Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.MalatesMalate Dehydrogenase (NADP+)Malate Synthase: An important enzyme in the glyoxylic acid cycle which reversibly catalyzes the synthesis of L-malate from acetyl-CoA and glyoxylate. This enzyme was formerly listed as EC 4.1.3.2.Hydrogenation: Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)L-Lactate Dehydrogenase: 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.Oxaloacetates: Derivatives of OXALOACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include a 2-keto-1,4-carboxy aliphatic structure.NAD: 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)SkatoleIsocitrate Dehydrogenase: 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.Oxaloacetic Acid: A dicarboxylic acid ketone that is an important metabolic intermediate of the CITRIC ACID CYCLE. It can be converted to ASPARTIC ACID by ASPARTATE TRANSAMINASE.Alcohol Dehydrogenase: 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.Alcohol Oxidoreductases: 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).Glutamate Dehydrogenase: 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.Kinetics: The rate dynamics in chemical or physical systems.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Succinate Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.Glucosephosphate DehydrogenaseGlyceraldehyde-3-Phosphate Dehydrogenases: 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.Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.Citrate (si)-Synthase: Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.Ketoglutarate Dehydrogenase ComplexOxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Glycerolphosphate DehydrogenaseNADP: 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)Fumarate Hydratase: An enzyme that catalyzes the reversible hydration of fumaric acid to yield L-malic acid. It is one of the citric acid cycle enzymes. EC 4.2.1.2.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Aldehyde Dehydrogenase: 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.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.CitratesAcyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Hydroxybutyrate DehydrogenaseMultiple Acyl Coenzyme A Dehydrogenase Deficiency: An autosomal recessive disorder of fatty acid oxidation, and branched chain amino acids (AMINO ACIDS, BRANCHED-CHAIN); LYSINE; and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1).Ketoglutaric Acids: A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)Mitochondria: 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)Succinates: 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.Isovaleryl-CoA Dehydrogenase: A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).Mitochondria, Liver: 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)Fumarates: Compounds based on fumaric acid.Formic Acid EstersCarbohydrate Dehydrogenases: Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.Mitochondria, Heart: The mitochondria of the myocardium.Phosphogluconate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.L-Iditol 2-Dehydrogenase: An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14Electron-Transferring Flavoproteins: Flavoproteins that serve as specific electron acceptors for a variety of DEHYDROGENASES. They participate in the transfer of electrons to a variety of redox acceptors that occur in the respiratory chain.Thermus: Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Electrophoresis, Starch Gel: Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.2,6-Dichloroindophenol: A dye used as a reagent in the determination of vitamin C.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Acyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.Hydrogen: The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.Acyl-CoA Dehydrogenase, Long-Chain: A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Citric Acid: A key intermediate in metabolism. It is an acid compound found in citrus fruits. The salts of citric acid (citrates) can be used as anticoagulants due to their calcium chelating ability.Aspartate Aminotransferases: 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.Oxidoreductases Acting on CH-NH Group Donors: Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Oxamic Acid: Amino-substituted glyoxylic acid derivative.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Rhodotorula: A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.Alcohols: Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.GlyoxylatesNADH Dehydrogenase: A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Flavin-Adenine Dinucleotide: 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)Oxidoreductases Acting on CH-CH Group Donors: A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.18-Hydroxycorticosterone: 11 beta,18,21-Trihydroxypregn-4-ene-3,20-dione.Fructose-Bisphosphatase: An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Ruthenium: A hard, brittle, grayish-white rare earth metal with an atomic symbol Ru, atomic number 44, and atomic weight 101.07. It is used as a catalyst and hardener for PLATINUM and PALLADIUM.Molecular Weight: The sum of the weight of all the atoms in a molecule.Glucose Dehydrogenases: D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Mitochondria, Muscle: Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.TartronatesSugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.Phosphoenolpyruvate Carboxylase: An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. EC 4.1.1.31.Hydrocarbons, Cyclic: Organic compounds composed exclusively of carbon and hydrogen forming a closed ring that may be either alicyclic or aromatic.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.MalonatesAnaerobiosis: 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)Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Spectrophotometry, Ultraviolet: 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)Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Stereoisomerism: 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)Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cytochrome P-450 CYP3A: A cytochrome P-450 suptype that has specificity for a broad variety of lipophilic compounds, including STEROIDS; FATTY ACIDS; and XENOBIOTICS. This enzyme has clinical significance due to its ability to metabolize a diverse array of clinically important drugs such as CYCLOSPORINE; VERAPAMIL; and MIDAZOLAM. This enzyme also catalyzes the N-demethylation of ERYTHROMYCIN.Flavins: 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.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Formate Dehydrogenases: 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.Electron Transport: 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)Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Biotransformation: The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Xanthine Dehydrogenase: An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.Aspartate Aminotransferase, Mitochondrial: An aspartate aminotransferase found in MITOCHONDRIA.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Chaperonin 10: A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.Uroporphyrins: Porphyrins with four acetic acid and four propionic acid side chains attached to the pyrrole rings.Chaperonin 60: A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Pyruvate Carboxylase: A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.Haloarcula marismortui: A species of halophilic archaea distinguished by its production of acid from sugar. This species was previously called Halobacterium marismortui.3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.Lipid Metabolism, Inborn Errors: Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Isocitrate Lyase: A key enzyme in the glyoxylate cycle. It catalyzes the conversion of isocitrate to succinate and glyoxylate. EC 4.1.3.1.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Indapamide: A benzamide-sulfonamide-indole derived DIURETIC that functions by inhibiting SODIUM CHLORIDE SYMPORTERS.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Dicarboxylic AcidsCoenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Succinic Acid: A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).Coenzyme AMicrosomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.Glutamates: Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.Oxygen Consumption: The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.11-beta-Hydroxysteroid Dehydrogenases: Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.Enzyme Stability: 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.PyruvatesMagnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Enoyl-CoA Hydratase: 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.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Carboxy-Lyases: 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.Aconitate Hydratase: An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. It is one of the citric acid cycle enzymes. EC 4.2.1.3.Chloroplast Thioredoxins: A subtype of thioredoxins found primarily in CHLOROPLASTS.Myocardium: The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.Glucosephosphate Dehydrogenase Deficiency: A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.TartratesEnzymes: Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.Protein Denaturation: Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Lactates: Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Iodobenzoates: Benzoic acid esters or salts substituted with one or more iodine atoms.Pyruvic Acid: An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.11-beta-Hydroxysteroid Dehydrogenase Type 1: A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.Hydroxylation: Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)Cytochrome P-450 Enzyme System: A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.Alanine Dehydrogenase: An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.Glyoxysomes: Microbodies which occur in plant cells, and in some eukaryotic microorganisms, and which contain enzymes of the glyoxylate cycle. (Singleton and Stainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Mannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Bacterial Proteins: Proteins found in any species of bacterium.Pyruvate Kinase: ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Benzene DerivativesFatty Acids: 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)Glycolysis: A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Quinone Reductases: NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Butyryl-CoA Dehydrogenase: 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.Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.Carbon: A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Oxygenases: Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.S-Adenosylmethionine: Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)Hexokinase: An enzyme that catalyzes the conversion of ATP and a D-hexose to ADP and a D-hexose 6-phosphate. D-Glucose, D-mannose, D-fructose, sorbitol, and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. (From Enzyme Nomenclature, 1992) EC 2.7.1.1.Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.20-Hydroxysteroid Dehydrogenases: A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.11-beta-Hydroxysteroid Dehydrogenase Type 2: An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Thioredoxins: Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.Mixed Function Oxygenases: Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.Cell Fractionation: Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.
Lamzin VS, Dauter Z, Wilson KS (May 1994). "Dehydrogenation through the looking-glass". Nature Structural Biology. 1 (5): 281-2 ... Malate dehydrogenases catalyzes the interconversion of malate to oxaloacetate. In the citric acid cycle, malate dehydrogenase ... The ΔG'° of malate dehydrogenase is +29.7 kJ/mol and the ΔG (in the cell) is 0 kJ/mol. Malate dehydrogenase is also involved in ... The Km value for malate dehydrogenase at which the concentration of malate dehydrogenase gives half the enzyme activity is 2 mM ...
Dehydrogenation by acyl-CoA dehydrogenase, yielding 1 FADH2 Hydration by enoyl-CoA hydratase Dehydrogenation by 3-hydroxyacyl- ... When malate is oxidatively decarboxylated by "NADP+-linked malic enzyme" pyruvate, CO2 and NADPH are formed. NADPH is also ... Only plants possess the enzymes to convert acetyl-CoA into oxaloacetate from which malate can be formed to ultimately be ... It can also not be converted to pyruvate as the pyruvate dehydrogenase complex reaction is irreversible. Instead the acetyl-CoA ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... Isovaleryl-CoA undergoes dehydrogenation, carboxylation and hydration to form another CoA-derivative intermediate before it is ... The oxaloacetate is returned to the mitochondrion as malate (and then converted back into oxaloacetate to transfer more acetyl- ... The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by ...
Malate dehydrogenases that catalyse the interconversion of malate to oxaloacetate and participate in the citric acid cycle, and ... It also catalyzes the dehydrogenation of 2-Hydroxybutyrate, but it is a much poorer substrate than lactate. LDH in humans uses ... Madern D (2002). "Molecular evolution within the L-malate and L-lactate dehydrogenase super-family". J Mol Evol. 54 (6): 825-40 ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... Acyl-CoA is then degraded in a four-step cycle of dehydrogenation, hydration, oxidation and thiolysis catalyzed by four ... The oxaloacetate is returned to the mitochondrion as malate (and then converted back into oxaloacetate to transfer more acetyl- ... The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by ...
In the former the electrons from NADH are transferred to cytosolic oxaloacetate to form malate. The malate then traverses the ... Pentose phosphate pathway, which begins with the dehydrogenation of glucose-6-phosphate, the first intermediate to be produced ... Glyceraldehyde-3-phosphate dehydrogenase NAD++ Pi NADH + H+ NAD++ Pi NADH + H+ 2 × 1,3-Bisphosphoglycerate 2 × Phosphoglycerate ... When malate is oxidatively decarboxylated by "NADP+-linked malic enzyme" pyruvate, CO2 and NADPH are formed. NADPH is also ...
... is a water-soluble calcium supplement. It is the calcium salt of citric acid and malic acid with variable composition. Calcium citrate malate's bioavailability stems from its water-solubility and its method of dissolution. When dissolved, it releases calcium ions and a calcium citrate complex. Calcium ions are absorbed directly into intestinal cells, and the citrate complex enters the body through paracellular absorption.[citation needed] Calcium citrate malate is similar to calcium malate and other calcium salts. The European Food Safety Authority has concluded that calcium citrate malate is "slightly more bioavailable" than other forms of calcium supplementation. Calcium citrate malate at Jost Chemical "Calcium citrate malate as source for calcium for use in foods for Particular Nutritional Uses and ...
... , the magnesium salt of malic acid, is a mineral supplement often used for nutritional concerns. It is represented by the chemical formula C4H4MgO5 and has a molecular weight of 156.376 g/mol. Magnesium malate is discussed as being a more bioavailable form of magnesium, along with other forms such as citrate and glycinate. Dimagnesium malate is another common form of this compound seen in the dietary supplement market, produced by such dimetalhydroxy malate-yielding processes as the one described by a 1997 patent awarded to Albion Minerals. The primary difference in this compound can be seen by its characteristic of having two elemental magnesium molecules, whereas magnesium malate has a single elemental magnesium molecule. "PubChem". PubChem. "Magnesium Malate". Isotrope, Inc. 7 July 2017. Retrieved 8 September 2017. "Dimetal Hydroxy ...
Diacetyl (or 2,3-butanedione) is the compound associated with the "buttery" aromas of Chardonnays, but it can affect any wine that has gone through malolactic fermentation. At an odor detection threshold of 0.2 mg/l in white wines and 2.8 mg/l in red wines, it can be perceived as slightly buttery or "nutty" while at concentrations greater than 5 to 7 mg/l (5-7 ppm) can overwhelm other aroma notes in the wine.[7][10]. Diacetyl can be produced by the LAB through metabolism of sugar or of citric acid.[11] While citric acid is naturally present in grapes, it is in a very small amount with most of it coming from deliberate addition by the winemaker to acidify the wine.[8] In the presence of both malic and citric acids, the LAB use both, but use the malic much more quickly, with the rate of citric use/diacetyl formation influenced by the particular bacterial strain (with most strains of O. oeni producing less diacetyl than Lactobacillus and Pediococcis species), as well as the redox potential of the ...
... is a compound with formula Ca(C2H4O(COO)2). It is the calcium salt of malic acid. As a food additive, it has the E number E352. It is related to, but different from, calcium citrate malate ...
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis. ...
... is a compound with formula NH4(C2H4O(COO)2). It is the ammonium salt of malic acid. It is used as a food additive and has the E number E349. There is a recommendation to avoid this food additive.[1] ...
Kaufman, S., Korkes, S. and del Campillo, A. (1951). „B'iosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further studies of the "malic" enzyme of Lactobacillus arabinosus". J. Biol. Chem. 192: 301-312. PMID 14917678. ...
... is a water-soluble calcium supplement. It is the calcium salt of citric acid and malic acid with variable composition. Calcium citrate malate's bioavailability stems from its water-solubility and its method of dissolution. When dissolved, it releases calcium ions and a calcium citrate complex. Calcium ions are absorbed directly into intestinal cells, and the citrate complex enters the body through paracellular absorption.[citation needed] Calcium citrate malate is similar to calcium malate and other calcium salts. The European Food Safety Authority has concluded that calcium citrate malate is "slightly more bioavailable" than other forms of calcium supplementation. Calcium citrate malate at Jost Chemical "Calcium citrate malate as source for calcium for use in foods for Particular Nutritional Uses and ...
... , the magnesium salt of malic acid, is a mineral supplement often used for nutritional concerns. It is represented by the chemical formula C4H4MgO5 and has a molecular weight of 156.376 g/mol. Magnesium malate is discussed as being a more bioavailable form of magnesium, along with other forms such as citrate and glycinate. Dimagnesium malate is another common form of this compound seen in the dietary supplement market, produced by such dimetalhydroxy malate-yielding processes as the one described by a 1997 patent awarded to Albion Minerals. The primary difference in this compound can be seen by its characteristic of having two elemental magnesium molecules, whereas magnesium malate has a single elemental magnesium molecule. "PubChem". PubChem. "Magnesium Malate". Isotrope, Inc. 7 July 2017. Retrieved 8 September 2017. "Dimetal Hydroxy ...
... was first isolated from apple juice by Carl Wilhelm Scheele in 1785.[3] Antoine Lavoisier in 1787 proposed the name acide malique, which is derived from the Latin word for apple, mālum-as is its genus name Malus.[4][5] In German it is named Äpfelsäure (or Apfelsäure) after plural or singular of the fruit apple, but the salt(s) Malat(e). Malic acid is the main acid in many fruits, including apricots, blackberries, blueberries, cherries, grapes, mirabelles, peaches, pears, plums, and quince[6] and is present in lower concentrations in other fruits, such as citrus.[7] It contributes to the sourness of unripe apples. Sour apples contain high proportions of the acid. It is present in grapes and in most wines with concentrations sometimes as high as 5 g/l.[8] It confers a tart taste to wine; the amount decreases with increasing fruit ripeness. The taste of malic acid is very clear and pure in rhubarb, a plant for which it is the primary flavor. It is also a component of some artificial ...
... is a compound with formula Ca(C2H4O(COO)2). It is the calcium salt of malic acid. As a food additive, it has the E number E352. It is related to, but different from, calcium citrate malate ...
... is a compound with formula NH4(C2H4O(COO)2). It is the ammonium salt of malic acid. It is used as a food additive and has the E number E349. There is a recommendation to avoid this food additive.[1] ...
Chargaff kuralları, Avusturyalı biyokimyacı Edwin Chargaff tarafından 1949-1951'de yayımlanan, DNA'daki çeşitli azotlu bazların miktarları arasındaki ilişkileri ifade eden empirik kurallardır.[1][2][3][4][5][6]. Chargaff'ın çalışmasına kadar "tetranükleotit" teorisi hakimdi, bu teoriye göre DNA dört farklı azotlu bazın ( adenin, timin, guanin ve sitozin) tekrar eden birimlerinden oluşmaktaydı. Chargaff ve yardımcıları DNA nükleotitlerini kâğıt kromatografisi ile ayrıştırıp farklı tiplerden nükleotitlerin miktarlarını ölçtüler. Eğer dört baz tekrar eden birimler içinde olsaydı oranlarının eşit olması beklenirdi, oysa ölçümler bunu doğrulamadı. Chargaff tarafından bulunan ilişkiler aşağıdaki gibiydi:[7]. ...
Lamzin VS, Dauter Z, Wilson KS (May 1994). "Dehydrogenation through the looking-glass". Nature Structural Biology. 1 (5): 281-2 ... Malate dehydrogenases catalyzes the interconversion of malate to oxaloacetate. In the citric acid cycle, malate dehydrogenase ... The ΔG° of malate dehydrogenase is +29.7 kJ/mol and the ΔG (in the cell) is 0 kJ/mol. Malate dehydrogenase is also involved in ... The Km value for malate dehydrogenase at which the concentration of malate dehydrogenase gives half the enzyme activity is 2 mM ...
What is malate dehydrogenase? Meaning of malate dehydrogenase medical term. What does malate dehydrogenase mean? ... Looking for online definition of malate dehydrogenase in the Medical Dictionary? malate dehydrogenase explanation free. ... ma·late de·hy·dro·gen·ase (MD), an enzyme that, using either NAD+ or NADP+, catalyzes the dehydrogenation of malate to ... mal·ate de·hy·dro·gen·ase (malāt dē-hīdrō-jĕ-nās) Any enzyme that catalyzes the dehydrogenation of malate to oxaloacetate. At ...
In other words, it catalyzes, by means of NAD+ or NADP, the dehydrogenation of malate to oxaloacetate or the decarboxylation of ... 3. Malate dehydrogenase[edit]. Malactate dehydrogenase oxidizes malate to oxaloactate in areversible reaction. NADH and NAD+ ... 2. L-Lactate dehydrogenase[edit]. L-lactate dehydrogenase oxidizes the reversible reaction of L-lactate to pyruvate by using ... 1. The alcohol dehydrogenases[edit]. The alcohol dehydrogenase catalyzes the reaction of alcohols to aldehydes and ketones by ...
... where it catalyzes the dehydrogenation of malic acid to... Explanation of Malate dehydrogenase (nadp+) ... Find out information about Malate dehydrogenase (nadp+). malic enzyme an enzyme of the oxidoreductase class widely distributed ... Malate Dehydrogenase. (redirected from Malate dehydrogenase (nadp+)). Also found in: Medical. malate dehydrogenase. [′ma‚lāt dē ... Malate dehydrogenase (nadp+). *malate dehydrogenase, NAD-linked malate dehydrogenase. *malate dehydrogenase, NAD-linked malate ...
Fumarate + H2O -, Malate. 10. Dehydrogenation:. Malate is dehydrogenated into Oxaloacetic acid by using NAD as a proton ... α-ketoglutarate dehydrogenase is inhibited by Arsinite. This again is a non-competitive inhibition. ... Malate + NAD+ -, Oxaloacetic acid + NADH + H+. Regulation of Citric Acid Cycle:. The capacity of TCA cycle to generate energy ... 6. Dehydrogenation:. α-ketoglutarate is converted into Succinyl~coA by taking one Acetyl~CoA and one molecule of NAD+. This ...
Dehydrogenation of saccharopine forms glutamate and aminoadipic semialdehyde, which is further oxidized to α-ketoadipate. ... that normally functions in the malate/aspartate shuttle. Depletion of α-KG prevents regeneration of oxaloacetate (OAA) needed ... CPTII, carnitine palmitoyltransferase II; PDH, pyruvate dehydrogenase.. Mechanism of age-dependent susceptibility and novel ...
1) Malate dehydrogenase (EC 1.1.1.38, EC 1.1.1.39) Reaction:. (2) Alcohol dehydrogenase (EC 1.1.1.1) Reaction:. (3) Glycerol ... The dehydrogenation of the substrate in the presence of the NADH oxidase by the dehydrogenase described above proceeds, for ... Using the aforesaid malate dehydrogenase as the dehydrogenase capable of being coupled with the NADH oxidase in accordance with ... 7) No production of succinic acid occurs from L-malic acid when used in a coupling reaction with malate dehydrogenase.. 2. The ...
One was specific for NAD+ and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate ... The NAD+-specific malate dehydrogenase showed high sequence similarity to l-malate dehydrogenase from Methanothermus fervidus, ... using malate dehyrogenase showed high sequence similarity to l-lactate dehydrogenase from Thermotoga maritima and l-malate ... dehydrogenase from Bacillus subtilis. A function of the two malate dehydrogenases in NADPH:NAD+ transhydrogenation is discussed ...
The malate is dehydrogenated in the presence of malic dehydrogenase and DPN+ forming oxaloacetate and DPNH. This reaction is ... and electrons liberated in the course of a dehydrogenation in the tricarboxylic acid cycle or other aerobic dehydrogenation ... Reaction 10 is a reversible hydration of fumarate to malate in the presence of fumarase. Although, in the liver, malate may ... formed and placed at the disposition of the cells.In the course of the successive dehydrogenations of the cycle, the greater ...
NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene-H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as ... malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with ... Methylene tetrahydromethanopterin dehydrogenase, NADP-binding domain (IPR035015). Short name: NAD-bd_H4MPT_DH ... Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1.. Structure 10 1127-37 2002 ...
... malate synthase; aceK, isocitrate dehydrogenase kinase/phosphatase; ldhA, lactate dehydrogenase; pflB, pyruvate formate lyase; ... Succinate dehydrogenase (SHD) encoded by sdh gene catalyzes the dehydrogenation of succinate to fumarate. The sdh expression ... alcohol/acetaldehyde dehydrogenase; maeAB, malic enzyme; mdh, malate dehydrogenase; fumABC, fumaraseABC; frd, fumarate ... The aceBAK operon coding isocitrate lyase, malate synthase and isocitrate dehydrogenase kinase is responsible for the ...
In astrocytes, however, cytosolic malate dehydrogenation was considered in the same direction as the mitochondrial one since it ... is known that the malate-aspartate shuttle is not active in astrocytes [29, 31], although cytosolic malate dehydrogenase is ... a cytosolic version of malate dehydrogenation (r69) in the reverse direction was included in neurons in addition to the ... Developmental regulation and cellular distribution of human cytosolic malate dehydrogenase (mdh1). J Cell Biochem. 2005, 94: ...
The first is acyl-CoA dehydrogenase, which catalyzes the initial dehydrogenation and yields FADH2. It comes in three different ... dehydrogenation of succinate to make a transdouble bond (fumarate), hydration across the double bond to make L-malate and ... dehydrogenation to create \(\text{FADH}_2\) and a fatty acyl group with a double bond in the trans configuration; ... The most interesting of the acyl-CoA dehydrogenases is the one that works on medium length fatty acids. This one, which is the ...
In addition to its dehydrogenation into lactate for the regeneration of NAD+, pyruvate can also enter the mitochondria where it ... and malate (Figure 4A). The magnitude of increased TCA cycle intermediates in blood was larger in the Gold group, suggesting ... lactate dehydrogenase oxidizes NADH back to NAD+ in the conversion of pyruvate to lactate, thereby maintaining necessary levels ... Nutritional status affects branched-chain oxoacid dehydrogenase activity during exercise in humans. Am. J. Physiol. 272, E233- ...
Dehydrogenation by acyl-CoA dehydrogenase, yielding 1 FADH2 Hydration by enoyl-CoA hydratase Dehydrogenation by 3-hydroxyacyl- ... When malate is oxidatively decarboxylated by "NADP+-linked malic enzyme" pyruvate, CO2 and NADPH are formed. NADPH is also ... Only plants possess the enzymes to convert acetyl-CoA into oxaloacetate from which malate can be formed to ultimately be ... It can also not be converted to pyruvate as the pyruvate dehydrogenase complex reaction is irreversible. Instead the acetyl-CoA ...
Finally, L-malate is dehydrogenated to oxaloacetate, which is catalyzed by the NAD-linked enzyme L-malate dehydrogenase. The ... which is much more susceptible than the acetyl group to the dehydrogenation and decarboxylation reactions needed to remove ... This enzyme uses the ATP to phosphorylate the pyruvate dehydrogenase into an inactive form, pyruvate dehydrogenase phosphate. ... Three pairs are used to reduce three molecules of NAD+ to NADH and one pair to reduce the FAD of succinate dehydrogenase to ...
The first is acyl-CoA dehydrogenase, which catalyzes the dehydrogenation in the first reaction and yields FADH2. The enzyme ... of the hydroxyl on carbon 3 in β-oxidation is repeated in the citric acid cycle reaction catalyzed by malate dehydrogenase ... The most interesting of the acyl-CoA dehydrogenases is the one that works on medium length fatty acids. This one, which is the ... The last two reactions are catalyzed by alcohol dehydrogenase and each requires NAD+. After the last oxidation, the fatty acid ...
... and malate dehydrogenase were still active in the light. It remains plausible that such data obtained in vitro may have been ... for the mitochondrial dehydrogenation steps of the TCA cycle. Such a scenario is consistent with the larger in vivo ... Dry IB, Wiskich JT (1987) 2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction ... through the reverse operation of the malate dehydrogenase, which was further followed by the fumarase (probability coefficient ...
... produced from the reduction of 2-KG by the promiscuous catalytic activity of l-malate dehydrogenase and l-lactate dehydrogenase ... dehydrogenation pathway, where glutaryl-CoA dehydrogenase (GcdH) is the key enzyme (11). In this pathway, glutarate is first ... reduction of 2-KG that results from the promiscuous catalytic activity of l-malate dehydrogenase and l-lactate dehydrogenase ... Lactate dehydrogenase C produces S-2-hydroxyglutarate in mouse testis. ACS Chem Biol 11:2420-2427. doi:10.1021/acschembio. ...
What is the function of decarboxylating malate dehydrogenase?. It breaks malate into pyruvate, NADH, and CO2. The function ... Branched chain dehydrogenase - similar in structure to pyruvate dehydrogenase - its the same for all 3. (requires Thiamine, ... Defect in BCAA dehydrogenase. It includes a failure to thrive and mental retardation - a result of toxic keto-acids - also have ... Glu (glu dehydrogenase releases ammonia) and Asp (an actual intermediate in the cycle - it can jump right in) ...
A vibrational analysis of the catalytically important C4-H bonds of NADH bound to lactate or malate dehydrogenase: ground‐state ... Quastel JH (1926) Dehydrogenations produced by resting bacteria. IV. A theory of the mechanism of oxidations and reductions in ... LaReau RD, Wan W and Anderson VE (1989) Isotope effects on binding of NAD+ to lactate dehydrogenase. Biochemistry 28: 3619-3624 ... Classical Raman spectroscopic studies of NADH and NAD+ bound to lactate dehydrogenase by difference techniques. Biochemistry 28 ...
... dehydrogenation explanation free. What is dehydrogenation? Meaning of dehydrogenation medical term. What does dehydrogenation ... Looking for online definition of dehydrogenation in the Medical Dictionary? ... lactic dehydrogenase. *malate dehydrogenase. *malic dehydrogenase. *malic enzyme. *multiple acyl CoA dehydrogenation deficiency ... dehydrogenation. Also found in: Dictionary, Thesaurus, Encyclopedia, Wikipedia. de·hy·dro·gen·a·tion. (dē-hīdrojen-āshŭn), ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... Acyl-CoA is then degraded in a four-step cycle of dehydrogenation, hydration, oxidation and thiolysis catalyzed by four ... The oxaloacetate is returned to the mitochondrion as malate (and then converted back into oxaloacetate to transfer more acetyl- ... The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by ...
... assay of d-aspartate and d-glutamate using d-aspartate oxidase with malate dehydrogenase and glutamate dehydrogenase. Anal ... of d-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation ...
The co-dehydrogenases and the yellow enzymes also take part in this system. I have attempted to add them in at the right place. ... the dehydrogenation of certain donors is linked to the presence of a co-enzyme. ... OAA + NADH - (MDH) - malate + NAD+ + H+. This malic acid now passes on the H-atoms, and thus reverts to oxaloacetic acid, ... Alcohol dehydrogenases occur in both the animal and the vegetable kingdoms, e.g. in liver, in yeast, and in peas. They are ...
  • Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. (ebi.ac.uk)
  • Reduction of NAD was varied by varying the concentration of palmitoyl-L-carnitine, pyruvate, 2-oxoglutarate or glutamate in the presence of malate as the oxidizable substrate. (semanticscholar.org)
  • As we have seen, it is along the respiratory chain that by a series of phosphorylations coupled to it by a still unknown mechanism (see p. 144 ) the main quota of energy-rich bonds is formed and placed at the disposition of the cells.In the course of the successive dehydrogenations of the cycle, the greater part of the protons and electrons liberated pass to the same series of carriers. (questia.com)
  • In this study, it was found that a GntR family protein, CsiR, and a LysR family protein, GcdR, regulate the catabolism of glutarate by repressing the transcription of csiD and lhgO , two key genes in the glutarate hydroxylation pathway, and by activating the transcription of gcdH and gcoT , two key genes in the glutaryl-CoA dehydrogenation pathway, respectively. (asm.org)