Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
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.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
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.
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.
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.
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 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 phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.
An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.
The rate dynamics in chemical or physical systems.
A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.
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.
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).
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.
An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
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 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)
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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 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.
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)
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
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.
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.
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.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
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.
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.
An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.
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.
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.
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.
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.-.
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.
The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.
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.
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.
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.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A 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 found in any species of bacterium.
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.
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.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Biological catalysts and their cofactors.
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)
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.
Compounds based on 2-amino-4-hydroxypteridine.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
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 art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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)
The 4-aminomethyl form of VITAMIN B 6. During transamination of amino acids, PYRIDOXAL PHOSPHATE is transiently converted into pyridoxamine phosphate.
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.
Proteins found in any species of archaeon.
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.
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.
The sum of the weight of all the atoms in a molecule.
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.
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 antilipemic fungal metabolite isolated from cultures of Nocardia autotrophica. It acts as a competitive inhibitor of HMG CoA reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES).
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.
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).
A strongly basic anion exchange resin whose main constituent is polystyrene trimethylbenzylammonium Cl(-) anion.
Salts and esters of hydroxybutyric acid.
The functional hereditary units of BACTERIA.
An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.
A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.
A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Azoles of one NITROGEN and two double bonds that have aromatic chemical properties.
The functional genetic units of ARCHAEA.
Proteins prepared by recombinant DNA technology.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
Cholesterol which is substituted by a hydroxy group in any position.
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.
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.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
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.
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 study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
The 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 complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.
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).
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
Compounds containing the -SH radical.
Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
The formation of dense connective tissue in the TYMPANIC MEMBRANE that does not necessarily cause or lead to loss of hearing.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
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.
Benzoate derivatives substituted by one or more hydroxy groups in any position on the benzene ring.
Fatty acids which are unsaturated in only one position.
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.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Compounds based on 5,6,7,8-tetrahydrofolate.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
A rare autosomal recessive degenerative disorder which usually presents in late childhood or adolescence. Clinical manifestations include progressive MUSCLE SPASTICITY; hyperreflexia; MUSCLE RIGIDITY; DYSTONIA; DYSARTHRIA; and intellectual deterioration which progresses to severe dementia over several years. (From Adams et al., Principles of Neurology, 6th ed, p972; Davis & Robertson, Textbook of Neuropathology, 2nd ed, pp972-929)
Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.
Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
Two-ring crystalline hydrocarbons isolated from coal tar. They are used as intermediates in chemical synthesis, as insect repellents, fungicides, lubricants, preservatives, and, formerly, as topical antiseptics.
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.
Substances used to lower plasma CHOLESTEROL levels.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
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.
Organic substances that are required in small amounts for maintenance and growth, but which cannot be manufactured by the human body.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
Salts and derivatives of acetoacetic acid.
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
An enzyme of the transferase class that catalyzes the conversion of sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate to D-ribose 5-phosphate and D-xylulose 5-phosphate in the PENTOSE PHOSPHATE PATHWAY. (Dorland, 27th ed) EC 2.2.1.1.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.
A class of compounds composed of repeating 5-carbon units of HEMITERPENES.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
Measurement of the intensity and quality of fluorescence.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Polymers of organic acids and alcohols, with ester linkages--usually polyethylene terephthalate; can be cured into hard plastic, films or tapes, or fibers which can be woven into fabrics, meshes or velours.
An antilipemic agent which lowers cholesterol, triglycerides, serum beta-lipoproteins and phospholipids. It acts by interfering with the enzymatic steps involved in the conversion of acetate to hydroxymethylglutaryl coenzyme A as well as inhibiting the activity of HYDROXYMETHYLGLUTARYL COA REDUCTASES which is the rate limiting enzyme in the biosynthesis of cholesterol.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A family of enzymes that catalyze the stereoselective, regioselective, or chemoselective syn-dehydrogenation reactions. They function by a mechanism that is linked directly to reduction of molecular OXYGEN.
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 genus of gram-positive, rod-shaped bacteria whose cells occur singly, in pairs or short chains, in V or Y configurations, or in clumps resembling letters of the Chinese alphabet. Its organisms are found in cheese and dairy products as well as on human skin and can occasionally cause soft tissue infections.
A class of enzymes that transfers nucleotidyl residues. EC 2.7.7.
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.
An essential amino acid that is required for the production of HISTAMINE.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
An order of anaerobic, coccoid to rod-shaped methanogens, in the kingdom EURYARCHAEOTA. They are nonmotile, do not catabolize carbohydrates, proteinaceous material, or organic compounds other than formate or carbon monoxide, and are widely distributed in nature.
The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)

Dietary pantothenic acid requirement of juvenile grass shrimp, Penaeus monodon. (1/978)

A feeding trial was conducted to estimate the minimal dietary pantothenic acid (PA) requirement for juvenile grass shrimp, Penaeus monodon. Purified diets with seven levels (0, 20, 40, 60, 120, 240, and 480 mg/kg) of supplemental PA were fed to P. monodon (mean weight 0.88 +/- 0.01 g) for 8 wk. The level of PA detected in the unsupplemented diet was 0.02 mg/kg. Each diet was fed to three replicate groups of shrimp. Feed efficiencies (FE) and protein efficiency ratios were highest in shrimp fed the diets supplemented with 120, 240, and 480 mg PA/kg diet, followed by the groups fed 60 mg/kg, then 40 mg/kg, and finally the unsupplemented control group (P < 0.05). Shrimp fed diets supplemented with PA had significantly higher survival percentages and lower hepatopancreatic lipid concentration than those fed the unsupplemented, control diets. Broken-line regression analyses of weight gain percentage and hepatopancreatic CoA and PA concentrations of the shrimp indicated that the adequate dietary PA concentration in growing P. monodon is 101-139 mg/kg.  (+info)

High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2). (2/978)

Binding of fluorescent fatty acids to bovine liver non-specific lipid-transfer protein (nsL-TP) was assessed by measuring fluorescence resonance energy transfer (FRET) between the single tryptophan residue of nsL-TP and the fluorophore. Upon addition of pyrene dodecanoic acid (Pyr-C12) and cis-parinaric acid to nsL-TP, FRET was observed indicating that these fatty acids were accommodated in the lipid binding site closely positioned to the tryptophan residue. Substantial binding was observed only when these fatty acids were presented in the monomeric form complexed to beta-cyclodextrin. As shown by time-resolved fluorescence measurements, translocation of Pyr-C12 from the Pyr-C12-beta-cyclodextrin complex to nsL-TP changed dramatically the direct molecular environment of the pyrene moiety: i.e. the fluorescence lifetime of the directly excited pyrene increased at least by 25% and a distinct rotational correlation time of 7 ns was observed. In order to evaluate the affinity of nsL-TP for intermediates of the beta-oxidation pathway, a binding assay was developed based on the ability of fatty acyl derivatives to displace Pyr-C12 from the lipid binding site as reflected by the reduction of FRET. Hexadecanoyl-CoA and 2-hexadecenoyl-CoA were found to bind readily to nsL-TP, whereas 3-hydroxyhexadecanoyl-CoA and 3-ketohexadecanoyl-CoA bound poorly. The highest affinities were observed for the very-long-chain fatty acyl-CoA esters (24:0-CoA, 26:0-CoA) and their enoyl derivatives (24:1-CoA, 26:1-CoA). Binding of non-esterified hexadecanoic acid and tetracosanoic acid (24:0) was negligible.  (+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. (3/978)

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)

The tricarboxylic acid cycle of Helicobacter pylori. (4/978)

The composition and properties of the tricarboxylic acid cycle of the microaerophilic human pathogen Helicobacter pylori were investigated in situ and in cell extracts using [1H]- and [13C]-NMR spectroscopy and spectrophotometry. NMR spectroscopy assays enabled highly specific measurements of some enzyme activities, previously not possible using spectrophotometry, in in situ studies with H. pylori, thus providing the first accurate picture of the complete tricarboxylic acid cycle of the bacterium. The presence, cellular location and kinetic parameters of citrate synthase, aconitase, isocitrate dehydrogenase, alpha-ketoglutarate oxidase, fumarate reductase, fumarase, malate dehydrogenase, and malate synthase activities in H. pylori are described. The absence of other enzyme activities of the cycle, including alpha-ketoglutarate dehydrogenase, succinyl-CoA synthetase, and succinate dehydrogenase also are shown. The H. pylori tricarboxylic acid cycle appears to be a noncyclic, branched pathway, characteristic of anaerobic metabolism, directed towards the production of succinate in the reductive dicarboxylic acid branch and alpha-ketoglutarate in the oxidative tricarboxylic acid branch. Both branches were metabolically linked by the presence of alpha-ketoglutarate oxidase activity. Under the growth conditions employed, H. pylori did not possess an operational glyoxylate bypass, owing to the absence of isocitrate lyase activity; nor a gamma-aminobutyrate shunt, owing to the absence of both gamma-aminobutyrate transaminase and succinic semialdehyde dehydrogenase activities. The catalytic and regulatory properties of the H. pylori tricarboxylic acid cycle enzymes are discussed by comparing their amino acid sequences with those of other, more extensively studied enzymes.  (+info)

ApoB100 secretion from HepG2 cells is decreased by the ACAT inhibitor CI-1011: an effect associated with enhanced intracellular degradation of ApoB. (5/978)

The concept that hepatic cholesteryl ester (CE) mass and the rate of cholesterol esterification regulate hepatocyte assembly and secretion of apoB-containing lipoproteins remains controversial. The present study was carried out in HepG2 cells to correlate the rate of cholesterol esterification and CE mass with apoB secretion by CI-1011, an acyl CoA:cholesterol acyltransferase (ACAT) inhibitor that is known to decrease apoB secretion, in vivo, in miniature pigs. HepG2 cells were incubated with CI-1011 (10 nmol/L, 1 micromol/L, and 10 micromol/L) for 24 hours. ApoB secretion into media was decreased by 25%, 27%, and 43%, respectively (P<0.0012). CI-1011 (10 micromol/L) inhibited HepG2 cell ACAT activity by 79% (P<0.002) and cellular CE mass by 32% (P<0.05). In contrast, another ACAT inhibitor, DuP 128 (10 micromol/L), decreased cellular ACAT activity and CE mass by 85% (P<0.002) and 42% (P=0.01), respectively, but had no effect on apoB secretion into media. To characterize the reduction in apoB secretion by CI-1011, pulse-chase experiments were performed and analyzed by multicompartmental modelling using SAAM II. CI-1011 did not affect the synthesis of apoB or albumin. However, apoB secretion into the media was decreased by 42% (P=0.019). Intracellular apoB degradation increased proportionately (P=0.019). The secretion of albumin and cellular reuptake of labeled lipoproteins were unchanged. CI-1011 and DuP 128 did not affect apoB mRNA concentrations. These results show that CI-1011 decreases apoB secretion by a mechanism that involves an enhanced intracellular degradation of apoB. This study demonstrates that ACAT inhibitors can exert differential effects on apoB secretion from HepG2 cells that do not reflect their efficacy in inhibiting cholesterol esterification.  (+info)

The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. (6/978)

Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that catalyses a rate-limiting step in coenzyme A (CoA) biosynthesis, by transferring an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA). Each phosphopantetheine adenylyltransferase (PPAT) subunit displays a dinucleotide-binding fold that is structurally similar to that in class I aminoacyl-tRNA synthetases. Superposition of bound adenylyl moieties from dPCoA in PPAT and ATP in aminoacyl-tRNA synthetases suggests nucleophilic attack by the 4'-phosphopantetheine on the alpha-phosphate of ATP. The proposed catalytic mechanism implicates transition state stabilization by PPAT without involving functional groups of the enzyme in a chemical sense in the reaction. The crystal structure of the enzyme from Escherichia coli in complex with dPCoA shows that binding at one site causes a vice-like movement of active site residues lining the active site surface. The mode of enzyme product formation is highly concerted, with only one trimer of the PPAT hexamer showing evidence of dPCoA binding. The homologous active site attachment of ATP and the structural distribution of predicted sequence-binding motifs in PPAT classify the enzyme as belonging to the nucleotidyltransferase superfamily.  (+info)

Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis. (7/978)

1. An acyl-thioester hydrolase was isolated from the cytosol of lactating-rabbit mammary gland. The purified enzyme terminates fatty acid synthesis at medium-chain (C8:0-C12:0) acids when it is incubated with fatty acid synthetase and rate-limiting concentrations of malonyl-CoA. These acids are characteristic products of the lactating gland. 2. The mol.wt. of the enzyme is 29000+/-500 (mean+/-S.D. of three independent preparations), as estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 3. The enzyme also hydrolyses acyl-CoA esters of chain lengths C10:0-C16:0 when these are used as model substrates. The greatest activity was towards dodecanoyl-CoA, and the three preparations had specific activities of 305, 1130 and 2010 nmol of dodecanoyl-CoA hydrolysed/min per mg of protein when 56muM substrate was used. 4. The way in which this enzyme controls the synthesis of medium-chain fatty acids by fatty acid synthetase is briefly discussed.  (+info)

Characterization of a novel spermidine/spermine acetyltransferase, BltD, from Bacillus subtilis. (8/978)

Overexpression of the BltD gene in Bacillus subtilis causes acetylation of the polyamines spermidine and spermine. BltD is co-regulated with another gene, Blt, which encodes a multidrug export protein whose overexpression facilitates spermidine export [Woolridge, Vazquez-Laslop, Markham, Chevalier, Gerner and Neyfakh (1997) J. Biol. Chem. 272, 8864-8866]. Here we show that BltD acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. In the presence of saturating concentrations of acetyl CoA, BltD rapidly acetylates spermine at both the N1 and N12 positions. The Km (app) values for spermine, spermidine and N1-acetylspermine are +info)

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Residues 4 to 115 (E-value = 4.8e-59) place CT822 in the CoA_binding family which is described as CoA binding domain (PF02629 ...
72-89-9:C23H38N7O17P3S, Coenzyme A, S-acetate, Acetyl CoA, Acetyl coenzyme A, Coenzyme A, S-acetate, S-acetilcoenzima A, S-Acetyl coenzyme A, S-Acetylcoenzym A, S-acetylcoenzyme A
The Km is a measure of the binding affinity of an enzyme for its ligand (substrate or coenzyme) and is defined as the concentration of ligand required to fill one- half Chat Online ...
Коферме́нт (коензим) - невелика небілкова (неамінокислотна) молекула, що вільно звязується з ферментом та важлива для його каталітичноїактивноті. Коферменти іноді називають косубстратами. Ці молекули не формують постійної частини структури ферментів і звільняються в процесі каталітичного циклу. Це відрізняє коферменти від простетичних груп. ...
கொழுப்பு அமிலங்கள், அல்லது கொழுப்பு அமிலத்தின் மீதங்கள் கொழுப்பு அமில தொகுப்பு எனப்படும் செயல்முறை மூலம் அசிட்டைல்- CoA உடன் மெலோனைல்-CoA அல்லது மெதில்மெலோனைல்-CoA தொகுதிகளை முன்தொடராகக் கொண்ட சங்கிலித் தொடர் நீட்சியாக்கத்தினால் கொழுப்பு அமில தொகுப்பு எனப்படும் செயல்முறை மூலம் தயாரிக்கப்பட்ட வேறுபட்ட மூலக்கூறுகளின் தொகுதியாகும்.[6][7] இவை ஐதரோகார்பன் சங்கிலி யால் ...
Coenzyme A (CoA) is an important cofactor (acyl-chain carrier) for many cellular functions including the citrate cycle and fatty acid biosynthesis and metabolism. Vitamin B5, also known as pantothenate is the precursor for CoA biosynthesis. Pantothenate synthesis takes place in plants, fungi and some bacteria, whereas animals salvage pantothenate from diet and CoA biosynthesis from pantothenate is present in most organisms. Plasmodium falciparum utilises pantothenate from host and converts it to CoA (CoA biosynthesis). In contrast, the Coccidians Toxoplasma gondii and Neospora caninum possess the four enzymes required for the generation of pantothenate from the branched chain amino acid valine. Except dephospho-CoA kinase (2.7.1.24), all other enzymes involved in the downstream conversion of pantothenate to CoA are present. Dephospho-CoA kinase, an enzyme present in P. falciparum is missing in T. gondii and N. caninum gene models. It has previously been suggested that T. gondii ...
Coenzyme A (CoA) is an essential cofactor in the metabolism of both prokaryotic and eukaryotic organisms and a universal five-step pathway is utilized to synthesize CoA from pantothenate. Null mutations in two of the five steps of this pathway led to embryo lethality and therefore viable reduction-o …
Following a request from the European Commission, the Panel on Dietetic Products, Nutrition and Allergies (NDA) derived Dietary Reference Values (DRVs) for pantothenic acid. Pantothenic acid is a water-soluble vitamin, which is a component of coenzyme A (CoA) and acyl-carrier proteins. Pantothenic acid is ubiquitous and deficiency is rare. There are no suitable biomarkers that can be used to derive the requirement for pantothenic acid. Data available on pantothenic acid intakes and health consequences are very limited and cannot be used to derive DRVs for pantothenic acid. As there is insufficient evidence available to derive an Average Requirement and a Population Reference Intake, an Adequate Intake (AI) is proposed. The setting of AIs is based on observed pantothenic acid intakes with a mixed diet and the apparent absence of signs of deficiency in the EU, suggesting that current intake levels are adequate. The AI for adults is set at 5 mg/day. The AI for adults also applies to pregnant women. ...
Coenzyme A (CoA) functions as a carrier of acetyl and acyl groups in cells and thus plays an important role in numerous synthetic and degradative metabolic pathways in all organisms. In eukaryotes, CoA and its derivatives are also involved in membrane trafficking and signal transduction. This gene encodes the bifunctional protein coenzyme A synthase (CoAsy) which carries out the last two steps in the biosynthesis of CoA from pantothenic acid (vitamin B5). The phosphopantetheine adenylyltransferase domain of this bifunctional protein catalyzes the conversion of 4-phosphopantetheine into dephospho-coenzyme A (dpCoA) while its dephospho-CoA kinase domain completes the final step by phosphorylating dpCoA to form CoA. Mutations in this gene are associated with neurodegeneration with brain iron accumulation (NBIA). Alternative splicing results in multiple isoforms. [provided by RefSeq, Apr 2014 ...
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Pantothenic Acid 250 mg - 250 tabletsRecommended Use:One tablet daily, or as recommended by your health care professional.Pantothenic acid is a member of the B-vitamin family, and is often referred to as Vitamin B-5. Its bioactive form, coenzyme a, plays many roles in the body, including the metabolism of proteins, fats and carbohydrates, the production of energy, and the synthesis or red blood cells and the key neurotransmitter, acetylcholine.Ingredients:Pantothenic Acid 250mg.WARNING: Keep out of the reach of children. Do not use if either tamper-evident seal is broken or missing. If you are pregnant or nursing, consult your health care professional before using this product. Suitable for vegetarians and hypoallergenic: contains no yeast, dairy, egg, gluten, corn, soy or wheat. Contains no sugar, starch, salt, preservatives, or artificial color, flavor or fragrance.
Abstract: Environmental citrate or malonate is degraded by a range of aerobic or anaerobic bacteria. For chosen illustrations, the genes encoding the specific enzymes with the degradation pathway are explained along with the encoded proteins and their catalytic mechanisms. Aerobic micro organism degrade citrate quickly by The fundamental enzyme products in the cell if a selected transporter for citrate is offered. Anaerobic degradation of citrate in Klebsiella pneumoniae needs the so-termed substrate activation module to transform citrate into its thioester Together with the phosphoribosyl dephospho-CoA prosthetic group of citrate lyase. The citryl thioester is subsequently cleaved into oxaloacetate as well as acetyl thioester, from which a whole new citryl thioester is formed given that the turnover carries on. The degradation of malonate Also features a substrate activation module by using a phosphoribosyl dephospho-CoA prosthetic group. The equipment receives Prepared for turnover just after ...
Why do you include Pantothenic Acid in JOINT NUTRITION? - Pantothenic Acid, or Vitamin B5, is required for the production of cortico-steroid hormones in the adrenal glands. These hormones are the body
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A substance that becomes essential for the working and function of an enzyme other than the protein compounds becomes known as a coenzyme. Coenzymes regularly work as the middle of the road bearers of electrons, molecules or practical gatherings that transfer in the general response. A case of this would be the part of NAD in the move of electrons in certainly coupled oxidation diminishment responses. A coenzyme is a substance that works with a compound to start or help the capacity of the protein. It might get viewed as an assistant particle for a biochemical response. Coenzymes are tiny, non-proteinaceous particles that give an exchange site to a working catalyst. They are moderate bearers of an iota or gathering of particles, enabling a response to happen. Coenzymes dont get considered some portion of a proteins structure; they here and there alluded to as substrates. A sort of cofactor, coenzymes, are fundamental particles that dilemma to compounds and help them work. The key here is that ...
By Nutri People. Vitamin B5 converts to co-enzyme A, which is involved in breaking down carbohydrates, fat and protein to make energy, and in making steroids, fatty acids, bile, haemoglobin and cholesterol. The brain contains high amounts of B5. Vitamin B5 helps make two important substances involved in nerve transmission - acetylcholine and sphingosine. B5 is important for a healthy immune system. It supports the adrenal glands and helps maintain healthy skin, digestion, nerves, bones and joints. Pantothenic acid helps balance cholesterol, blood sugar, blood pressure, stress, mood and sleep. Antibiotics, illness and alcohol deplete levels.. ...
Pantothenic acid is a vitamin b5, likewise referred to as vitamin B5. It is extensively found in both plants and animals consisting of meat, vegetables, cereal grains, legumes, eggs, and milk.
Health benefits of Vitamin B5 (Pantothenic Acid) include relief from asthma, hair loss, allergies, stress & anxiety, respiratory disorders and stronger immune system.
Solgar Pantothenic Acid is an essential co-enzyme in the body. It is a vitamin B5. It is essential to the metabolism of fats, carbohydrates and protein.
Also known as vitamin B, pantothenic acid is essential for a number of basic bodily functions. It participates in the continual breakdown of carbohydr
Sometimes referred to as Vitamin B-5, Pantothenic Acid has been studied closely for its apparent role in helping metabolize a range of food types and for the nutritional support of nervous-system signal transmission. Natures Plus uses the most c
Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme used in up to 4% of enzymatic reactions within all living cells. Notably, it is used in fatty acid synthesis, the Krebs cycle, and the oxidation of pyruvate to acetyl-CoA. ...
Coenzyme A (CoA) is an essential cofactor for all forms of life. The biochemistry underpinning the assembly of CoA in Escherichia coli and other enterobacteria is well understood, except for the events leading to maturation of the L-aspartate-α-decarboxylase (PanD) enzyme that converts pantothenate …
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Enzymes for DNA repair or Coenzyme Q10 for antioxidant and antiaging benefits have become typical ingredients in todays skin care. Here, industry expert OLenick illustrates the difference between cofactors and coenzymes.
Coenzyme Q-10 is an essential component of the mitochondria and so is involved in energy production within body cells. Solgars Coenzyme Q-10 is obtained fr
Save 28% Country Life (Biochem) - Coenzyme B-Complex Caps 60 Capsules B complex vitamins replace what daily living and stress take away*
Coenzyme occurs naturally in the body but as we age and our nutritional deficiencies increase, it is reduced in our body. Increases vitality, energy and promotes the function of muscles and heart.
Although I am fully convinced of the truth of the views given in this volume, I by no means expect to convince experienced naturalists whose minds are stocked with a multitude of facts all viewed, during a long course of years, from a point of view directly opposite to mine. It is so easy to hide our ignorance under such expressions as plan of creation, unity of design, etc., and to think that we give an explanation when we only restate a fact. Any one whose disposition leads him to attach more weight to unexplained difficulties than to the explanation of a certain number of facts will certainly reject the theory. ...
MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPantothenate and coenzyme A2-dehydropantoate 2-reductase (TIGR00745; EC 1.1.1.-; HMM-score: 304) ...
MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPantothenate and coenzyme A2-dehydropantoate 2-reductase (TIGR00745; EC 1.1.1.-; HMM-score: 31.2) ...
Coenzyme A is an essential metabolite known for its central role in over one hundred cellular metabolic reactions. In cells, Coenzyme A is synthesized de novo in five enzymatic steps with vitamin B5 as the starting metabolite, phosphorylated by pantothenate kinase. Mutations in the pantothenate kinase 2 gene cause a severe form of neurodegeneration for which no treatment is available. One therapeutic strategy is to generate Coenzyme A precursors downstream of the defective step in the pathway. Here we describe the synthesis, characteristics and in vivo rescue potential of the acetyl-Coenzyme A precursor S-acetyl-4-phosphopantetheine as a possible treatment for neurodegeneration associated with pantothenate kinase deficiency. ...
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SWISS-MODEL Repository entry for C4ZXM6 (COAD_ECOBW), Phosphopantetheine adenylyltransferase. Escherichia coli (strain K12 / MC4100 / BW2952)
SWISS-MODEL Repository entry for A0A073FPV4 (A0A073FPV4_ECOLX), Phosphopantetheine adenylyltransferase. Escherichia coli 2-427-07_S4_C3
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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Learn more about Pantothenic Acid and Pantethine at Sky Ridge Medical Center Supplement Forms / Alternate Names Pantothenate; Vitamin B5 Uses Principal Proposed...
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Applications and Uses of Coenzyme Q10 Coenzyme Q10 is widely used . Coenzyme Q10 can be used in a wide variety of industries . Coenzyme Q10 in Food Production N…
Coenzyme Q10, molecular model. This is the fully oxidised version of the molecule, known as ubiquinone. Coenzyme Q10 is involved in the electron transport chain that synthesises (ATP) adenosine triphosphate. It is therefore found in large quantities in mitochondria, the organelles that produce energy, in the form of ATP, for a cell. Coenzyme Q10 also acts as an antioxidant. - Stock Image C014/2293
We explored the uptake of B12 and its accumulation and conversion to the coenzymes in rats kept on a low-B12 diet for 4 weeks followed by a 2-week diet containing HO-B12 or CN-B12 or a 2-week continuum on a low-B12 diet.. We found major differences in both the distribution and the degree of conversion to the B12 coenzymes for HO-B12 and CN-B12 supplementations. Notably, more than half of the administered CN-B12 remained in this form in the kidneys, whereas HO-B12 was largely converted to the bioactive ADO-B12 providing more than the doubled amount of active coenzymes to the kidney tissues than CN-B12. The degree of conversion becomes even larger if subtracting ADO-B12 in the low-B12 organs and counting only its increments, accumulated in the cause of HO-B12 and CN-B12 supplementation. Our study also highlights the uncertainty of using plasma B12 as a sole marker of B12 tissue content.. The work has some limitations. Even though no B12 had been added, the low-B12 diet still contained 5 µg/kg ...
Vitamins & Coenzymes describe the coenzyme factors found in organic compounds of natural foods, essential for the normal processes of growth and higher forms of the body.
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Coenzyme Q10 (CoQ10) is used to produce energy your body needs for cell growth and maintenance. It also functions as an antioxidant, which protects the body from damage caused by harmful molecules. - WebMD
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Western blotting results of adipogenesis-specific markers.Representative image of 3 repeats and quantification of (A) PPARγ, (B) C/EBPα, and (C) Acetyl CoA ca
... , also known as ubiquinone, ubidecarenone, coenzyme Q, and abbreviated at times to CoQ10 /ˌkoʊˌkjuːˈtɛn/, CoQ, or Q ... "Coenzyme Q10". National Cancer Institute.. *. Bonakdar, Robert Alan; Guarneri, Erminia. "Coenzyme Q10". American Family ... "4 Coenzyme Q oxidation reduction reactions in mitochondrial electron transport". In Kagan, V. E.; Quinn, P. J. Coenzyme Q: ... "Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations". Mitochondrion. 7 (Suppl.): S78-S88. doi:10.1016/j ...
NADP+/NADPH coenzyme-inspired catalyst[edit]. In natural photosynthesis, the NADP+ coenzyme is reducible to NADPH through ... The coenzyme is recyclable in a natural photosynthetic cycle, but this process is yet to be artificially replicated. ...
Enzymes that use NADP(H) as a coenzyme[edit]. *Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms.[5] ... Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ...
Coenzyme Q10 --> MitoQ Anti-oxidants are substances that may protect cells from the damage caused by free radicals. Sunscreens ...
Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It ... "Entrez Gene: PANK4 pantothenate kinase 4". Robishaw JD, Neely JR (1985). "Coenzyme A metabolism". Am. J. Physiol. 248 (1 Pt 1 ... Coenzyme A Pantothenate ENSG00000273494 GRCh38: Ensembl release 89: ENSG00000157881, ENSG00000273494 - Ensembl, May 2017 GRCm38 ...
Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It ... Ramaswamy G, Karim MA, Murti KG, Jackowski S (2004). "PPARalpha controls the intracellular coenzyme A concentration via ... "Coenzyme A metabolism". Am. J. Physiol. 248 (1 Pt 1): E1-9. PMID 2981478. Hong BS, Senisterra G, Rabeh WM, et al. (2007). " ...
... acetoacetyl coenzyme A-succinic thiophorase, succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA ... Menon GK, Stern JR (1960). "Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl coenzyme A". J. Biol. Chem. 235 ... Other names in common use include 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A ... Hersh LB, Jencks WP (1967). "Coenzyme A transferase. Kinetics and exchange reactions". J. Biol. Chem. 242: 3468-3480. Lynen F, ...
Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It ... Kotzbauer PT, Truax AC, Trojanowski JQ, Lee VM (2005). "Altered neuronal mitochondrial coenzyme A synthesis in ... "Coenzyme A metabolism". Am. J. Physiol. 248 (1 Pt 1): E1-9. PMID 2981478. Hayflick SJ (2007). "Neurodegeneration with brain ...
It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid ... Other names in common use include long-chain fatty-acyl-CoA hydrolase, palmitoyl coenzyme A hydrolase, palmitoyl thioesterase, ... Srere PA, Seubert W, Lynen F (1959). "Palmityl coenzyme A deacylase". Biochim. Biophys. Acta. 33 (2): 313-319. doi:10.1016/0006 ... palmitoyl coenzyme A hydrolase, palmitoyl-CoA deacylase, palmityl thioesterase, palmityl-CoA deacylase, fatty acyl thioesterase ...
Methylmalonyl coenzyme A racemase". J. Biol. Chem. 237: 3065-3068. PMID 13934211. Overath, P.; Kellerman, G.M.; Lynen, F.; ... Methylmalonyl CoA epimerase (EC 5.1.99.1, methylmalonyl-CoA racemase, methylmalonyl coenzyme A racemase, DL-methylmalonyl-CoA ...
COQ2 Coenzyme Q10 deficiency; 607426; COQ9 Coenzyme Q10 deficiency; 607426; PDSS1 Coenzyme Q10 deficiency; 607426; PDSS2 Coffin ... CHUK Coenzyme Q10 deficiency; 607426; APTX Coenzyme Q10 deficiency; 607426; CABC1 Coenzyme Q10 deficiency; 607426; ...
... propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [ ... Galivan JH, Allen SH (1968). "Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus ...
The coenzyme is FAD. This enzyme belongs to the family of oxidoreductases, specifically the monooxygenases. The systematic name ...
... enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA ... Butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 1-12. PMID 13130521. Beinert, H.; Lardy, H.; Myrbäck, K. (1963). " ... The prosthetic group of butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 13-26. PMID 13130522. Green, D.E.; Mii, S.; ... "Acyl coenzyme A dehydrogenase". In Boyer, P.D. The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447-466. CS1 maint: ...
Goodridge AG (November 1972). "Regulation of the activity of acetyl coenzyme A carboxylase by palmitoyl coenzyme A and citrate ... Coenzyme A now enters the enzyme and another intermediate is formed which consists of AMP-long chain fatty acid-Coenzyme A. ( ... Bækdal T, Schjerling CK, Hansen JK, Knudsen J (1997). "Analysis of long-chain acyl-Coenzyme A esters". In Christie W. Advances ... Guynn RW, Veloso D, Veech RL (November 1972). "The concentration of malonyl-coenzyme A and the control of fatty acid synthesis ...
Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase ... "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase ... Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. The Enzymes. 7 (2nd ed.). New York ... medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ACADM (gene name).) is an ...
... acetyl coenzyme A carboxylase] synthetase, acetyl coenzyme A holocarboxylase synthetase, acetyl CoA holocarboxylase synthetase ... Landman AD, Darkshinamurti K (March 1975). "Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme ...
MacPhee, G. B.; Logan, R. W.; Mitchell, J. S.; Howells, D. W.; Tsotsis, E.; Thorburn, D. R. (October 1993). "Malonyl coenzyme a ...
2003). "Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro ... Lin S; Lu X; Chang CC; Chang TY (2004). "Human Acyl-Coenzyme A:Cholesterol Acyltransferase Expressed in Chinese Hamster Ovary ... 1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". J. Biol. ... "Acyl-coenzyme A:cholesterol acyltransferase". Annu. Rev. Biochem. 66: 613-38. doi:10.1146/annurev.biochem.66.1.613. PMID ...
... o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. ... CS1 maint: Multiple names: authors list (link) Sieweke, Leistner (August 1991). "o-Succinylbenzoate: coenzyme A ligase, an ... 4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis". Z. Naturforsch. C. 42: 1207-14. PMID ... and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli". J Bacteriol. 178: 6778-81. PMC 178575 . PMID ...
Coenzyme Q6 monooxygenase is a protein that in humans is encoded by the COQ6 gene. The protein encoded by this gene belongs to ... It is an evolutionarily conserved monooxygenase required for the biosynthesis of coenzyme Q10 (or ubiquinone), which is an ... Mutations in this gene are associated with autosomal recessive coenzyme Q10 deficiency-6 (COQ10D6), which manifests as ... Coenzyme Q6 monooxygenase". Heeringa SF, Chernin G, Chaki M, Zhou W, Sloan AJ, Ji Z, Xie LX, Salviati L, Hurd TW, Vega-Warner V ...
... produce the reduced coenzyme NADH. This coenzyme contains electrons that have a high transfer potential; in other words, they ... As coenzyme Q is reduced to ubiquinol on the inner side of the membrane and oxidized to ubiquinone on the other, a net transfer ... Unlike coenzyme Q, which carries two electrons, cytochrome c carries only one electron. As only one of the electrons can be ... NADH-coenzyme Q oxidoreductase, also known as NADH dehydrogenase or complex I, is the first protein in the electron transport ...
... (EC 2.7.1.33, PanK; CoaA) is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It ... Leonardi, Roberta; Zhang, Yong-Mei; Rock, Charles O.; Jackowski, Suzanne (2005-03-01). "Coenzyme A: Back in action". Progress ... Jackowski, S.; Rock, C. O. (1981-12-01). "Regulation of coenzyme A biosynthesis". Journal of Bacteriology. 148 (3): 926-932. ... in Control of Coenzyme A Levels in Escherichia coli". Journal of Bacteriology. 185 (11): 3410-3415. doi:10.1128/JB.185.11.3410- ...
Mue S, Tuboi S, Kikuchi G (December 1964). "On malyl-coenzyme A synthetase". J. Biochem. 56: 545-551. PMID 14244056. Molecular ... malyl coenzyme A synthetase, and malate thiokinase. This enzyme participates in glyoxylate and dicarboxylate metabolism. ...
1-specific DPN-linked beta-hydroxybutyric dehydrogenase 3-hydroxyacetyl-coenzyme A dehydrogenase 3-hydroxyacyl coenzyme A ... beta-Hydroxyacyl coenzyme A dehydrogenase". J. Biol. Chem. 207 (2): 631-8. PMID 13163047. Molecular and Cellular Biology portal ... In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity: HADH - Hydroxyacyl-Coenzyme A ... A dehydrogenase beta-keto-reductase beta-ketoacyl-CoA reductase L-3-hydroxyacyl CoA dehydrogenase L-3-hydroxyacyl coenzyme A ...
MASON M (1957). "Kynurenine transaminase of rat kidney; a study of coenzyme dissociation". J. Biol. Chem. 227 (1): 61-8. PMID ...
Organic cofactors are sometimes further divided into coenzymes and prosthetic groups. The term coenzyme refers specifically to ... A coenzyme that is tightly or even covalently bound is termed a prosthetic group. Cosubstrates are transiently bound to the ... White HB (1976). "Coenzymes as fossils of an earlier metabolic state". J. Mol. Evol. 7 (2): 101-4. doi:10.1007/BF01732468. PMID ... However, the author could not arrive at a single all-encompassing definition of a "coenzyme" and proposed that this term be ...
ChAT functions to transfer an acetyl group from acetyl co-enzyme A to choline in the synapses of nerve cells and exists in two ... The donor is often a coenzyme. Some of the most important discoveries relating to transferases occurred as early as the 1930s. ... Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, the action of ...
The protein encoded by this gene is an enzyme that elongates the prenyl side-chain of coenzyme Q, or ubiquinone, one of the key ... 1995). "Regulation of coenzyme Q biosynthesis". Mol. Aspects Med. 15 Suppl: s37-46. doi:10.1016/0098-2997(94)90011-6. PMID ... the first step in coenzyme Q biosynthesis. The protein may be peripherally associated with the inner mitochondrial membrane, ... "Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency". Lancet. 356 (9227): 391- ...
Other names in common use include acetyl-CoA deacylase, acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A ... "Succinyl and acetyl coenzyme A deacylases". J. Biol. Chem. 198 (1): 323-334. PMID 12999747. Molecular and Cellular Biology ... deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol esterase. This enzyme participates in pyruvate metabolism. As of ...
Acetyl coenzyme A, Coenzyme A, S-acetate, S-acetilcoenzima A, S-Acetyl coenzyme A, S-Acetylcoenzym A, S-acetylcoenzyme A ...
Coenzyme A (CoA) Biosynthesis Pathway and Vitamin B5. 24 Aug 2018 Lesson on Coenzyme A Biosynthesis and Vitamin B5. Coenzyme A ... coenzyme q10 - German translation - Linguee. vitamins A, C and E or even coenzyme Q 10 should be applied [] in the evening to ... coenzyme , Infoplease. Those coenzymes that have been found to be necessary in the diet are vitamins . One such compound, ... Effect of Methylmalonyl Coenzyme A, a Metabolite Which Coenzyme A, a Metabolite. Which. Accumulates in Vitamin B,, Deficiency, ...
Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the ... Coenzyme A is one of five essential coenzymes that is necessary in the reaction mechanism of the citric acid cycle. Its acetyl- ... The coenzyme was named coenzyme A to stand for "activation of acetate." In 1953, Fritz Lipmann won the Nobel Prize in ... Coenzyme A, three ADP, one monophosphate, and one diphosphate are harvested from biosynthesis. New research shows that coenzyme ...
Coenzyme Q10, also known as ubiquinone, ubidecarenone, coenzyme Q, and abbreviated at times to CoQ10 /ˌkoʊˌkjuːˈtɛn/, CoQ, or ... "Coenzyme Q10". National Cancer Institute. Bonakdar, Robert Alan; Guarneri, Erminia. "Coenzyme Q10". American Family Physician. ... Bhagavan, H. N.; Chopra, R. K. (Jun 2007). "Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations". ... "4 Coenzyme Q oxidation reduction reactions in mitochondrial electron transport". In Kagan, V. E.; Quinn, P. J. Coenzyme Q: ...
Coenzyme Q10, also known as ubiquinone, ubidecarenone, coenzyme Q, and abbreviated at times to CoQ10 /ˌkoʊˌkjuːˈtɛn/, CoQ, or Q ... "Coenzyme Q10". National Cancer Institute.. *. Bonakdar, Robert Alan; Guarneri, Erminia. "Coenzyme Q10". American Family ... "4 Coenzyme Q oxidation reduction reactions in mitochondrial electron transport". In Kagan, V. E.; Quinn, P. J. Coenzyme Q: ... "Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations". Mitochondrion. 7 (Suppl.): S78-S88. doi:10.1016/j ...
... has role Escherichia coli metabolite (CHEBI:76971) coenzyme A (CHEBI:15346) has role coenzyme (CHEBI: ... coenzyme A (CHEBI:15346) is a adenosine 3,5-bisphosphate (CHEBI:37240) coenzyme A (CHEBI:15346) is conjugate acid of coenzyme ... vinylacetyl-CoA (CHEBI:15543) has functional parent coenzyme A (CHEBI:15346). coenzyme A(4−) (CHEBI:57287) is conjugate base of ... CHEBI:15346 - coenzyme A. Main. ChEBI Ontology. Automatic Xrefs. Reactions. Pathways. Models. ...
The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is ... It catalyzes the reduction of cytochrome c by oxidation of coenzyme Q (CoQ) and the concomitant pumping of 4 protons from the ... coenzyme Q: cytochrome C oxidoreductase) is known as the ubiquinone ("Q") cycle. In this cycle four protons get released into ... Calculated positions of bc1 and related complexes in membranes Coenzyme Q-Cytochrome-c Reductase at the US National Library of ...
Primary coenzyme Q10 deficiency is a disorder that can affect many parts of the body, especially the brain, muscles, and ... Coenzyme Q10 deficiency can also be caused by mutations in genes that are not directly related to the synthesis of coenzyme Q10 ... In these cases, the condition is referred to as secondary coenzyme Q10 deficiency. Secondary coenzyme Q10 deficiency is a ... coenzyme Q10 plays an essential role in a process called oxidative phosphorylation. , which converts the energy from food into ...
Coenzyme Q10 or CoQ10 is an extremely important nutrient that every cell in your body must have in order to produce energy. ... Examples of coenzymes are vitamin B6, vitamin B12, folic acid, and coenzyme Q10. As mentioned previously, coenzyme Q10 is ... How Does Coenzyme Q10 Work?. Biological chemical reactions require helper substances known as enzymes. These enzymes are ... Coenzyme Q10 or CoQ10 is an extremely important nutrient that every cell in your body must have in order to produce energy. ...
... (CoQ10, also called ubiquinone) is a vitamin-like substance thats present in foods and is also produced by your ... You can buy coenzyme Q10 at almost any health-food store, at many supermarkets, and over the Internet. Its usually sold in the ... Coenzyme Q10 (CoQ10, also called ubiquinone) is a vitamin-like substance thats present in foods and is also produced by your ... Coenzyme Q10 grabs the electrons that are generated as you digest food and shuttles them around inside the cells, a process ...
The nutritional supplement coenzyme Q10 could slow the progress of early-stage Parkinsons. ...
Lovastatin decreases coenzyme Q levels in humans.. K Folkers, P Langsjoen, R Willis, P Richardson, L J Xia, C Q Ye, H Tamagawa ... Lovastatin decreases coenzyme Q levels in humans.. K Folkers, P Langsjoen, R Willis, P Richardson, L J Xia, C Q Ye, H Tamagawa ... Lovastatin decreases coenzyme Q levels in humans.. K Folkers, P Langsjoen, R Willis, P Richardson, L J Xia, C Q Ye, and H ... The mechanism of action of lovastatin is inhibition of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, an enzyme involved in ...
METHYL-COENZYME M REDUCTASE I ALPHA SUBUNITMETHYL-COENZYME M REDUCTASE I BETA SUBUNITMETHYL-COENZYME M REDUCTASE I GAMMA ...
Coenzyme F420. non-vitamins: ATP , CTP , SAM , PAPS , GSH , Coenzyme B , Coenzyme M , Coenzyme Q , Methanofuran , BH4 , H4MPT ... for example coenzyme A and ATP, and redox reactions, such as coenzyme Q10 and NAD+. Coenzymes are consumed and recycled ... or coenzyme A, the coenzyme that carries acyl groups. Most coenzymes are found in a huge variety of species, and some are ... Coenzymes. vitamins: NAD+ (B3) , NADP+ (B3) , Coenzyme A (B5) , THF / H4F (B9), DHF, MTHF , Ascorbic acid (C) , Menaquinone (K ...
Coenzyme A biosynthetic machinery in mammalian cells.. Martinez DL1, Tsuchiya Y1, Gout I1. ... CoA (coenzyme A) is an essential cofactor in all living organisms. CoA and its thioester derivatives [acetyl-CoA, malonyl-CoA, ...
The nutritional supplement coenzyme Q10 could slow the progress of early-stage Parkinsons.. Eighty patients with early ... Tagged asCoenzyme Q10CoQ10disease progressioneffectivenessnutritional supplementsParkinsons diseaseUbiquinoneWhat Doctors ... Coenzyme Q10 could slow Parkinsons. What Doctors Dont Tell You1 min read ... The patients taking placebo showed a slight disease progression whereas the groups treated with coenzyme Q10 experienced less ...
Coenzyme Q10 (CoQ10), found in all human cells, is involved in cellular respiration and energy production. It is promoted as a ... Coenzyme Q10 Supplementation in Orthostatic Hypotension and Multiple-System Atrophy: A Report on 7 Cases. Am J Med. 2017 Dec 11 ... Effects of Coenzyme Q10 on Statin-Induced Myopathy: An Updated Meta-Analysis of Randomized Controlled Trials. J Am Heart Assoc. ... The effect of coenzyme Q10 on the pharmacokinetic parameters of theophylline. Arch Pharm Res. 2008 Jul;31(7):938-44. ...
The known crystal structures of the inactive nickel (II) enzyme in complex with coenzyme M and coenzyme B (MCR-ox1-silent) and ... METHYL-COENZYME M REDUCTASE I BETA SUBUNIT. B, E. 442. Methanothermobacter thermautotrophicus. Mutation(s): 0 EC: 2.8.4.1. ... METHYL-COENZYME M REDUCTASE I ALPHA SUBUNIT. A, D. 549. Methanothermobacter thermautotrophicus. Mutation(s): 5 EC: 2.8.4.1. ... METHYL-COENZYME M REDUCTASE I GAMMA SUBUNIT. C, F. 248. Methanothermobacter thermautotrophicus. Mutation(s): 0 EC: 2.8.4.1. ...
Brands A-Z California Gold Nutrition, CGN Coenzyme Q10 (CoQ10) Formulas Categories Supplements Antioxidants Coenzyme Q10 (CoQ10 ... California Gold Nutrition, Coenzyme Q10 (CoQ10) Formulas 8 Results (showing 1 - 8) Visit Manufacturers Website » ...
... there is another group of coenzymes known as metabolite coenzymes, usually made from nucleotides. Coenzymes act as agents for ... Coenzyme from Vitamin B-5. Vitamin B-5, or pantothenic acid, is used to make coenzyme A, often termed CoA. This has a free ... Many coenzymes are called vitamin-derived coenzymes, which are formed from the vitamins that are part of our diet. Water ... Electron Transfer Coenzymes. Some coenzymes function by ferrying electrons or negative charges to enhance a reaction. Vitamins ...
Coenzyme Q10, Total. 27923-2. 120252. Coenzyme Q10, Total. ug/mL. 27923-2. ... Measurement of reduced and oxidized coenzyme Q9 and coenzyme Q10 levels in mouse tissues by HPLC with coulometric detection. ... Coenzyme Q10 in the treatment of hypertension: a meta-analysis of the clinical trials. J Hum Hypertens. 2007 Apr;21(4):297-306. ... Coenzyme Q10 in human blood: native levels and determinants of oxidation during processing and storage. Free Radic Biol Med. ...
Brands A-Z Natural Factors Coenzyme Q10 (CoQ10) Formulas Categories Supplements Antioxidants Coenzyme Q10 (CoQ10) Coenzyme Q10 ... Natural Factors, Coenzyme Q10 (CoQ10) Formulas 6 Results (showing 1 - 6) Visit Manufacturers Website » @media (max-width: ...
Coenzyme Q 10 is a compound that is made naturally in the body. Studies have shown that Coenzyme Q10 helps the immune system ... CO Enzyme Q10 is a fantastic supplement designed to promote a healthy cardiovascular system for all dogs and cats. ... There are currently no questions for CO Enzyme Q10 - be the first to ask one! ...
Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure. P Gornicki, J Podkowinski, L A Scappino, J DiMaio, E Ward, R ... Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure. P Gornicki, J Podkowinski, L A Scappino, J DiMaio, E Ward, R ... Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure. P Gornicki, J Podkowinski, L A Scappino, J DiMaio, E Ward, and ...
Treating Parkinsons disease patients with the antioxidant coenzyme (CoQ10) boosts plasma levels of the substance ... Explain to patients who ask that coenzyme (CoQ10) is an antioxidant sold over the counter and reputed to have neuroprotective ... "Randomized, Double-blind, Placebo-Controlled Trial on Symptomatic Effects of Coenzyme Q10 in Parkinson Disease." ArchNeurol. ... DRESDEN, Germany, May 14 -- Treating Parkinsons disease patients with the antioxidant coenzyme (CoQ10) boosts plasma levels of ...
Coenzyme Q10 may be indicated in cardiovascular disease, particularly in congestive heart failure. It may also be indicated to ... "Coenzyme Q10 may be indicated in cardiovascular disease, particularly in congestive heart failure. It may also be indicated to ...
Coenzyme Q10 (CoQ10) is a vitamin-like enzyme found in mitochondria, the power plants of cells. CoQ10s primary role is to help ... Coenzyme Q10 (CoQ10) is a vitamin-like enzyme found in mitochondria, the power plants of cells. CoQ10s primary role is to help ...
Get the lowest price on Sunmark Coenzyme Q-10 Dietary Supplement, online at AllegroMedical.com. ... Sunmark Coenzyme Q-10 Dietary Supplement. *100 mg.. *Coenzyme Q-10 plays an important role in cells and is utilized in the ... Coenzyme Q-10 plays an important role in cells and is utilized in the normal process of energy production. Coenzyme Q-10 is a ... Sunmark Coenzyme Q-10 Dietary Supplement. 49348060544 - Sunmark Coenzyme Q-10 Dietary Supplement - Bottle of 1 - $14.34 ...
Get detailed information about Coenzyme Q10 use in cancer in this summary for clinicians. ... Coenzyme Q10 is a dietary supplement, and use of it as a treatment for cancer in humans has been investigated in only a limited ... Coenzyme Q10 is made naturally by the human body.. *Coenzyme Q10 helps cells to produce energy, and it acts as an antioxidant. ... coenzyme Q10 can also behave as an antioxidant.[1,25-27,29-32] In this capacity, coenzyme Q10 is thought to stabilize cell ...
J The dose depends on what medications you are taking for your health since some medications can lower Coenzyme Q-10. ... Coenzyme q-10 is a powerful antioxidant that protects heart muscles, improves energy levels, and may have some other health ... The dose depends on what medications you are taking for your health since some medications can lower Coenzyme Q-10. ...
Discusses Coenzyme Q10 (CoQ10), also known as Q10, vitamin Q10, or ubiquinone. Looks at use to treat heart failure, cancer, ... What is coenzyme Q10?. Coenzyme Q10 (CoQ10) is a substance similar to a vitamin. It is found in every cell of the body. Your ... Coenzymes help enzymes work to digest food and perform other body processes, and they help protect the heart and skeletal ... Gaby AR, Mischley LK (2006). Coenzyme Q10. In JE Pizzorno Jr, MT Murray, eds., Textbook of Natural Medicine, 3rd ed., pp. 859- ...
... Identifiers CAS number 85-61-0 PubChem 317 MeSH Coenzyme+A SMILES CC(C)(COP(=O)(O)OP(=O)(O)OCC1C (C(C(O1) ... Coenzymes. NAD+ - NADP+ - Coenzyme A - Tetrahydrofolic acid - Menaquinone - Ascorbic acid - Coenzyme F420 - Adenosine ... Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the ... A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group ...
  • Coenzyme Q10 or CoQ10 is an extremely important nutrient that every cell in your body must have in order to produce energy. (healthy.net)
  • Coenzyme Q10 (CoQ10, also called ubiquinone) is a vitamin-like substance that's present in foods and is also produced by your cells to help convert food into energy. (healthday.com)
  • Inhibition of this enzyme could also inhibit the intrinsic biosynthesis of coenzyme Q10 (CoQ10), but there have not been definitive data on whether lovastatin reduces levels of CoQ10 as it does cholesterol. (pnas.org)
  • Coenzyme Q10 (CoQ10), also known as ubiquinone, is involved in cellular respiration and energy production. (mskcc.org)
  • Coenzyme Q10 (CoQ10) is also referred to as ubiquinone because it can be found in almost all eukaryotic cells. (labcorp.com)
  • Coenzyme Q10, also known as ubiquinone, ubidecarenone, coenzyme Q, and abbreviated at times to CoQ10 /ˌkoʊˌkjuːˈtɛn/, CoQ, or Q10 is a coenzyme that is ubiquitous in animals and most bacteria (hence the name ubiquinone). (wikipedia.org)
  • A 2016 Cochrane review concluded that studies looking at the effects of CoQ10 on blood pressure provided moderately strong evidence that coenzyme Q10 does not lower blood pressure. (wikipedia.org)
  • Coenzyme Q10 (CoQ10) is a vitamin-like enzyme found in mitochondria, the power plants of cells. (livestrong.com)
  • Coenzyme Q10 (CoQ10) is a substance similar to a vitamin. (cardiosmart.org)
  • Coenzyme Q10 is often abbreviated to CoQ10 and referred to by chemists as ubiquinone because it belongs to a class of compounds known as quinines. (lifescript.com)
  • Coenzyme Q10 (CoQ10) is a substance that helps convert food into energy. (umm.edu)
  • In a study published in the Nov. 1 issue of Neural Computation , researchers at the University of California, San Diego School of Medicine report that a high quality brand of coenzyme Q10 (CoQ10) - a compound commonly sold as a dietary supplement - provides health benefits to persons suffering from Gulf War illness symptoms. (eurekalert.org)
  • The cause of statin muscle pain is not known, but it is thought that a reduction of a vitamin-like substance called Coenzyme Q10 (CoQ10) during statin treatment may play a role. (clinicaltrials.gov)
  • Facts are easy to distort in medicine, particularly when talking about coenzyme Q10 (CoQ10, a natural antioxidant synthesized by the body, found in many foods and available as a suplement. (edmontonsun.com)
  • To determine the concentration of coenzyme Q10 (CoQ10) in the human retina. (nih.gov)
  • Coenzyme Q10 (CoQ10) is a vital lipophilic molecule found in all respiratory eukaryotic cells, including spermatozoa. (ingentaconnect.com)
  • Background: Coenzyme Q10 (CoQ10) plays a critical role in mitochondrial oxidative phosphorylation by serving as an electron carrier in the respiratory electron transport chain. (ingentaconnect.com)
  • Our study is aimed at exploring the protective effect of coenzyme Q10 (CoQ10) against pancreatic fibrosis. (hindawi.com)
  • Coenzyme Q10 (CoQ10) is a naturally occurring coenzyme with powerful antioxidant effects that is involved in electron transport in the mitochondria, as well as being an anti-inflammatory agent [ 11 , 12 ]. (hindawi.com)
  • Coenzyme Q10 ( CoQ10 ) is a potent antioxidant that supports cardiovascular health and is absolutely essential for healthy mitochondrial function. (breathing.com)
  • Bulk API Ubidecarenone Coenzyme Q10 Antioxidant Coq10 Powder Remain Gums Healthy Best coq10 Introduction: Product name: Best coq10 Cas no.: 303-98-0 Apperance: Yellow to orange crystalline powder Shelf time: 2 years Coenzyme Q10 migraines Powder. (opencroquet.org)
  • Muscles Coq10 Dietary Supplement 99% Purity Ubidecarenone Coenzyme Q10 We are able to supply good quality Coenzyme Q10 with competitive price. (opencroquet.org)
  • Coenzyme Q10 , alson know as (CoQ10), could be. (opencroquet.org)
  • CAS 303-98-0 Soluble CoQ10 USP Grade Ubiquinone Coenzyme Q10 Powder 10% 98% 99% Coenzyme Q10 (also known as ubidecarenone , CoQ10 and Vitamin Q) is a 1, 4-benzoquinone, playing an important role in generating energy and improving vitality. (opencroquet.org)
  • Coenzyme Q10 (CoQ10) is a fat-soluble, vitamin-like substance in every human cell. (natural-medicinal-herbs.com)
  • Coenzyme Q10 (CoQ10) is also called ubiquinone, a name that signifies its ubiquitous (widespread) distribution in the human body. (peacehealth.org)
  • Both preliminary and double-blind trials have reported that supplementation with coenzyme Q10 (CoQ10) leads to a significant decrease in blood pressure in people with hypertension. (peacehealth.org)
  • Strenuous physical activity lowers blood levels of coenzyme Q10 (CoQ10). (peacehealth.org)
  • As is true for several other heart conditions, coenzyme Q10 (CoQ10) has been reported to help people with congestive heart failure, sometimes dramatically. (peacehealth.org)
  • Questions have been raised about the potential role of coenzyme Q10 (CoQ10) insufficiency in the development of MSA. (eurekalert.org)
  • Orlando, Florida - Individuals taking statins may significantly benefit from taking a CoQ10 supplement as it may replenish their Coenzyme Q10 levels. (pitchengine.com)
  • These individuals may be able to replenish their Coenzyme Q10 levels by taking a CoQ10 supplement, though. (pitchengine.com)
  • Coenzyme Q10 (or CoQ10) is a quinone, a substance that aids in providing energy to cells in all oxygen-breathing organisms. (purebulk.com)
  • When coenzyme Q10 was administered to middle-age and old-age rats, the level of CoQ10 increased by 10% to 40% in the cerebral cortex region of the brain. (emaxhealth.com)
  • Coenzyme Q10 (CoQ10) is implicated in mitochondrial energy flow, which is important in sperm maturation. (nutraingredients.com)
  • In human studies, blood levels of Coenzyme Q10 (CoQ10) decrease with statin use. (greenmedinfo.com)
  • Coenzyme Q10 (CoQ10): Miracle Supplement or Not? (everydayhealth.com)
  • The antioxidant coenzyme Q10 (CoQ10) is found in most living things and is used by our cells to process energy and function properly. (everydayhealth.com)
  • The body naturally produces coenzyme Q10 in quantities sufficient to prevent deficiency, and no symptoms related to CoQ10 deficiency have been observed in the general population. (everydayhealth.com)
  • Natural Factors Coenzyme Q10 30 mg is 100% natural, consisting only of the trans isomer identical to the body's own CoQ10. (naturalfactors.com)
  • 94(4):363-8, 1997 Oct. Abstract Treatment with oral coenzyme Q10 (CoQ10, 10 mg/kg per day for 6 days) was compared with no treatment in a previously described rabbit model of symptomatic cerebral vasospasm [Endo et al. (cryonet.org)
  • Coenzyme Q 10 , also known as ubiquinone , ubidecarenone , coenzyme Q , and abbreviated at times to CoQ 10 / ˌ k oʊ ˌ k juː ˈ t ɛ n / , CoQ , or Q 10 is a coenzyme that is ubiquitous in animals and most bacteria (hence the name ubiquinone). (wikipedia.org)
  • The reaction mechanism for complex III (cytochrome bc1, coenzyme Q: cytochrome C oxidoreductase) is known as the ubiquinone ("Q") cycle. (wikipedia.org)
  • Coenzyme Q 10 (also known as CoQ 10 , Q 10 , vitamin Q 10 , ubiquinone, and ubidecarenone) is a benzoquinone compound synthesized naturally by the human body. (cancer.gov)
  • Ubiquinone is likely effective in alternative medicine as an aid in treating coenzyme Q-10 deficiency, or reducing the symptoms of mitochondrial disorders (conditions that affect energy-production in the cells of the body). (cigna.com)
  • Coenzyme Q 10 (CoQ 10 ), also known as ubiquinone, is a major part of the body's mechanism for producing energy. (stdavids.com)
  • Coenzyme Q can exist in three oxidation states: the fully reduced ubiquinol form (CoQH2), the radical semiquinone intermediate (CoQH), and the fully oxidized ubiquinone form (CoQ). (life-enthusiast.com)
  • Co Q10 is an oil-soluble quinone, also called ubiquinone (which means "found everywhere", referring to its presence in all of the body's cells) or Vitamin Q. Coenzyme Q10 deficiency is associated with aging, as well as with various pathologies , like heart failure, cardiomyopathy, cardiac ischemia, angina pectoris, gum disease and Parkinson's disease. (hubpages.com)
  • In fact, the scientists who identified coenzyme Q 10 in 1957 initially honored its ubiquitous presence--it's found in every human cell and in all living organisms--by naming it "ubiquinone. (wholehealthmd.com)
  • Also called ubiquinone, coenzyme Q10 is a component of the electron transport chain that drives the generation of ATP in mitochondria. (alzforum.org)
  • Perspectives on therapy of cardiovascular diseases with coenzyme Q10 (ubiquinone). (evitamins.com)
  • Coenzyme Q-10, also known as Ubiquinone, is a vitamin-like substance that resembles Vitamin E but is an even more powerful antioxidant. (life-enthusiast.com)
  • Bioconcepts Coenzyme (also known as ubiquinone and ubidecarenone) is a well-known for its ability to help with chronic heart failure. (chemistdirect.co.uk)
  • The neurological problems gradually get worse unless treated with coenzyme Q10 supplementation. (medlineplus.gov)
  • If not treated with coenzyme Q10 supplementation, affected individuals eventually develop irreversible kidney failure (end-stage renal disease). (medlineplus.gov)
  • Oxidative stress and coenzyme Q10 supplementation in renal transplant recipients," International Urology and Nephrology , vol. 36, no. 2, pp. 253-258, 2004. (hindawi.com)
  • Because no coenzyme Q10 side effects are normally produced, supplementation with this product can have benefit for many types of disease, and for prevention of such diseases in dogs. (vetinfo.com)
  • Coenzyme Q10 supplementation has been widely used in such targeted therapies, including aging, stroke, neuromuscular diseases, Parkinson s disease, Alzheimer's disease, progressive supranuclear palsy, autosomal recessive cerebellar ataxias, amyotrophic lateral sclerosis and Huntington s disease. (ozon.ru)
  • Individuals taking these types of medications should talk to their doctor about whether Coenzyme Q10 supplementation is right for them. (purebulk.com)
  • Modern research supports the benefits to both performance and health by oral supplementation of Coenzyme Q-10 The New England Institute reports that Coenzyme Q-10 alone is effective in reducing mortality in experimental animals suffering from tumors and leukemia. (life-enthusiast.com)
  • Similar studies have noted conclusively that Coenzyme Q-10 supplementation reduces the risk of heart attack, increases respiration efficiency in the heart muscle, lowers blood pressure, and enhances immune system functions. (life-enthusiast.com)
  • A 14-day coenzyme Q10 supplementation is more effective than the acute supplementation to overcome the exercise induced adverse responses. (greenmedinfo.com)
  • Effect of coenzyme Q10 supplementation on exercise-induced response of inflammatory indicators and blood lactate in male runners. (greenmedinfo.com)
  • The purpose of present study was to determine the effect of acute and 14-day Coenzyme Q10 supplementation on inflammatory, blood lactate and muscle damage in male middle-distance runners. (greenmedinfo.com)
  • The results showed that acute and short-term Coenzyme Q10 supplementation had not significant effect on basal parameters. (greenmedinfo.com)
  • The acute coenzyme Q10 supplementation attenuated only the exercise-induced increase in response of the plasma CRP. (greenmedinfo.com)
  • The short-term (14-day) coenzyme Q10 supplementation attenuated the exercise-induced increase in response of the lactate, serum interleukin- 6, tumor necrosis factor-alpha, and CRP in male middle-distance runners. (greenmedinfo.com)
  • However, the acute and short-term coenzyme Q10 supplementation had not any significant effect on the exerciseinduced increase response of total serum creatine kinase. (greenmedinfo.com)
  • Based on the present results, it can be concluded that the 14-day coenzyme Q10 supplementation (5mg.kg-1.day-1) is more effective than the acute supplementation to overcome the exercise-induced adverse responses in some oxidative, inflammatory and biochemical parameters. (greenmedinfo.com)
  • Therefore, short-term coenzyme Q10 supplementation is recommended to reduce exercise-induced adverse consequences. (greenmedinfo.com)
  • This study aims to determine the effect of Coenzyme Q10 supplementation on conventional therapy of children with heart failure due to idiopathic dilated cardiomyopathy. (clinicaltrials.gov)
  • Known cases of idiopathic dilated cardiomyopathy who received supplementation of coenzyme Q10 as a part of their medical regimen. (clinicaltrials.gov)
  • Enzymes are specialized protein molecules, which generally require a mineral, such as magnesium or zinc, and a non-protein organic chemical, called a coenzyme. (healthy.net)
  • Coenzyme is any of a diverse group of small organic , non- protein , freely diffusing molecules that are loosely associated with and essential for the activity of enzymes , serving as carrier molecules that transfer chemical groups. (newworldencyclopedia.org)
  • Coenzymes are consumed and recycled continuously in metabolism, with one set of enzymes adding a chemical group to the coenzyme and another set removing it. (newworldencyclopedia.org)
  • Each class of group-transfer reaction is carried out by a particular coenzyme, which is the substrate for a set of enzymes that produce it, and a set of enzymes that consume it. (newworldencyclopedia.org)
  • Sometimes the actions of these enzymes are enhanced by other molecules called coenzymes. (livestrong.com)
  • All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester, such as acetyl-CoA) as a substrate. (wikipedia.org)
  • This pathways allows for 4′-phosphopantetheine to be replenished in the cell and allows for the conversion to coenzyme A through enzymes, PPAT and PPCK. (wikipedia.org)
  • Coenzymes help enzymes work to digest food and perform other body processes, and they help protect the heart and skeletal muscles. (cardiosmart.org)
  • Devoted to naturally occurring metal-carbon bonds, the book sums up recent work in the field, with chapters on organometallic chemistry of B12 coenzymes, cobalamin- and corrinoid-dependent enzymes, nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase, and nickel-alkyl bonds in acetyl-coenzyme A synthases. (thefreedictionary.com)
  • A member of a family of compounds called quinones, coenzyme Q 10 (sometimes called Co Q 10 ) works in concert with enzymes (hence the name "coenzyme") that are necessary for chemical reactions throughout the body. (wholehealthmd.com)
  • Vestiges of these nucleic acid enzymes persist in contemporary coenzymes. (springer.com)
  • Buckel W and Golding BT (1996) Glutamate and 2‐methyleneglutarate mutase: from microbial curiosities to paradigms for coenzyme B12‐dependent enzymes. (els.net)
  • Coenzyme Q10 plays an important role as the co-enzyme for at least three mitochondrial enzymes (complexes I, II and III) as well as enzymes in other parts of the cell. (purebulk.com)
  • Your liver itself requires Coenzyme Q-10 for energy to produce Coenzyme Q-10 and other enzymes. (life-enthusiast.com)
  • Without sufficient Coenzyme Q-10, your production of all enzymes enters the downward spiral characteristic of aging, and all the signs from poor health to reduced physical mobility and low-mindedness begin to set in. (life-enthusiast.com)
  • These findings may support that reactive oxygen species increased in malignant cells, and may cause overexpression of antioxidant enzymes and the consumption of coenzyme Q10. (chiro.org)
  • The mechanism of action of lovastatin is inhibition of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, an enzyme involved in the biosynthesis of cholesterol from acetyl-CoA. (pnas.org)
  • Both coenzymes and prosthetic groups are types of the broader group of cofactors, which are any non-protein molecules (usually organic molecules or metal ions) that are required by an enzyme for its activity (IUPAC 1997c). (newworldencyclopedia.org)
  • The known crystal structures of the inactive nickel (II) enzyme in complex with coenzyme M and coenzyme B (MCR-ox1-silent) and in complex with the heterodisulfide CoM-S-S-CoB (MCR-silent) were now refined at 1.16 A and 1.8 A resolution, respectively. (rcsb.org)
  • The structure of the novel enzyme state MCR-red1-silent at 1.8 A resolution revealed an active site only partially occupied by coenzyme M and coenzyme B. Increased flexibility and distinct alternate conformations were observed near the active site and the substrate channel. (rcsb.org)
  • As a consequence, the binding of coenzyme M induced specific conformational changes that postulate a molecular mechanism by which the enzyme ensures that methylcoenzyme M enters the substrate channel prior to coenzyme B as required by the active-site geometry. (rcsb.org)
  • The term "coenzyme" denotes it as an organic (contains carbon atoms), nonprotein molecule necessary for the proper functioning of its protein partner (an enzyme or an enzyme complex). (cancer.gov)
  • Because this enzyme is naturally produced in the body, adding coenzyme Q10 supplements can be beneficial to a dog's health, especially if symptoms show that a dog may be deficient in this substance. (vetinfo.com)
  • Coenzyme Q10 is a naturally occurring enzyme that helps the body create energy which assists many functions when fighting disease, illness and infection. (vetinfo.com)
  • A supplement of coenzyme Q10 can help to restore this enzyme to the dog's body, therefore increasing energy and necessary immune system function. (vetinfo.com)
  • Despite the fact that no coenzyme Q10 side effects are expected when giving a dog this enzyme supplement , there are still few considerations that you may want to keep in mind before you make a decision to begin using this product. (vetinfo.com)
  • Enzyme-reduced coenzyme binary complexes produce previously unreported shifts in the spectrum of the free coenzyme. (sciencemag.org)
  • These shifts give rise to difference spectra which resemble a general environmental change for reduced diphosphopyridine nucleotide (DPNH) in the glutamic dehydrogenase-DPNH complex, and indicate a more specific enzyme-coenzyme interaction for yeast alcohol dehydrogenase-DPNH, isocitrate dehydrogenase-TPNH, and lactic dehydrogenase-DPNH complexes. (sciencemag.org)
  • Once a fatty acid molecule is "activated" (attached to coenzyme A), a series of four reactions, each catalyzed by a different enzyme, is required to remove each acetyl-coenzyme A molecule. (bionity.com)
  • We determined coenzyme Q10 (Q) concentrations, antioxidant enzyme activities (mitochondrial and total superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), catalase), and malondialdehyde (MDA) levels in tumor and surrounding tumor-free tissues. (chiro.org)
  • Effects of coenzyme Q10 in early Parkinson Disease: Evidence of slowing of the functional decline. (healthday.com)
  • Effects of coenzyme Q10 on exercise tolerance in chronic stable angina pectoris. (evitamins.com)
  • Effects of coenzyme Q10 on ischemic myocardium during coronary artery occlusion-evaluation of the time needed to change irreversible myocardium. (evitamins.com)
  • All Verified ubidecarenone coenzyme q10 suppliers & ubidecarenone coenzyme q10 manufacturers have passed our Business License Check, they can provide quality ubidecarenone coenzyme q10 products. (opencroquet.org)
  • 80 Mesh Coenzyme Q10 Powder Ubidecarenone Diminishing Fine Lines Restore Skin Elasticity 1. (opencroquet.org)
  • Amino Acid Medicine Grade Supplements Coenzyme Q10 Anti Aging Raw Ubidecarenone Powder CAS:303-98-0 Basic Info. (opencroquet.org)
  • Ubidecarenone ( Coenzyme Q10 ) [Form]: Powder [Color]:Yellow fine Powder. (opencroquet.org)
  • Low blood levels of coenzyme Q 10 have been detected in patients with some types of cancer. (cancer.gov)
  • Scientists have found that people suffering from coronary artery disease have very low levels of coenzyme Q 10 (3). (wholehealthmd.com)
  • The importance of having sufficient levels of Coenzyme Q10 cannot be overstated as the substance is vital for cellular energy production. (pitchengine.com)
  • Although the body is able to produce sufficient levels of Coenzyme Q10 under normal circumstances, there are certain factors that cause its levels to deplete. (pitchengine.com)
  • Studies have shown that reduced levels of Coenzyme Q-10 contribute directly to the aging process, while increasing Coenzyme Q-10 intake will actually retard and slow down the effects of "Father Time" on all of us. (life-enthusiast.com)
  • It's also interesting that some of the medications that may decrease levels of coenzyme Q10 are taken by migraineurs - such as tricyclic antidepressants and beta-blockers. (relieve-migraine-headache.com)
  • DRESDEN, Germany, May 14 -- Treating Parkinson's disease patients with the antioxidant coenzyme (CoQ 10 ) boosts plasma levels of the substance but doesn't improve disease symptoms, said investigators here. (medpagetoday.com)
  • Formulated with antioxidant coenzyme Q10 to build collagen and firm skin, Matrixyl 3000 to reduce wrinkles, and hyaluronic acid to moisturize skin. (yesstyle.com)
  • A lack of functional protein produced from any one of the COQ genes decreases the normal production of coenzyme Q10. (medlineplus.gov)
  • Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl carrier protein and formyltetrahydrofolate dehydrogenase. (wikipedia.org)
  • Furthermore, theaflavins also inhibited acetyl-coenzyme A carboxylase activities by stimulating AMP-activated protein kinase (AMPK) through the LKB1 and reactive oxygen species pathways. (thefreedictionary.com)
  • Masuda J, Shibata N, Morimoto Y, Toraya T and Yasuoka N (2000) How a protein generates a catalytic radical from coenzyme B12: X‐ray structure of a diol‐dehydratase‐adeninylpentylcobalamin complex. (els.net)
  • The midway gene encodes a protein similar to mammalian acyl coenzyme A: diacylglycerol acyltransferase (DGAT), which converts diacylglycerol (DAG) into triacylglycerol (TAG). (genetics.org)
  • Primary coenzyme Q10 deficiency is a disorder that can affect many parts of the body, especially the brain, muscles, and kidneys. (medlineplus.gov)
  • As its name suggests, the disorder involves a shortage (deficiency) of a substance called coenzyme Q10. (medlineplus.gov)
  • The severity, combination of signs and symptoms, and age of onset of primary coenzyme Q10 deficiency vary widely. (medlineplus.gov)
  • A type of kidney dysfunction called nephrotic syndrome is another common feature of primary coenzyme Q10 deficiency. (medlineplus.gov)
  • can also occur in primary coenzyme Q10 deficiency. (medlineplus.gov)
  • The prevalence of primary coenzyme Q10 deficiency is thought to be less than 1 in 100,000 people. (medlineplus.gov)
  • Primary coenzyme Q10 deficiency is caused by mutations in genes that provide instructions for making proteins involved in the production (synthesis) of a molecule called coenzyme Q10. (medlineplus.gov)
  • Smaller numbers of mutations in other COQ genes have also been found to cause primary coenzyme Q10 deficiency. (medlineplus.gov)
  • Studies suggest that a shortage (deficiency) of coenzyme Q10 impairs oxidative phosphorylation and increases the vulnerability of cells to damage from free radicals. (medlineplus.gov)
  • A deficiency of coenzyme Q10 may also disrupt the production of pyrimidines. (medlineplus.gov)
  • These changes can cause cells throughout the body to malfunction, which may help explain the variety of organs and tissues that can be affected by primary coenzyme Q10 deficiency. (medlineplus.gov)
  • Coenzyme Q10 deficiency can also be caused by mutations in genes that are not directly related to the synthesis of coenzyme Q10. (medlineplus.gov)
  • Many patients with heart failure have Coenzyme Q10 deficiency at myocardial level (the myocardium is the heart's muscular wall). (hubpages.com)
  • Medium-chain acyl-coenzyme A dehydrogenase deficiency is a fatty acid oxidation disorder associated with inborn errors of metabolism . (bionity.com)
  • Coenzyme Q10 is a substance found in the cells of the human body, necessary for cellular respiration and the production of energy. (hubpages.com)
  • Coenzyme Q10, essentially a vitamin-like substance, acts as a coenzyme in the body and has a variety of critical functions. (purebulk.com)
  • The assimilation and absorption of Coenzyme Q-10 may be improved if taken with a fatty substance such as oil, peanut butter, or olive oil. (purebulk.com)
  • Methyl-coenzyme M reductase (MCR) catalyzes the final reaction of the energy conserving pathway of methanogenic archaea in which methylcoenzyme M and coenzyme B are converted to methane and the heterodisulfide CoM-S-S-CoB. (rcsb.org)
  • Recombinant fragment within Human Methylmalonyl Coenzyme A mutase (internal sequence). (abcam.com)
  • 1996) How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl‐coenzyme A mutase at 2 Å resolution. (els.net)
  • We offer Methylmalonyl Coenzyme A mutase Lysates for use in common research applications: Western Blot. (novusbio.com)
  • Each Methylmalonyl Coenzyme A mutase Lysate is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Our Methylmalonyl Coenzyme A mutase Lysates can be used in a variety of model species. (novusbio.com)
  • In these pathways, coenzyme A needs to be provided from an external source, such as food, in order to produce 4′-phosphopantetheine. (wikipedia.org)
  • A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. (wikipedia.org)
  • Its acetyl-coenzyme A form is the primary input in the citric acid cycle and is obtained from glycolysis, amino acid metabolism, and fatty acid beta oxidation. (wikipedia.org)
  • Goat acetyl-coenzyme A carboxylase alpha: molecular characterization, polymorphism, and association with milk traits. (thefreedictionary.com)
  • the hepatic-TG DNL index was also associated with expression of the hepatic lipogenic genes acetyl-Coenzyme A carboxylase alpha (ACACA), fatty acid synthase (FASN), and sterol regulatory element binding transcription factor 1 (SREBP-1), and changes in the expression of these genes were also closely reflected by the VLDL-TG DNL index. (thefreedictionary.com)
  • Ki-Han K Regulation of mammalian acetyl-coenzyme a carboxylase. (thefreedictionary.com)
  • In addition, the expression of acetyl-Coenzyme A synthetase 2 (categorized as a "Fatty acid oxidation" gene) was three-fold higher in mammary than liver tissue, consistent with its function of activating acetate for use in ruminant lipid synthesis and fuel support (Smith and Prior, 1986). (thefreedictionary.com)
  • These acids are made from acetyl-coenzyme A (acetyl-CoA), which is also the starting material for biosynthesis of waxes, flavonoids, certain amino acids and other compounds. (thefreedictionary.com)
  • The licensed technology may provide the enhanced production of bio-diesel feedstocks, whereby over expression of Acetyl-Coenzyme A Carboxylase in algae leads to overproduction of triglycerides. (thefreedictionary.com)
  • The expression levels of 3-hydroxyacyl-CoA dehydrogenase type-2 (HCDH), acetyl-Coenzyme A acetyltransferase 2 (ACAT) and elongation factor Tu were down-regulated, and alpha-enolase and creatine kinase were up-regulated in the livers of ketotic cows. (thefreedictionary.com)
  • The fatty acids are broken down in stages by the successive removal of molecules of acetyl-coenzyme A, which contains 2 carbon atoms. (bionity.com)
  • Your search "coenzyme q10 capsules" did not match any products. (opencroquet.org)
  • Coenzyme Q 10 is a compound that is made naturally in the body. (viovet.co.uk)
  • Although several naturally occurring forms of coenzyme Q have been identified, Q 10 is the predominant form found in humans and most mammals, and it is the form most studied for therapeutic potential. (cancer.gov)
  • Coenzyme Q 10 is made naturally by the human body. (cancer.gov)
  • Coenzyme Q10 is a naturally occurring nutrient found in each cell of the body. (purebulk.com)
  • Coenzyme Q10 is a naturally occurring antioxidant that our bodies need for energy. (everydayhealth.com)
  • Coenzyme Q10 is a chemical compound found naturally in the human body (and in other animals as well). (relieve-migraine-headache.com)
  • Taking daily supplements of Coenzyme Q10 can have many benefits, especially after the age of 35. (hubpages.com)
  • One of the world's most popular supplements, the chemical coenzyme Q 10 has generated great excitement as a heart disease remedy and a cure for countless other conditions. (wholehealthmd.com)
  • People with congestive heart failure, in which a weakened heart pumps inefficiently, may stand to benefit the most from coenzyme Q 10 supplements. (wholehealthmd.com)
  • Subsequently, Coenzyme Q10 oral supplements are commonly sold as gel caps dissolved in soybean oil. (purebulk.com)
  • Nutritional supplements like coenzyme Q10 and L-carnitine may contribute to higher sperm quality says a review, which points to little evidence linking sperm health with more pregnancies and births. (nutraingredients.com)
  • The nutritional supplement coenzyme Q10 could slow the progress of early-stage Parkinson's. (healthy.net)
  • Eighty patients with early Parkinson's disease, recruited from 10 centres across the USA, were randomly assigned to receive wafers containing coenzyme Q10 at a dose of 300, 600 or 1200 mg/day, or placebo. (healthy.net)
  • Coenzyme Q10 treatment does not slow the progression of Parkinson's disease (PD). (alzforum.org)
  • The coenzyme Q10 molecule has several critical functions in cells throughout the body. (medlineplus.gov)
  • Ectonucleotide pyrophosphates (ENPP) degrade coenzyme A to 4′-phosphopantetheine, a stable molecule in organisms. (wikipedia.org)
  • Coenzyme Q 10 is a very large molecule with some chemical properties that affect the rate in which the body can use it (hydrophobic). (purebulk.com)
  • Coenzyme Q 10 may be indicated in cardiovascular disease, particularly in congestive heart failure. (healingwell.com)
  • Most of these investigations have focused on coenzyme Q 10 as a treatment for cardiovascular disease. (cancer.gov)
  • Higher daily dosages of Coenzyme Q10 (50 mg and over) may provide even more cardiovascular and antioxidant protection than daily dosages below 30 mg. (discount-vitamins-herbs.net)
  • Thus, it will be the only form of coenzyme Q discussed in this summary. (cancer.gov)
  • Randomized, double-blind placebo-controlled trial of coenzyme q10 in patients with acute myocardial infarction. (healthday.com)
  • No report of a randomized clinical trial of coenzyme Q 10 as a treatment for cancer has been published in a peer-reviewed scientific journal. (cancer.gov)
  • Effect of coenzyme Q10 on risk of atherosclerosis in patients with recent myocardial infarction. (evitamins.com)
  • Administration of coenzyme Q10 by nutrition may induce the protective effect of coenzyme Q10 on breast tissue. (chiro.org)
  • The patients taking placebo showed a slight disease progression whereas the groups treated with coenzyme Q10 experienced less progression. (healthy.net)
  • In a 12-month placebo-controlled trial of more than 2,500 people suffering from this disease, 80% experienced an improvement in symptoms--less ankle swelling and shortness of breath, and better color and sleep habits--when they supplemented their standard medications with a daily 100 mg dose of coenzyme Q 10 (1). (wholehealthmd.com)
  • In a recent six-month trial of 46 individuals with moderate to severe congestive heart failure, those assigned to take coenzyme Q 10 (rather than a placebo) experienced no apparent improvement in heart function or symptom relief. (wholehealthmd.com)
  • Eighteen male middle-distance runners in a randomized and quasi experimental study were allocated into two equal groups: supplement group (n=9, Coenzyme Q10: 5mg/kg/day) and placebo group (n= 9, Dextrose: 5mg/kg/day). (greenmedinfo.com)
  • In a prospective, randomized, double-blinded, placebo-controlled trial, patients younger than 18 years with idiopathic dilated cardiomyopathy randomizes to receive either Coenzyme Q10 or placebo. (clinicaltrials.gov)
  • Coenzyme A biosynthetic machinery in mammalian cells. (nih.gov)
  • A branch of the mevalonate cholesterol biosynthetic pathway in mammalian cells leads to the formation of Coenzyme Q 10 [reviewed by Brown and Goldstein, J. Lipid Res. (freepatentsonline.com)
  • Coenzyme q-10 is a powerful antioxidant that protects heart muscles, improves energy levels, and may have some other health benefits by protecting the mitochondria (energy factories) in our cells from oxidative stress. (thebody.com)
  • In addition, coenzyme Q 10 acts as a powerful antioxidant to prevent the cellular damage caused by unstable oxygen molecules called free radicals. (wholehealthmd.com)
  • Coenzyme Q10 grabs the electrons that are generated as you digest food and shuttles them around inside the cells, a process that helps to produce energy. (healthday.com)
  • Coenzymes act as agents for transferring different groups such as electrons or molecules during reactions. (livestrong.com)
  • Some coenzymes function by ferrying electrons or negative charges to enhance a reaction. (livestrong.com)
  • Vitamin B-3, on the other hand, is the precursor for the nicotinamide coenzymes, nicotinamide adenine dinucleotide, or NAD, and nicotinamide adenine dinucleotide 2'-phosphate, or NADP, which carry electrons between different proteins. (livestrong.com)
  • These include the B-vitamins and vitamin C. In addition to those derived from vitamins, there is another group of coenzymes known as metabolite coenzymes, usually made from nucleotides. (livestrong.com)
  • This proposal rationalizes the fact that many coenzymes are nucleotides or heterocyclic bases which could be derived from nucleotides. (springer.com)
  • Given the importance of coenzyme Q 10 in optimizing cellular energy production, use of this compound as a treatment for diseases other than cancer has been explored. (cancer.gov)
  • Coenzyme Q10 is a vitamin-like essential nutrient that helps increase levels of cellular energy production and is required by every cell in our body. (naturalfactors.com)
  • The dose depends on what medications you are taking for your health since some medications can lower Coenzyme Q-10. (thebody.com)
  • Coenzyme Q10 may interact with some blood pressure medications and some blood thinners. (purebulk.com)
  • Caution should be taken if you're taking blood pressure medications, as coenzyme Q10 may enhance them beyond what your doctor would want. (relieve-migraine-headache.com)
  • Primary endpoint is the difference of acute rejection episodes during 6 month follow-up stratified by coenzyme Q10 level. (nova.edu)
  • This is the first study to investigate coenzyme Q10 level on acute graft survival. (nova.edu)
  • 8. Kuklinski B, Weissenbacher E, Fahnrich A. Coenzyme Q10 and antioxidants in acute myocardial infarction. (evitamins.com)
  • Coenzyme Q10 protects ischemic myocardium in an open-chest swine model. (evitamins.com)
  • Title Oral coenzyme Q10 administration prevents the development of ischemic brain lesions in a rabbit model of symptomatic vasospasm. (cryonet.org)
  • Lovastatin decreases coenzyme Q levels in humans. (pnas.org)
  • Serum concentration of lipoprotein (a) decreases on treatment with hydrosoluble coenzyme Q10 in patients with coronary artery disease: discovery of a new role. (evitamins.com)
  • In cell membranes, coenzyme Q10 acts as an antioxidant, protecting cells from damage caused by unstable oxygen-containing molecules (free radicals), which are byproducts of energy production. (medlineplus.gov)
  • AllegroMedical.com presents The Sunmark Coenzyme Q-10 Dietary Supplement. (allegromedical.com)
  • Coenzyme Q 10 is marketed in the United States as a dietary supplement . (cancer.gov)
  • Coenzyme Q10 plays a pivotal role in mitochondrial respiratory chain for cell power supply. (ozon.ru)
  • Coenzyme Q-10 is a key nutrient that may help maintain a healthy heart. (allegromedical.com)
  • A vitamin-like essential nutrient, coenzyme Q10 facilitates energy delivery to metabolic processes in the body. (naturalfactors.com)
  • This Coenzyme Q10 is a pharmaceutical-grade pure bulk nutritional powder. (purebulk.com)
  • Statin drugs adversely effect memory likely through depletion of coenzyme q10 and interference with mitochondrial function in the brain. (greenmedinfo.com)
  • The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (EC 1.10.2.2), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). (wikipedia.org)
  • This reduced coenzyme is then a substrate for any of the reductases in the cell that need to reduce their substrates (Pollak et al. (newworldencyclopedia.org)
  • Biochemical Rationale and Myocardial Tissue Data on the Effective Therapy of Cardiomyopathy with Coenzyme Q.sub.10, K. Folker et al. (freepatentsonline.com)
  • Most studies using coenzyme Q10 in treating cardiomyopathy have shown positive results, including improved quality of life, heart function tests, and survival rates. (peacehealth.org)
  • Coenzyme Q10 also has been shown to improve cardiac function in people with hypertrophic cardiomyopathy-a less common form of cardiomyopathy. (peacehealth.org)
  • In blood and tissue samples taken from patients suffering from cardiomyopathy, Coenzyme Q-10 was found to be deficient in two separate independent studies. (life-enthusiast.com)
  • Bioconcepts Coenzyme Q10 100mg can be used in the treatment of high blood pressure and may help reduce high levels of cholesterol, which can reduce visible signs of ageing. (chemistdirect.co.uk)
  • Subject: coenzyme q10 and ischemia Authors Grieb P. Ryba MS. Sawicki J. Chrapusta SJ. (cryonet.org)