Coenzymes. Medical search

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.

The mitochondria of the myocardium.

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)

Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames. (1/1288)

A universal molybdenum-containing cofactor (MoCo) is essential for the activity of all human molybdoenzymes, including sulphite oxidase. The free cofactor is highly unstable, and all organisms share a similar biosynthetic pathway. The involved enzymes exhibit homologies, even between bacteria and humans. We have exploited these homologies to isolate a cDNA for the heterodimeric molybdopterin (MPT)-synthase. This enzyme is necessary for the conversion of an unstable precursor into molybdopterin, the organic moiety of MoCo. The corresponding transcript shows a bicistronic structure, encoding the small and large subunits of the MPT-synthase in two different open reading frames (ORFs) that overlap by 77 nucleotides. In various human tissues, only one size of mRNA coinciding with the bicistronic transcript was detected. In vitro translation and mutagenesis experiments demonstrated that each ORF is translated independently, leading to the synthesis of a 10-kDa protein and a 21-kDa protein for the small and large subunits, respectively, and indicated that the 3'-proximal ORF of the bicistronic transcript is translated by leaky scanning. (+info)

Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B. (2/1288)

Biosynthesis of the molybdenum cofactor (MoCo) can be divided into (1) the formation of a precursor and (2) the latter's subsequent conversion, by molybdopterin synthase, into the organic moiety of MoCo. These two steps are reflected by the complementation groups A and B and the two formally distinguished types of MoCo deficiency that have an identical phenotype. Both types of MoCo deficiency result in a pleiotropic loss of all molybdoenzyme activities and cause severe neurological damage. MOCS1 is defective in patients with group A deficiency and has been shown to encode two enzymes for early synthesis via a bicistronic transcript with two consecutive open reading frames (ORFs). MOCS2 encodes the small and large subunits of molybdopterin synthase via a single transcript with two overlapping reading frames. This gene was mapped to 5q and comprises seven exons. The coding sequence and all splice site-junction sequences were screened for mutations, in MoCo-deficient patients in whom a previous search for MOCS1 mutations had been negative. In seven of the eight patients whom we investigated, we identified MOCS2 mutations that, by their nature, are most likely responsible for the deficiency. Three different frameshift mutations were observed, with one of them found on 7 of 14 identified alleles. Furthermore, a start-codon mutation and a missense mutation of a highly conserved amino acid residue were found. The locations of the mutations confirm the functional role of both ORFs. One of the patients with identified MOCS2 mutations had been classified as type B, in complementation studies. These findings support the hypothetical mechanism, for both forms of MoCo deficiency, that formerly had been established by cell-culture experiments. (+info)

Human biotinidase isn't just for recycling biotin. (3/1288)

For years, the major role of biotin has been as the coenzyme for four carboxylases in humans. Although there has been evidence that biotin might have other functions, none has been firmly established. The discovery that human serum biotinidase has biotinyl-transferase activity, in addition to biotinidase hydrolase activity, presents new possibilities for the role of biotinidase in biotin metabolism. Specific transfer of biotin to histones by biotinidase provides a possible explanation for why biotin is found in the nucleus and the nature of its role in the regulation of protein transcription. Future studies will help to determine the functions of biotinidase in biotin metabolism and in disease states. (+info)

Re-design of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Enhancement of adenosine N1-oxide reductase activity. (4/1288)

The periplasmic DMSO reductase from Rhodobacter sphaeroides f. sp. denitrificans has been expressed in Escherichia coli BL21(DE3) cells in its mature form and with the R. sphaeroides or E. coli N-terminal signal sequence. Whereas the R. sphaeroides signal sequence prevents formation of active enzyme, addition of a 6x His-tag at the N terminus of the mature peptide maximizes production of active enzyme and allows for affinity purification. The recombinant protein contains 1.7-1.9 guanines and greater than 0.7 molybdenum atoms per molecule and has a DMSO reductase activity of 3.4-3.7 units/nmol molybdenum, compared with 3.7 units/nmol molybdenum for enzyme purified from R. sphaeroides. The recombinant enzyme differs from the native enzyme in its color and spectrum but is indistinguishable from the native protein after redox cycling with reduced methyl viologen and Me2SO. Substitution of Cys for the molybdenum-ligating Ser-147 produced a protein with DMSO reductase activity of 1.4-1.5 units/nmol molybdenum. The mutant protein differs from wild type in its color and absorption spectrum in both the oxidized and reduced states. This substitution leads to losses of 61-99% of activity toward five substrates, but the adenosine N1-oxide reductase activity increases by over 400%. (+info)

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (5/1288)

In order to investigate the effects of trace elements on different metabolic pathways, the thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been cultivated on various carbon substrates in the presence and absence of molybdate. When grown on glucose (but neither on glutamate nor casein hydrolysate) as sole carbon source, the lack of molybdate results in serious growth inhibition. By analysing cytosolic fractions of glucose adapted cells for molybdenum containing compounds, an aldehyde oxidoreductase was detected that is present in the cytosol to at least 0.4% of the soluble protein. With Cl2Ind (2,6-dichlorophenolindophenol) as artificial electron acceptor, the enzyme exhibits oxidizing activity towards glyceraldehyde, glyceraldehyde-3-phosphate, isobutyraldehyde, formaldehyde, acetaldehyde and propionaldehyde. At its pH-optimum (6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant. The protein has an apparent molecular mass of 177 kDa and consists of three subunits of 80.5 kDa (alpha), 32 kDa (beta) and 19.5 kDa (gamma). It contains close to one Mo, four Fe, four acid-labile sulphides and four phosphates per protein molecule. Methanol extraction revealed the existence of 1 FAD per molecule and 1 molybdopterin per molecule, which was identified as molybdopterin guanine dinucleotide on the basis of perchloric acid cleavage and thin layer chromatography. EPR-spectra of the aerobically prepared enzyme exhibit the so-called 'desulpho-inhibited'-signal, known from chemically modified forms of molybdenum containing proteins. Anaerobically prepared samples show both, the signals arising from the active molybdenum-cofactor as well as from the two [2Fe-2S]-clusters. According to metal-, cofactor-, and subunit-composition, the enzyme resembles the members of the xanthine oxidase family. Nevertheless, the melting point and long-term thermostability of the protein are outstanding and perfectly in tune with the growth temperature of S. acidocaldarius (80 degrees C). The findings suggest the enzyme to function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylated Entner-Doudoroff pathway and thereby may attribute a new physiological role to this class of enzyme. (+info)

A function for the vitamin E metabolite alpha-tocopherol quinone as an essential enzyme cofactor for the mitochondrial fatty acid desaturases. (6/1288)

A critical analysis of the changes in fatty acid patterns and their metabolism elicited by vitamin E deficiency leads to the proposal that a major role of dietary RRR-alpha-tocopherol (alpha-TOC) is as an enzymatic precursor of alpha-tocopherolquinone (alpha-TQ) whose semiquinone radical functions as an essential enzyme cofactor for the fatty acid desaturases of the recently elucidated carnitine-dependent, channeled, mitochondrial desaturation-elongation pathway; a detailed mechanism for its function is proposed. Pathophysiological states produced by vitamin E deficiency and alpha-TOC transfer protein defects, such as ataxia, myopathy, retinopathy, and sterility are proposed to develop from the effects of impaired alpha-TQ-dependent desaturases and the resulting deficiency of their polyenoic fatty acid products. (+info)

Structure and function of a cysBJIH gene cluster in the purple sulphur bacterium Thiocapsa roseopersicina. (7/1288)

A gene cluster containing homologues of the genes cysB, cysJI and cysH was found in the genome of the sulphur-oxidizing purple bacterium Thiocapsa roseopersicina. The nucleotide sequence indicated four open reading frames encoding homologues of 3'-phosphoadenylylsulphate (PAPS) reductase (CysH), sulphite reductase flavoprotein (CysJ) and haem protein (CysI) subunits, and a transcriptional regulator (CysB). Genes cysJIH are separated by a short cis-active intergenic region from cysB which is transcribed divergently. cysB encodes a polypeptide of 35.9 kDa consisting of 323 amino acid residues with 40% identity to the CysB regulator from enterobacteria. cysH encodes a protein with 239 amino acid residues and a calculated mass of 27.7 kDa; cysJ encodes a protein with 522 amino acid residues and a mass of 57.8 kDa; and cysI encodes a protein with 559 amino acid residues and a mass of 62.3 kDa. The cysJIH gene products have been expressed and used for complementation of cys mutants from Escherichia coli Biochemical analysis. The gene product CysH is a thioredoxin-dependent PAPS reductase (EC 1.8.99.4). It was repressed under photoautotrophic growth using hydrogen sulphide as electron donor and derepressed under conditions of sulphate deficiency. Products of the cysJI genes were identified as the two subunits of NADPH-sulphite reductase (EC 1.8.1.2). cysJ encoded the flavoprotein, with > or = 39% identity to the protein from E. coli, and cysI encoded the haem protein, with > or = 53% identity. A cysI clone was used to complement the corresponding mutant from E. coli and to express enzymically active methylviologen-sulphite reductase. (+info)

Specificity of coenzyme analogues and fragments in promoting or impeding the refolding of clostridial glutamate dehydrogenase. (8/1288)

NAD+ facilitates high-yield reactivation of clostridial glutamate dehydrogenase (GDH) after unfolding in urea. The specificity of this effect has been explored by using analogues and fragments of NAD+. The adenine portion, unlike the nicotinamide portion, is important for reactivation. Alteration in the nicotinamide portion, in acetylpyridine adenine dinucleotide, has little effect, whereas loss of the 6-NH2 substitution on the adenine ring, in 6-deamino NAD, diminishes the effectiveness of the nucleotide in promoting refolding. Also ADP-ribose, lacking nicotinamide, promotes reactivation whereas NMN-phosphoribose, lacking the adenine, does not. Of the smaller fragments, those containing an adenosine moiety, and especially those with one or more phosphate groups, impede the refolding ability of NAD+, and are able to bind to the folding intermediate though unable to facilitate refolding. These results are interpreted in terms of the known 3D structure for clostridial glutamate dehydrogenase. It is assumed that the refolding intermediate has a more or less fully formed NAD+-binding domain but a partially disordered substrate-binding domain and linking region. Binding of NAD+ or ADP-ribose appears to impose new structural constraints that result in completion of the correct folding of the second domain, allowing association of enzyme molecules to form the native hexamer. (+info)

... , 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 ...

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

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. ...

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

... (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic ... Dolphin D, Poulson R, Avramovic O (1986). "Vitamin B6: Pyridoxal Phosphate" (PDF). Coenzymes and Cofactors. 1, Part B. New York ... PLP acts as a coenzyme in all transamination reactions, and in certain decarboxylation, deamination, and racemization reactions ... a unique coenzyme B6-dependent enzyme". Protein Science. 15 (9): 2093-106. doi:10.1110/ps.062328306. PMC 2242600. PMID 16943443 ...

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

Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly ... Organic cofactors are sometimes further divided into coenzymes and prosthetic groups. The term coenzyme refers specifically to ... Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is ... However, the author could not arrive at a single all-encompassing definition of a "coenzyme" and proposed that this term be ...

https://en.wikipedia.org/wiki/Cofactor_(biochemistry)

Coenzymes are small organic molecules that can be loosely or tightly bound to an enzyme. Coenzymes transport chemical groups ... For example, about 1000 enzymes are known to use the coenzyme NADH. Coenzymes are usually continuously regenerated and their ... These coenzymes cannot be synthesized by the body de novo and closely related compounds (vitamins) must be acquired from the ... Organic cofactors can be either coenzymes, which are released from the enzyme's active site during the reaction, or prosthetic ...

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

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 ...

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

Methanogenesis involves a range of coenzymes that are unique to these archaea, such as coenzyme M and methanofuran. Other ... DiMarco AA, Bobik TA, Wolfe RS (1990). "Unusual coenzymes of methanogenesis". Annual Review of Biochemistry. 59: 355-94. doi: ... two unusual coenzymes, 3. results of 16S ribosomal RNA gene sequencing. To emphasize this difference, Woese, Otto Kandler and ...

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

As a result of the need to produce high energy phosphate-containing organic compounds (generally in the form of Coenzyme A- ... such as coenzyme M and methanofuran. These cofactors are responsible (among other things) for the establishment of a proton ... "Unusual coenzymes of methanogenesis". Annu. Rev. Biochem. 59: 355-94. doi:10.1146/annurev.bi.59.070190.002035. PMID 2115763. ...

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

It became obvious coenzymes are involved in biochemistry of methanogens as kilogram scale of cell was developed and utilized ... DiMarco AA, Bobik TA, Wolfe RS (1990-01-01). "Unusual coenzymes of methanogenesis". Annual Review of Biochemistry. 59 (1): 355- ...

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

"Nucleotide Co-Enzymes: A Study in Synthesis , Berkeley Graduate Lectures". gradlectures.berkeley.edu. Retrieved 27 January 2018 ... Todd, Alexander R (1949). Vitamins, coenzymes and nucleotides; a series of lectures presented at the University of Notre Dame ... and nucleotide coenzymes gained him the Nobel Prize for Chemistry. Todd was born in Cathcart in outer Glasgow, the son of ...

https://en.wikipedia.org/wiki/Alexander_R._Todd

Coenzyme M. *Coenzyme Q. *Heme / Haem (A, B, C, O). *Lipoic Acid ...

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

The structure of the coenzyme was famously determined by Dorothy Hodgkin and co-workers, for which she received a Nobel Prize ...

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

Coenzyme M. *Coenzyme Q. *Heme / Haem (A, B, C, O). *Lipoic Acid ...

https://en.wikipedia.org/wiki/Riboflavin-5-Sodium_Phosphate

Role in coenzyme Q10 synthesisEdit. Tyrosine (or its precursor phenylalanine) is needed to synthesize the benzoquinone ... This cis-trans-isomerase contains glutathione as a coenzyme. Fumarylacetoacetate is finally split by the enzyme ...

https://en.m.wikipedia.org/wiki/Tyrosine

These coenzymes are therefore continuously made, consumed and then recycled. One central coenzyme is adenosine triphosphate ( ... This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to reduce their ... Each class of group-transfer reactions is carried out by a particular coenzyme, which is the substrate for a set of enzymes ... The electrons then flow through photosystem I and can then either be used to reduce the coenzyme NADP+.fThese cooenzyme can be ...

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

For recent partial syntheses of vitamin B12 and coenzyme B12 from cobyric acid, see Widner, Florian J.; Gstrein, Fabian; ... Glusker, Jenny P. (1995). "Vitamin B12 and the B12 Coenzymes". Vitamins and Hormones. 50: 1-76. Bernhauer, K.; Dellweg, H.; ... Synthesis of Coenzyme B12: A Vehicle for the Teaching of Organic Synthesis". In Quinkert, Gerhard; Kisakürek, M. Volkan (eds ... Kräutler, Bernhard (2017). "Partial Synthesis of Coenzyme B12 from Cobyric Acid". Helvetica Chimica Acta. 100 (9): e1700170. ...

https://en.wikipedia.org/wiki/Vitamin_B12_total_synthesis

The discovery of co-enzymes by Sir Arthur Harden FRS and his colleagues was recognised by the co-award to him of the Nobel ... "Structure of Coenzyme. A. J. Baddiley, E. M .Thain, G. D. Novelli & F. Lipmann - Lister Institute of Preventive Medicine; ... by Alexander Todd PRS in 1949 the structure of co-enzyme A was defined by James Baddiley, together with other workers at ...

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

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 ...

https://en.wikipedia.org/wiki/PANK4

Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It ... "Entrez Gene: PANK1 pantothenate kinase 1". CS1 maint: discouraged parameter (link) Robishaw JD, Neely JR (1985). "Coenzyme A ... Ramaswamy G, Karim MA, Murti KG, Jackowski S (2004). "PPARalpha controls the intracellular coenzyme A concentration via ...

https://en.wikipedia.org/wiki/PANK1

... 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 ... Preparation and properties of coenzyme A transferase". J. Biol. Chem. 221 (1): 15-31. PMID 13345795. Biology portal v t e. ...

https://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase

Pantothenate kinase is a key regulatory enzyme in the biosynthesis of coenzyme A (CoA) in bacteria and mammalian cells. It ... "Entrez Gene: PANK2 pantothenate kinase 2 (Hallervorden-Spatz syndrome)". Robishaw JD, Neely JR (1985). "Coenzyme A metabolism ... Kotzbauer PT, Truax AC, Trojanowski JQ, Lee VM (2005). "Altered neuronal mitochondrial coenzyme A synthesis in ...

https://en.wikipedia.org/wiki/PANK2_(gene)

It transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). In humans, cytochrome c is ...

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

Ubiquinol (coenzyme Q) Lipid 5[84] 200 (human)[85] Uric acid[edit]. Uric acid is by far the highest concentration antioxidant ... "Serum coenzyme Q10 concentrations in healthy men supplemented with 30 mg or 100 mg coenzyme Q10 for two months in a randomised ... Turunen M, Olsson J, Dallner G (January 2004). "Metabolism and function of coenzyme Q". Biochimica et Biophysica Acta. 1660 (1- ... For example, ubiquinol (coenzyme Q) is poorly absorbed from the gut and is made through the mevalonate pathway.[85] Another ...

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

Intravenous and oral formulations of acetylcysteine are available for the treatment of paracetamol (acetaminophen) overdose.[13] When paracetamol is taken in large quantities, a minor metabolite called N-acetyl-p-benzoquinone imine (NAPQI) accumulates within the body. It is normally conjugated by glutathione, but when taken in excess, the body's glutathione reserves are not sufficient to deactivate the toxic NAPQI. This metabolite is then free to react with key hepatic enzymes, thereby damaging liver cells. This may lead to severe liver damage and even death by acute liver failure. In the treatment of acetaminophen overdose, acetylcysteine acts to maintain or replenish depleted glutathione reserves in the liver and enhance non-toxic metabolism of acetaminophen.[14] These actions serve to protect liver cells from NAPQI toxicity. It is most effective in preventing or lessening hepatic injury when administered within 8-10 hours after overdose.[14] Research suggests that the rate of liver toxicity ...

https://en.wikipedia.org/wiki/N-Acetylcysteine

... is capable of killing a variety of human cancer cells in vitro while leaving healthy cells unharmed.[9] While apoptosis requires between 16 and 24 hours, oleocanthal operated within 30 minutes to one hour. Oleocanthal pierces cancer cells' lysosomes, the containers that store the cell's waste products, releasing enzymes that kill the cell. In healthy cells, the application of oleocanthal caused a temporary halt in their life cycles, but after 24 hours they returned to normal.[10] Oleocanthal inhibits the enzymatic activity of mammalian target of rapamycin (mTOR) with an IC50 value of 708 nM.[11] Oleocanthal inhibits the growth of several breast cancer cell lines at low micromolar concentration in a dose-dependent manner. Oleocanthal treatment caused a marked downregulation of phosphorylated mTOR in metastatic breast cancer cell line (MDA-MB-231). These results strongly indicate that mTOR inhibition is at least one of the factors of the reported anticancer and neuroprotective ...

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

... (SDH) or succinate-coenzyme Q reductase (SQR) or respiratory Complex II is an enzyme complex, found in ... The fundamental role of succinate-coenzyme Q reductase in the electron transfer chain of mitochondria makes it vital in most ...

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

Complex III/Coenzyme Q - cytochrome c reductase. *Cytochrome c. *Complex IV/Cytochrome c oxidase ...

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

Coenzyme A‎; 23:20 . . (0)‎ . . ‎. Kristenfdz. (talk , contribs)‎ (changed Coenzyme A to coenzyme A) (Tag: Visual edit) ... m Coenzyme A‎; 23:25 . . (-50)‎ . . ‎. Kristenfdz. (talk , contribs)‎ (changed fatty acid synthesis sentence) (Tag: Visual edit ... Coenzyme A‎; 09:24 . . (0)‎ . . ‎. Kristenfdz. (talk , contribs)‎ (changed picture location) (Tag: Visual edit) ... Coenzyme A‎; 01:16 . . (-241)‎ . . ‎. Me, Myself, and I are Here. (talk , contribs)‎ (minus sign, dash, pmc fmt, refpunct., ...

https://en.wikipedia.org/wiki/Special:RecentChangesLinked/Acyl_CoA_dehydrogenase

Organic cofactors are sometimes further divided into coenzymes and prosthetic groups. The term coenzyme refers specifically to ... "coenzymes and cofactors". Retrieved 2007-11-17.. *^ "Enzyme Cofactors". Archived from the original on 2003-05-05. Retrieved ... Coenzyme Q [46]. Electrons. Bacteria, archaea and eukaryotes Cytidine triphosphate [47]. Diacylglycerols and lipid head groups ... Coenzyme A [35]. Pantothenic acid (B5). ADP. Acetyl group and other acyl groups. Bacteria, archaea and eukaryotes ...

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

... is an ingredient in the common bronchodilator drug aminophylline, where it serves to solubilize the active ingredient theophylline. Ethylenediamine has also been used in dermatologic preparations, but has been removed from some because of causing contact dermatitis.[10] When used as a pharmaceutical excipient, after oral administration its bioavailability is about 0.34, due to a substantial first-pass effect. Less than 20% is eliminated by urinal excretion.[11] Ethylenediamine-derived antihistamines are the oldest of the five classes of first-generation antihistamines, beginning with piperoxan aka benodain, discovered in 1933 at the Pasteur Institute in France, and also including mepyramine, tripelennamine, and antazoline. The other classes are derivatives of ethanolamine, alkylamine, piperazine, and others (primarily tricyclic and tetracyclic compounds related to phenothiazines, tricyclic antidepressants, as well as the cyproheptadine-phenindamine family) ...

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

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 ...

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

... 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. ...

https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15346

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 ...

https://en.wikipedia.org/wiki/Coenzyme_Q_%E2%80%93_cytochrome_c_reductase

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 ...

https://medlineplus.gov/genetics/condition/primary-coenzyme-q10-deficiency/

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. ...

http://www.healthy.net/Health/Article/Coenzyme_Q10/534

Coenzyme Q10 (CoQ10) is an antioxidant that your body produces naturally. Your cells use CoQ10 for growth and maintenance. ... The impact of coenzyme Q10 on metabolic and cardiovascular disease profiles in diabetic patients: A systematic review and meta- ... Coenzyme Q10 supplementation: Efficacy, safety, and formulation challenges. Comprehensive Reviews in Food Science and Food ... Coenzyme Q10. National Center for Complementary and Integrative Health. https://www.nccih.nih.gov/health/coenzyme-q10. Accessed ...

https://www.mayoclinic.org/drugs-supplements-coenzyme-q10/art-20362602?p=1

The nutritional supplement coenzyme Q10 could slow the progress of early-stage Parkinsons. ...

https://healthy.net/tag/coenzyme-q10/

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the ... Coenzyme A is one of five crucial coenzymes that are necessary in the reaction mechanism of the citric acid cycle. Its acetyl- ... Coenzyme A is available from various chemical suppliers as the free acid and lithium or sodium salts. The free acid of coenzyme ... The coenzyme was named coenzyme A to stand for "activation of acetate". In 1953, Fritz Lipmann won the Nobel Prize in ...

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

Coenzyme Q, also known as ubiquinone, is a coenzyme family that is ubiquitous in animals and most bacteria (hence the name ... 1958). "Coenzyme Q. I. structure studies on the coenzyme Q group". Journal of the American Chemical Society. 80 (17): 4752. doi ... "Coenzyme Q10". American Cancer Society. Watts TL (March 1995). "Coenzyme Q10 and periodontal treatment: is there any beneficial ... Bhagavan HN, Chopra RK (June 2007). "Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations". ...

https://en.wikipedia.org/wiki/Coenzyme_Q10

Coenzyme Evolution Nucleic Acid Enzymes Metabolic Pathways Nucleotide-Binding Domain This is a preview of subscription content ... This proposal rationalizes the fact that many coenzymes are nucleotides or heterocyclic bases which could be derived from ... Vestiges of these nucleic acid enzymes persist in contemporary coenzymes. ...

https://link.springer.com/article/10.1007/BF01732468

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 ...

https://www.pnas.org/content/87/22/8931?ijkey=3b2c6bca0d70c82a2c7b2ace7358c5efcaf7265b&keytype2=tf_ipsecsha

METHYL-COENZYME M REDUCTASE I ALPHA SUBUNITMETHYL-COENZYME M REDUCTASE I BETA SUBUNITMETHYL-COENZYME M REDUCTASE I GAMMA ...

https://www.ncbi.nlm.nih.gov/Structure/pdb/1HBM

Coenzyme A. Galactoside O-acetyltransferase. target. DB01992. Coenzyme A. 3-hydroxy-3-methylglutaryl-coenzyme A reductase. ... 3-Hydroxybutyryl-Coenzyme A. Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial. target. DB03699. Succinyl-Coenzyme A. 2,3,4,5 ... Coenzyme A. Formyl-coenzyme A transferase. target. DB01992. Coenzyme A. Dihydrolipoyllysine-residue acetyltransferase component ... Coenzyme A. 3-hydroxy-3-methylglutaryl-coenzyme A reductase. target. DB01992. Coenzyme A. Phosphopantetheine ...

https://www.drugbank.ca/categories/DBCAT000223

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 ...

https://www.newworldencyclopedia.org/entry/Coenzyme

1996) How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl‐coenzyme A mutase at 2 Å resolution. ... Masuda J, Shibata N, Morimoto Y, Toraya T and Yasuoka N (2000) How a protein generates a catalytic radical from coenzyme B12: X ... Buckel W, Kratky C and Golding BT (2005) Stabilisation of methylene radicals by cob(ii)alamin in coenzyme B12 dependent mutases ... Barker HA, Weissbach H and Smyth RD (1958) A coenzyme containing pseudovitamin B12. Proceedings of the National Academy of ...

http://www.els.net/WileyCDA/ElsArticle/refId-a0000666.html

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, ...

https://www.ncbi.nlm.nih.gov/pubmed/25110011

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 ...

https://healthy.net/2006/07/02/coenzyme-q10-could-slow-parkinsons/

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. ...

https://www.mskcc.org/cancer-care/integrative-medicine/herbs/coenzyme-q10

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. ...

https://www.rcsb.org/structure/1hbn

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 » ...

https://www.iherb.com/c/california-gold-nutrition/Coenzyme-Q10-CoQ10-Formulas

Many coenzymes are called vitamin-derived coenzymes, which are formed from the vitamins that are part of our diet. ... Sometimes the actions of these enzymes are enhanced by other molecules called coenzymes. ... 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 ...

https://www.livestrong.com/article/402487-types-of-coenzyme/

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. ...

https://www.labcorp.com/test-menu/22931/coenzyme-q10-total

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: ...

https://www.iherb.com/c/natural-factors/Coenzyme-Q10-CoQ10-Formulas

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! ...

https://www.viovet.co.uk/CO-Enzyme-Q10/c27621/

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 ...

https://www.pnas.org/content/91/15/6860?ijkey=266e982ed640a7a1f8791a6c0a348723c3efe88b&keytype2=tf_ipsecsha

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 ...

https://www.medpagetoday.com/neurology/parkinsonsdisease/5645

... - Free download as PDF File (.pdf), Text File (.txt) or view presentation slides online. ... COENZYME NAD: anaerobic. A (CoA): ethanol. + lactate. pathways.. Coenzymes. in respiration. Can also carry. acetate groups. ...

https://www.scribd.com/document/343908684/Coenzymes-Involved-in-Respiration

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 ...

https://www.healingwell.com/community/default.aspx?f=42&m=321365

Coenzyme Q10 (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 ...

https://consumer.healthday.com/encyclopedia/holistic-medicine-25/mis-alternative-medicine-news-19/coenzyme-q10-648329.html

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 ...

https://www.livestrong.com/article/91983-coenzyme-q10-deficiency-symptoms/

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) is an antioxidant that your body produces naturally. (mayoclinic.org)
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 (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)
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)
A study performed at Harvard Medical School (HMS) in the United States by Maria Fernanda Hornos Carneiro and her research group shows that the harmful effects of BPA can be reversed by administering a supplement known as CoQ10 (coenzyme Q10), a substance naturally produced by the human body and found in beef and fish. (news-medical.net)
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)
In both production of energy and free radicals, coenzyme Q10 (CoQ10) plays a crucial role in electron transport. (frontiersin.org)
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)

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, also known as ubiquinone, is a coenzyme family that is ubiquitous in animals and most bacteria (hence the name ubiquinone). (wikipedia.org)
In humans, the most common form is Coenzyme Q10 or ubiquinone-10. (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)

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)
Young Jm, Florkowski CM, Molyneux RG, Frampton CM, George PM, Scott RS: Effect of coenzyme Q (10) supplementation on simvastatin-induced myalgia. (aerzteblatt.de)
Coenzyme Q10 supplementation: Efficacy, safety, and formulation challenges. (mayoclinic.org)
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)

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)
Vestiges of these nucleic acid enzymes persist in contemporary coenzymes. (springer.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) 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)
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)
Buckel W and Golding BT (1996) Glutamate and 2‐methyleneglutarate mutase: from microbial curiosities to paradigms for coenzyme B12‐dependent enzymes. (els.net)
Sometimes the actions of these enzymes are enhanced by other molecules called coenzymes. (livestrong.com)
Editor's note: Enzymes for DNA repair or Coenzyme Q10 for antioxidant and antiaging benefits have become typical ingredients in today's skin care . (cosmeticsandtoiletries.com)
Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. (cosmeticsandtoiletries.com)
Coenzymes help enzymes work to digest food and perform other body processes, and they help protect the heart and skeletal muscles. (cardiosmart.org)
The Enzymes Coenzymes and Metabolic Pathways Gordon Research Conference has chronicled advances in the study of enzymes and related fields for 70 of those years. (grc.org)
This GRC will be held in conjunction with the "Enzymes, Coenzymes and Metabolic Pathways (GRS)" Gordon Research Seminar (GRS). (grc.org)
The 2016 Enzymes, Coenzymes, and Metabolic Pathways GRC will highlight the latest advances in enzymology from the fundamentals of determining enzyme function to the interplay of large enzyme systems. (grc.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)
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)

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)
Organic cofactors can either be prosthetic groups, which are tightly bound to an enzyme , or coenzymes, which are released from the enzyme's active site during the reaction. (cosmeticsandtoiletries.com)
Coenzymes are small organic molecules that transport chemical groups from one enzyme to another. (cosmeticsandtoiletries.com)
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)

As its name suggests, the disorder involves a shortage (deficiency) of a substance called coenzyme Q10. (medlineplus.gov)
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)
Coenzyme Q10 or CoQ 10 is a vitamin or vitamin like substance. (vitaminsdiary.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)
The importance of having sufficient levels of Coenzyme Q10 cannot be overstated as the substance is vital for cellular energy production. (pitchengine.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)

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)

In its acetyl form, coenzyme A is a highly versatile molecule, serving metabolic functions in both the anabolic and catabolic pathways. (wikipedia.org)
In these pathways, coenzyme A needs to be provided from an external source, such as food, in order to produce 4′-phosphopantetheine. (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)

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)
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)

Coenzyme Q10 is available either in pressed tablets, powder filled capsules or oil based gel caps. (vitaminsdiary.com)

Primary coenzyme Q10 deficiency is a disorder that can affect many parts of the body, especially the brain, muscles, and kidneys. (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)

Formulated with antioxidant coenzyme Q10 to build collagen and firm skin, Matrixyl 3000 to reduce wrinkles, and hyaluronic acid to moisturize skin. (yesstyle.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)

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)
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)

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)

Caso G, Kelly P, McNurlan MA, Lawson WE: Effects of coenzyme q10 on myopathic symptoms in patients treated with statins. (aerzteblatt.de)
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)

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)
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)

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)

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)

Coenzymes are also commonly made from nucleotides , such as adenosine triphosphate , the biochemical carrier of phosphate groups, or coenzyme A, the coenzyme that carries acyl groups. (newworldencyclopedia.org)
The most common metabolite coenzyme is adenosine triphosphate, or ATP. (livestrong.com)
Coenzymes include the reduced form of nicotinamide adenine dinucleotide (NADH), the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) and adenosine triphosphate. (cosmeticsandtoiletries.com)
One of CoEnzyme Q-10s most prominent roles is helping with the production of adenosine triphosphate (ATP). (hollandandbarrett.com)

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)

Studies further suggest that coenzyme Q10 does not interfere with the antineoplastic action of anthracyclines and might even enhance their anticancer effects. (nih.gov)

Here, industry expert O'Lenick illustrates the difference between cofactors and coenzymes. (cosmeticsandtoiletries.com)

Coenzyme Q10 is also involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. (medlineplus.gov)
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)
Coenzymes molecules are often vitamins or are made from vitamins. (newworldencyclopedia.org)
Coenzymes act as agents for transferring different groups such as electrons or molecules during reactions. (livestrong.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)

Many VITAMINS are coenzymes. (drugbank.ca)
Acting as coenzymes in organisms is the major role of vitamins , although vitamins do have other functions in the body (Bolander 2006). (newworldencyclopedia.org)
Many coenzymes are called vitamin-derived coenzymes, which are formed from the vitamins that are part of our diet. (livestrong.com)
Water soluble vitamins typically function as the precursors to coenzymes. (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)
Vitamins B-2, B-3 and C are all precursors of electron-carrying coenzymes. (livestrong.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)

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)
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 are involved in the transfer of hydrogen ions and electrons. (cosmeticsandtoiletries.com)

8. Kuklinski B, Weissenbacher E, Fahnrich A. Coenzyme Q10 and antioxidants in acute myocardial infarction. (evitamins.com)

The impact of coenzyme Q10 on metabolic and cardiovascular disease profiles in diabetic patients: A systematic review and meta-analysis of randomized controlled trials. (mayoclinic.org)
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)

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)
A molecule of coenzyme A carrying an acyl group is also referred to as acyl-CoA. (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)

This proposal rationalizes the fact that many coenzymes are nucleotides or heterocyclic bases which could be derived from nucleotides. (springer.com)

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)
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)

The International Union of Pure and Applied Chemistry (IUPAC) draws a distinction between coenzymes and prosthetic groups. (newworldencyclopedia.org)
This article will restrict coenzyme to the definition used by IUPAC. (newworldencyclopedia.org)

The nutritional supplement coenzyme Q10 could slow the progress of early-stage Parkinson's. (healthy.net)
Coenzyme Q10 treatment does not slow the progression of Parkinson's disease (PD). (alzforum.org)

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)

Your search returned 39 coenzyme Q10 homolog B (S. cerevisiae) ELISA ELISA Kit across 1 supplier. (biocompare.com)
Your search "coenzyme q10 capsules" did not match any products. (opencroquet.org)

needs update] While statins may reduce coenzyme Q10 in the blood it is unclear if they reduce coenzyme Q10 in muscle. (wikipedia.org)

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)

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)

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 Q10 (CoQ 10 ) acts by scavenging reactive oxygen species for protecting neuronal cells against oxidative stress in neurodegenerative diseases. (springer.com)

Since coenzyme A is chemically a thiol, it can react with carboxylic acids to form thioesters , thus functioning as an acyl group carrier. (bionity.com)

Coenzyme Q-10 is a key nutrient that may help maintain a healthy heart. (allegromedical.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)

While coenzyme Q 10 may show indirect anticancer activity through its effect(s) on the immune system, there is evidence to suggest that analogs of this compound can suppress cancer growth directly. (cancer.gov)
Analogs of coenzyme Q 10 have been shown to inhibit the proliferation of cancer cells in vitro and the growth of cancer cells transplanted into rats and mice. (cancer.gov)
12 , 34 ] In view of these findings, it has been proposed that analogs of coenzyme Q 10 may function as antimetabolites to disrupt normal biochemical reactions that are required for cell growth and/or survival and, thus, that they may be useful as chemotherapeutic agents . (cancer.gov)

Studies have shown that Coenzyme Q10 helps the immune system work better and makes the body better able to resist certain infections and types of cancer, as well as helps protect heart. (viovet.co.uk)
Coenzyme Q 10 has shown an ability to stimulate the immune system and to protect the heart from damage caused by certain chemotherapy drugs. (cancer.gov)
Coenzyme Q10 could also be beneficial to the immune system, since an interesting relationship has been discovered between the vitamin and the body's immune system. (vitaminsdiary.com)
Use of coenzyme Q10 may increase energy levels and correct age-related decline of immune system functionality. (vetinfo.com)
Coenzyme Q10 increases energy via efficient ATP production, strengthens the immune system and provides the benefits of an antioxidant. (purebulk.com)
Your heart is perhaps the most vital Coenzyme Q-10 consuming community of cells, however, your immune system isn't far behind. (life-enthusiast.com)

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)

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. (wikipedia.org)

The term coenzymes is sometimes defined in such a way as to include prosthetic groups (Alberts et al. (newworldencyclopedia.org)

Only some of the studies of coenzyme Q10 showed that it helps heart failure symptoms. (cardiosmart.org)

Anatomy5

Organisms20

Diseases2

Chemicals and Drugs170

Analytical, Diagnostic and Therapeutic Techniques and Equipment19

Phenomena and Processes35

Disciplines and Occupations1

Technology, Industry, Agriculture3

Information Science3

Health Care1

Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames. (1/1288)

Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B. (2/1288)

Human biotinidase isn't just for recycling biotin. (3/1288)

Re-design of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Enhancement of adenosine N1-oxide reductase activity. (4/1288)

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (5/1288)

A function for the vitamin E metabolite alpha-tocopherol quinone as an essential enzyme cofactor for the mitochondrial fatty acid desaturases. (6/1288)

Structure and function of a cysBJIH gene cluster in the purple sulphur bacterium Thiocapsa roseopersicina. (7/1288)

Specificity of coenzyme analogues and fragments in promoting or impeding the refolding of clostridial glutamate dehydrogenase. (8/1288)

Coenzyme A

Coenzymes

Ubiquinone

Coenzyme A Ligases

Acetyl Coenzyme A

Cobamides

Coenzyme A-Transferases

Hydroxymethylglutaryl CoA Reductases

Mesna

Pantothenic Acid

NAD

Euryarchaeota

Propanediol Dehydratase

Kinetics

Methanosarcina barkeri

NADP

Acetate-CoA Ligase

Mevalonic Acid

Hydroxymethylglutaryl-CoA Reductase Inhibitors

Alcohol Oxidoreductases

Riboflavin

Pantetheine

Palmitoyl Coenzyme A

Methanobacterium

Lovastatin

Malonyl Coenzyme A

Oxidoreductases

Molecular Sequence Data

Substrate Specificity

Pyridoxal Phosphate

Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent

Methylmalonyl-CoA Mutase

Oxidation-Reduction

Acyltransferases

Amino Acid Sequence

Methane

Acetates

Escherichia coli

Corrinoids

Simvastatin

Vitamin B 12

Phosphate Acetyltransferase

Binding Sites

Flavin-Adenine Dinucleotide

Liver

Catalysis

Glutamate Dehydrogenase

Aldehyde Oxidoreductases

Oxo-Acid-Lyases

Hydroxymethylglutaryl-CoA Synthase

Ethanolamine Ammonia-Lyase

Alcohol Dehydrogenase

Methanosarcina

Methyltransferases

Mercaptoethanol

Glutarates

Apoenzymes

Succinate-CoA Ligases

Cloning, Molecular

Cholesterol

Propylene Glycol

Xanthobacter

Spectrophotometry, Ultraviolet

Sterol O-Acyltransferase

Clostridium

Carboxy-Lyases

Hydrogen-Ion Concentration

Methanobacteriaceae

Bacterial Proteins

Heptanoic Acids

Acetyltransferases

Flavin Mononucleotide

Fatty Acids

Sterols

Intramolecular Transferases

Sequence Homology, Amino Acid

Enzymes and Coenzymes

Parabens

Dimethylamines

Acetyl-CoA Carboxylase