancer (such as human papillomavirus, or HPV)
7. Participating in screening programs for early detection of cancer (such as mammograms for breast cancer and colonoscopies for colon cancer)
8. Avoiding excessive exposure to sunlight and using protective measures such as sunscreen and hats to prevent skin cancer.

It's important to note that not all cancers can be prevented, and some may be caused by factors that are not yet understood or cannot be controlled. However, by taking these steps, individuals can reduce their risk of developing cancer and improve their overall health and well-being.

A vitamin B6 deficiency happens when the body does not get enough of this essential nutrient. Vitamin B6 is needed for many bodily functions, such as making new blood cells, keeping the nervous system healthy, and helping to convert food into energy.

The symptoms of a vitamin B6 deficiency can range from mild to severe and may include:

1. Fatigue or weakness: A lack of vitamin B6 can cause tiredness, weakness, and a general feeling of being unwell.
2. Irritability or depression: Vitamin B6 plays a role in the production of neurotransmitters, such as serotonin and dopamine, which are important for mood regulation. A deficiency can lead to feelings of irritability, anxiety, and depression.
3. Nausea and vomiting: Vitamin B6 helps with the absorption of nutrients from food, so a deficiency can cause nausea and vomiting.
4. Skin problems: Vitamin B6 is important for the health of the skin, and a deficiency can lead to conditions such as acne, eczema, and dermatitis.
5. Weight loss: A vitamin B6 deficiency can make it harder to gain weight or maintain weight loss.

Causes of Vitamin B6 Deficiency:

1. Poor diet: A diet that is low in vitamin B6 can lead to a deficiency. Foods rich in vitamin B6 include meat, fish, poultry, whole grains, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease or inflammatory bowel disease, can make it harder for the body to absorb vitamin B6 from food.
3. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher need for vitamin B6 and may be more likely to develop a deficiency if they do not consume enough of this nutrient.
4. Alcoholism: Heavy alcohol consumption can interfere with the absorption of vitamin B6, leading to a deficiency.
5. Certain medications: Some medications, such as antidepressants and anti-inflammatory drugs, can interfere with the absorption of vitamin B6.

Signs and Symptoms of Vitamin B6 Deficiency:

1. Depression or anxiety
2. Fatigue or weakness
3. Irritability or mood swings
4. Skin problems, such as acne or eczema
5. Nausea and vomiting
6. Weight loss or difficulty gaining weight
7. Difficulty walking or maintaining balance
8. Headaches or migraines
9. Muscle weakness or cramps
10. Seizures or convulsions (in severe cases)

Treatment of Vitamin B6 Deficiency:

1. Dietary changes: Increasing the intake of vitamin B6-rich foods, such as lean meats, whole grains, and vegetables, can help treat a deficiency.
2. Supplements: Taking a vitamin B6 supplement can help treat a deficiency. The recommended daily dose is 1.3-2.0 mg per day for adults.
3. Addressing underlying causes: If the deficiency is caused by an underlying medical condition, such as celiac disease or alcoholism, treating the condition can help resolve the deficiency.
4. Vitamin B complex supplements: Taking a vitamin B complex supplement that contains all eight B vitamins can help ensure that the body is getting enough of this essential nutrient.

In conclusion, vitamin B6 is an essential nutrient that plays a crucial role in many bodily functions. Deficiency in this vitamin can lead to a range of health problems, from mild discomforts like fatigue and nausea to more severe conditions like seizures and convulsions. Treatment of a deficiency typically involves dietary changes, supplements, and addressing any underlying medical conditions. It is important to seek medical advice if symptoms persist or worsen over time.

There are several types of hypercholesterolemia, including:

1. Familial hypercholesterolemia: This is an inherited condition that causes high levels of low-density lipoprotein (LDL) cholesterol, also known as "bad" cholesterol, in the blood.
2. Non-familial hypercholesterolemia: This type of hypercholesterolemia is not inherited and can be caused by a variety of factors, such as a high-fat diet, lack of exercise, obesity, and certain medical conditions, such as hypothyroidism or polycystic ovary syndrome (PCOS).
3. Mixed hypercholesterolemia: This type of hypercholesterolemia is characterized by high levels of both LDL and high-density lipoprotein (HDL) cholesterol in the blood.

The diagnosis of hypercholesterolemia is typically made based on a physical examination, medical history, and laboratory tests, such as a lipid profile, which measures the levels of different types of cholesterol and triglycerides in the blood. Treatment for hypercholesterolemia usually involves lifestyle changes, such as a healthy diet and regular exercise, and may also include medication, such as statins, to lower cholesterol levels.

The exact cause of cachexia is not fully understood, but it is thought to be related to a combination of factors such as inflammation, hormonal imbalances, and changes in metabolism. Treatment for cachexia often focuses on addressing the underlying cause of the wasting, such as managing cancer or HIV/AIDS, as well as providing nutritional support and addressing any related complications.

In the medical field, cachexia is a serious condition that requires careful management to improve quality of life and outcomes for patients. It is important for healthcare providers to be aware of the signs and symptoms of cachexia and to provide appropriate treatment and support to affected individuals.

Mitochondrial encephalomyopathies can be classified into several types based on the specific symptoms and the location of the mutations in the mitochondrial DNA. Some of the most common forms of these disorders include:

1. MELAS syndrome (mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes): This is a rare condition that affects the brain, muscles, and other organs. It is characterized by recurrent stroke-like episodes, seizures, and muscle weakness.
2. Kearns-Sayre syndrome: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive weakness and paralysis of the muscles, as well as vision loss and cognitive impairment.
3. Chronic progressive external ophthalmoplegia (CPEO): This is a rare disorder that affects the muscles of the eyes and the extraocular system. It is characterized by progressive weakness of the eye muscles, which can lead to droopy eyelids, double vision, and other vision problems.
4. Mitochondrial DNA depletion syndrome: This is a group of disorders that are caused by a decrease in the amount of mitochondrial DNA. These disorders can affect various parts of the body, including the brain, muscles, and other organs. They can cause a wide range of symptoms, including muscle weakness, seizures, and vision loss.
5. Myoclonic dystonia: This is a rare genetic disorder that affects the muscles and the nervous system. It is characterized by muscle stiffness, spasms, and myoclonus (involuntary jerky movements).
6. Neuronal ceroid lipofuscinoses (NCL): These are a group of rare genetic disorders that affect the brain and the nervous system. They can cause progressive loss of cognitive and motor functions, as well as vision loss and seizures.
7. Spinocerebellar ataxia: This is a group of rare genetic disorders that affect the cerebellum and the spinal cord. They can cause progressive weakness, coordination problems, and other movement disorders.
8. Friedreich's ataxia: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive loss of coordination and balance, as well as muscle weakness and wasting.
9. Charcot-Marie-Tooth disease: This is a group of rare genetic disorders that affect the peripheral nerves. They can cause muscle weakness, numbness or tingling in the hands and feet, and other problems with movement and sensation.
10. Progressive supranuclear palsy: This is a rare genetic disorder that affects the brain and the nervous system. It is characterized by progressive loss of movement control, as well as dementia and behavioral changes.

It is important to note that this list is not exhaustive and there may be other rare movement disorders that are not included here. If you suspect that you or a loved one may have a rare movement disorder, it is important to consult with a healthcare professional for proper diagnosis and treatment.

... (EC 6.3.2.31, CofE-AF, MJ0768, CofE) is an enzyme with systematic name L-glutamate:coenzyme ... Coenzyme+F420-0:L-glutamate+ligase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... coenzyme F420-0 + L-glutamate ⇌ {\displaystyle \rightleftharpoons } GDP + phosphate + coenzyme F420-1 This protein catalyses ... Li H, Graupner M, Xu H, White RH (August 2003). "CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme ...

https://en.wikipedia.org/wiki/Coenzyme_F420-0:L-glutamate_ligase

Coenzyme F420-1:γ-L-glutamate ligase (EC 6.3.2.34, F420:gamma-glutamyl ligase, CofE-AF, MJ0768, CofE) is an enzyme with ... coenzyme F420-1 ligase (GDP-forming). This enzyme catalyses the following chemical reaction GTP + coenzyme F420-1 + L-glutamate ... Coenzyme+F420-1:gamma-L-glutamate+ligase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Li H, Graupner M, Xu H, White RH (August 2003). "CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme ...

https://en.wikipedia.org/wiki/Coenzyme_F420-1:gamma-L-glutamate_ligase

Coenzyme gamma-F420-2:α-L-glutamate ligase (EC 6.3.2.32, MJ1001, CofF protein, gamma-F420-2:alpha-L-glutamate ligase) is an ... Coenzyme+gamma-F420-2:alpha-L-glutamate+ligase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... coenzyme α-F420-3 The enzyme caps the γ-glutamyl tail of the hydride carrier [[coenzyme F420]]. Li H, Xu H, Graham DE, White RH ... August 2003). "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and ...

https://en.wikipedia.org/wiki/Coenzyme_gamma-F420-2:alpha-L-glutamate_ligase

... ligase (AMP-forming). Other names in common use include: biotin-[acetyl-CoA carboxylase] synthetase, biotin-[acetyl coenzyme A ... carbon-dioxide ligase (ADP-forming)] The 3 substrates of this enzyme are ATP, biotin, and apo-[acetyl-CoA:carbon-dioxide ligase ... In enzymology, a biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) is an enzyme that catalyzes the chemical reaction ATP + ... The systematic name of this enzyme class is biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ...

https://en.wikipedia.org/wiki/Biotin—(acetyl-CoA-carboxylase)_ligase

CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family ... Sieweke HJ, Leistner E (August 1991). "o-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) ... o-Succinylbenzoate-CoA ligase (EC 6.2.1.26), encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in ... The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This enzyme is a tetramer, meaning it has four ...

https://en.wikipedia.org/wiki/O-succinylbenzoate—CoA_ligase

... and coenzyme A (CoA), whereas its 3 products are AMP, diphosphate, and oxalyl-CoA. This enzyme belongs to the family of ligases ... The systematic name of this enzyme class is oxalate:CoA ligase (AMP-forming). Other names in common use include oxalyl-CoA ... In enzymology, an oxalate-CoA ligase (EC 6.2.1.8) is an enzyme that catalyzes the chemical reaction ATP + oxalate + CoA ⇌ {\ ... Giovanelli J (1966). "Oxalyl-coenzyme A synthetase from pea seeds". Biochim. Biophys. Acta. 118 (1): 124-43. doi:10.1016/s0926- ...

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

Coenzyme A Ligase in Hybrid Poplar". Plant Physiology. 116 (2): 743-754. doi:10.1104/pp.116.2.743. ISSN 0032-0889. PMC 35134. ... In the second step, 4-coumarate-CoA ligase (4CL) converts cinnamic acid to cinnamoyl-CoA by an acid-thiol ligation. 4CL uses ... Li, Zhi; Nair, Satish K. (2015-11-03). "Structural Basis for Specificity and Flexibility in a Plant 4-Coumarate:CoA Ligase". ... Beuerle, Till; Pichersky, Eran (2002-03-15). "Enzymatic Synthesis and Purification of Aromatic Coenzyme A Esters". Analytical ...

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

... (EC 6.2.1.7, BAL, bile acid CoA ligase, bile acid coenzyme A ligase, choloyl-CoA synthetase, choloyl ... Wheeler JB, Shaw DR, Barnes S (December 1997). "Purification and characterization of a rat liver bile acid coenzyme A ligase ... strain VPI 12708 encodes a bile acid-coenzyme A ligase". Journal of Bacteriology. 174 (7): 2065-71. PMC 205821. PMID 1551828. ... CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase, 3alpha,7alpha,12alpha-trihydroxy-5beta- ...

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

Wilson DB, Prescott SM, Majerus PW (1982). "Discovery of an arachidonoyl coenzyme A synthetase in human platelets". J. Biol. ... 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 + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

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

The systematic name of this enzyme class is 2-furoate:CoA ligase (AMP-forming). This enzyme is also called 2-furoyl coenzyme A ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. ... In enzymology, a 2-furoate-CoA ligase (EC 6.2.1.31) is an enzyme that catalyzes the chemical reaction ATP + 2-furoate + CoA ...

https://en.wikipedia.org/wiki/2-furoate—CoA_ligase

Ehlting, J.; Shin, J. J.; Douglas, C. J. (September 2001). "Identification of 4-coumarate:coenzyme A ligase (4CL) substrate ...

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

Loffler F, Muller R, Lingens F (1992). "Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. ... 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 ... systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate ...

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

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

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

4-hydroxybenzoate-coenzyme A ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A synthetase, and 4-hydroxybenzoyl-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-hydroxybenzoate-CoA ligase (EC 6.2.1.27) is an enzyme that catalyzes the chemical reaction ATP + 4- ... Merkel SM, Eberhard AE, Gibson J, Harwood CS (1989). "Involvement of coenzyme A thioesters in anaerobic metabolism of 4- ...

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

This gene encodes the alpha subunit of the heterodimeric enzyme succinate coenzyme A ligase. This enzyme is targeted to the ... "Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA ... Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial is an enzyme that in humans is encoded by the SUCLG1 gene. The ... Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic ...

https://en.wikipedia.org/wiki/SUCLG1

The systematic name of this enzyme class is geranoyl-CoA:carbon-dioxide ligase (ADP-forming). Other names in common use include ... geranoyl coenzyme A carboxylase, and geranyl-CoA carboxylase. It employs one cofactor, biotin. Seubert W, Fass E, Remberger U ( ... Portal: Biology v t e (EC 6.4.1, Biotin enzymes, Enzymes of unknown structure, All stub articles, Ligase stubs). ... This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. ...

https://en.wikipedia.org/wiki/Geranoyl-CoA_carboxylase

No FAD binding is observed in oxalyl-CoA decarboxylase, but an excess of coenzyme A in the crystal structure has led to the ... Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz AL, Allison MJ (July 1990). "Purification and ... lactis: impact of acidic conditions on the transcriptional levels of the oxalyl coenzyme A (CoA) decarboxylase and formyl-CoA ... Other names in common use include oxalyl coenzyme A decarboxylase, and oxalyl-CoA carboxy-lyase. This enzyme participates in ...

https://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase

"Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... "Synthases and Ligases". IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN), and Nomenclature Commission of IUB (NC- ... Galperin MY, Koonin EV (1997). "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". ...

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

"Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin ... Tetrahydrosarcinapterin synthase (EC 6.3.2.33, H4MPT:alpha-L-glutamate ligase, MJ0620, MptN protein) is an enzyme with ... systematic name tetrahydromethanopterin:alpha-L-glutamate ligase (ADP-forming). This enzyme catalyses the following chemical ...

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

Mue S, Tuboi S, Kikuchi G (December 1964). "On malyl-coenzyme A synthetase". J. Biochem. 56: 545-551. PMID 14244056. Portal: ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... malyl coenzyme A synthetase, and malate thiokinase. This enzyme participates in glyoxylate and dicarboxylate metabolism. ...

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

Izumi Y, Morita H, Sato K, Tani Y, Ogata K (1972). "Synthesis of biotin-vitamers from pimelic acid and coenzyme A by cell-free ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 6-carboxyhexanoate-CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction ATP + 6- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

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

... and biotinyl coenzyme A synthetase. This enzyme participates in biotin metabolism. CHRISTNER JE, SCHLESINGER MJ, COON MJ (1964 ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a biotin-CoA ligase (EC 6.2.1.11) is an enzyme that catalyzes the chemical reaction ATP + biotin + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

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

The protein encoded by this gene is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in ... Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y (Oct 1998). "Assignment of human fatty-acid-coenzyme A ligase, very ... Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA (1999). "Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA ...

https://en.wikipedia.org/wiki/Very_long-chain_acyl-CoA_synthetase

... the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... Phosphopantothenate-cysteine ligase from the bacterium Escherichia coli uses cytidine triphosphate (CTP) as an energy donor, ... In enzymology, a phosphopantothenate-cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme ( ...

https://en.wikipedia.org/wiki/Phosphopantothenate—cysteine_ligase

Schuhle, K.; Gescher, J.; Feil, U.; Paul, M.; Jahn, M.; Schagger, H.; Fuchs, G. (2003). "Benzoate-Coenzyme A Ligase from ...

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

Edgar AJ, Polak JM (Mar 2000). "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs". ... of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase ... which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The encoded ...

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

... (SCS, also known as succinyl-CoA synthetase or succinate thiokinase or succinate-CoA ligase) is ... Biology portal Citric acid cycle Succinate dehydrogenase Succinate-CoA ligase (ADP-forming) Succinate-CoA ligase (GDP-forming) ... "Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA ... Succinyl+Coenzyme+A+Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) (Metabolism, EC 6.2). ...

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

... and acyl coenzyme A synthetase (guanosine diphosphate forming). Rossi CR, Gibson DM (June 1964). "Activation of fatty acids by ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acid-CoA ligase (GDP-forming) (EC 6.2.1.10) is an enzyme that catalyzes the chemical reaction GTP + an acid ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...

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

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in ... Fatty acid-CoA ligase 4 (FACL4), the protein encoded by the ACSL4 gene, is an acyl-CoA synthetase, which is an essential class ... Hu, C; Chen, L; Jiang, Y; Li, Y; Wang, S (January 2008). "The effect of fatty acid-CoA ligase 4 on the growth of hepatic cancer ... 2003). "A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal ...

https://en.wikipedia.org/wiki/ACSL4

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in ... Long-chain-fatty-acid-CoA ligase 5 is an enzyme that in humans is encoded by the ACSL5 gene. ...

https://en.wikipedia.org/wiki/ACSL5

2000). "The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase". J. Biol. Chem. 275 (21 ... Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA (Oct 1999). "Human liver-specific very-long-chain acyl-coenzyme A synthetase: ...

https://en.wikipedia.org/wiki/SLC27A6

Coumarate is condensed with coenzyme-A in the presence of 4-coumarate-CoA ligase: ATP + 4-coumarate + CoA ⇌ {\displaystyle \ ... Coumaroyl-coenzyme A is the thioester of coenzyme-A and coumaric acid. Coumaroyl-coenzyme A is a central intermediate in the ... Thioesters of coenzyme A, Hydroxycinnamic acid esters, Vinylogous carboxylic acids, All stub articles, Aromatic compound stubs) ... O-hydroxycinnamoyltransferase Anthocyanin 5-aromatic acyltransferase Chalcone synthase 4-Coumarate-CoA ligase 6'-Deoxychalcone ...

https://en.wikipedia.org/wiki/Coumaroyl-CoA

CS1 maint: uses authors parameter, Articles with short description, Short description matches Wikidata, Ligases, Organometallic ... "Elucidation of the biosynthesis of the methane catalyst coenzyme F430". Nature. 543 (7643): 78-82. doi:10.1038/nature21427. ...

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

... methylmalonyl Coenzyme A mutase (6p12.3) NHLRC1: NHL repeat containing E3 ubiquitin protein ligase 1 (6p22.3) NOL7: nucleolar ... ubiquitin protein ligase E3 component n-recognin 2 (6p21.2) UNC5CL: encoding protein Unc-5 homolog C (C. elegans)-like VEGF: ... E3 ubiquitin protein ligase 1 (6q21) HEBP2: heme binding protein 2 (6q24.1) IDDM8: insulin dependent diabetes mellitus 8 IDDM15 ...

https://en.wikipedia.org/wiki/Chromosome_6

HSCoA, Coenzyme A. L-Tyr, L-tyrosine, L-Phe, L-phenylalanine. Flavan-3-ols are abundant in teas derived from the tea plant ... CoA-ligase, E5, chalcone synthase (naringenin-chalcone synthase), E6, chalcone isomerase, E7, Flavonoid 3'-hydroxylase, E8, ... These enzyme do not use ACPSs, but instead employ coenzyme A esters and have a single active site to perform the necessary ...

https://en.wikipedia.org/wiki/Flavan-3-ol

Accordingly, many p97/CDC48 coenzymes and adaptors have domains that can recognize ubiquitin. It has become evident that the ... Some p97-interacting proteins are also enzymes such as N-glycanase, ubiquitin ligase, and deubiquitinase, which assist p97 in ...

https://en.wikipedia.org/wiki/Valosin-containing_protein

... coenzyme F420-0:L-glutamate ligase EC 6.3.2.35: D-alanine-D-serine ligase EC 6.3.2.36: 4-phosphopantoate-β-alanine ligase EC ... coenzyme F420-0:L-glutamate ligase EC 6.3.2.32: coenzyme γ-F420-2:α-L-glutamate ligase EC 6.3.2.33: tetrahydrosarcinapterin ... 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 6.2.1.10: ... threonine-tRNA ligase EC 6.1.1.4: leucine-tRNA ligase EC 6.1.1.5: isoleucine-tRNA ligase EC 6.1.1.6: lysine-tRNA ligase EC 6.1. ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)

The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names ... Roth JR, Lawrence JG, Bobik TA (1996). "Cobalamin (coenzyme B12): synthesis and biological significance" (PDF). Annu. Rev. ... c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans". J. Bacteriol. 174 (22): 7445-7451. doi:10.1128/jb. ... c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans". J. Bacteriol. 174 (22): 7445-51. doi:10.1128/JB. ...

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

Pyruvate is oxidized into acetyl coenzyme A catalyzed by pyruvate:ferredoxin oxidoreductase. Two molecules of carbon dioxide ( ... also known as butyrate-CoA ligase. The metabolite produced by this reaction is butyryl-CoA, and is produced as follows: ... Butyric acid is metabolized by various human XM-ligases (ACSM1, ACSM2B, ASCM3, ACSM4, ACSM5, and ACSM6), ... Adenosine triphosphate + butyric acid + coenzyme A → adenosine monophosphate + pyrophosphate + butyryl-CoA As a short-chain ...

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

PCC has been classified both as a ligase and a lyase. The enzyme is biotin-dependent. The product of the reaction is (S)- ... holoenzyme of propionyl-coenzyme A carboxylase". Nature. 466 (7309): 1001-1005. doi:10.1038/nature09302. PMC 2925307. PMID ...

https://en.wikipedia.org/wiki/Propionyl-CoA_carboxylase

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in ... Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT (May 1997). "Human acyl-coenzyme A synthetase 3 cDNA and ... Long-chain-fatty-acid-CoA ligase 3 is an enzyme that in humans is encoded by the ACSL3 gene. ... "Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in ...

https://en.wikipedia.org/wiki/ACSL3

... catalyzed by phosphoribosylamine-glycine ligase (GAR synthetase). Due to the chemical lability of PRA, which has a half-life of ... which are transferred from the coenzyme tetrahydrofolate as 10-formyltetrahydrofolate, and a carbon atom from bicarbonate (1). ...

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

Long-chain-fatty-acid-CoA ligase catalyzes the reaction between a fatty acid with ATP to give a fatty acyl adenylate, plus ... Thiolase enzyme catalyzes the reaction when a new molecule of coenzyme A breaks the bond by nucleophilic attack on C3. This ... which are co-enzymes used in the electron transport chain. It is named as such because the beta carbon of the fatty acid ... requiring B12 as a coenzyme) to form succinyl-CoA. The succinyl-CoA formed can then enter the citric acid cycle. However, ...

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

Lysine residues 89 and 248 can become ubiquinated by ER-resident E3 ligases. The identity of the multiple E3 ligases involved ... HMG-CoA reductase (3-hydroxy-3-methyl-glutaryl-coenzyme A reductase, official symbol HMGCR) is the rate-controlling enzyme ( ... Song BL, Sever N, DeBose-Boyd RA (September 2005). "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and ... Meigs TE, Roseman DS, Simoni RD (April 1996). "Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the ...

https://en.wikipedia.org/wiki/HMG-CoA_reductase

... is a molecule formed by condensing the thiol group of coenzyme A (CoA) with the carboxylic acid group of 3 ... In organisms such as plants, this can be formed using the 3-hydroxybenzoate-CoA ligase enzyme. This uses ATP, 3-hydroxybenzoate ... "BRENDA - Information on EC 6.2.1.37 - 3-hydroxybenzoate-CoA ligase". www.brenda-enzymes.org. "bcrA - Benzoyl-CoA reductase ...

https://en.wikipedia.org/wiki/3-Hydroxybenzoyl-CoA

... may refer to: Church of England Council of Europe Coenzyme F420-0:L-glutamate ligase, an enzyme Coenzyme F420-1:gamma-L- ... glutamate ligase, an enzyme This disambiguation page lists articles associated with the title Cofe. If an internal link led you ...

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

... succinyl coenzyme A synthetase (adenosine diphosphate-forming), succinyl coenzyme A synthetase, A-STK (adenin nucleotide-linked ... This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ...

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

... hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional protein), alpha ... Ubiquitin ligase PLGLB2: Plasminogen-related protein B POLR1A: DNA-directed RNA polymerase I subunit RPA1 PREPL: Prolyl ... hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional protein), beta ... encoding protein Neuralized E3 ubiquitin protein ligase 3 NCL: Nucleolin NR4A2: nuclear receptor subfamily 4, group A, member 2 ...

https://en.wikipedia.org/wiki/Chromosome_2

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 6.2.1.10: ... Coenzyme Q - cytochrome c reductase EC 1.10.2.2 Category:EC 1.10.3 (with oxygen as acceptor) Catechol oxidase EC 1.10.3.1 ... ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2.1.26: o- ... Arachidonate-CoA ligase EC 6.2.1.16: Acetoacetate-CoA ligase EC 6.2.1.17: Propionate-CoA ligase EC 6.2.1.18: Citrate-CoA ligase ...

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

define Coenzyme A Ligases. Explain Coenzyme A Ligases. What is Coenzyme A Ligases? Coenzyme A Ligases FAQ. ... Coenzyme A Ligases. Medical Dictionary -> Coenzyme A Ligases. Search: Coenzyme A Ligases. Enzymes that catalyze the formation ...

http://medicaldictionaryweb.com/Coenzyme+A+Ligases-definition/

... phytanic acid to pristanic acid in peroxisomes isolated from human liver demonstrate that phytanoyl-CoA ligase is present in ... phytanoyl-CoA ligase * Coenzyme A Grant support * NS 22576/NS/NINDS NIH HHS/United States ... phytanoyl-CoA ligase regulates the alpha-oxidation of phytanic acid at the organellar (peroxisomal) level. ... phytanic acid to pristanic acid in peroxisomes isolated from human liver demonstrate that phytanoyl-CoA ligase is present in ...

https://pubmed.ncbi.nlm.nih.gov/8224157/

Succinate-CoA ligase deficiency is an inherited disorder that affects the early development of the brain and other body systems ... Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA ... Succinate-CoA ligase deficiency results from mutations in the SUCLA2 or SUCLG1 gene. SUCLG1 gene mutations can cause fatal ... Succinate-CoA ligase deficiency is an inherited disorder that affects the early development of the brain and other body systems ...

https://medlineplus.gov/genetics/condition/succinate-coa-ligase-deficiency/

MUT: methylmalonyl Coenzyme A mutase (6p12.3). *NHLRC1: NHL repeat containing E3 ubiquitin protein ligase 1 (6p22.3) ... UBR2: ubiquitin protein ligase E3 component n-recognin 2 (6p21.2). *UNC5CL: encoding protein Unc-5 homolog C (C. elegans)-like ... HACE1: HECT domain and Ankyrin repeat containing, E3 ubiquitin protein ligase 1 (6q21) ...

https://wikidoc.org/index.php/Chromosome_6

Enzymes and Coenzymes [D08] * Enzymes [D08.811] * Ligases [D08.811.464] * Ubiquitin-Protein Ligase Complexes [D08.811.464.938] ... They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.. Entry Term(s). ... They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.. Terms. ... Ligases (1989-2003). Ubiquitins (1986-1988). Public MeSH Note. 2004; UBIQUITIN-CONJUGATING ENZYME E2 ( UBIQUITIN-CONJUGATING ...

https://meshb.nlm.nih.gov/record/ui?ui=D044763

... or coenzyme Q10 (CoQ10). The third defense line present repair enzymes responsible for nucleic acids damage overhaul, e.g., DNA ... ligase (EC 6.5.1.1) [48].. ROS can inflict cell injury as an effect of reaction with lipids in cellular membranes [49], ...

https://link.springer.com/article/10.1186/s11671-017-2007-y

Coenzyme A Ligase Coenzyme A Synthetase Coenzyme A Synthetases Ligases, Acid-Thiol Ligases, Co A Ligases, Coenzyme A ... Coenzyme A Ligase. Coenzyme A Synthetase. Coenzyme A Synthetases. Ligases, Acid-Thiol. Ligases, Co A. Ligases, Coenzyme A. ... Coenzyme A Ligases Entry term(s). Acid Thiol Ligases Acid-Thiol Ligases Acyl CoA Synthetase Acyl CoA Synthetases Acyl Coenzyme ... Coenzyme A ligases Entry term(s):. Acid Thiol Ligases. Acid-Thiol Ligases. Acyl CoA Synthetase. Acyl CoA Synthetases. Acyl ...

https://decs.bvsalud.org/en/ths/resource/?id=3097

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Ligases [D08.811.464]. *Ubiquitin-Protein Ligase Complexes [D08.811.464.938] ... KEAP1 E3 ligase-mediated downregulation of NF-kappaB signaling by targeting IKKbeta. Mol Cell. 2009 Oct 09; 36(1):131-40. ... BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs. Nature. 2012 Nov 22; 491(7425):618-21. ... They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES. ...

https://profiles.uchicago.edu/profiles/display/28145

4-coumarate coenzyme CoA ligase (Fs4CL); and F. suspensa Caffeoyl-CoA O-methyltransferase (FsCCoAOMT) etc. The qRT-PCR ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=au:Hou,+Dianyun

Align Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 ( ... Align candidate WP_011386526.1 AMB_RS21140 (acetate--CoA ligase) to HMM TIGR02188 (acs: acetate--CoA ligase (EC 6.2.1.1)) ... to candidate WP_011386526.1 AMB_RS21140 acetate--CoA ligase. Query= SwissProt::P27550 (652 letters) >NCBI__GCF_000009985.1:WP_ ... CoA ligase # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to envfrom env to acc ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=NCBI__GCF_000009985.1&path=4-hydroxybenzoate&step=acs&locusId=WP_011386526.1

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Ligases [D08.811.464]. *Carbon-Carbon Ligases [D08.811.464.257] ...

https://profiles.ucdenver.edu/display/219348

ALDH2 directly oxidizes formaldehyde to formic acid by using NAD+ as a coenzyme [28]. ADH3 and ALDH2, metabolizing enzymes of ... Keap1 binds to E3 ubiquitin ligase and promotes ubiquitination and degradation of Nrf2 [27] and prevents the nuclear ...

https://www.hindawi.com/journals/omcl/2022/5981353/

A benzoate-coenzyme A ligase from Rhodopseudomonas palustris was also included in some constructs. Fermentations with the ... A benzoate-coenzyme A ligase from Rhodopseudomonas palustris was also included in some constructs. Fermentations with the ... A benzoate-coenzyme A ligase from Rhodopseudomonas palustris was also included in some constructs. Fermentations with the ... A benzoate-coenzyme A ligase from Rhodopseudomonas palustris was also included in some constructs. Fermentations with the ...

https://cris.vtt.fi/en/publications/heterologous-production-of-the-antifugal-polyketide-antibiotic-so

HACE1: HECT domain and Ankyrin repeat containing, E3 ubiquitin protein ligase 1 (6q21) ... MUT: methylmalonyl Coenzyme A mutase. *MYO6: myosin VI. *PARK2: Parkinson disease (autosomal recessive, juvenile) 2, parkin ...

https://tl.wikipedia.org/wiki/Kromosomang_6_

... ligase activity, forming aminoacyl-tRNA and related compounds;6.88236359218716e-08!GO:0004812;aminoacyl-tRNA ligase activity; ... coenzyme biosynthetic process;1.60379902949655e-07!GO:0044431;Golgi apparatus part;1.68507473802442e-07!GO:0006888;ER to Golgi ... small conjugating protein ligase activity;3.08030010980232e-10!GO:0004842;ubiquitin-protein ligase activity;3.93503033545011e- ... acid-amino acid ligase activity;4.27841701028717e-09!GO:0008219;cell death;5.47883239669253e-09!GO:0016265;death; ...

https://fantom.gsc.riken.jp/resource_browser/index.php?title=FF:10693-109F9&action=edit

coumarate-CoA ligase (4CL). These enzymes represent the first steps in the phenylpropanoid pathway and convert l-phenylalanine ... Coniferyl alcohol is derived from the reduction of cinnamic acid by a NADPH-dependent reaction with coenzyme A, followed by ...

https://www.intechopen.com/chapters/75709

phenylalanine-tRNA ligase complex phosphatase complex + A protein complex which is capable of phosphatase activity. ... methyl-tetrahydromethanopterin:coenzyme M methyltransferase complex methylcrotonoyl-CoA carboxylase complex + mitochondrial ...

https://rgd.mcw.edu/rgdweb/ontology/view.html?acc_id=GO:1903293

... coenzyme (non-protein organic part). Holoenzyme (active enzyme) Apoenzyme + Coenzyme (protein part) (non-protein part) 9 ... 6. Ligases : Enzymes catalysing the synthetic reactions (Greek : ligate-to bind) where two molecules are joined together and ... chemistry of enzymes, ES complex theories, co factors and coenzymesmuti ullah3.1K. visualizações•28. slides ... coenzyme (if any) and the type of the reaction catalysed by the enzyme. ...

https://pt.slideshare.net/sayalipowar/chapter-6pptx-256740567

Acetyl Coenzyme A 100% * Acetylation 79% * Histones 71% * Fear 66% * Acetate-CoA Ligase 63% ...

https://profiles.wustl.edu/en/organisations/center-for-drug-discovery/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle

"Coenzyme metabolism.coenzyme A synthesis.pantothenate synthesis.pantoate:beta-alanine ligase","protein_coding" "Cre02.g107300 ... ","alanine-tRNA ligase","protein_coding" "Gb_36250","No alias","Gingko biloba","no hits & (original description: none)"," ... ","Coenzyme metabolism.iron-sulfur cluster assembly machineries.plastidial SUF system.transfer phase.HCF101 component","protein ... ","Methionine--tRNA ligase, cytoplasmic OS=Arabidopsis thaliana","protein_coding" "Cre08.g379650","No alias","Chlamydomonas ...

https://evorepro.sbs.ntu.edu.sg/go/sequences/table/5383

2-amino-3-ketobutyrate coenzyme A ligase. QuickGO ontology. BLASTP. 79124. 80149. 1026. L-threonine 3-dehydrogenase. QuickGO ... lipid A core - O-antigen ligase and related enzyme. QuickGO ontology. BLASTP. ...

http://pregi.bi.up.ac.za/pre_gi_gene.php?source_accession=NC_013508&gi_accession=NC_013508:63914

Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), Biotin protein ligase, Helix-turn-helix [Interproscan]."," ... ","hydroxymethylglutaryl-CoA synthase [Ensembl]. Hydroxymethylglutaryl-coenzyme A synthase C-terminal domain [Interproscan]."," ... ","D-alanine-D-alanine ligase A [Ensembl]. D-ala D-ala ligase C-terminus, D-ala D-ala ligase N-terminus [Interproscan]."," ... ","lipoate-protein ligase A [Ensembl]. catalytic domain, Biotin/lipoate A/B protein ligase family [InterProScan].","protein_ ...

https://bacteria.sbs.ntu.edu.sg/go/sequences/table/24159

Text is available under the Creative Commons Attribution-ShareAlike License 3.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization ...

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

... and coenzyme-A binding in fatty acid β-oxidation and tricarboxylic acid cycle enzymes. These changes show a remarkable ... Succinyl-CoA ligase deficiency in pro-inflammatory and tissue-invasive T cells. Cell Metab. 32, 967-980.e965 (2020). ... and coenzyme-A binding in fatty acid β-oxidation and tricarboxylic acid cycle enzymes. These changes show a remarkable ...

https://www.nature.com/articles/s43587-023-00366-5?error=cookies_not_supported&code=c95c1bae-dba3-4bc8-84be-6927eea47be9

... precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence ... 3, 363-377 (1996) REFERENCE 7 AUTHORS Arn,E.A. and Abelson,J.N. TITLE The 2-5 RNA ligase of Escherichia coli. Purification, ... CoA ligase genes in parsley JOURNAL Eur. J. Biochem. 176, 661-667 (1988) REFERENCE 75 AUTHORS Jaiswal,A.K., McBride,O.W., ...

http://getentry.ddbj.nig.ac.jp/getentry/aa/BAB96591.1

A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate ... Ubiquitin lysine 63 chain-forming ligases regulate apical dominance in Arabidopsis. Plant Cell 19 (6), pp. 1898 - 1911 (2007) ...

https://www.mpipz.mpg.de/publication-search/4670802?deactivate_global_blacklist=false&page=1&person=%2Fpersons%2Fresource%2Fpersons39949

Note: In a study on Japanese patients, Atorvastatin reduced Coenzyme Q10 level but not Pitavastatin (Ref.). I think this aspect ... Reductase-Insig binding results in recruitment of a membrane-associated ubiquitin ligase called gp78, which initiates ... The target of pitavastatin, hydroxymethylglutarate coenzyme-A reductase (HMGCR), was found to be over-expressed in all ovarian ... These adverse effects may be due to a coenzyme Q10 (CoQ10) deficiency because inhibition of cholesterol biosynthesis also ...

https://www.cancertreatmentsresearch.com/cholesterol-lowering-statin-drugs-to-fight-cancer/

UBIQUITIN-PROTEIN Enzymes Protein Enzyme Glutamate Escherichia Substrate Gene Live only into childhood or adolescence Succinate-coenzyme Subunit Deficiency Mutations

They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES . (nih.gov)
They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES. (uchicago.edu)

6. Ligases : Enzymes catalysing the synthetic reactions (Greek : ligate-to bind) where two molecules are joined together and ATP is used. (slideshare.net)
Specifically, we identify age-related changes in protein cross-links relating to assembly of electron transport system complexes I and IV, activity of glutamate dehydrogenase, and coenzyme-A binding in fatty acid β-oxidation and tricarboxylic acid cycle enzymes. (nature.com)

coenzyme (non-protein organic part). (slideshare.net)

Studies of the intraorganellar site of alpha-oxidation of [1-14C]phytanic acid to pristanic acid in peroxisomes isolated from human liver demonstrate that phytanoyl-CoA ligase is present in the peroxisomal membrane and that the enzyme system for alpha-oxidation of phytanic acid to pristanic acid is in the peroxisomal matrix. (nih.gov)
The SUCLA2 and SUCLG1 genes each provide instructions for making one part (subunit) of an enzyme called succinate-CoA ligase. (medlineplus.gov)
Each enzyme is given a specific name indicating the substrate, coenzyme (if any) and the type of the reaction catalysed by the enzyme. (slideshare.net)

Glutamate-cysteine ligase family 2(GCS2) [Interproscan]. (ntu.edu.sg)

3, 363-377 (1996) REFERENCE 7 AUTHORS Arn,E.A. and Abelson,J.N. TITLE The 2'-5' RNA ligase of Escherichia coli. (nig.ac.jp)

Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. (uchicago.edu)

Succinate-CoA ligase deficiency results from mutations in the SUCLA2 or SUCLG1 gene. (medlineplus.gov)
Mutations in either the SUCLA2 or SUCLG1 gene disrupt the normal function of succinate-CoA ligase. (medlineplus.gov)

These infections can be life-threatening, and most people with succinate-CoA ligase deficiency live only into childhood or adolescence. (medlineplus.gov)

DNA sequencing revealed a homozygous 2-bp deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle enzyme succinate-coenzyme A ligase (SUCL). (nih.gov)

The SUCLA2 and SUCLG1 genes each provide instructions for making one part (subunit) of an enzyme called succinate-CoA ligase. (medlineplus.gov)

Succinate-CoA ligase deficiency is an inherited disorder that affects the early development of the brain and other body systems. (medlineplus.gov)
Most children with succinate-CoA ligase deficiency also experience a failure to thrive, which means that they gain weight and grow more slowly than expected. (medlineplus.gov)
Succinate-CoA ligase deficiency causes breathing difficulties that often lead to recurrent infections of the respiratory tract. (medlineplus.gov)
A few individuals with succinate-CoA ligase deficiency have had an even more severe form of the disorder known as fatal infantile lactic acidosis. (medlineplus.gov)
Although the exact prevalence of succinate-CoA ligase deficiency is unknown, it appears to be very rare. (medlineplus.gov)
Succinate-CoA ligase deficiency results from mutations in the SUCLA2 or SUCLG1 gene. (medlineplus.gov)
These problems lead to hypotonia, muscle weakness, and the other characteristic features of succinate-CoA ligase deficiency. (medlineplus.gov)

Mutations in either the SUCLA2 or SUCLG1 gene disrupt the normal function of succinate-CoA ligase. (medlineplus.gov)

Anatomy8

Organisms15

Diseases1

Chemicals and Drugs151

Analytical, Diagnostic and Therapeutic Techniques and Equipment20

Phenomena and Processes57

Technology, Industry, Agriculture1

Information Science4

Health Care1

Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. (1/783)

The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat. (2/783)

Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane. (3/783)

Development and initial evaluation of a novel method for assessing tissue-specific plasma free fatty acid utilization in vivo using (R)-2-bromopalmitate tracer. (4/783)

Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35. (5/783)

Preventing neurodegeneration in the Drosophila mutant bubblegum. (6/783)

The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. (7/783)

Biosynthesis of 1,2-dieicosapentaenoyl-sn-glycero-3-phosphocholine in Caenorhabditis elegans. (8/783)

Ubiquitin-Protein Ligases

Coenzyme A

Coenzymes

DNA Ligases

SKP Cullin F-Box Protein Ligases

Coenzyme A Ligases

Cullin Proteins

Ubiquinone

Ubiquitination

Acetyl Coenzyme A

Polynucleotide Ligases

Ubiquitin

RING Finger Domains

Ubiquitin-Conjugating Enzymes

Cobamides

Coenzyme A-Transferases

RNA Ligase (ATP)

Hydroxymethylglutaryl CoA Reductases

Mesna

Molecular Sequence Data

Amino Acid Sequence

Substrate Specificity

F-Box Proteins

NAD

Endosomal Sorting Complexes Required for Transport

Peptide Synthases

Pantothenic Acid

Ubiquitins

Proteasome Endopeptidase Complex

Kinetics

Protein Binding

Protein Structure, Tertiary

Ubiquitin-Protein Ligase Complexes

Polyubiquitin

Euryarchaeota

Ubiquitin-Activating Enzymes

Propanediol Dehydratase

Carbon-Oxygen Ligases

Catalysis

Sequence Homology, Amino Acid

Binding Sites

Proto-Oncogene Proteins c-cbl

Methanosarcina barkeri

Mutation

NADP

Acetate-CoA Ligase

Proteolysis

Mevalonic Acid

Hydroxymethylglutaryl-CoA Reductase Inhibitors

Alcohol Oxidoreductases

S-Phase Kinase-Associated Proteins

Riboflavin

Protein Inhibitors of Activated STAT

Pantetheine

SUMO-1 Protein

Small Ubiquitin-Related Modifier Proteins

Adenosine Monophosphate

Escherichia coli

Palmitoyl Coenzyme A

Models, Molecular

Methanobacterium

Lovastatin

Malonyl Coenzyme A

Sequence Alignment

Cloning, Molecular

Saccharomyces cerevisiae

Sumoylation

Carrier Proteins

Saccharomyces cerevisiae Proteins

Amino Acid Motifs

Oxidoreductases

Pyridoxal Phosphate

Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent

Methylmalonyl-CoA Mutase

Crystallography, X-Ray

Base Sequence

Lysine

Recombinant Proteins

Cell Line

Bacterial Proteins