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)

... (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 ... Coenzyme A can be synthesized through alternate routes when intracellular coenzyme A level are reduced and the de novo pathway ...

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

Coenzyme Q, also known as ubiquinone and marketed as CoQ10, is a coenzyme family that is ubiquitous in animals and most ... Coenzyme Q10 has potential to inhibit the effects of theophylline as well as the anticoagulant warfarin; coenzyme Q10 may ... 1958). "Coenzyme Q. I. structure studies on the coenzyme Q group". Journal of the American Chemical Society. 80 (17): 4752. doi ... While statins may reduce coenzyme Q10 in the blood it is unclear if they reduce coenzyme Q10 in muscle. Evidence does not ...

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

The coenzyme is the C1 donor in methanogenesis. It is converted to methyl-coenzyme M thioether, the thioether CH3SCH2CH2SO−3, ... Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens, and in the ... Methyl-coenzyme M reacts with coenzyme B, 7-thioheptanoylthreoninephosphate, to give a heterodisulfide, releasing methane: CH3- ... The coenzyme is an anion with the formula HSCH 2CH 2SO− 3. It is named 2-mercaptoethanesulfonate and abbreviated HS-CoM. The ...

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

... , more commonly known as COQ5, is a coenzyme involved in the electron transport chain. It is a shorter-chain homolog ... of coenzyme Q10 (ubiquinone), the more-common coenzyme of this family. Ubiquinone-5 National Center for Biotechnology ...

https://en.wikipedia.org/wiki/Coenzyme_Q5

... is a coenzyme required for redox reactions in methanogens. The full chemical name of coenzyme B is 7- ... Two separate experiment that were performed, one with coenzyme B and other without coenzyme B, indicated that using coenzyme B ... Coenzyme B reacts with 2-methylthioethanesulfonate (methyl-Coenzyme M, abbreviated CH 3-S-CoM), to release methane in ... It acts as a two electron-donor to reduce coenzyme M (methyl-coenzyme) into two molecules a methane and a heterodisulfide. ...

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

... -0:L-glutamate ligase puts a glutamate residue at the -COOH end, producing Coenzyme F420-1. Coenzyme F420-1:gamma- ... Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme (sometimes called a cofactor) involved in redox reactions in methanogens ... Coenzyme F420 is synthesized via a multi-step pathway: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase produces Coenzyme FO ... The coenzyme is a substrate for coenzyme F420 hydrogenase, 5,10-methylenetetrahydromethanopterin reductase and ...

https://en.wikipedia.org/wiki/Coenzyme_F420

... is a deficiency of coenzyme Q10. It can be associated with COQ2, APTX, PDSS2, PDSS1, CABC1, and COQ9. ... 8th Conference of the International Coenzyme Q10 Association v t e (Articles with short description, Short description is ... May 2009). "A nonsense mutation in COQ9 causes autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency: a ...

https://en.wikipedia.org/wiki/Coenzyme_Q10_deficiency

It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas ... In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as ... Ellermann J, Rospert S, Thauer RK, Bokranz M, Klein A, Voges M, Berkessel A (September 1989). "Methyl-coenzyme-M reductase from ... Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK (November 1997). "Crystal structure of methyl-coenzyme M reductase: the ...

https://en.wikipedia.org/wiki/Coenzyme-B_sulfoethylthiotransferase

... reduced coenzyme F420 Thus, the two substrates of this enzyme are H2 and coenzyme F420, whereas its product is reduced coenzyme ... In enzymology, a coenzyme F420 hydrogenase (EC 1.12.98.1) is an enzyme that catalyzes the chemical reaction H2 + coenzyme F420 ... The systematic name of this enzyme class is hydrogen:coenzyme F420 oxidoreductase. Other names in common use include 8-hydroxy- ... Baron SF, Ferry JG (1989). "Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from ...

https://en.wikipedia.org/wiki/Coenzyme_F420_hydrogenase

... (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an ...

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

... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index page lists ...

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

... , more commonly known as COQ5, is an enzyme involved in the electron transport chain. COQ5 is ... Coenzyme Q10 Deficiency is associated with COQ5. Therefore, to maintain CoQ10 levels in human cells, COQ5 is required. ... "COQ5 Gene - Coenzyme Q5, Methyltransferase". GeneCards human gene database. Weizmann Institute of Science. Dai YN, Zhou K, Cao ... COQ5 has the role of catalyst in the C-methylation in the coenzyme Q biosynthesis, on the benzoic ring of CoQ6, the ...

https://en.wikipedia.org/wiki/Coenzyme_Q5,_methyltransferase

... (HADH) is an enzyme which in humans is encoded by the HADH gene. The HADH gene is located ... Craig I, Tolley E, Bobrow M (1976). "A preliminary analysis of the segregation of human hydroxyacyl coenzyme A dehydrogenase in ... "Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Molven A, Matre ... A deficiency is associated with 3-hydroxyacyl-coenzyme A dehydrogenase deficiency. Mutations also cause 3-hydroxyacyl-CoA ...

https://en.wikipedia.org/wiki/Hydroxyacyl-Coenzyme_A_dehydrogenase

Exogenous Coenzyme Q10 does not influence the biosynthesis of endogenous Coenzyme Q10; Coenzyme Q10 does not accumulate in ... Safety of Coenzyme Q10 The association supported work on a review of the safety profile of Coenzyme Q10 based on animal and ... Coenzyme Q molecules are naturally occurring lipid-soluble redox molecules. In humans, they are found in the form of Coenzyme ... Coenzyme Q10 also regenerates alpha-tocopherol, the active form of vitamin E. Together with vitamin E, Coenzyme Q10 protects ...

https://en.wikipedia.org/wiki/International_Coenzyme_Q10_Association

... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme ...

https://en.wikipedia.org/wiki/NADH-coenzyme_Q_reductase

... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme ...

https://en.wikipedia.org/wiki/DPNH-coenzyme_Q_reductase

... may refer to: Methylmalonyl-CoA decarboxylase, an enzyme Propionyl-CoA carboxylase, an enzyme ...

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

... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...

https://en.wikipedia.org/wiki/NADH-coenzyme_Q_oxidoreductase

... (SCS, also known as succinyl-CoA synthetase or succinate thiokinase or succinate-CoA ligase) is ... Succinyl+Coenzyme+A+Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) (Metabolism, EC 6.2). ... 1]. Crystal structures for the E. coli SCS provide evidence that the coenzyme A binds within each α-subunit (within a Rossmann ... "Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA ...

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

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_–_cytochrome_c_reductase

... is a rare metabolic disorder in which the body is unable to process certain ... Isobutyryl-coenzyme A dehydrogenase deficiency at NLM Genetics Home Reference (Articles lacking in-text citations from March ... Isobutyryl-coenzyme A "Isobutyryl-CoA dehydrogenase deficiency , Genetic and Rare Diseases Information Center (GARD) - an NCATS ... Defects in the ACAD8 gene cause isobutyryl-coenzyme A dehydrogenase deficiency. The ACAD8 gene provides instructions for making ...

https://en.wikipedia.org/wiki/Isobutyryl-coenzyme_A_dehydrogenase_deficiency

... (EC 2.1.1.251, mtsA (gene)) is an enzyme with systematic name methylated-thiol: ... Methylated-thiol---coenzyme+M+methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Tallant TC, Paul L, Krzycki JA (February 2001). "The MtsA subunit of the methylthiol:coenzyme M methyltransferase of ... Tallant TC, Krzycki JA (November 1997). "Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of ...

https://en.wikipedia.org/wiki/Methylated-thiol-coenzyme_M_methyltransferase

... also known as solute carrier family 33 member 1 (SLC33A1) is a protein that in humans is ...

https://en.wikipedia.org/wiki/Acetyl-coenzyme_A_transporter_1

... may refer to: 3-hydroxybutyryl-CoA dehydratase, an enzyme Enoyl-CoA hydratase, an enzyme This set ...

https://en.wikipedia.org/wiki/Enoyl_coenzyme_A_hydrase_(D)

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

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

... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non- ...

https://en.wikipedia.org/wiki/Dihydronicotinamide_adenine_dinucleotide-coenzyme_Q_reductase

... is a rare condition that prevents the body from converting certain fats to ... Mutations in the HADH gene lead to inadequate levels of an enzyme called 3-hydroxyacyl-coenzyme A dehydrogenase. Medium-chain ... People with 3-hydroxyacyl-coenzyme A dehydrogenase deficiency have inadequate levels of an enzyme required for a step that ... Problems related to 3-hydroxyacyl-coenzyme A dehydrogenase deficiency can be triggered by periods of fasting or by illnesses ...

https://en.wikipedia.org/wiki/3-hydroxyacyl-coenzyme_A_dehydrogenase_deficiency

... (EC 1.1.98.2, coenzyme F420-dependent glucose-6-phosphate dehydrogenase, F420 ... Purwantini E, Daniels L (May 1996). "Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from ... Glucose-6-phosphate+dehydrogenase+(coenzyme-F420) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal ... This enzyme catalyses the following chemical reaction D-glucose 6-phosphate + oxidized coenzyme F420 ⇌ {\displaystyle \ ...

https://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase_(coenzyme-F420)

... may stand for NADH dehydrogenase NADH:ubiquinone reductase (non- ... This disambiguation page lists articles associated with the title Reduced nicotinamide adenine dinucleotide-coenzyme Q ...

https://en.wikipedia.org/wiki/Reduced_nicotinamide_adenine_dinucleotide-coenzyme_Q_reductase

... (SCADD) is an autosomal recessive fatty acid oxidation disorder which ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Scholia has a topic profile for Short-chain acyl-coenzyme A dehydrogenase deficiency. (Articles with short description, Short ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ...

https://en.wikipedia.org/wiki/Short-chain_acyl-coenzyme_A_dehydrogenase_deficiency

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/

... forming malonyl coenzyme A, before participating in fatty acid synthesis. The carboxylation reaction is catalyzed by acetyl CoA ... Other articles where malonyl coenzyme A is discussed: metabolism: Fatty acids: …first undergoes a carboxylation, ... first undergoes a carboxylation, forming malonyl coenzyme A, before participating in fatty acid synthesis. The carboxylation ...

https://www.britannica.com/science/malonyl-coenzyme-A

Light Teaches (Co)Enzymes New Tricks. Scientists investigated the reaction of a specific class of enzymes to light. July 31, ... Biology uses light sparingly in this way, but coenzymes such as flavin can be driven to excited states by light. A team of ...

https://www.bnl.gov/nsls2/news/highlights/news.php?a=216711

Facial Moisturizer/Treatment Products Containing Coenzyme A Sort best to worst. Sort worst to best. Sort alphabetical A-Z. Sort ...

https://www.ewg.org/skindeep/browse/ingredients/701579COENZYME_A/?category=facial+moisturizer%2Ftreatment

Here, industry expert OLenick illustrates the difference between cofactors and coenzymes. ... Enzymes for DNA repair or Coenzyme Q10 for antioxidant and antiaging benefits have become typical ingredients in todays skin ... Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special ... Coenzymes. Coenzymes are small organic molecules that transport chemical groups from one enzyme to another. Some of these ...

https://www.cosmeticsandtoiletries.com/research/literature-data/article/21834499/comparatively-speaking-cofactors-vs-coenzymes

Archives for coenzyme q10. Home Remedies to Prevent / Cure Gum Disease (or) Periodontal Disease. May 21, 2012. By Dr. Chetan 1 ... Filed Under: Dental Tips Tagged With: coenzyme q10, gingivitis, gum disease, natural remedies, periodontal disease, ...

https://www.drchetan.com/tag/coenzyme-q10

Nucleotides and coenzymes. Main Author:. Hutchinson, D. W.. Format:. Book. Language:. English. Subjects:. Nucleotides. ...

https://openagricola.nal.usda.gov/catalog/CAT10915406

Coenzyme Q10 is a powerful antioxidant for skin wellness & fights free radicals that accelerate signs of aging. DHCs CoQ10 ... In the Japanese beauty scene, few antioxidants are considered as powerful as Coenzyme Q10 to promote skins wellness and fight ...

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Coenzymes Q10 Market Growth, Analysis and Forecast Upto 2028. Coenzymes Q10 Market Growth, Analysis and Forecast Upto 2028. ... Coenzyme Q10 A Miracle for Skin A recent study carried out by a leading skin care company, Beiersdorf AG, slates that the CoQ10 ... A recently collated, insightful Fact.MR report foresees the global coenzyme Q10 market to rise at a value CAGR of 9.2% between ... Roughly 2,670,000 kgs of coenzyme Q10 are pegged to be sold globally by 2028-end. CoQ10 for Minimizing Outcomes of Specific ...

https://www.clickpress.com/releases/Detailed/810485005cp.shtml

Ive read an article (actually an advertisement) that said Coenzyme Q10 absorption is improved dramatically by including ... Posted: Sat Mar 12, 2005 1:18 am Post subject: Coenzyme Q10. ... Coenzyme Q10. Smart Skin Care Forum Index -> Cell Energy ...

http://www.smartskincare.com/forum/viewtopic.php?t=252&start=0&postdays=0&postorder=asc&highlight=

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... also known as Coenzyme Q10, is sold as an anti-aging pill, but theres new evidence its likely ineffective. ... Global sales of ubiquinone, also known as Coenzyme Q10, are estimated to amount to hundreds of millions of dollars a year. ( ... The popular dietary supplement ubiquinone, also known as Coenzyme Q10, is widely believed to function as an antioxidant, ...

https://www.futurity.org/coenzyme-q10-ubiquinone-871392/

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Coenzyme Q10: The Miracle Nutrient This is the first in a two-part series on coenzyme Q10, which is sometime referred to as The ... Coenzyme Q10: The New Era In Part 1 of this series, we reviewed the discovery of coenzyme Q10 and the initial studies that ... Coenzyme Q10 Doubles Lifespan in Mice: Emile Bliznakov, MD, who wrote "The Miracle Nutrient: Coenzyme Q10," conducted the ... Coenzyme Q10: A Critical Antioxidant. Coenzyme Q10 in the reduced form (Ubiquinol) is a fat-soluble antioxidant that is made in ...

https://totalhealthmagazine.com/tag/coenzyme-q10.html

US-2009318476-A1 chemical patent summary.

https://pubchem.ncbi.nlm.nih.gov/patent/US-2009318476-A1

Purified Methyl-Coenzyme-M Reductase is Activated when the Enzyme-Bound Coenzyme F430 is Reduced to the Nickel(I) Oxidation ... Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 ... Divergent methyl-coenzyme M reductase genes in a deep-subseafloor Archaeoglobi journal, January 2019 * Boyd, Joel A.; Jungbluth ... The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase journal, February 2000 * ...

https://www.osti.gov/pages/biblio/1603218-functional-interactions-between-posttranslationally-modified-amino-acids-methyl-coenzyme-reductase-methanosarcina-acetivorans

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Insight Into Acetyl-Coenzyme A Regulation Through The Molecular Mechanism Of Atp-Citrate Lyase ... Bazilevsky, Gleb, "Insight Into Acetyl-Coenzyme A Regulation Through The Molecular Mechanism Of Atp-Citrate Lyase" (2019). ...

https://repository.upenn.edu/edissertations/3492/

3-hydroxy-3-methylglutaryl-coenzyme A reductase. Details. Name. 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Synonyms. *1.1 ... coenzyme binding / hydroxymethylglutaryl-CoA reductase (NADPH) activity / hydroxymethylglutaryl-CoA reductase activity / NADPH ... aging / cellular lipid metabolic process / cholesterol biosynthetic process / coenzyme A metabolic process / isoprenoid ... Stormo C, Kringen MK, Grimholt RM, Berg JP, Piehler AP: A novel 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) splice ...

https://go.drugbank.com/polypeptides/P04035

Calbiochem A lipophilic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor that blocks Ras function through ... A lipophilic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor that blocks Ras function through inhibition of ... A lipophilic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor that blocks Ras function through inhibition of ... A lipophilic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor that blocks Ras function through inhibition of ...

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NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain ... Timeline for Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain from c.3.1.5: ... Lineage for Protein: NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain. *Root: SCOPe ... More info for Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase, N- and C-terminal domain from c.3.1.5 ...

http://scop.berkeley.edu/sunid=418948

Learn more about these coenzymes, and the role they play to help you stay healthy. ... Coenzymes are molecules that aid in the way enzymes function. ... Where do coenzymes come into play?. Coenzymes are a molecule ... Coenzyme Q10. Another important coenzyme within the body is coenzyme Q10 (CoQ10). CoQ10 is a coenzyme that is found within the ... Namely, coenzymes act as the sidekick to every enzyme superhero. Coenzymes act to support enzymes and improve their ability to ...

https://www.mitoq.com/journal/what-are-coenzymes

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Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in ...

https://www.yeastrc.org/pdr/viewGONode.do?acc=GO:0050662

Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes with recurrent abdominal symptoms and coenzyme ... Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes with recurrent abdominal symptoms and coenzyme ... Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes with recurrent abdominal symptoms and coenzyme ...

https://jnnp.bmj.com/content/50/11/1475.citation-tools

Abstract OBJECTIVE To determine the dose of coenzyme Q10 (CoQ10) needed to achieve at least a 3-fold increase in plasma CoQ10 ... Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations. Mitochondrion 2007;7:S78-S88. ... Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations. Mitochondrion 2007;7:S78-S88. ... Sharma A, Fonarow GC, Butler J, et al. Coenzyme Q10 and heart failure: a state-of-the-art review. Circ Heart Fail 2016;9: ...

https://avmajournals.avma.org/view/journals/ajvr/82/4/ajvr.82.4.280.xml?rskey=qN0JNd&result=1

... International Journal ... Abstract: Beta-hydroxy-beta-methylglutaryl coenzyme a reductase (HMG CoA reductase) is the key enzyme in cholesterol ... Inhibitory Activity of Some Plant Methanol Extracts on 3-Hydroxy-3-Methylglutaryl Coenzyme a Reductase. ...

https://scialert.net/abstract/?doi=ijp.2010.705.711

The U.S. Food and Drug Administration (FDA) designates coenzyme Q10 (CoQ10) as GRAS Generally Recognized as Safe, implying its safe incorporation as food additive. (clickpress.com)
CoQ10 also acts as excellent antioxidant outside mitochondria by working synergistically with various other antioxidants such as vitamin E. Widely available as an OTC supplement, coenzyme Q10 has gained momentum in light of its therapeutic effectiveness in minimizing outcomes of specific metabolic disorders, namely, cancer, neurodegenerative disease, diabetes, and cardiovascular diseases. (clickpress.com)
CoQ10 is a potent antioxidant and coenzyme, critical for the production of energy in the mitochondria of the cell. (dillons.com)
Coenzyme Q10, or CoQ10, found in the mitochondria of all cells. (vitadigest.com)
Primary coenzyme Q10 (CoQ10) deficiency is due to mutations in genes involved in CoQ biosynthesis. (ugr.es)
However, coenzyme Q10 (CoQ10) is different. (txfertility.com)
In previous study, we found that coenzyme Q10 (CoQ10) improved glucolipid profile in dyslipidemic individuals, but the mechanism is not yet clear. (biomedcentral.com)
Coenzyme Q10 (CoQ10) is also known as "ubiquinone" or "ubidecarenone," but most commonly as CoQ10. (ourkidsasd.com)
Coenzyme Q10 (CoQ10) is used to produce energy your body needs for cell growth and maintenance. (1vit.com)
Why do you need to consider taking Coenzyme Q10 (CoQ10)? (biosenseclinic.com)
Ubiquinol is the reduced and active free radical quencher form of Coenzyme Q10 (CoQ10). (frysfood.com)
Apparently, the coenzyme CoQ10 supplied by rashers works favorably in keeping metabolism working well. (bentonshams.com)
Coenzyme Q10 (CoQ10) - Known also as ubiquinone (from the word "ubiquitous," meaning it exists just about everywhere), CoQ10 is a vitally important substrate (think "spark plug") for the efficient production of energy from your food and oxygen intake. (hammernutrition.com)

Global sales of ubiquinone, also known as Coenzyme Q10, are estimated to amount to hundreds of millions of dollars a year. (futurity.org)
The popular dietary supplement ubiquinone, also known as Coenzyme Q10, is widely believed to function as an antioxidant, protecting cells against damage from free radicals. (futurity.org)
Coenzyme Q 10, which is also called Ubiquinone, is present ubiquitously (thus the name! (diabeteslibrary.org)
and University of Granada, Spain reviewed 149 cases of coenzyme Q10 (ubiquinone) deficiency, including their own cohort of 76 patients diagnosed from 1997-2010. (pediatricneurologybriefs.com)
Addition of coenzyme Q (ubiquinone), 200 ppm or a-tocopherol (1000 ppm) to the basal diet had no effect on either NOS levels or ROS generation. (cdc.gov)

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 act to support enzymes and improve their ability to catalyze a reaction and function as intended. (mitoq.com)
The actions of coenzyme assistance can vary, but they all aid enzymes in some capacity. (mitoq.com)
Coenzymes are a molecule that aid in the way that enzymes function. (mitoq.com)
Coenzymes are organic molecules that attach to the enzymes that contribute to their ability to help facilitate chemical reactions. (mitoq.com)
Metabolomics revealed that coenzyme A biosynthetic enzymes converted pantothenamides into coenzyme A analogs that interfered with parasite acetyl-coenzyme A anabolism. (elsevier.com)
Will Coenzyme Q10 Elevate Liver Enzymes? (healthfully.com)
Our work involves characterization of a group of acyl-CoA thioesterase enzymes, that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH). (avhandlingar.se)

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)
The National Institutes of Health (NIH) recommends coenzyme Q10 supplementation for patients with Parkinson s disease. (clickpress.com)
Hernández-Camacho JD , Bernier M , López-Lluch G , Coenzyme Q 10 supplementation in aging and disease . (avma.org)
We investigated the effects of curcumin and/or coenzyme Q10 supplementation on metabolic syndrome components including systolic blood pressure (SBP), diastolic blood pressure (DBP), waist circumference (WC), triglyceride (TG), high density lipoprotein-cholesterol (HDL-c) and fasting plasma glucose (FPG) as primary outcomes, and total cholesterol (TC), low density lipoprotein-cholesterol (LDL-c) and body mass index (BMI) as secondary outcomes in subjects with MetS. (biomedcentral.com)

The enzyme methyl-coenzyme M reductase (MCR) plays an important role in mediating global levels of methane by catalyzing a reversible reaction that leads to the production or consumption of this potent greenhouse gas in methanogenic and methanotrophic archaea. (osti.gov)
Calbiochem A lipophilic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitor that blocks Ras function through inhibition of farnesylation. (sigmaaldrich.com)
Beta-hydroxy-beta-methylglutaryl coenzyme a reductase (HMG CoA reductase) is the key enzyme in cholesterol biosynthesis. (scialert.net)
HMG-coenzyme A reductase inhibition, type 2 diabetes, and bodyweight: evidence from genetic analysis and randomised trials. (ucl.ac.uk)
Hydroxymethyl glutaryl-coenzyme A reductase (HMG-CoA) inhibitors (also called statins) are the most commonly prescribed first-line medications for lowering serum cholesterol. (empr.com)
3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors (statins) effectively reduce cholesterol levels and decrease the incidence of cardiovascular and cerebrovascular events (4). (cdc.gov)

People that are always feeling tired can benefit from the effects of Coenzyme Q10 supplements. (topnaturalremedies.net)

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)
Namely, coenzymes act as the sidekick to every enzyme superhero. (mitoq.com)
Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed. (yeastrc.org)
We have investigated the efficacy of a new strategy to limit pathological retinal neovascularization (RNV) during ischemic retinopathy by targeting the cholesterol metabolizing enzyme acyl- coenzyme A cholesterol transferase 1 (ACAT1). (bvsalud.org)

Most of the studies have not been able to establish the glucose lowering effect of coenzyme Q10 in diabetic patients but some studies have shown a reduction of HbA1c levels 5,6 . (diabeteslibrary.org)

Coenzyme Q10 deficiency can also be caused by mutations in genes that are not directly related to the synthesis of coenzyme Q10. (medlineplus.gov)
However, bio-synthesis of Coenzyme Q10 begins to decline once humans reach their adult years. (q10facts.com)
With increasing age, however, it may be that the body's own synthesis of coenzyme Q10 decreases. (kingnature.ch)

An endogenously produced compound, coenzyme Q10 is found in human cells, and plays an imperative role in production of energy by serving as mobile electron carrier in electron transport chain within mitochondria. (clickpress.com)
Specifically, coenzyme Q10 is present in the mitochondria, which we learned in school is the powerhouse of the cell. (txfertility.com)
This coenzyme vitamin is made to support energy & healthy cognitive function as well as metabolism of fats and cholesterol** In fact, B vitamins promote energy in your cells from the inside out, starting in the mitochondria. (countrylifevitamins.com)
Nicotinamide adenine dinucleotide (NAD) is a coenzyme which functions in the electron transfer system within the mitochondria. (cdc.gov)

Primary coenzyme Q10 deficiency is a disorder that can affect many parts of the body, especially the brain, muscles, and kidneys. (medlineplus.gov)
As its name suggests, the disorder involves a shortage (deficiency) of a substance called coenzyme Q10. (medlineplus.gov)
The severity, combination of signs and symptoms, and age of onset of primary coenzyme Q10 deficiency vary widely. (medlineplus.gov)
A type of kidney dysfunction called nephrotic syndrome is another common feature of primary coenzyme Q10 deficiency. (medlineplus.gov)
can also occur in primary coenzyme Q10 deficiency. (medlineplus.gov)
The prevalence of primary coenzyme Q10 deficiency is thought to be less than 1 in 100,000 people. (medlineplus.gov)
Primary coenzyme Q10 deficiency is caused by mutations in genes that provide instructions for making proteins involved in the production (synthesis) of a molecule called coenzyme Q10. (medlineplus.gov)
Smaller numbers of mutations in other COQ genes have also been found to cause primary coenzyme Q10 deficiency. (medlineplus.gov)
Studies suggest that a shortage (deficiency) of coenzyme Q10 impairs oxidative phosphorylation and increases the vulnerability of cells to damage from free radicals. (medlineplus.gov)
A deficiency of coenzyme Q10 may also disrupt the production of pyrimidines. (medlineplus.gov)
These changes can cause cells throughout the body to malfunction, which may help explain the variety of organs and tissues that can be affected by primary coenzyme Q10 deficiency. (medlineplus.gov)
Coenzyme Q 10 is abundantly available in nature and its deficiency is generally unknown. (diabeteslibrary.org)
Coenzyme Q10 deficiency in children: Frequent type 2C muscle fibers with normal morphology. (pediatricneurologybriefs.com)
2012). Heterogeneity of coenzyme Q10 deficiency: patient study and literature review. (pediatricneurologybriefs.com)

In cell membranes, coenzyme Q10 acts as an antioxidant, protecting cells from damage caused by unstable oxygen-containing molecules (free radicals), which are byproducts of energy production. (medlineplus.gov)
Coenzyme Q10 acts as an antioxidant in the human body. (kingnature.ch)

60 vegan capsules with 50 mg ubiquinol (coenzyme Q10) each from natural biofermentative production. (kingnature.ch)

A recently collated, insightful Fact.MR report foresees the global coenzyme Q10 market to rise at a value CAGR of 9.2% between the period of forecast 2018 and 2028. (clickpress.com)

Coenzyme Q10 has, among other things, an important function in the energy metabolism in the cells. (kingnature.ch)

Coenzyme Q10, or CoQ-10, is a vitamin-like substance found in the internal organs of the human body, in small amounts in certain foods, and in nutritional supplements 1 . (healthfully.com)
Coenzyme Q10 molecules are fat-soluble molecules that are both synthesized in the body and ingested in the diet and in supplements. (q10facts.com)

The coenzyme Q10 molecule has several critical functions in cells throughout the body. (medlineplus.gov)
Even though some studies do not confirm the positive role of Coenzyme Q10, it is a molecule important not only for energy production but also as an antioxidant. (diabeteslibrary.org)

Kirkman ® offers hypoallergenic Coenzyme Q10 in 25 mg capsules. (ourkidsasd.com)
90 vegan capsules with 50 mg coenzyme Q10 from natural biofermentative production for more energy. (kingnature.ch)

In the Japanese beauty scene, few antioxidants are considered as powerful as Coenzyme Q10 to promote skin's wellness and fight the free radicals that can accelerate signs of aging. (dhccare.com)
Like most other antioxidants, coenzyme Q10 can prevent heart disease and lower cholesterol levels. (kingnature.ch)
Mackeral is rich in coenzyme Q10, antioxidants, and omega-3 fats. (dogbar.com)

While a cofactor sounds similar to a coenzyme and the terms are sometimes mistakenly utilized interchangeably, it is important to acknowledge they are two different entities. (mitoq.com)

It is known to function as a coenzyme of metabolic processes. (medscape.com)
as coenzymes and precursors of coenzymes in the regulation of metabolic processes but do not provide energy or serve as building units, and are present in natural foodstuffs or sometimes produced within the body. (howstuffworks.com)

Clinical findings regarding the effects of coenzyme Q10 on dyslipidemia, hypertension, and obesity are conflicting. (biomedcentral.com)

IMSEAR at SEARO: Studies on biosynthesis of coenzyme A in vitro by rat tissues. (who.int)

Coenzymes represent the organic molecules that help contribute to the enzymatic function. (mitoq.com)

Coenzyme Q10 is synthesized in the body in the same biological pathway as cholesterol. (q10facts.com)
CRISPR Interference Reveals That All-Trans-Retinoic Acid Promotes Macrophage Control of Mycobacterium tuberculosis by Limiting Bacterial Access to Cholesterol and Propionyl Coenzyme A. (harvard.edu)
Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization. (bvsalud.org)

Resistant parasites generated in vitro showed mutations in acetyl-coenzyme A synthetase and acyl-coenzyme A synthetase 11. (elsevier.com)

I've read an article (actually an advertisement) that said Coenzyme Q10 absorption is improved dramatically by including Bioperine which is an extract obtained from the black pepper fruit. (smartskincare.com)
To increase the absorption in the intestine, we process the coenzyme Q10 for our products in liposomal form. (kingnature.ch)

Coenzymes include the reduced form of nicotinamide adenine dinucleotide (NADH), the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) and adenosine triphosphate. (cosmeticsandtoiletries.com)
Nicotinamide, the water-soluble amide of nicotinic acid, is a component of the two most important coenzymes - nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate. (enzolifesciences.com)

A lack of functional protein produced from any one of the COQ genes decreases the normal production of coenzyme Q10. (medlineplus.gov)

In addition to our Coenzyme B-Complex Caps , we carry Vitamin B12 1000 mcg and B12 Gummies to help support your nutritional goals. (countrylifevitamins.com)

As a dietary supplement, take 1 capsule of coenzyme q10 1 to 2 times daily, preferably with meals. (vitadigest.com)
Sometimes, coenzyme Q10 is called vitamin Q. It can be purchased as a standalone supplement or as an ingredient in a multi supplement. (topnaturalremedies.net)
Hence Coenzyme Q10 can definitely be recommended as a supplement along with other anti-diabetic medication for better control of blood sugar and more importantly reduction of complications. (diabeteslibrary.org)
Some tests in this panel may exhibit interference when sample is collected from a person who is consuming a supplement with a high dose of biotin (also termed as vitamin B7 or B8, vitamin H or coenzyme R). Patient should be cautioned to stop biotin consumption at least 72 hours prior to the collection of a sample. (privatemdlabs.com)

Hypertension, retinopathy, nephropathy and neuropathy are essential complications of diabetes and Coenzyme Q10 may be helpful in long term prevention of these complications 7 . (diabeteslibrary.org)

The company's main coenzyme products, represented by NMN, NADH, NADPH and NR, have obtained stable and effective patent protection for the relevant products. (bontac.com)
En la fermentación alcohólica cataliza el paso final de reducción de un aldehído a un alcohol en presencia de NADH e hidrógeno. (bvsalud.org)

1975. Drug-biomolecule interations: Drug toxicity and vitamin coenzyme depletion. (cdc.gov)

Therefore, we cloned several genes encoding fatty acyl-coenzyme A reductases from wheat and analyzed their function in yeast and plants. (biomedcentral.com)

Martelli A , Testai L , Colletti A , Coenzyme Q10: clinical applications in cardiovascular diseases . (avma.org)

first undergoes a carboxylation, forming malonyl coenzyme A, before participating in fatty acid synthesis. (britannica.com)
Three endoplasmic reticulum-associated fatty acyl-coenzyme a reductases were involved in the production of primary alcohols in hexaploid wheat (Triticum aestivum L. (biomedcentral.com)
We reported the cloning and characterization of three TaFARs, namely TaFAR6 , TaFAR7 and TaFAR8 , encoding fatty acyl-coenzyme A reductases (FAR) in wheat leaf cuticle. (biomedcentral.com)
Lipid fractionation studies showed that by 10 min these two beta-hydroxy fatty acids were distributed approximately as 60% acylcarnitine, 20% acyl-coenzyme A (CoA), and 20% free fatty acids. (jci.org)

How coenzyme Q10 can help in Diabetes Mellitus? (diabeteslibrary.org)
There have been many studies to assess the role of coenzyme Q10 in reducing blood pressure and controlling blood sugars in diabetes mellitus. (diabeteslibrary.org)
As discussed earlier there is increased production of free radicals in diabetes mellitus, Coenzyme Q10 along with Vit C and Vit E scavenge these free radicals so that the cell damage is minimum. (diabeteslibrary.org)

Several researchers have performed studies that have examined the use of coenzyme Q10 for fertility. (txfertility.com)
Also, the researchers hope that this coenzyme can have a strong effect for women suffering from breast cancer. (topnaturalremedies.net)

Coenzyme Q10 is a vitamin-like substance that can also be produced by the body itself. (kingnature.ch)

One of the most crucial coenzymes within the body is adenosine triphosphate (ATP). (mitoq.com)
The body makes coenzyme Q10 by using an amino acid called tyrosine and vitamin B6. (txfertility.com)
Coenzyme B-Complex contains essential B Vitamins in its active, body-ready or "coenzymated" form. (countrylifevitamins.com)
Coenzyme Q10 is a naturally-occurring compound found in every cell of the body. (topnaturalremedies.net)
Coenzyme Q10 helps protect your body against toxins. (topnaturalremedies.net)

Coenzymes are usually regenerated and their concentrations are maintained at a steady level inside the cell. (cosmeticsandtoiletries.com)
Tissue concentrations of coenzyme Q10 in the rat following its oral and intraperitoneal administration. (aspetjournals.org)

Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues. (kegg.jp)

A coenzyme is a chemical substance that helps various chemical reactions to take place in the cell. (diabeteslibrary.org)

Coenzyme Q10: More than just an anti-wrinkle miracle! (kingnature.ch)

Coenzyme Q 10 can directly neutralize these free radicals. (diabeteslibrary.org)

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)

Supplementing with the nutritionally non-essential Coenzyme Q10 can augment the levels of this general purpose fat-soluble antioxidant and critical component for cellular energy generation, which may be of particular significance for older consumers. (totalhealthmagazine.com)

Evidence suggested that intake of curcumin and coenzyme Q10 may have therapeutic effects in the management of MetS. (biomedcentral.com)

Buy Coenzyme Q10 and minerals products and order Online. (vitamarket.net)
Bontac Bio is a Chinese high-tech enterprise that uses biocatalytic technology to produce coenzyme factors, drug intermediates and natural products on a large scale. (bontac.com)

The reduced production of Coenzyme Q10 cannot be compensated for in the diet in any practical way. (q10facts.com)

What Are Coenzymes & What Role Do They Play In Your Health? (mitoq.com)
Below is a closer look at coenzymes and what role they play in your overall health. (mitoq.com)

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