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.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Disulfiram: A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.Acetaldehyde: A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.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.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.Betaine-Aldehyde Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.Cyanamide: A cyanide compound which has been used as a fertilizer, defoliant and in many manufacturing processes. It often occurs as the calcium salt, sometimes also referred to as cyanamide. The citrated calcium salt is used in the treatment of alcoholism.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)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.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).Glyceraldehyde-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.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.BenzaldehydesGlutamate 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.Glucosephosphate DehydrogenaseSjogren-Larsson Syndrome: An autosomal recessive neurocutaneous disorder characterized by severe ichthyosis MENTAL RETARDATION; SPASTIC PARAPLEGIA; and congenital ICHTHYOSIS. It is caused by mutation of gene encoding microsomal fatty ALDEHYDE DEHYDROGENASE leading to defect in fatty alcohol metabolism.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Isocitrate 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.Phosphoramide Mustards: A group of nitrogen mustard compounds which are substituted with a phosphoramide group or its derivatives. They are usually cytotoxic and used as antineoplastic agents.Kinetics: The rate dynamics in chemical or physical systems.NADP: 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)Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Chloral Hydrate: A hypnotic and sedative used in the treatment of INSOMNIA.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 1.1.1.14Dihydrolipoamide 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.Carbohydrate 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.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.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)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Ethanol: A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.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.Oxidation-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 DehydrogenaseAldehyde Reductase: An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Succinate-Semialdehyde Dehydrogenase: An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).Flushing: A transient reddening of the face that may be due to fever, certain drugs, exertion, stress, or a disease process.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.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.Sugar 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.Ketoglutarate Dehydrogenase ComplexAcroleinCoenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.p-Aminoazobenzene: Used in the form of its salts as a dye and as an intermediate in manufacture of Acid Yellow, diazo dyes, and indulines.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.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.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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.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)NADH 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.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.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Alkadienes: Acyclic branched or unbranched hydrocarbons having two carbon-carbon double bonds.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 1.2.1.2.2,2'-Dipyridyl: A reagent used for the determination of iron.Acyl-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.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Neoplastic Stem Cells: Highly proliferative, self-renewing, and colony-forming stem cells which give rise to NEOPLASMS.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)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Hydroxybutyrate DehydrogenaseCloning, 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.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.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.Nitroglycerin: A volatile vasodilator which relieves ANGINA PECTORIS by stimulating GUANYLATE CYCLASE and lowering cytosolic calcium. It is also sometimes used for TOCOLYSIS and explosives.Ditiocarb: A chelating agent that has been used to mobilize toxic metals from the tissues of humans and experimental animals. It is the main metabolite of DISULFIRAM.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.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).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.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.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.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.Pentaerythritol Tetranitrate: A vasodilator with general properties similar to NITROGLYCERIN but with a more prolonged duration of action. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1025)Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.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)Molecular Weight: The sum of the weight of all the atoms in a molecule.Retinaldehyde: A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.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)Betaine: A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Alcohol Deterrents: Substances interfering with the metabolism of ethyl alcohol, causing unpleasant side effects thought to discourage the drinking of alcoholic beverages. Alcohol deterrents are used in the treatment of alcoholism.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.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.Enzyme Induction: An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.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)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.Sheep: Any of the ruminant mammals with curved horns in the genus Ovis, family Bovidae. They possess lachrymal grooves and interdigital glands, which are absent in GOATS.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.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.Fatty Alcohols: Usually high-molecular-weight, straight-chain primary alcohols, but can also range from as few as 4 carbons, derived from natural fats and oils, including lauryl, stearyl, oleyl, and linoleyl alcohols. They are used in pharmaceuticals, cosmetics, detergents, plastics, and lube oils and in textile manufacture. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Benzaldehyde Dehydrogenase (NADP+)Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.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.EsterasesSpectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Glyceraldehyde20-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).Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.NitrophenolsChlorpropamide: A sulfonylurea hypoglycemic agent used in the treatment of non-insulin-dependent diabetes mellitus not responding to dietary modification. (From Martindale, The Extra Pharmacopoeia, 30th ed, p277)Mitochondrial Proteins: Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.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.Benzodioxoles: Compounds based on benzene fused to oxole. They can be formed from methylated CATECHOLS such as EUGENOL.KetonesMutation: 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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Tretinoin: An important regulator of GENE EXPRESSION during growth and development, and in NEOPLASMS. Tretinoin, also known as retinoic acid and derived from maternal VITAMIN A, is essential for normal GROWTH; and EMBRYONIC DEVELOPMENT. An excess of tretinoin can be teratogenic. It is used in the treatment of PSORIASIS; ACNE VULGARIS; and several other SKIN DISEASES. It has also been approved for use in promyelocytic leukemia (LEUKEMIA, PROMYELOCYTIC, ACUTE).Genes, Bacterial: The functional hereditary units of BACTERIA.Metabolic Detoxication, Drug: Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.Choline Dehydrogenase: An enzyme bound to the inner mitochondrial membrane that catalyzes the oxidation of CHOLINE to BETAINE.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).3-Isopropylmalate Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.Sequence Alignment: 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.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Dimethyl Adipimidate: Bifunctional cross-linking agent that links covalently free amino groups of proteins or polypeptides, including those in cell membranes. It is used as reagent or fixative in immunohistochemistry and is a proposed antisickling agent.Malate Dehydrogenase (NADP+)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.Horses: 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.Pyruvate Dehydrogenase (Lipoamide)-Phosphatase: (Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.Leucine Dehydrogenase: An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.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.Phosphoglycerate Dehydrogenase: An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.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.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.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.Estradiol Dehydrogenases: Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62Alcohol Drinking: Behaviors associated with the ingesting of alcoholic beverages, including social drinking.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Alkanes: The generic name for the group of aliphatic hydrocarbons Cn-H2n+2. They are denoted by the suffix -ane. (Grant & Hackh's Chemical Dictionary, 5th ed)MercaptoethanolEstersAcetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.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)Glutamate Dehydrogenase (NADP+)Vibrio: A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (1/1111)
Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction. (+info)Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (2/1111)
Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3. (+info)Stimulation of premature retinoic acid synthesis in Xenopus embryos following premature expression of aldehyde dehydrogenase ALDH1. (3/1111)
In order for nuclear retinoic acid receptors to mediate retinoid signaling, the ligand retinoic acid must first be produced from its vitamin A precursor retinal. Biochemical studies have shown that retinal can be metabolized in vitro to retinoic acid by members of the aldehyde dehydrogenase enzyme family, including ALDH1. Here we describe the first direct evidence that ALDH1 plays a physiological role in retinoic acid synthesis by analysis of retinoid signaling in Xenopus embryos, which have plentiful stores of maternally derived retinal. The Xenopus ALDH1 gene was cloned and shown to be highly conserved with chick and mammalian homologs. Xenopus ALDH1 was not expressed at blastula and gastrula stages, but was expressed at the neurula stage. We used a retinoic acid bioassay to demonstrate that retinoic acid is normally undetectable in embryos from fertilization to the initial gastrula stage, but that a tremendous increase in retinoic acid occurs during neurulation when ALDH1 is first expressed. Overexpression of ALDH1 by injection of Xenopus embryos with mRNAs encoding the mouse, chick or Xenopus ALDH1 homologs induced high levels of retinoic acid detection during the blastula stage. Thus, premature expression of ALDH1 stimulates premature synthesis of retinoic acid. These findings reveal an important conserved role for ALDH1 in retinoic acid synthesis in vivo, and demonstrate that conversion of retinoids from the aldehyde form to the carboxylic acid form is a crucial regulatory step in retinoid signaling. (+info)The negative regulation of the rat aldehyde dehydrogenase 3 gene by glucocorticoids: involvement of a single imperfect palindromic glucocorticoid responsive element. (4/1111)
Glucocorticoids repressed the polycyclic aromatic hydrocarbon-dependent induction of Class 3 aldehyde dehydrogenase (ALDH3) enzyme activity and mRNA levels in isolated rat hepatocytes by more than 50 to 80%, with a concentration-dependence consistent with the involvement of the glucocorticoid receptor (GR). No consistent effect on the low basal transcription rate was observed. This effect of glucocorticoids (GC) on polycyclic aromatic hydrocarbon induction was effectively antagonized at the mRNA and protein level by the GR antagonist RU38486. The response was cycloheximide-sensitive, because the protein synthesis inhibitor caused a GC-dependent superinduction of ALDH3 mRNA levels. This suggests that the effects of GC on this gene are complex and both positive and negative gene regulation is possible. The GC-response was recapitulated in HepG2 cells using transient transfection experiments with CAT reporter constructs containing 3.5 kb of 5'-flanking region from ALDH3. This ligand-dependent response was also observed when a chimeric GR (GR DNA-binding domain and peroxisome proliferator-activated receptor ligand-binding domain) was used in place of GR in the presence of the peroxisome proliferator, nafenopin. A putative palindromic glucocorticoid-responsive element exists between -930 and -910 base pairs relative to the transcription start site. If this element was either deleted or mutated, the negative GC-response was completely lost, which suggests that this sequence is responsible, in part, for the negative regulation of the gene. Electrophoretic mobility shift analysis demonstrated that this palindromic glucocorticoid-responsive element is capable of forming a specific DNA-protein complex with human glucocorticoid receptor. In conclusion, the negative regulation of ALDH3 in rat liver is probably mediated through direct GR binding to its canonical responsive element. (+info)Molecular analysis of two closely related mouse aldehyde dehydrogenase genes: identification of a role for Aldh1, but not Aldh-pb, in the biosynthesis of retinoic acid. (5/1111)
Mammalian class I aldehyde dehydrogenase (ALDH1) has been implicated as a retinal dehydrogenase in the biosynthesis of retinoic acid, a modulator of gene expression and cell differentiation. As the first step towards studying the regulation of ALDH1 and its physiological role in the biosynthesis of retinoic acid, mouse ALDH1 cDNA and genomic clones have been characterized. During the cloning process, an additional closely related gene was also isolated and named Aldh-pb, owing to its high amino acid sequence identity (92%) with the rat phenobarbitol-inducible ALDH protein (ALDH-PB). Aldh1 spans about 45 kb in length, whereas Aldh-pb spans about 35 kb. Both genes are composed of 13 exons, and the positions of all the exon/intron boundaries are conserved with those of human ALDH1. The promoter regions of Aldh1 and Aldh-pb demonstrate high sequence similarity with those of human ALDH1 and rat ALDH-PB. Expression of Aldh1 and Aldh-pb is tissue-specific, with mRNAs for both genes being found in the liver, lung and testis, but not in the heart, spleen or muscle. Expression of Aldh-pb, but not Aldh1, was also detected at high levels in the kidney. Aldh1 and Aldh-pb encode proteins of 501 amino acids with 90% positional identity. To examine the relative roles of these two enzymes in retinoic acid synthesis in vivo, Xenopus embryos were injected with mRNAs encoding these enzymes to assay the effect on conversion of endogenous retinal into retinoic acid. Injection of ALDH1, but not ALDH-PB, mRNA stimulated retinoic acid synthesis in Xenopus embryos at the blastula stage. Thus our results indicate that Aldh1 can function in retinoic acid synthesis under physiological conditions, but that the closely related Aldh-pb does not share this property. (+info)Relationships within the aldehyde dehydrogenase extended family. (6/1111)
One hundred-forty-five full-length aldehyde dehydrogenase-related sequences were aligned to determine relationships within the aldehyde dehydrogenase (ALDH) extended family. The alignment reveals only four invariant residues: two glycines, a phenylalanine involved in NAD binding, and a glutamic acid that coordinates the nicotinamide ribose in certain E-NAD binary complex crystal structures, but which may also serve as a general base for the catalytic reaction. The cysteine that provides the catalytic thiol and its closest neighbor in space, an asparagine residue, are conserved in all ALDHs with demonstrated dehydrogenase activity. Sixteen residues are conserved in at least 95% of the sequences; 12 of these cluster into seven sequence motifs conserved in almost all ALDHs. These motifs cluster around the active site of the enzyme. Phylogenetic analysis of these ALDHs indicates at least 13 ALDH families, most of which have previously been identified but not grouped separately by alignment. ALDHs cluster into two main trunks of the phylogenetic tree. The largest, the "Class 3" trunk, contains mostly substrate-specific ALDH families, as well as the class 3 ALDH family itself. The other trunk, the "Class 1/2" trunk, contains mostly variable substrate ALDH families, including the class 1 and 2 ALDH families. Divergence of the substrate-specific ALDHs occurred earlier than the division between ALDHs with broad substrate specificities. A site on the World Wide Web has also been devoted to this alignment project. (+info)The loss in hydrophobic surface area resulting from a Leu to Val mutation at the N-terminus of the aldehyde dehydrogenase presequence prevents import of the protein into mitochondria. (7/1111)
An apparent conservative mutation, Leu to Val, at the second residue of the rat liver mitochondrial aldehyde dehydrogenase (ALDH) presequence resulted in a precursor protein that was not imported into mitochondria. Additional mutants were made to substitute various amino acids with nonpolar side chains for Leu2. The Ile, Phe, and Trp mutants were imported to an extent similar to that of the native precursor, but the Ala mutant was imported only about one-fourth as well. It was shown that the N-terminal methionine was removed from the L2V mutant in a reaction catalyzed by methionine aminopeptidase. The N-terminal methionine of native pALDH and the other mutant presequences was blocked, presumably by acetylation. Because of the difference in co-translational modification, the L2V mutant sustained a significant loss in the available hydrophobic surface of the presequence. Import competence was restored to the L2V mutant when it was translated using a system that did not remove Met1. The removal of an Arg-Gly-Pro helix linker segment (residues 11-14) from the L2V mutant, which shifted three leucine residues toward the N-terminus, also restored import competence. These results lead to the conclusion that a minimum amount of hydrophobic surface area near the N-termini of mitochondrial presequences is an essential property to determine their ability to be imported. As a result, both electrostatic and hydrophobic components must be considered when trying to understand the interactions between precursor proteins and proteins of the mitochondrial import apparatus. (+info)In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. (8/1111)
The positive charges and structural properties of the mitochondrial leader sequence of aldehyde dehydrogenase have been extensively studied in vitro. The results of these studies showed that increasing the helicity of this leader would compensate for reduced import from positive charge substitutions of arginine with glutamine or the insertion of negative charged residues made in the native leader. In this in vivo study, utilizing the green fluorescent protein (GFP) as a passenger protein, import results showed the opposite effect with respect to helicity, but the results from mutations made within the native leader sequence were consistent between the in vitro and in vivo experiments. Leader mutations that reduced the efficiency of import resulted in a cytosolic accumulation of a truncated GFP chimera that was fluorescent but devoid of a mitochondrial leader. The native leader efficiently imported before GFP could achieve a stable, import-incompetent structure, suggesting that import was coupled with translation. As a test for a co-translational mechanism, a chimera of GFP that contained the native leader of aldehyde dehydrogenase attached at the N terminus and a C-terminal endoplasmic reticulum targeting signal attached to the C terminus of GFP was constructed. This chimera was localized exclusively to mitochondria. The import result with the dual signal chimera provides support for a co-translational mitochondrial import pathway. (+info)"aldehyde dehydrogenase - Homo sapiens". BRENDA. Technische Universität Braunschweig. January 2015. Retrieved 13 April 2015. ... and then aldehyde dehydrogenase (ALDH), which convert it to phenylacetic acid. This means that for significant concentrations ... product which is produced by monoamine oxidase and then further metabolized into β-phenylacetic acid by aldehyde dehydrogenase ... urinary metabolite of phenethylamine and is produced via monoamine oxidase metabolism and subsequent aldehyde dehydrogenase ...
3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... long-chain-3-hydroxyacyl-CoA dehydrogenase activity. • GO:0001948 protein binding. • catalytic activity. • transferase activity ... HADHB, ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ...
acyl-CoA dehydrogenase activity. • identical protein binding. • oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase ... ACADM, acyl-CoA dehydrogenase, C-4 to C-12 straight chain, ACAD1, MCAD, MCADH, acyl-CoA dehydrogenase medium chain. ... "Mitochondrially encoded NADH dehydrogenase 1". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).. *^ Matsubara Y, Kraus ... ACADM (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ...
2cg5: STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL ... "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1-3): 94- ...
The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by ... Aldehyde dehydrogenase 3 family, member B1 also known as ALDH3B1 is an enzyme that in humans is encoded by the ALDH3B1 gene. ... Hsu LC, Chang WC, Yoshida A (Dec 1994). "Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase ... Hsu LC, Chang WC, Yoshida A (Apr 1997). "Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene ...
Aldehyde dehydrogenase 1 family, member A3, also known as ALDH1A3 or retinaldehyde dehydrogenase 3 (RALDH3), is an enzyme that ... Aldehyde dehydrogenase isozymes are thought to play a major role in the detoxification of aldehydes generated by alcohol ... Rexer BN, Zheng WL, Ong DE (2001). "Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase ... Yoshida A, Rzhetsky A, Hsu LC, Chang C (1998). "Human aldehyde dehydrogenase gene family". Eur. J. Biochem. 251 (3): 549-57. ...
DOPAL is detoxified mainly by aldehyde dehydrogenase. "3,4-dihydroxyphenylacetaldehyde - Compound Summary". PubChem Compound. ... Li, W., Spaziano, V.T., Burke, WJ., "Synthesis of a biochemicallly important aldehyde - 3,4-dihydroxyphenylacetaldehyde", Bio- ...
Gama-Castro S.; Núñez C.; Segura D.; Moreno S.; Guzmán J. & Espín G. (2001). "Azotobacter vinelandii Aldehyde Dehydrogenase ... it is also affected by aldehyde dehydrogenase[13] and the response regulator AlgR.[14] ...
NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ ... alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD- ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; ...
Human ALDH1A1 aldehyde dehydrogenase is capable of oxidizing malondialdehyde. Malondialdehyde and other thiobarbituric reactive ... This compound is a reactive aldehyde and is one of the many reactive electrophile species that cause toxic stress in cells and ... The production of this aldehyde is used as a biomarker to measure the level of oxidative stress in an organism. Malondialdehyde ...
Betaine aldehyde is further oxidised in the mitochondria in mice to betaine by the enzyme betaine aldehyde dehydrogenase (EC ... In humans betaine aldehyde activity is performed by a nonspecific cystosolic aldehyde dehydrogenase enzyme (EC 1.2.1.3) TMG is ... "BRENDA - Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase". Brenda-enzymes.org. Retrieved 2016-07-07. Chern, M. K.; ... Pietruszko, R. (1999). "Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, ...
Other studies have suggested that reduced activity by the enzyme aldehyde dehydrogenase may be responsible for a build-up of ... March 1993). "Analysis of corneal aldehyde dehydrogenase patterns in pathologic corneas". Cornea. 12 (2): 146-54. doi:10.1097/ ...
The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies ... ALDH1L1 aldehyde dehydrogenase 1 family, member L1". Human ALDH1L1 genome location and ALDH1L1 gene details page in the UCSC ... 10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene. The protein encoded by this ... Krupenko SA, Oleinik NV (2002). "10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in ...
Aldehyde dehydrogenase family 3 member B2 is an enzyme that in humans is encoded by the ALDH3B2 gene. This gene encodes a ... "Entrez Gene: ALDH3B2 aldehyde dehydrogenase 3 family, member B2". Human ALDH3B2 genome location and ALDH3B2 gene details page ... member of the aldehyde dehydrogenase family, a group of isozymes that may play a major role in the detoxification of aldehydes ... Hsu LC, Chang WC, Yoshida A (Jun 1997). "Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene ...
Aldehyde dehydrogenase 1 family, member A2, also known as ALDH1A2 or retinaldehyde dehydrogenase 2 (RALDH2), is an enzyme that ... "Entrez Gene: ALDH1A2 aldehyde dehydrogenase 1 family, member A2". Duester G (September 2008). "Retinoic Acid Synthesis and ... This protein belongs to the aldehyde dehydrogenase family of proteins. The product of this gene is an enzyme that catalyzes the ... Wang X, Penzes P, Napoli JL (1996). "Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia ...
Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines. Curr Pharm Des. 1999 Aug;5(8):607-25 ...
Dyck, Lillian E.. "Polymorphism of a class 3 aldehyde dehydrogenase present in human saliva and in hair roots."Alcoholism, ... Dyck, Lillian E."Absence of the atypical mitochondrial aldehyde dehydrogenase (ALDH2) isozyme in Saskatchewan Cree Indians." ... "Isoenzymes of aldehyde dehydrogenase in human lymphocytes." Alcoholism, Clinical and Experimental Research. 14:4 (August 1990 ...
... is then oxidized to lactic acid by aldehyde dehydrogenase. Lactaldehyde exists in several forms: in open-chain ... Methylglyoxal is converted to D-lactaldehyde by glycerol dehydrogenase (gldA). ...
This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... Aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1 or retinaldehyde dehydrogenase 1 (RALDH1), is an enzyme that ... 2009). "Aldehyde dehydrogenase 1 is a putative marker for cancer stem cells in head and neck squamous cancer". Biochem. Biophys ... 2009). "Aldehyde dehydrogenase-expressing colon stem cells contribute to tumorigenesis in the transition from colitis to cancer ...
Aldehyde dehydrogenase 8 family, member A1 also known as ALDH8A1 is an enzyme that in humans is encoded by the ALDH8A1 gene. ... This protein belongs to the aldehyde dehydrogenase family of proteins. It plays a role in a pathway of 9-cis-retinoic acid ... Therefore, it is the first known aldehyde dehydrogenase to show a preference for 9-cis-retinal relative to all-trans-retinal. ... "cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ...
Algar EM, Abedinia M, VandeBerg JL, Holmes RS (1991). "Purification and properties of baboon corneal aldehyde dehydrogenase: ... King G, Holmes RS (Sep 1993). "Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic ... PDB: 1K87; Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ (Feb 2003). "Structure of the proline dehydrogenase domain of the ... In the case of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), in addition to the large number of ...
"This protein belongs to the aldehyde dehydrogenase family of proteins. Aldehyde dehydrogenase is the second enzyme of the major ... The enzyme associated with the chemical transformation from acetaldehyde to acetic acid is aldehyde dehydrogenase 2 family ( ... Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic ... The enzyme encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a ...
Mitochondrial aldehyde dehydrogenase belongs to the aldehyde dehydrogenase family of enzymes that catalyze the chemical ... This protein belongs to the aldehyde dehydrogenase family of enzymes. Aldehyde dehydrogenase is the second enzyme of the major ... Aldehyde dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH2 gene located on chromosome 12. ... "Entrez Gene: ALDH2 aldehyde dehydrogenase 2 family (mitochondrial)". Seitz HK, Meier P (2007). "The role of acetaldehyde in ...
Cheung C, Smith CK, Hoog JO, Hotchkiss SA (Jul 1999). "Expression and localization of human alcohol and aldehyde dehydrogenase ... This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members ... "Genetics of human alcohol and aldehyde dehydrogenases". Advances in Human Genetics. 15: 249-90. doi:10.1007/978-1-4615-8356-1_5 ... Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high ...
Alcohol dehydrogenase Aldehyde dehydrogenase GRCh38: Ensembl release 89: ENSG00000196616 - Ensembl, May 2017 "Human PubMed ... There are more genes in the family of alcohol and aldehyde dehydrogenase genes. These genes are now referred to as ADH1A, ADH1C ... "Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai". Human Genetics. 96 (2): 151- ... "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249-90. doi:10.1007/978-1-4615-8356-1_5. PMID ...
... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... Glutaryl-CoA dehydrogenase. *Isovaleryl coenzyme A dehydrogenase. *3-oxo-5beta-steroid 4-dehydrogenase ...
Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought. E A ... In plants, the last step in betaine synthesis is catalyzed by betaine-aldehyde dehydrogenase (BADH, EC 1.2.1.8), a nuclear- ... Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought ... Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought ...
Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes that are ... Abstract:Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes ... Keywords: 4-hydroxy-2-nonenal (4-HNE), Alda-1, aldehyde, ischemia/reperfusion injury, mitochondrial aldehyde dehydrogenase ( ... Keywords:4-hydroxy-2-nonenal (4-HNE), Alda-1, aldehyde, ischemia/reperfusion injury, mitochondrial aldehyde dehydrogenase ( ...
Treatment Fatty aldehyde dehydrogenase deficiency. Symptoms and causes Fatty aldehyde dehydrogenase deficiency Prophylaxis ... Fatty aldehyde dehydrogenase deficiency». *. Fatty aldehyde dehydrogenase deficiency - WrongDiagnosis.com. Fatty aldehyde ... Fatty aldehyde dehydrogenase deficiency definition - Medical .... Fatty aldehyde dehydrogenase deficiency: Also known as the ... Fatty aldehyde dehydrogenase deficiency: Also known as the Sjogren-Larsson syndrome, this is a genetic (inherited) disease ...
T1 - Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ...
title = "Betaine aldehyde dehydrogenase in plants",. abstract = "Plant betaine aldehyde dehydrogenases (BADHs) have been the ... Betaine aldehyde dehydrogenase in plants. Together they form a unique fingerprint. * betaine-aldehyde dehydrogenase ... Fitzgerald, T. L., Waters, D. L. E., & Henry, R. J. (2009). Betaine aldehyde dehydrogenase in plants. Plant Biology, 11(2), 119 ... Fitzgerald, T. L. ; Waters, D. L E ; Henry, R. J. / Betaine aldehyde dehydrogenase in plants. In: Plant Biology. 2009 ; Vol. 11 ...
Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa ... The binding sites of Potassium atom in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From ... Potassium in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa (pdb ...
Aldehyde Dehydrogenase 8. Messenger RNA (mRNA) 9. Hydrogen 10. Urea (Carbamide) Related Therapies and Procedures. 1. Oral ...
keywords = "Aldehyde dehydrogenase, Ichthyosis, Mental retardation, Spasticity",. author = "{De Laurenzi}, Vincenzo and Rogers ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ...
... aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ultimately oxidized to carbon ... Other articles where Aldehyde dehydrogenase is discussed: alcohol consumption: Processing in the liver: …acted upon by another ... acted upon by another enzyme, aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ...
... this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ethanal ... Or ALDH, this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ...
Aldehyde dehydrogenases (EC 1.2.1.3) are a group of enzymes that catalyse the oxidation of aldehydes. Despite the name " ... Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the ... Marchitti, SA; Brocker, C; Stagos, D; Vasiliou, V (Jun 2008). "Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase ... "Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related ...
Aldehyde dehydrogenaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p ... tr,Q7M053,Q7M053_RAT Aldehyde dehydrogenase OS=Rattus norvegicus OX=10116 PE=1 SV=1 BSGZPTAVMYILFHKR Align. Format. Add to ...
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde ... Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme ... ROTHSCHILD HA, BARRON ES (1954). "The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase". J. Biol. Chem. 209 (2 ... Eklund H; El-Ahmad, M; Ramaswamy, S; Hjelmqvist, L; Jörnvall, H; Eklund, H (1998). "Structure of betaine aldehyde dehydrogenase ...
GO:0008802 betaine-aldehyde dehydrogenase activity GO:0016491 oxidoreductase activity GO:0016620 oxidoreductase activity, ... acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor GO:0046872 metal ion binding ...
Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead (IPR000674). Short name: Ald_Oxase/Xan_DH_a/b ... The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [PMID: ... Aldehyde oxidase (EC:1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and ... Xanthine dehydrogenase (EC:1.1.1.204) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and ...
NAD-dependent aldehyde dehydrogenase activity, NAD-linked aldehyde dehydrogenase activity, aldehyde dehydrogenase (NAD+), ... aldehyde dehydrogenase (NAD+), aldehyde:NAD+ oxidoreductase activity, CoA-independent aldehyde dehydrogenase activity, m- ... propionaldehyde dehydrogenase activity, CoA-independent aldehyde dehydrogenase activity, NAD-aldehyde dehydrogenase activity, ... NAD-aldehyde dehydrogenase activity, NAD-dependent 4-hydroxynonenal dehydrogenase activity, NAD-dependent aldehyde ...
aldehyde dehydrogenase X, mitochondrial. Names. ALDH class 2. acetaldehyde dehydrogenase 5. aldehyde dehydrogenase 5. ... ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo sapiens] ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo ... This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... aldehyde dehydrogenase 1 family member B1provided by HGNC. Primary source. HGNC:HGNC:407 See related. Ensembl:ENSG00000137124 ...
Aldehyde dehydrogenase activity promotes survival of human muscle precursor cells.. Jean E1, Laoudj-Chenivesse D, Notarnicola C ... Aldehyde dehydrogenases (ALDH) are a family of enzymes that efficiently detoxify aldehydic products generated by reactive ...
Keywords: Arabidopsis thaliana; Craterostigma plantagineum; abscisic acid; aldehyde dehydrogenase; dehydration; enzyme activity ... Phylogenetically, the Cp- and Ath-ALDH3 and -ALDH4 proteins are closely related to aldehyde dehydrogenases from bacteria and ... Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma ... a gene was isolated with homology to class 3 variable substrate aldehyde dehydrogenases (ALDH). The C. plantagineum gene Cp- ...
Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ...
SEARCH RESULTS for: Acetyl Aldehyde Dehydrogenase Inhibitors [Drug Class] (10 results) * Share : JavaScript needed for Sharing ...
Aldehyde dehydrogenase, mitochondrial. A, B, C, D, E, F, G, H. 500. Homo sapiens. Mutation(s): 1 Gene Names: ALDH2, ALDM. EC: ... T244A mutant of human mitochondrial aldehyde dehydrogenase, NAD complex. *DOI: 10.2210/pdb3N83/pdb ...
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids (PubMed:25286108). Responsible for conversion of the ... Fatty aldehyde dehydrogenaseAdd BLAST. 484. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... aldehyde dehydrogenase (NAD) activity Source: MGI ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the ... Fatty aldehyde dehydrogenase (EC:1.2.1.31 Publication. ,p>Manually curated information for which there is published ...
2011) Aldehyde dehydrogenase: Its role as a cancer stem cell marker comes down to the specific isoform. Cell Cycle 10(9):1378- ... Aldehyde Dehydrogenase 1A3 Activity Is Markedly Elevated in Mes GSCs Compared with Mes Non-GSCs and PN GSCs.. Based on the ... 2009) Aldehyde dehydrogenase 1 is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation ... 2011) Aldehyde dehydrogenase activity of breast cancer stem cells is primarily due to isoform ALDH1A3 and its expression is ...
We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze ... Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?. Jennifer M. Petrosino. ... Petrosino, J.M.; DiSilvestro, D.; Ziouzenkova, O. Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism? Nutrients ... "Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?" Nutrients 6, no. 3: 950-973. ...
ALDHMitochondrial aldehyde dehydrogenaseFALDHBetaineActivityBADHEnzymeALDH1AbstractGeneEnzymesRetinoic acidIsozymesMitochondrial aldehydeToxic aldehydesLipid peroxidationInhibitorFattyMajor aldehyde dehydrogenaseSubstrateAcetaldehyde dehydrogenaseExpression of aldehydeCatalyzes the oxidationReactiveAromaticStem cellSuccinic semialdehyde dehydrogenaseMarkerELISAReactionExogenousEndogenous
- Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes that are responsible for clearance of aldehydes in the body. (eurekaselect.com)
- Among the isoenzymes of ALDH, ALDH2 is believed to play a major role in clearance of toxic aldehydes. (eurekaselect.com)
- After transplantation into β-glucuronidase (GUSB)-deficient NOD/SCID/mucopolysaccharidosis type VII mice, we characterized the distribution of lineage-depleted human umbilical cord blood-derived cells purified by selection using high aldehyde dehydrogenase (ALDH) activity with CD133 coexpression. (elsevier.com)
- Xiu-Ju Luo, Bin Liu, Qi-Lin Ma and Jun Peng, "Mitochondrial Aldehyde Dehydrogenase, A Potential Drug Target for Protection of Heart and Brain from Ischemia/Reperfusion Injury", Current Drug Targets (2014) 15: 948. (eurekaselect.com)
- Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty alcohol oxidation. (nebraska.edu)
- In plants, the last step in betaine synthesis is catalyzed by betaine-aldehyde dehydrogenase (BADH, EC 1.2.1.8), a nuclear-encoded chloroplastic enzyme. (pnas.org)
- Plant betaine aldehyde dehydrogenases (BADHs) have been the target of substantial research, especially during the last 20 years. (edu.au)
- Nolta, Jan A. / Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase activity . (elsevier.com)
- The amino acid sequence deduced from the BADH cDNA sequence showed substantial similarities to those for nonspecific aldehyde dehydrogenases (EC 1.2.1.3 and EC 1.2.1.5) from several sources, including absolute conservation of a decapeptide in the probable active site. (pnas.org)
- acted upon by another enzyme, aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ultimately oxidized to carbon dioxide and water. (britannica.com)
- Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the liver and are metabolized by the body's muscle and heart. (wikipedia.org)
- The active site of the aldehyde dehydrogenase enzyme is largely conserved throughout the different classes of the enzyme and, although the number of amino acids present in a subunit can change, the overall function of the site changes little. (wikipedia.org)
- A magnesium may be used to help the enzyme function, although the amount it helps the enzyme can vary between different classes of aldehydes. (wikipedia.org)
- The overall reaction catalysed by the aldehyde dehydrogenases is: RCHO + NAD+ + H2O → RCOOH + NADH + H+ In this NAD(P)+-dependent reaction, the aldehyde enters the active site through a channel located on the outside of the enzyme. (wikipedia.org)
- In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde + NAD+ + H2O ⇌ {\displaystyle \rightleftharpoons } betaine + NADH + 2 H+ The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, NADH, and H+. (wikipedia.org)
- This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. (wikipedia.org)
- The systematic name of this enzyme class is betaine-aldehyde:NAD+ oxidoreductase. (wikipedia.org)
- The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups. (ebi.ac.uk)
- Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. (nih.gov)
- In plants, the last step in betaine synthesis is catalyzed by betaine-aldehyde dehydrogenase (BADH, EC 1.2.1.8), a nuclear-encoded chloroplastic enzyme. (pnas.org)
- This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP - and NADPH -dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities. (wikidoc.org)
- Low-autocrine RA generation by the cytosolic aldehyde dehydrogenase 1 (Aldh1a1, -a2, and -a3) enzyme family ( 14 ) stimulates adipogenesis via mechanisms dependent on transcription factors ZFP423 and PPARγ ( 15 ). (diabetesjournals.org)
- Another marker with functional significance is aldehyde dehydrogenase (ALDH1), a detoxifying metabolic enzyme often associated with stem and progenitor cell populations ( 8 ). (aacrjournals.org)
- The 3 substrates of this enzyme are betaine aldehyde , NAD + , and H 2 O , whereas its 3 products are betaine , NADH , and H + . (academic.ru)
- Aldehyde dehydrogenase is the next enzyme after alcohol dehydrogenase in the major pathway of alcohol metabolism. (creative-biogene.com)
- Gene expression studies indicate that the RF2C gene, which is strongly expressed in all organs, appears essential, suggesting that the crucial role of the enzyme would certainly be linked to the cell wall formation using aldehydes from phenylpropanoid pathway as substrates. (biochemj.org)
- The kinetic properties of the mitochondrial enzyme, compared with those reported for the cytoplasmic aldehyde dehydrogenase from sheep liver, show significant differences, which may be important in the oxidation of aldehydes in vivo. (biochemj.org)
- There is a deficiency of an enzyme called fatty aldehyde dehydrogenase 10 (FALDH10)in the Sjogren-Larsson syndrome. (drugster.info)
- Betaine aldehyde dehydrogenase (BADH) is an important enzyme which has dual roles in cereals influencing abiotic stress tolerance and rice fragrance. (edu.au)
- The topic of this work is of major importance since we show that invasion and metastasis in IBC are mediated by a cellular subcomponent with stem cell characteristics expressing the stem cell marker aldehyde dehydrogenase 1 (ALDH1). (aacrjournals.org)
- In models of triple-negative breast cancer (TNBC), it has recently been shown that the epidermal growth factor receptor (EGFR) pathway is up-regulated in the aldehyde dehydrogenase 1 (ALDH1)-positive cancer stem cell fraction. (uzh.ch)
- SR-T100 downregulated the expression of stem cell markers, including aldehyde dehydrogenase 1 (ALDH1), Notch1, and FoxM1, and reduced sphere formation in ovarian cancer cells. (jcancer.org)
- The present study is to determine the expression of aldehyde dehydrogenase 1 (ALDH1) and ATPbinding cassette superfamily G member 2 (ABCG2) in patients with triple-negative breast cancer, and to understand the relationship of ALDH1 and ABCG2 with triple-negative breast cancer. (alliedacademies.org)
- The purpose of this study was to compare the expression and the prognostic effect of the breast cancer stem cell marker aldehyde dehydrogenase-1 (ALDH1) in young and elderly breast cancer patients. (biomedcentral.com)
- abstract = "Plant betaine aldehyde dehydrogenases (BADHs) have been the target of substantial research, especially during the last 20 years. (edu.au)
- A gene on chromosome 11q13 that encodes an aldehyde dehydrogenase that plays a major role in detoxifying aldehydes generated by alcohol metabolism and lipid peroxidation. (thefreedictionary.com)
- Gene expression profiling revealed that Aldehyde dehydrogenase 1 family, member A3 (ALDH1A3) is up regulated in OcMMP. (bl.uk)
- The gene products are similar to nonacylating aldehyde dehydrogenases (ThnG) and to proteins representing a complete beta-oxidation pathway (ThnH to ThnP). (sigmaaldrich.com)
- A gene on chromosome 17p11.2 that encodes an aldehyde dehydrogenase that plays a major role in detoxifying alcohol-derived acetaldehyde, metabolising corticosteroids, biogenic amines, neurotransmitters and in lipid peroxidation. (thefreedictionary.com)
- The ALDH3A1 gene product forms a homodimer that preferentially oxidises aromatic and medium-chain (6 carbons or more) saturated and unsaturated aldehyde substrates. (thefreedictionary.com)
- Holmes, R. S., 1977, The genetics of a-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3, Genetics 87:709. (springer.com)
- Holmes, R. S., 1979a, Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse - evidence for a cis-acting regulator gene (Adh-3-t) controlling C 2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adh-3-t on chromosome 3, Biochem. (springer.com)
- The protein encoded by this gene belongs to the aldehyde dehydrogenase family. (creative-biogene.com)
- The ABA2 gene product belongs to the family of short-chain dehydrogenases/reductases, which are known to be NAD- or NADP-dependent oxidoreductases. (plantcell.org)
- This study identified a NADPH-dependent alcohol dehydrogenase gene ZMO1771 from Z. mobilis ZM4, which is responsible for the efficient reduction of furfural and HMF. (biomedcentral.com)
- A genetically modified Z. mobilis by co-expressing alcohol dehydrogenase gene ZMO1771 with transhydrogenase gene udhA showed enhanced conversion rate of furfural and HMF and accelerated ethanol fermentability from lignocellulosic hydrolysate. (biomedcentral.com)
- A cDNA clone of the E3 isozyme of human liver aldehyde dehydrogenase consisting of a 1320-base pair (bp) coding region and a 180-bp non-coding region at the 3′ end was used for chromosomal localization of the E3 gene. (elsevier.com)
- Aldehyde dehydrogenases (EC 1.2.1.3) are a group of enzymes that catalyse the oxidation of aldehydes. (wikipedia.org)
- We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze conversion of retinaldehyde to retinoic acid. (mdpi.com)
- Harvey WK, Lindahl R: Activity of various aldehyde-metabolizing enzymes in chemically-induced rat hepatomas. (springer.com)
- Well, it is very important to know that aldehyde dehydrogenases are also a group of enzymes that catalyse the oxidation or dehydrogenation of aldehydes. (steadyhealth.com)
- We investigated the role of retinoic acid (RA) production by aldehyde dehydrogenase 1 (Aldh1a1, -a2, and -a3), the major RA-producing enzymes on sex-specific fat depot formation. (diabetesjournals.org)
- Aldehyde dehydrogenases (ALDHs) constitute a superfamily of NAD(P) + -dependent enzymes that catalyse irreversible oxidation of aldehydes to the corresponding carboxylic acids. (biochemj.org)
- Here we describe the immobilisation of two biocatalytically relevant co-factor recycling enzymes, glucose dehydrogenase (GDH) and NADH oxidase (NOD) on aldehyde functional ReSynTM polymer microspheres with varying functional group densities. (csir.co.za)
- Both enzymes oxidize a variety of aliphatic and aromatic aldehydes and show strong specificity for nicotinamide adenine dinucleotide (NAD) over nicotinamide adenine dinucleotide phosphate (NADP). (umn.edu)
- Conversely, aldehyde dehydrogenase activation using retinoic acid added to control conjunctival fibroblasts cultures promoted OcMMP-like phenotype in the scarring assays. (bl.uk)
- Finally, the three retinaldehyde dehydrogenases cooperatively mediate retinoic acid signaling during the eye development. (ovid.com)
- A fluorimetric assay of aldehyde dehydrogenase isozymes, based on naphthaldehyde oxidation, is compared with Western Blotting analysis on several clinical samples obtained from surgery. (mdpi.com)
- Holmes, R.S., 1978b, Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: localization of Ahd-1 encoding the mitochondrial isozymes on chromosome 4, Biochem. (springer.com)
- This chapter describes the assay method, purification, and properties of isozymes of aldehyde dehydrogenase. (umn.edu)
- Xiu-Ju Luo, Bin Liu, Qi-Lin Ma and Jun Peng, "Mitochondrial Aldehyde Dehydrogenase, A Potential Drug Target for Protection of Heart and Brain from Ischemia/Reperfusion Injury", Current Drug Targets (2014) 15: 948. (eurekaselect.com)
- It is also important in metabolizing other toxic aldehydes such as 4-hydroxy-2-nonenal (4-HNE) and acrolein [ 2 ]. (hindawi.com)
- In animal myocardial or cerebral ischemia/ reperfusion (I/R) models, accumulation of toxic aldehydes, such as 4-hydroxy-2-nonenal and malondialdehyde, is thought to be an important mechanism for myocardial and cerebral I/R injury. (eurekaselect.com)
- The results presented last week suggest the potential therapeutic applicability of aldehyde traps as a novel approach to treating SSADH Deficiency by sequestering succinic semialdehyde and other toxic aldehydes. (businessinsider.com)
- 4-HNE is an α , β -unsaturated aldehyde formed during lipid peroxidation in vivo [ 17 ]. (hindawi.com)
- Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. (biochemj.org)
- Ogier G, Chantepie J, Quash G, Doutheau A, Gord J, Marion C: The effect of a novel inhibitor of aldehyde dehydrogenase on viral replication. (springer.com)
- Addition of disulfiram, a selective aldehyde dehydrogenase inhibitor restored phenotype and function of OcMMP fibroblasts to control cell levels. (bl.uk)
- Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:2831537). (rcsb.org)
- This fatty aldehyde dehydrogenase deficiency is in fact a genetic disease. (steadyhealth.com)
- Mutagenesis studies have shown that these genes are not essential for growth on tetralin or fatty acids, although a thnG disruption mutant showed threefold less pimelic semialdehyde dehydrogenase activity. (sigmaaldrich.com)
- Restoration of fatty aldehyde dehydrogenase deficiency in Sjögren-Larsson syndrome. (drugster.info)
- There is a single major alcohol dehydrogenase (ADH) and a single major aldehyde dehydrogenase (AldDH) in Aspergillus nidulans . (royalsocietypublishing.org)
- A cysteine and a glutamate will interact with the aldehyde substrate. (wikipedia.org)
- There is no doubt- aldehyde dehydrogenases have broad substrate specificity. (steadyhealth.com)
- Other names in common use include NADP+-acetaldehyde dehydrogenase, NADP+-dependent aldehyde dehydrogenase, and aldehyde dehydrogenase (NADP+). (creative-enzymes.com)
- We recently showed that epithelial cells with the increased expression of aldehyde dehydrogenase in sporadic colon cancer correlate closely with tumor-initiating ability. (aacrjournals.org)
- Expression of Aldehyde Dehydrogenase in Dysplastic Lesions Arising fro" by Adam D. Toll, Bruce M. Boman et al. (jefferson.edu)
- Aldehyde Dehydrogenase, Yeast, CAS 9028-88-0, is a native aldehyde dehydrogenase from yeast that catalyzes the oxidation of acetaldehyde to acetic acid. (merckmillipore.com)
- On the other hand, aldehydes are highly reactive compounds, which can form adducts with proteins, DNA, and lipids, affecting the function of these biomolecules and leading to cell toxicity. (hindawi.com)
- Aldehydes, which are highly reactive molecules, are toxic at high concentrations. (biochemj.org)
- These results strongly suggest that elevated reactive aldehyde concentration, like that observed in the presence of chronic pain, may render cardiomyocytes more susceptible to I/R injury by SIRT1 carbonylative inactivation and impairment the cardioprotection of LKB1-mediated AMPK activation. (onlinejacc.org)
- Preferentially oxidizes aromatic aldehyde substrates (PubMed:2831537). (rcsb.org)
- acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. (creative-enzymes.com)
- One theory is that a certain type of stem cell, aldehyde dehydrogenase bright stem cells, may stimulate the growth of new vessels. (clinicaltrials.gov)
- The protein may also be known as SSADH, SSDH, succinate-semialdehyde dehydrogenase, mitochondrial, and NAD(+)-dependent succinic semialdehyde dehydrogenase. (biocompare.com)
- Aldeyra Therapeutics Presents Evidence for Aldehyde Sequestration as a Potential Therapeutic Approach in Succinic Semialdehyde Dehydrogenase Deficiency at the American Society of Human Genetics. (businessinsider.com)
- Succinic Semialdehyde Dehydrogenase (SSADH) Deficiency is a neurological disease caused by genetic mutations that result in elevated levels of succinic semialdehyde, which are toxic and ultimately result in severe neurological dysfunction, including motor dysfunction, seizures, speech impairment, intellectual disability, and autistic behavior. (businessinsider.com)
- and the potential of ADX-102 as an agent for the treatment of Succinic Semialdehyde Dehydrogenase Deficiency (SSADHD). (businessinsider.com)
- Your search returned 21 aldehyde dehydrogenase 1 family member L1 ELISA ELISA Kit across 3 suppliers. (biocompare.com)
- Oxidation of aldehydes is considered to be generally a detoxification reaction because it is based on removing the electrophilic products of alcohol oxidation. (steadyhealth.com)
- Several researches done in the past have proven that Aldehyde Dehydrogenases are able to oxidize a wide range of endogenous and exogenous aldehydes. (steadyhealth.com)
- Aldeyra Therapeutics, Inc. is a biotechnology company devoted to improving lives by inventing, developing and commercializing products that treat diseases thought to be related to endogenous aldehydes, a naturally occurring class of pro-inflammatory and toxic molecules. (businessinsider.com)