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)

*Glyceraldehyde 3-phosphate dehydrogenase

... in which an aldehyde is converted into a carboxylic acid (ΔG°'=-50 kJ/mol (−12kcal/mol)) and NAD+ is simultaneously reduced ... Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) (EC 1.2.1.12) is an enzyme of ~37kDa ... Wang D, Moothart DR, Lowy DR, Qian X (2013). "The expression of glyceraldehyde-3-phosphate dehydrogenase associated cell cycle ... Piszczatowski RT, Rafferty BJ, Rozado A, Tobak S, Lents NH (August 2014). "The glyceraldehyde 3-phosphate dehydrogenase gene ( ...

*ADH1B

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 ...

*Aldose reductase

The second and last step in the pathway is catalyzed by sorbitol dehydrogenase, which catalyzes the NAD-linked oxidation of ... The reaction mechanism of aldose reductase in the direction of aldehyde reduction follows a sequential ordered path where NADPH ... Jedziniak JA, Yates EM, Kinoshita JH (June 1973). "Lens polyol dehydrogenase". Exp. Eye Res. 16 (2): 95-104. doi:10.1016/0014- ... Grimshaw CE, Shahbaz M, Putney CG (October 1990). "Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by ...

*Alcohol dehydrogenase

... (NAD(P)+) Aldehyde dehydrogenase Oxidoreductase Blood alcohol content for rates of metabolism This ... Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the ... leading to NADH and a zinc bound aldehyde or ketone Release of the product aldehyde. The mechanism in yeast and bacteria is the ... alcohol dehydrogenases. Brewer's yeast also has another alcohol dehydrogenase, ADH2, which evolved out of a duplicate version ...

*Aldehyde dehydrogenase

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 ...

*Betaine-aldehyde dehydrogenase

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 ...

*Aldehyde dehydrogenase (NAD+)

NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, and aldehyde ... Other names in common use include CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, NAD-aldehyde ... In enzymology, an aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) is an enzyme that catalyzes the chemical reaction an aldehyde + ... Racker E (1949). "Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme" (PDF). J. Biol. Chem. 177 (2): 883-892 ...

*Coniferyl-aldehyde dehydrogenase

... a coniferyl-aldehyde dehydrogenase (EC 1.2.1.68) is an enzyme that catalyzes the chemical reaction coniferyl aldehyde + H2O + ... Achterholt S, Priefert H, Steinbuchel A (1998). "Purification and characterization of the coniferyl aldehyde dehydrogenase from ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase. ...

*Aldehyde dehydrogenase (NADP+)

Other names in common use include NADP+-acetaldehyde dehydrogenase, NADP+-dependent aldehyde dehydrogenase, and aldehyde ... In enzymology, an aldehyde dehydrogenase (NADP+) (EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction an aldehyde + ... SEEGMILLER JE (1953). "Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast". J. Biol. Chem. 201 (2): 629-37 ... "Crystallization and properties of NADP-dependent aldehyde dehydrogenase from Gluconobacter melanogenus". Agric. Biol. Chem. 44 ...

*Aryl-aldehyde dehydrogenase

... an aryl-aldehyde dehydrogenase (EC 1.2.1.29) is an enzyme that catalyzes the chemical reaction an aromatic aldehyde + NAD+ + ... aromatic aldehyde dehydrogenase from rabbit liver". Biochim. Biophys. Acta. 118 (2): 285-98. doi:10.1016/s0926-6593(66)80037-1 ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is aryl-aldehyde:NAD+ oxidoreductase. This enzyme participates in tyrosine metabolism ...

*Long-chain-aldehyde dehydrogenase

Fatty aldehyde dehydrogenase (or Long-chain-aldehyde dehydrogenase) is an aldehyde dehydrogenase enzyme that in human is ... Aldehyde dehydrogenase enzymes function to remove toxic aldehydes that are generated by the metabolism of alcohol and by lipid ... long-chain-aldehyde dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... The ALDH3A2 belongs to the aldehyde dehydrogenase superfamily and is a membrane-associated protein typically containing 485 ...

*Aldehyde dehydrogenase (FAD-independent)

... an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O ... Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd. As of late 2007, only one ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Fujishiro K, Aisaka K, Uwajima T (2003). "Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690 ...

*Aldehyde dehydrogenase (pyrroloquinoline-quinone)

In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical ... Patel RN, Hou CT, Derelanko P, Felix A (1980). "Purification and properties of a heme-containing aldehyde dehydrogenase from ... This enzyme is also called aldehyde dehydrogenase (acceptor). This enzyme participates in 4 metabolic pathways: fatty acid ... Ameyama M; Adachi O (1982). "Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound". Methods Enzymol. 89: 491-497. ...

*Aryl-aldehyde dehydrogenase (NADP+)

... an aryl-aldehyde dehydrogenase (NADP+) (EC 1.2.1.30) is an enzyme that catalyzes the chemical reaction an aromatic aldehyde + ... and aryl-aldehyde dehydrogenase (NADP+). Gross GG (1972). "Formation and reduction of intermediate acyladenylate by aryl- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... Gross GG, Zenk MH (1969). "[Reduction of aromatic acids to aldehydes and alcohols in the cell-free system. 1. Purification and ...

*Aldehyde dehydrogenase (NAD(P)+)

In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Other names in common use include aldehyde dehydrogenase [NAD(P)+], and ALDH. This enzyme participates in 5 metabolic pathways ... Black S (1951). "Yeast aldehyde dehydrogenase". Arch. Biochem. Biophys. 34 (1): 86-97. doi:10.1016/S0003-9861(51)80013-4. PMID ... Steinman CR, Jakoby WB (1967). "Yeast aldehyde dehydrogenase. I. Purification and crystallization". J. Biol. Chem. 242 (21): ...

*Aldehyde dehydrogenase 3 family, member A1

"Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. ' ... Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene. Aldehyde ... "Entrez Gene: ALDH3A1 aldehyde dehydrogenase 3 family, memberA1". Estey T, Piatigorsky J, Lassen N, Vasiliou V (January 2007). " ... Dyck LE (1995). "Polymorphism of a class 3 aldehyde dehydrogenase present in human saliva and in hair roots". Alcohol. Clin. ...

*Aldehyde dehydrogenase 18 family, member A1

"Entrez Gene: ALDH18A1 aldehyde dehydrogenase 18 family, member A1". Pérez-Arellano I, Carmona-Álvarez F, Gallego J, Cervera J ( ... This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial ... The gamma-glutamic semi-aldehyde is in tautomeric equilibrium with P5C and it is the obligatory intermediate in the ... in the gamma-glutamyl kinase domain and then the gamma-glutamyl phosphate is the made into gamma-glutamic semi-aldehyde in the ...

*Aldehyde dehydrogenase 6 family, member A1

"CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA ... "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA ... "Entrez Gene: ALDH6A1 aldehyde dehydrogenase 6 family, member A1". Marcadier JL, Smith AM, Pohl D, Schwartzentruber J, Al- ... This protein belongs to the aldehyde dehydrogenases family of proteins. This enzyme plays a role in the valine and pyrimidine ...

*Aldehyde dehydrogenase 4 family, member A1

"Entrez Gene: ALDH4A1 aldehyde dehydrogenase 4 family, member A1". Human ALDH4A1 genome location and ALDH4A1 gene details page ... This protein belongs to the aldehyde dehydrogenase family of proteins. This enzyme is a mitochondrial matrix NAD-dependent ... Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH4A1 gene. ... 1998). "Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia". Hum. Mol. Genet. 7 ( ...

*Aldehyde dehydrogenase 9 family, member A1

"Entrez Gene: ALDH9A1 aldehyde dehydrogenase 9 family, member A1". Human ALDH9A1 genome location and ALDH9A1 gene details page ... 1994). "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4- ... This protein belongs to the aldehyde dehydrogenase family of proteins. It has a high activity for oxidation of gamma- ... Kurys G, Ambroziak W, Pietruszko R (1989). "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme ...

*Aldehyde dehydrogenase 5 family, member A1

"Entrez Gene: ALDH5A1 aldehyde dehydrogenase 5 family, member A1 (succinate-semialdehyde dehydrogenase)". Human ALDH5A1 genome ... "A functional polymorphism in the succinate-semialdehyde dehydrogenase (aldehyde dehydrogenase 5 family, member A1) gene is ... This protein belongs to the aldehyde dehydrogenase family of proteins. This gene encodes a mitochondrial NAD+-dependent ... Succinate-semialdehyde dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH5A1 gene. ...

*Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain

The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain. Aldehyde ... Xanthine dehydrogenase (EC 1.1.1.204) catalyzes the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and ... Dobbek H, Gremer L, Meyer O, Huber R (August 1999). "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur ... The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through ...

*Phenethylamine

"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 ...

*ALDH3B1

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 ...

*ALDH1A3

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. ...

*Molybdopterin

... carbon monoxide dehydrogenase, aldehyde oxidase. Prosthetic group of: formate dehydrogenase, purine hydroxylase, thiosulfate ... Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. The first tungsten-requiring enzyme to be ... Although a tungsten-containing xanthine dehydrogenase from bacteria has been found to contain tungsten-molydopterin and also ... Schräder T, Rienhöfer A, Andreesen JR (September 1999). "Selenium-containing xanthine dehydrogenase from Eubacterium barkeri". ...

*Acetaldehyde dehydrogenase

Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A (Jun 1985). "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2". ... Xiao Q, Weiner H, Crabb DW (Nov 1996). "The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for ... Hempel J, von Bahr-Lindström H, Jörnvall H (May 1984). "Aldehyde dehydrogenase from human liver. Primary structure of the ... Crabb D, Xiao Q (Jun 1998). "Studies on the enzymology of aldehyde dehydrogenase-2 in genetically modified HeLa cells". ...
Preparations of sheep liver cytoplasmic aldehyde dehydrogenase obtained by published methods were found by analytical isoelectric focusing in the pH range 5-8 to contain 5-10% by weight of the mitochondrial aldehyde dehydrogenase. Under the conditions used the pI of the cytoplasmic enzyme is 6.2 and that of the mitochondrial enzyme 6.6. The mitochondrial enzyme can be removed from the preparation by selective precipitation of the cytoplasmic enzyme with (NH4)2SO4. Kinetic experiments and inhibition experiments with disulfiram show that the properties of the two sheep liver enzymes are so different that the presence of 10% mitochondrial enzyme in preparations of the cytoplasmic enzyme can introduce serious errors into results. Our results suggest that the presence of 10 microM-disulfiram in assays may completely inactivate the pure cytoplasmic enzyme. This result is in contrast with a previous report [kitson (1978) Biochem. U. 175, 83-90]. ...
TY - JOUR. T1 - Order and disorder in mitochondrial aldehyde dehydrogenase. AU - Hurley, Thomas. AU - Perez-Miller, Samantha. AU - Breen, Heather. PY - 2001/1/30. Y1 - 2001/1/30. N2 - One of the most notable and currently unexplained features of the mitochondrial form of aldehyde dehydrogenase is its property of half-of-the-sites reactivity. An appropriate description of this phenomenon can be to consider this as the extreme example of negative cooperativity. This implies, therefore, that a pathway of communication must exist between active sites in order to convey the structural consequences of ligand binding. Data from four different structures of human ALDH2 collected during the past 2 years may shed some light on one possible pathway for the propagation of structural information. We recently published a 2.6 Å structure of a binary complex between ALDH2 and NAD+ in which the predominant conformation of the cofactor differed between different subunits in the structure. We now have three ...
Goat anti Human aldehyde dehydrogenase 1 antibody recognizes aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1. Goat anti
ALDH2.2; aldehyde dehydrogenase 2 family (mitochondrial), tandem duplicate 2; aldh2; cb154; aldh2b; aldh2l; zgc:85659; wu:fi26c02; aldehyde dehydrogenase 2b; aldehyde dehydrogenase 2.2; aldehyde dehydrogenase 2, like; aldehyde dehydrogenase 2, tandem dupl ...
Kinetic studies were carried out on mitochondrial aldehyde dehydrogenase (EC 1.2.1.3) isolated from sheep liver. Steady-state studies over a wide range of acetaldehyde concentrations gave a non-linear double-reciprocal plot. The dissociation of NADH from the enzyme was a biphasic process with decay constants 0.6s-1 and 0.09s-1. Pre-steady-state kinetic data with propionaldehyde as substrate could be fitted by using the same burst rate constant (12 +/- 3s-1) over a wide range of propionaldehyde concentrations. The quenching of protein fluorescence on the binding of NAD+ to the enzyme was used to estimate apparent rate constants for binding (2 × 10(4) litre.mol-1.s-1) and dissociation (4s-1). 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. ...
Aldehyde dehydrogenases (ALDHs) represent a group of enzymes that detoxify aldehydes by facilitating their oxidation to carboxylic acids, and have been shown to play roles in plant response to abiotic stresses. However, the comprehensive analysis of ALDH superfamily in soybean (Glycine max) has been limited. In present study, a total of 53 GmALDHs were identified in soybean, and grouped into 10 ALDH families according to the ALDH Gene Nomenclature Committee and phylogenetic analysis. These groupings were supported by their gene structures and conserved motifs. Soybean ALDH superfamily expanded mainly by whole genome duplication/segmental duplications. Gene network analysis identified 1146 putative co-functional genes of 51 GmALDHs. Gene Ontology (GO) enrichment analysis suggested the co-functional genes of these 51 GmALDHs were enriched (FDR < 1e-3) in the process of lipid metabolism, photosynthesis, proline catabolism, and small molecule catabolism. In addition, 22 co-functional genes of GmALDHs are
The precise phenotype and biology of acute myeloid leukemia stem cells remain controversial, in part because the "gold standard" immunodeficient mouse engraftment assay fails in a significant fraction of patients and identifies multiple cell-types in others. We sought to analyze the clinical utility of a novel assay for putative leukemia stem cells in a large prospective cohort. The leukemic clones most primitive hematopoietic cellular phenotype was prospectively identified in 109 newly-diagnosed acute myeloid leukemia patients, and correlated with clinical risk groups and outcomes. Most (80/109) patients harbored CD34+CD38- leukemia cells. The CD34+CD38- leukemia cells in 47 of the 80 patients displayed intermediate aldehyde dehydrogenase expression, while normal CD34+CD38- hematopoietic stem cells expressed high levels of aldehyde dehydrogenase. In the other 33/80 patients, the CD34+CD38- leukemia cells exhibited high aldehyde dehydrogenase activity, and most (28/33, 85%) harbored poor-risk ...
2ONP: Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487.
Heavy alcohol drinking is a risk factor of colorectal cancer (CRC), but little is known on the effect of polymorphisms in the alcohol-metabolizing enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) on the alcohol-related risk of C
Exogenous aldehydes can cause pain in animal models, suggesting that aldehyde dehydrogenase-2 (ALDH2), which metabolizes many aldehydes, may regulate nociception. To test this hypothesis, we generated a knock-in mouse with an inactivating point mutation in ALDH2 (ALDH2*2), which is also present in human ALDH2 of ~540 million East Asians. The ALDH2*1/*2 heterozygotic mice exhibited a larger response to painful stimuli than their wild-type littermates, and this heightened nociception was inhibited by an ALDH2-selective activator (Alda-1). No effect on inflammation per se was observed. Using a rat model, we then showed that nociception tightly correlated with ALDH activity (R2 = 0.90) and that reduced nociception was associated with less early growth response protein 1 (EGR1) in the spinal cord and less reactive aldehyde accumulation at the insult site (including acetaldehyde and 4-hydroxynonenal). Further, acetaldehyde- and formalin-induced nociceptive behavior was greater in the ALDH2*1/*2 mice ...
The purpose of this comprehensive meta-analysis was to assess the association of aldehyde dehydrogenase (ALDH) expression with overall survival (OS) and disease-free survival (DFS)/progression-free survival (PFS) in ovarian cancer patients. Systematic searches of Pubmed databases was performed to identify relevant literature published before February 28, 2018. A total of 14 studies (13 articles) with 2210 ovarian cancer patients were pooled. All included studies were performed by using Immunohistochemistry (IHC) for detection of ALDH expression. Hazard ratio (HR) and 95% confidence interval (CI) were extracted from included studies to evaluate the correlation of ALDH expression with OS and DFS/PFS. High expression of ALDH was associated with worse OS (HR: 1.43; 95% CI: 1.18-1.73) and poor DFS/PFS (HR: 1.55, 95% CI: 1.12-2.14). No evidence of publication bias was observed in OS (Beggs test, P = 0.113; Eggers test, P = 0.355) and DFS/PFS (Beggs test, P = 0.655; Eggers test, P = 0.189) in ovarian
Melanoma is one of the most aggressive types of human cancer, characterized by enhanced heterogeneity and resistance to conventional therapy at advanced stages. We and others have previously shown that HEDGEHOG-GLI (HH-GLI) signaling is required for melanoma growth and for survival and expansion of melanoma-initiating cells (MICs). Recent reports indicate that HH-GLI signaling regulates a set of genes typically expressed in embryonic stem cells, including SOX2 (sex-determining region Y (SRY)-Box2). Here we address the function of SOX2 in human melanomas and MICs and its interaction with HH-GLI signaling. We find that SOX2 is highly expressed in melanoma stem cells. Knockdown of SOX2 sharply decreases self-renewal in melanoma spheres and in putative melanoma stem cells with high aldehyde dehydrogenase activity (ALDH(high)). Conversely, ectopic expression of SOX2 in melanoma cells enhances their self-renewal in vitro. SOX2 silencing also inhibits cell growth and induces apoptosis in melanoma ...
Cardiovascular disease (CVD) remains a leading cause of premature death worldwide. Despite advances in treatment of ischemic diseases including myocardial infarction and peripheral arterial disease (PAD) there remains a need for effective revascularization therapies. Although early cell therapy trials investigated use of MNC from autologous bone marrow, emerging evidence indicates that purified progenitor cell populations are required to induce optimal vascular regeneration. In addition, autologous cells show reduced efficacy due to CVD-related progenitor dysfunction. This thesis presents preclinical studies characterizing several blood-derived cell types for the development of cellular therapies to treat PAD, focusing on the use of allogeneic umbilical cord blood (UCB) hematopoietic progenitor cells (HPC) and bone marrow multipotent stromal cells (MSC). First, I demonstrated that human UCB cells prospectively purified based on high aldehyde dehydrogenase activity (ALDHhi), promote the recovery of
Aldehyde dehydrogenase (ALDH) activity is commonly used as a marker to identify cancer stem-like cells. The three ALDH1A isoforms have all been individually implicated in cancer stem-like cells and in chemoresistance; however, which isoform is preferentially expressed varies between cell lines. We sought to explore the structural determinants of ALDH1A isoform selectivity in a series of small-molecule inhibitors in support of research into the role of ALDH1A in cancer stem cells. An SAR campaign guided by a cocrystal structure of the HTS hit CM39 (7) with ALDH1A1 afforded first-in-class inhibitors of the ALDH1A subfamily with excellent selectivity over the homologous ALDH2 isoform. We also discovered the first reported modestly selective single isoform 1A2 and 1A3 inhibitors. Two compounds, 13g and 13h, depleted the CD133+ putative cancer stem cell pool, synergized with cisplatin, and achieved efficacious concentrations in vivo following IP administration. Compound 13h additionally synergized ...
1EZ0: Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.
Background: Inherited human aldehyde dehydrogenase 2 (ALDH-2) deficiency reduces the risk for alcoholism. Kudzu plants and extracts have been used for 1,000 years in traditional Chinese medicine to treat alcoholism. Kudzu contains daidzin, which inhibits ALDH-2 and suppresses heavy drinking in rodents. Decreased drinking due to ALDH-2 inhibition is attributed to aversive properties of acetaldehyde accumulated during alcohol consumption. However, daidzin can reduce drinking in some rodents without necessarily increasing acetaldehyde. Therefore, a selective ALDH-2 inhibitor might affect other metabolic factors involved in regulating drinking.. Methods: Aldehyde dehydrogenase 2 inhibitors were synthesized based on the co-crystal structure of ALDH-2 and daidzin. We tested the efficacy of a highly selective reversible ALDH-2 inhibitor, CVT-10216, in models of moderate and high alcohol drinking rats. We studied 2-bottle choice and deprivation-induced drinking paradigms in Fawn Hooded (FH) rats, ...
Aldehyde dehydrogenases (ALDH, EC 1.2.1.3) are a group of enzymes that catalyze the oxidation (dehydrogenation) of aldehydes to carboxylic acids, an action also performed by xanthine oxidase (XO) and aldehyde oxidase (AO).. The aldehyde cinnamaldehyde commonly used as a food flavoring is rapidly oxidized by aldehyde dehydrogenases into the carboxylic acid cinnamic acid.. ...
Oxidizes medium and long chain saturated and unsaturated aldehydes (PubMed:17382292, PubMed:23721920). Metabolizes also benzaldehyde (PubMed:17382292). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (PubMed:17382292). May have a protective role against the cytotoxicity induced by lipid peroxidation (PubMed:17382292).
ALDH activity measured fluorimetrically using a high concentration of aliphatic aldehyde as substrate was studied in human glioblastomas grafted in nude mice. Compared with normal brain, ALDH...
TY - JOUR. T1 - Characterization of the molecular mechanisms underlying increased ischemic damage in the aldehyde dehydrogenase 2 genetic polymorphism using a human induced pluripotent stem cell model system. AU - Ebert, Antje D.. AU - Kodo, Kazuki. AU - Liang, Ping. AU - Wu, Haodi. AU - Huber, Bruno C.. AU - Riegler, Johannes. AU - Churko, Jared. AU - Lee, Jaecheol. AU - De Almeida, Patricia. AU - Lan, Feng. AU - Diecke, Sebastian. AU - Burridge, Paul W.. AU - Gold, Joseph D.. AU - Mochly-Rosen, Daria. AU - Wu, Joseph C.. PY - 2014/9/24. Y1 - 2014/9/24. N2 - Nearly 8% of the human population carries an inactivating point mutation in the gene that encodes the cardioprotective enzyme aldehyde dehydrogenase 2 (ALDH2). This genetic polymorphism (ALDH2∗2) is linked to more severe outcomes from ischemic heart damage and an increased risk of coronary artery disease (CAD), but the underlying molecular bases are unknown. We investigated the ALDH2∗2 mechanisms in a human model system of induced ...
15 min with 200 ml of 50 mM NH4HCO3 at RT. A volume of 200 ml of 100 acetonitrile was added to this solution and incubated for 15 min at room temperature. Solvent was removed and gel plugs were allowed to dry for 30 min at RT under a flow hood. Plugs were rehydrated with 20 ng/ml of modified trypsin (Promega, Madison, WI, USA) in 50 mM NH4HCO3 in a shaking incubator overnight at 37uC. Enough trypsin solution was added in order to completely submerge the gel plugs.sample was acquired for a total of ,2.5 min. MS/MS spectra were searched against the International Protein Index (IPI) database using SEQUEST with the following parameters: two trypsin miscleavages, fixed carbamidomethyl modification, variable methionine oxidation, parent tolerance 10 ppm, and fragment tolerance of 25 mmu or 0.01 Da. Results were filtered with the following criteria: Xcorr1.5, 2.0, 2.5, 3.0 for 1, 2, 3, and 4 charge states, respectively, Delta CN0.1, and P-value (protein and peptide) 0.01. IPI accession numbers were ...
Evaluation of aldehyde dehydrogenase 1 and transcription factors in both primary breast cancer and axillary lymph node metastases as a prognostic factorEvaluation of aldehyde dehydrogenase 1 and transcription factors in both primary breast cancer and axillary lymph node metastases as a prognostic factor ...
Conditioned medium (CM) from clonal sub-populations of the pancreatic cancer cell line, MiaPaCa-2 with differing invasive abilities, were examined for their effect on in vitro invasion. Conditioned medium from Clone #3 (CM#3) strongly promoted invasion, while CM from Clone #8 (CM#8) inhibited invasion in vitro. 2D DIGE followed by MALDI-TOF MS analysis of CM#3 and CM#8 identified 41 proteins which were differentially regulated; 27 proteins were down-regulated and 14 proteins up-regulated in the invasion-promoting CM#3 when compared to CM#8. Western blotting analysis confirmed the down-regulated expression of gelsolin and the up-regulation of aldehyde dehydrogenase 1A1 in CM#3. Down-regulation of aldehyde dehydrogenase 1A1 in Clone #3 CM and gelsolin levels in Clone #8 CM by siRNA transfection revealed an important involvement of these proteins in promoting and inhibiting invasion in these pancreatic cancer cell lines. ...
TY - JOUR. T1 - Metabolic remodeling induced by mitochondrial aldehyde stress stimulates tolerance to oxidative stress in the heart. AU - Endo, Jin. AU - Sano, Motoaki. AU - Katayama, Takaharu. AU - Hishiki, Takako. AU - Shinmura, Ken. AU - Morizane, Shintaro. AU - Matsuhashi, Tomohiro. AU - Katsumata, Yoshinori. AU - Zhang, Yan. AU - Ito, Hideyuki. AU - Nagahata, Yoshiko. AU - Marchitti, Satori. AU - Nishimaki, Kiyomi. AU - Wolf, Alexander Martin. AU - Nakanishi, Hiroki. AU - Hattori, Fumiyuki. AU - Vasiliou, Vasilis. AU - Adachi, Takeshi. AU - Ohsawa, Ikuroh. AU - Taguchi, Ryo. AU - Hirabayashi, Yoshio. AU - Ohta, Shigeo. AU - Suematsu, Makoto. AU - Ogawa, Satoshi. AU - Fukuda, Keiichi. PY - 2009/11. Y1 - 2009/11. N2 - RATIONALE:: Aldehyde accumulation is regarded as a pathognomonic feature of oxidative stress-associated cardiovascular disease. OBJECTIVE:: We investigated how the heart compensates for the accelerated accumulation of aldehydes. METHODS AND RESULTS:: Aldehyde dehydrogenase 2 ...
Semantic Scholar extracted view of Aldehyde dehydrogenase activity and level of dopamine in certain sections of the brain of rats preferring and refusing ethanol by Kharchenko Nk
Application of stem cell biology to breast cancer research has been limited by the lack of simple methods for identification and isolation of normal and malignant stem cells. Utilizing in vitro and in vivo experimental systems, we show that normal and cancer human mammary epithelial cells with increased aldehyde dehydrogenase activity (ALDH) have stem/progenitor properties. These cells contain the subpopulation of normal breast epithelium with the broadest lineage differentiation potential and greatest growth capacity in a xenotransplant model. In breast carcinomas, high ALDH activity identifies the tumorigenic cell fraction, capable of self-renewal and of generating tumors that recapitulate the heterogeneity of the parental tumor. In a series of 577 breast carcinomas, expression of ALDH1 detected by immunostaining correlated with poor prognosis. These findings offer an important new tool for the study of normal and malignant breast stem cells and facilitate the clinical application of stem cell ...
Hematopoiesis is sustained throughout adult life by balanced self-renewal and differentiation divisions of multipotent cells. The restriction of these cells to specific lineages takes place in an orderly sequence that spans several cell generations, thus creating hierarchies of daughter cells with distinct properties. Hematopoietic stem cells (HSC) represent the cells that head up this hierarchy and are thus able to regenerate and sustain the long term production of all blood cell types when transplanted at low numbers into suitable hosts. Quantification of HSC is achieved by coupling the end-points of donor-derived lymphoid and myeloid cell output to long term limiting dilution transplantation assays.1 In mice, phenotypically distinct cells with different repopulating activities in vivo have been described.2-7 Some short-term repopulating cells (STRC) lack the extensive self-renewal ability of HSC but retain a broad lympho-myeloid differentiation repertoire. Others also show partial restriction ...
The root cause is a genetic predisposition to acetaldehyde build-up that is most commonly observed in people of Asian decent, hence it being colloquially termed "Asian flush" despite it not being exclusive to Asians.. Acetaldehyde is a toxic by-product of alcohol metabolism that is usually broken down by enzymes in our body in order to stop it from accumulating and causing a toxic reaction - i.e. the various symptoms of Asian flush. All that is required is one of more specific gene variants to be present for acetaldehyde build-up to occur.. One gene variant, observable in approximately 50% of Asian people, is called the mitochondrial ALDH2 allele, which results in a deficient aldehyde dehydrogenase enzyme that works at about 10% of its usual capacity. This enzyme is normally responsible for preventing acetaldehyde build up by catalyzing its conversion into non-toxic acetic acid.. In addition to this, and contrary to common belief, a study confirmed that 80% of Asians and nearly all Japanese, ...
Rabbit monoclonal antibody raised against recombinant human ALDH1A1. Recombinant protein corresponding to human ALDH1A1. (MAB21821) - Products - Abnova
Aldehyde dehydrogenases in rat brain: subcellular distribution, properties and involvement in acetaldehyde and dopamine metabolism ...
Aldehyde dehydrogenase 10山羊多克隆抗体(ab103902)可与小鼠, 大鼠样本反应并经WB实验严格验证。所有产品均提供质保服务,中国75%以上现货。
ALDH2 - ALDH2 (untagged)-Human aldehyde dehydrogenase 2 family (mitochondrial) (ALDH2), nuclear gene encoding mitochondrial protein, transcript variant 1 available for purchase from OriGene - Your Gene Company.
ALDH1A2 - ALDH1A2 (untagged)-Human aldehyde dehydrogenase 1 family, member A2 (ALDH1A2), transcript variant 2 available for purchase from OriGene - Your Gene Company.
Aldehyde dehydrogenases (ALDHs) are important enzymes that eliminate toxic aldehydes by catalysing their oxidation to non-reactive acids. It is reported that a deficiency in the ALDH2 is associated with the alcohol flush reaction. More than 40% of the East Asians population carries a common ALDH2 mutant allele, which results in a dramatic reduction in the enzymatic activity when compared with the wild-type allele ...
In this review, we summarize recent advances in understanding vitamin A-dependent regulation of sex-specific differences in metabolic diseases, inflammation, and certain cancers. We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze conversion of retinaldehyde to retinoic acid. Additionally, we propose a
J:63682 Vaz FM, et al., Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4 ...
Some flower cytoplasms express novel mitochondrial genes that cause male sterility. encodes a soluble protein that accumulates in the mitochondrial matrix. Three independent lines of evidence establish that the RF2 protein is an aldehyde dehydrogenase (ALDH). The finding that T cytoplasm plants that are homozygous for the allele are male sterile but accumulate normal amounts of RF2 protein that lacks normal mitochondrial (mt) ALDH activity provides strong evidence that gene also is required for anther development in normal cytoplasm maize. Hence it appears that the gene was recruited recently to function as a nuclear restorer. ALDHs typically have very broad substrate specificities. Indeed the RF2 protein is capable of oxidizing at least three aldehydes. Hence the specific metabolic pathway(s) within which the and gene in restoration relates to its ability to modify the expression of gene was cloned via transposon tagging (Cui et al. 1996 The gene is equivalent to ALDH2B1. Only a few studies of ...
Purpose: Lung cancer stem cells (CSC) with elevated aldehyde dehydrogenase (ALDH) activity are self-renewing, clonogenic, and tumorigenic. The purpose of our study is to elucidate the mechanisms by which lung CSCs are regulated.. Experimental Design: A genome-wide gene expression analysis was performed to identify genes differentially expressed in the ALDH+ versus ALDH− cells. RT-PCR, Western blot analysis, and Aldefluor assay were used to validate identified genes. To explore the function in CSCs, we manipulated their expression followed by colony and tumor formation assays.. Results: We identified a subset of genes that were differentially expressed in common in ALDH+ cells, among which ALDH1A3 was the most upregulated gene in ALDH+ versus ALDH− cells. shRNA-mediated knockdown of ALDH1A3 in non-small cell lung cancer (NSCLC) resulted in a dramatic reduction in ALDH activity, clonogenicity, and tumorigenicity, indicating that ALDH1A3 is required for tumorigenic properties. In contrast, ...
Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487 ...
Marc Weiner is Associate Research Professor at the Edward J. Bloustein School of Planning and Public Policy at Rutgers University. His research interests include quantitative and qualitative research methodologies; survey research planning, design, operations, data analysis; quantitative data modeling; his teaching interests include demography and population studies; and social movements and power relations. Weiner currently serves as the Bloustein Schools Director of Program Assessment and Conflict of Interest Monitor; previously, he served as Associate Director of the Bloustein Center for Survey Research, as well as Project Director for the Office of Population Research, and Assistant Director for the Survey Research Center, both at Princeton University. Weiner was the founding President of the New Jersey-Pennsylvania Chapter of the American Association for Public Opinion Research and served on the Executive Council of the Association of Academic Survey Research Organizations.. Weiner ...
Abstract : Tumour microenvironment determines the fate of treatments. Reconstitution of tumour conditions is mandatory for alternative in vitro methods devoted to cancer development and the selection of therapeutic strategies. This work describes a 3D model of melanoma growth in its environment. Introducing means to mimic tumour angiogenesis, which turns on tumour progression, the model shows that melanoma tumour spheroids allow reconstitution of solid tumours with stromal cells. Angiogenesis evidenced the differential recruitment of endothelial cells (EC) from early progenitors (EEPCs) to mature ECs. Hypoxia was the key parameter that selected and stabilized melanoma cancer stem like cells (CSCs) phenotype based on aldehyde dehydrogenase expression as the best criterion. The 3D-tumour-model demonstrated the distinct reactivity of ECs toward tumour cells in terms of cellular cross-talk and humoral response. Intra-spheroid cell-to-cell membrane dye exchanges, mediated by intercellular ...
The class-3 aldehyde dehydrogenase that is overexpressed (,100-fold) in human breast adenocarcinoma MCF-7/0 cells made resistant (,30-fold as judged by LC90s) to oxazaphosphorines, such as mafosfamide, by growing them in the presence of polycyclic aromatic hydrocarbons, e.g., methylcholanthrene (3 µm for 5 days), was isolated and characterized. Its physical and catalytic properties were identical to those of the prototypical human stomach mucosa cytosolic class-3 aldehyde dehydrogenase, type-1 ALDH-3, except that it catalyzed, though not very rapidly, the oxidation of aldophosphamide, whereas the stomach mucosa enzyme essentially did not; hence, it was judged to be a slight variant of the prototypical enzyme. Carcinogens that are not ligands for the Ah receptor, barbiturates known to induce hepatic cytochrome P450s, steroid hormones, an antiestrogen, and oxazaphosphorines did not induce the enzyme or the largely oxazaphosphorine-specific acquired resistance. Whereas methylcholanthrene induced ...
Our results suggest that the recombinant strain E. coli 029A functionally express our biobrick BBa_K398029. From the statistical analysis that we performed we concluded that the expression of the biobrick BBa_K398006 under the promoter-rbs combination BBa_J23100-BBa_J61117 increases the dodecanal dehydrogenase activity in E. coli cell extracts 2-fold. Moreover, the enzymatic activities measured for the construct BBa_K398029 were equivalent to 33.98% of the Pseudomonas putida aldehyde dehydrogenase activity. Read more about it in our results page View BBa_K398029 in the parts registry Specified Components ...
Mouse monoclonal antibody raised against recombinant ALDH1A1. Recombinant protein corresponding to human ALDH1A1. (MAB10443) - Products - Abnova
摘要 旨在研究氨基酸平衡低蛋白质日粮对育肥猪肠道抗菌肽与微生物区系的影响。将20头(60±2.5)kg的育肥猪(杜×长×大)随机分为4个处理:14.0% CP日粮(14.0% CP),添加Glu、Lys、Met、Thr和Trp的12.5% CP日粮(12.5% CP),添加Glu、Lys、Met、Thr和Trp的11.0% CP日粮(11.0% CP),添加Glu、Lys、Met、Thr、Trp和BCAA(Val、Ile、Leu)的11.0% CP日粮(11.0% CP+BCAA)。每个处理5个重复,每个重复1头猪。试验分为5 d预试期和30 d正试期。结果表明:(1)尿液尿素氮和尿酸含量随日粮蛋白质水平降低而显著降低(P,0.05);(2)低蛋白质水平日粮显著降低空肠黏膜、回肠黏膜β-defensin-2水平和ANG1、ANG4 mRNA表达水平(P,0.05);(3)不同蛋白质水平日粮对部分回肠、直肠食糜微生物氨基酸组成有显著影响(P,0.05);(4)与14.0% CP组相比,12.5% CP组Observed species显著提高(P,0.05),11.0% ...
Or ALDH, this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ethanal the breakdown prod...
Sigma-Aldrich offers abstracts and full-text articles by [Kwok Ki Ho, Abhijit Mukhopadhyay, Yi Feng Li, Soma Mukhopadhyay, Henry Weiner].
View mouse Aldh7a1 Chr18:56509687-56572951 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
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Here, we show that SOX11, an embryonic mammary marker that is normally silent in postnatal breast cells, is expressed in many oestrogen receptor-negative preinvasive ductal carcinoma in situ (DCIS) lesions. Mature mammary epithelial cells engineered to express SOX11 showed alterations in progenitor cell populations, including an expanded basal-like population with increased aldehyde dehydrogenase (ALDH) activity, and increased mammosphere-forming capacity. DCIS.com cells engineered to express SOX11 showed increased ALDH activity, which is a feature of cancer stem cells. The CD44+/CD24-/ALDH+ cell population was increased in DCIS.com cells that expressed SOX11. Upregulating SOX11 expression in DCIS.com cells led to increased invasive growth both in vitro and when they were injected intraductally in a mouse model of DCIS that recapitulates human disease. Invasive lesions formed sooner and tumour growth was augmented in vivo, suggesting that SOX11 contributes to the progression of DCIS to invasive ...
ptr:464931 K00128 aldehyde dehydrogenase (NAD+) [EC:1.2.1.3] , (RefSeq) ALDH1B1; aldehyde dehydrogenase 1 family member B1 (A) MLRFLAPRLLSLQGRTARYSSVAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNRLADLVERDRVYLA SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKCHGKTIPMDGQHFCFTRHEPVGVCG QIIPWNFPLVMQGWKLAPALATGSTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP VQPLFKFKKIEEVIERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS ...
Although this isnt so popular medical subject- it is certain that everyone has at least heard about some of the many enzyme found in our body.
Rep. Anthony Weiner (D-NY) doled out his first apologies to his wife and his constituents, but also apologized to the media and to Andrew Breitbart specifically during a long and rambling press conference in which he seemed determined to answer every last reporters question. Breitbart had demanded an apology a few minutes before from the same podium, where he climbed after Weiner did not show up on time to his own press conference.
Complete information for ALDH2 gene (Protein Coding), Aldehyde Dehydrogenase 2 Family (Mitochondrial), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for ALDH2 gene (Protein Coding), Aldehyde Dehydrogenase 2 Family (Mitochondrial), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
House Minority Leader Nancy Pelosi of California scolded former Democratic colleagues Anthony Weiner of New York and Bob Filner of California for their reprehensible behavior amid sex scandals.
Representative Anthony D. Weiner said he would request a leave of absence from the House and seek treatment, after Democratic leaders called on him to resign.
Drugs for Pregnant and Lactating Women, 2nd Edition, by Carl P. Weiner, MD, MBA, FACOG, and Catalin Buhimschi, MD, is a must-have reference that details how virtually all of today s drugs and herbal supplements interact with pregnancy and lactation. Updated thoroughly and covering nearly 2,000 substances, the new edition explains whether each drug is FDA-approved for use by expecting or nursing mothers...is known to be safe for use...or is known to pose a danger. An alphabetical organization by both trade and generic name...a special index listing drugs by category...and an easy-to-read page format make reference more efficient.Describes each substance's mechanism of action, side effects, drug-drug interactions, dosage, cost of therapy, and degree of safety during pregnancy or lactation, providing the thorough details you need to choose the most effective course of treatment. Indicates not only whether the FDA has approved a drug based on clinical trials, but also whether the drug is generally
If MLBPA head Michael Weiner is correct in his estimated time-frame, then A-Rods going to play the entirety of the 2013 season.
Multiple factors may affect where Anthony Weiner will serve his 21-month sentence, including his notoriety, his record and his status as a sex offender.
Full nutritional breakdown of the calories in weiner and egg taquito based on the calories and nutrition in each ingredient, including Flour Tortillas, Egg, fresh, whole, raw, Crisco Pure Vegetable Oil and the other ingredients in this recipe.
AbeBooks.com: Achievement Motivation and Attribution Theory (9780382250651) by Bernard Weiner and a great selection of similar New, Used and Collectible Books available now at great prices.
Rep. Anthony Weiner (D-N.Y.) pauses during a news conference in New York on Monday, after acknowledging inappropriate online communications with women ...
While learning that consuming alcohol basically increases the chance of cancer could be disheartening, the research also examined the way the body attempts to safeguard itself from this kind of damage. Enzymes known as aldehyde dehydrogenases (ALDH) break lower dangerous acetaldehyde into acetate, which our cells may use as an origin of energy. However, huge numbers of people worldwide either lack these enzymes or carry faulty versions of these.. Rodents missing such protective enzymes led to four occasions just as much DNA damage within their cells when compared with rodents which had fully functioning ones.. "Our study highlights that the inability to process alcohol effectively can result in a level greater chance of alcohol-related DNA damage and for that reason certain cancers. But its remember this that alcohol clearance and DNA repair systems arent perfect and alcohol can continue to cause cancer diversely, even just in people whose disease fighting capability are intact," added ...
Aldh3A1 is a member of the aldehyde dehydrogenase superfamily, a group of NAD(P)(+)-dependent enzymes that catalyze the oxidation of a wide spectrum…
Aldh3A1 is a member of the aldehyde dehydrogenase superfamily, a group of NAD(P)(+)-dependent enzymes that catalyze the oxidation of a wide spectrum…
Aldh3A1 is a member of the aldehyde dehydrogenase superfamily, a group of NAD(P)(+)-dependent enzymes that catalyze the oxidation of a wide spectrum…
ALDH2 antibody, Internal (aldehyde dehydrogenase 2 family (mitochondrial)) for ELISA, WB. Anti-ALDH2 pAb (GTX88073) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
ALDH3A2 antibody (aldehyde dehydrogenase 3 family, member A2) for WB. Anti-ALDH3A2 pAb (GTX110363) is tested in Human samples. 100% Ab-Assurance.
Aldehyde Dehydrogenase, Biology, Blood, Cells, Cord Blood, Dehydrogenase, Identification, Nature, Populations, Research, Stem, Stem Cells, Therapeutic, Umbilical Cord, Umbilical Cord Blood
NEW YORK Dominos Pizza has appointed Russell Weiner, 39, its new CMO. He fills a post vacated by Ken Calwell, who left the pizza delivery chain after seven years to head up marketing at Wendys.. Weiner, who was most recently vp, marketing at Pepsi-Cola North America, will assume the post on Sept. 22. Weiner was named one of Brandweeks Marketers of the Next Generation, thanks in part to his role in launching Diet Pepsi Max and the latest iteration of Pepsi Stuff.. He had reported to former PCNA CMO Cie Nicholson, who was replaced last month by Pepsi veteran Dave Burwick. Prior to joining Pepsi, he worked at DraftFCB and Philip Morris. ...
Former Gov. Eliot Spitzer kicked off his first full day of campaigning as a city comptroller candidate Monday, collecting petition signatures in Manhattans Union Square amid a swarm of reporters and
Rep. has called an afternoon news conference Monday amid a fresh round of sordid allegations involving the married congressman, including the release of a new
This "Cited by" count includes citations to the following articles in Scholar. The ones marked * may be different from the article in the profile ...
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Endocrine Today | In this issue, Susan Weiner, MS, RDN, CDE, CDN, talks with certified endocrine coder Mary Ann Hodorowicz, RDN, MBA, CDE, about the basic structure of the coding format. Also reviewed are several tips to help conquer the common hurdles to selecting a billable code — all aimed at increasing claims processing confidence and success. Hodorowicz: ICD-10-PCS stands for the International
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In order to determine the specificity of abnormalities of alcohol metabolism in patients with alcoholic liver disease, blood acetaldehyde concentrations after oral ethanol challenge and the activities of alcohol metabolising enzymes in liver biopsy samples have been determined in patients with alcoholic liver disease and a wide variety of non-alcoholic liver disorders. Significant decreases in hepatic cytosolic aldehyde dehydrogenase activity were associated with significant increases in acetaldehyde concentrations after ethanol in both patient groups compared with control subjects. There was a significant correlation between hepatic cytosolic aldehyde dehydrogenase and mean blood acetaldehyde concentration 30-180 min after ethanol ingestion (y = 17.4-0.45x; r = -0.56; p less than 0.01) confirming the importance of this enzyme in controlling blood acetaldehyde concentrations. These findings suggest that disturbances in alcohol metabolism in patients with alcoholic liver disease are the ...
Looking for online definition of Aldehyde Dehydrogenase 5 Family, Member A1 in the Medical Dictionary? Aldehyde Dehydrogenase 5 Family, Member A1 explanation free. What is Aldehyde Dehydrogenase 5 Family, Member A1? Meaning of Aldehyde Dehydrogenase 5 Family, Member A1 medical term. What does Aldehyde Dehydrogenase 5 Family, Member A1 mean?
The inactivation of low-KM rat liver mitochondrial aldehyde dehydrogenase (ALDH) by the alcohol-sensitizing agent cyanamide (H2NCN) has been studied in vitro. The effect of the concentrations of NAD+ at different concentrations of catalase on the inactivation of ALDH by cyanamide (20 and 200 microM) in vitro point to an ALDH-NAD(+)-catalase complex prior to the binding to cyanamide to form the holoenzyme-inhibitor complex. Cyanamide itself could be responsible for the inactivation of ALDH. The possibility that both irreversibly inactivated ALDH and cyanamide remain free at the end of the inactivation process is discussed. The effects of pH and ionic strength on the inactivation process are also described. The pseudo-first order rate constants for inactivation of low-KM ALDH depends on both effects, suggesting that electrostatic forces are involved in the process and that a group with pK approximately 6.8, presumably a histidine residue, at the active site of ALDH could be involved. A ...
Although aldehyde dehydrogenase (ALDH) from sheep liver cytosol has a broad specificity, it will not oxidize the aldehyde group of glyoxylic acid which is in fact an inhibitor of the enzyme. The inhibition pattern is non-linear but competitive at high propionaldehyde concentrations (2-20 mM); however, a simple non-competitive pattern is observed at low (less than 100 microM) propionaldehyde concentrations (Ki = 1.6 mM). The esterase activity was unaffected by glyoxylic acid in the absence of NAD+ but a simple competitive inhibition pattern (Ki = 2.5 mM) was observed with respect to 4-nitrophenyl acetate in the presence of NAD+. The data require a two-site model in which ester and aldehyde binding sites are distinct but with a second propionaldehyde molecule, and glyoxylic acid, binding at or near the ester binding site. Consistent with this model is the fact that chloral hydrate was a non-competitive inhibitor of the esterase activity in the presence of NAD+ but a competitive inhibitor in its ...
TY - JOUR. T1 - Association of aldehyde dehydrogenase 2 genotype with prevalence of diabetic retinopathy. AU - Suzuki, Yoshihiko. AU - Murata, Chisato. AU - Atsumi, Yoshito. AU - Matsuoka, Kempei. AU - Asahina, Takayuki. AU - Shimada, Akira. AU - Hosokawa, Kazuhiro. AU - Taniyama, Matsuo. AU - Muramatsu, Taro. PY - 1997/8. Y1 - 1997/8. N2 - The influence of aldehyde dehydrogenase 2 (ALDH 2) genotype on diabetic retinopathy was investigated in 212 individuals with non-insulin dependent diabetes mellitus (NIDDM). The prevalence of proliferative retinopathy was lower [p , 0.05) in the 92 patients with inactive ALDH 2 than in the 120 patients with active ALDH2. In patients with NIDDM of less than 10 years duration, the prevalence of proliferative retinopathy was 6.5% (4/62) in those with active ALDH 2 and 0% (0/45) in those with inactive ALDH 2. In patients with NIDDM of more than 10 years duration, the prevalence of proliferative retinopathy was 12.1% (7/58) among those with active ALDH 2 and ...
Author: Kliefoth, Michael et al.; Genre: Journal Article; Published in Print: 2012-02; Keywords: Methanosarcina acetivoran; Carbon monoxide; Acclimation; Aldehyde dehydrogenase; Sensing; Regulation; Title: Genetic analysis of MA4079, an aldehyde dehydrogenase homolog, in Methanosarcina acetivorans
Yokoyama, A., Yokoyama, T., Matsui, T., Mizukami, T., Matsushita, S., Higuchi, S. and Maruyama, K. (2013), Alcohol Dehydrogenase-1B Genotype (rs1229984) is a Strong Determinant of the Relationship Between Body Weight and Alcohol Intake in Japanese Alcoholic Men. Alcoholism: Clinical and Experimental Research, 37: 1123-1132. doi: 10.1111/acer.12069 ...
Mammalian ALDH3 isozymes participate in peroxidic and fatty aldehyde metabolism, and in anterior eye tissue UV-filtration. BLAT analyses were undertaken of the opossum genome using rat ALDH3A1, ALDH3A2, ALDH3B1, and ALDH3B2 amino acid sequences. Two predicted opossum ALDH3A1-like genes and an ALDH3A2-like gene were observed on chromosome 2, as well as an ALDH3B-like gene, which showed similar intron-exon boundaries w ith other mammalian ALDH3-like genes. Opossum ALDH3 subunit sequences and structures were highly conserved, including residues previously shown to be involved in catalysis and coenzyme binding for rat ALDH3A1. Eleven glycine residues were conserved for all of the opossum ALDH3-like sequences examined, including two glycine residues previously located within the stem of the rat ALDH3A1 active site funnel. Phylogeny studies of human, rat, opossum, and chicken ALDH3-like sequences indicated that the common ancestor for ALDH3A- and ALDH3B-like genes predates the appearance of birds ...
A single point mutation in ALDH2-gene provides conclusive evidence for a causal relationship between acetaldehyde and upper GI tract cancer. Mutation results in deficient activity of the main acetaldehyde metabolizing enzyme mitochondrial aldehyde dehydrogenase (ALDH2). When drinking alcohol, ALDH2-deficients are exposed via saliva to 2-3 times and via gastric juice to 5-6 times higher acetaldehyde concentrations than individuals with active ALDH2-enzyme. Parallel to increased local acetaldehyde exposure, the risk of ALDH2-deficient alcohol drinkers for oral, pharyngeal, esophageal and gastric cancer is many fold compared to alcohol drinking ALDH2-actives. Based on strong gene-epidemiological and gene-biochemical evidence, the International Agency for Research on Cancer (IARC) has reclassified acetaldehyde associated with the consumption of alcoholic beverages as a group 1 human carcinogen. Equal gene mutation based human cancer model is not available for any other of the 118 group 1 human ...
It seems that benomyl triggers a series of events leading to Parkinsons disease onset. It is assumed that the chemical interferes with an enzyme called ALDH (aldehyde dehydrogenase). In this way, aldehyde dehydrogenase can not prevent accumulation of DOPAL, a toxic substance that has harmful effect on neurons and which greatly increases the risk of developing Parkinsons disease. Benomyl is a substance that has been widely used in the U.S. until it was banned in 2001 because it was found to have toxic effects on health. It seems that this toxic can cause brain malformations, tumors of the liver, reproductive abnormalities, etc.. Furthermore, the destructive effect of benomyl on dopaminergic neurons has been shown in cell culture experiments. Now neuroscientists at UCLA believe that this cascade of events occurs in all patients with Parkinsons disease. If they were create a drug to protect aldehyde dehydrogenase enzyme activity, they could treat or prevent Parkinsons disease. Parkinsons ...
Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. gamma gamma ADH isozy
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. Because high-grade serous ovarian carcinoma (HGSC) reveals strong molecular similarities to TNBC, we aimed to investigate the potential link between ALDH1 and EGFR in this entity. Expression of ALDH1 was investigated in 131 primary HGSCs using immunohistochemistry. Expression data were correlated with EGFR expression as well as with clinicopathologic parameters and survival. Forty-two carcinomas (32.1%) were positive for ALDH1 protein expression. Data on EGFR expression were available for 112 tumors. In these cases ALDH1 was significantly linked to EGFR expression (P , .0001). ALDH1 positivity was a significant negative prognostic factor for overall survival both in univariate (P = .010) and in multivariate survival analyses (P = .041). Tumors that were positive for both ...
Sulforaphane [SF, 1-isothiocyano-4-(methylsulfinyl)butane] derived from its glucosinolate precursor contained in cruciferous vegetables and related inducers of the Keap1/Nrf2/ARE pathway were assessed for their potencies to induce ALDH in murine hepatoma Hepa1c1c7 cells. Inducer potencies for ALDH were compared with those for NQO1, a prototypical cytoprotective enzyme present downstream of the Keap1/Nrf2/ARE pathway. SF (5 or 20 µmol/day) was fed to CD-1 mice for 7 days prior to a single administration of ethanol, and then ALDH induction in organs and pharmacokinetics of acetaldehyde was examined. ...
In the liver, ethanol is predominantly metabolised by alcohol dehydrogenase (ADH) and CYP 2E1, resulting in acetaldehyde (AA) formation. AA, the extremely toxic first intermediate of ethanol metabolism, binds rapidly to cellular proteins and also possibly to DNA. These AA adducts represent neoantigens leading to the formation of specific antibodies.26 AA has mutagenic and carcinogenic properties leading to metaplasia, inhibition of DNA repair,27 sister chromatid exchanges,28 stimulation of apoptosis, and enhanced cell injury associated with hyperregeneration.29 According to the International Agency for Research on Cancer, there is sufficient evidence to identify AA as a carcinogen in animals.. Ethanol is metabolised by the successive action of ADH and aldehyde dehydrogenase (ALDH). For both ADH and ALDH, genetic polymorphisms have been described that influence the rate of conversion of ethanol to AA and of the latter to acetate.30 It has been consistently reported that ALDH2 is the most ...
RALDH2, RALDH 2, RALDH(II), aldehyde dehydrogenase 1A2, aldehyde dehydrogenase family 1 member A2, retinal dehydrogenase 2, retinaldehyde dehydrogenase 2, retinaldehyde-specific dehydrogenase type 2, Retinal dehydrogenase 2, RALDH 2, Aldehyde dehydrogenase family 1 member A2, Retinaldehyde-specific dehydrogenase type ...
Posted on 06/11/2011 9:19:29 PM PDT by 2ndDivisionVet. An Anthony Weiner action figure is in the works and is expected to be released soon. Do you need a gift for that person that has everything? Its guaranteed that they dont own an Anthony Weiner doll! The doll is being offered in two versions, the standard Weiner and the Weiner Weiner Doll (for adults only). The site doesnt say exactly what the difference is between the two models, but you can probably use your imagination to figure it out. Both Weiner dolls come dressed in an outfit consisting of a plain white shirt and white shorts emblazoned with the words, Tweet This. Click here to see the dolls. If you want to get fancy with your Weiner doll, you can add a stand or a Blackberry for only $18 more. The dolls will be available for shipping on June 20. It was really only a matter of time before a retailer stepped up to try to profit from Anthony Weiners unfortunate controversy. Hey, its capitalism at its finest, right? Besides, he ...
Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1B gene. The protein encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. This encoded protein, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster. The human gene is located on chromosome 4 in 4q22. Previously ADH1B was called ADH2. There are more genes in the family of alcohol and aldehyde dehydrogenase genes. These genes are now referred to as ADH1A, ADH1C, and ADH4, ADH5, ADH6 and ADH7. A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47. The ...
This is from a British nurse of my acquaintance - she contests the paragraph in the Toxicity section dealing with drinking ethanol to avoid methanol poisoning. I asked her because I thought that that paragraph could be useful to remember for first aid purposes, but I figured I should verify it with a medical professional first. Can SOMEBODY, PLEASE, verify one over the other? I know Wikipedia is not a doctor, but for Chrissakes my age group will read this and think, Oh, Johnnys dying of Listerine ingestion, well just get some Jager into him... --207.216.10.77 08:28, 31 October 2006 (UTC). Ethanol is toxic, and the body begins to dispose of it immediately upon its consumption. Over 90% of it is processed by the liver. In the liver, the alcohol dehydrogenase enzyme converts ethanol into acetaldehyde, which is itself toxic. Acetaldehyde is destroyed almost immediately by the aldehyde dehydrogenase enzyme, which converts it to acetate ions.. The hydrogen atoms represented by these equations are ...
Looking for online definition of Aldehyde dehydrogenase E3 isozyme in the Medical Dictionary? Aldehyde dehydrogenase E3 isozyme explanation free. What is Aldehyde dehydrogenase E3 isozyme? Meaning of Aldehyde dehydrogenase E3 isozyme medical term. What does Aldehyde dehydrogenase E3 isozyme mean?
Effect of Elaeagnus Conferta Roxb (Elaeagnaceae) Dry Fruit on the Activities of Hepatic Alcohol Dehydrogenase and Aldehyde Dehydrogenase in Mice. Chongming Wu; Rongji Dai; Jingmiao Bai; Yan Chen; Yuhong Yu; Weiwei Meng; Yulin Deng // Tropical Journal of Pharmaceutical Research;Dec2011, Vol. 10 Issue 6, p761 Purposes: To determine the effect of Elaeagnus conferta Roxb dry fruit powder (ECR) on blood alcohol clearance and on the activities of hepatic alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Methods: In a randomized controlled study, acute alcohol intoxication was induced in mice... ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Potassium atom in PDB 2wme: Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa
Title: The Gene Expression Profiles of Medulloblastoma Cell Lines Resistant to Preactivated Cyclophosphamide. VOLUME: 8 ISSUE: 3. Author(s):M. D. Bacolod, S. M. Lin, S. P. Johnson, N. S. Bullock, M. Colvin, D. D. Bigner and H. S. Friedman. Affiliation:Cornell University Weill Medical College, New York, NY 10021, USA.. Keywords:Cyclophosphamide, drug resistance, medulloblastoma, brain tumor, oxazaphosphorine, aldehyde dehydrogenase, microarray, aldo-keto reductase. Abstract: The total expression profiles of two medulloblastoma cell lines resistant to the preactivated form of cyclophosphamide (4-hydroperoxycyclophosphamide, 4-HC) were examined using the Affymetrix GeneChip U133A array. Our primary objective was to look for possible genes, other than the well-studied aldehyde dehydrogenases (ALDH) that may be involved in cyclophosphamide (CP) resistance in medulloblastomas. We present here the lists of the most highly upregulated [30 for D341 MED (4-HCR); 20 for D283 MED (4-HCR)] and downregulated ...
Diallyl sulfide (DAS), diallyl disulfide (DADS) and diallyl trisulfide (DATS) are major oil-soluble organosulfur compounds of garlic responsible for most of its pharmacological effects. The present study investigated the influence of repeated intraperitoneally (ip) administration of DAS, DADS and DATS on the total level of sulfane sulfur, bound sulfur (S-sulfhydration) and hydrogen sulfide (H2S) and on the activity of enzymes, which catalyze sulfane sulfur formation and transfer from a donor to an acceptor in the normal mouse kidney, i.e., γ-cystathionase (CSE) and rhodanese (TST). The activity of aldehyde dehydrogenase (ALDH), which is a redox-sensitive protein, containing an -SH group in its catalytic center, was also determined. The obtained results indicated that all tested compounds significantly increased the activity of TST. Moreover, DADS and DATS increased the total sulfane sulfur level and CSE activity in the normal mouse kidney. ALDH activity was inhibited in the kidney after DATS
Protection against corrosion and deposition of sludge and varnish is provided by lubricating oils containing a minor amount of the ashless type addition agents which are prepared by reacting under conditions of the Mannich Reaction (1) a high molecular weight alkyl-substituted hydroxy aromatic compound, in which the alkyl-substituent has an average molecular weight of from about 600 to about 100,000, (2) an amine compound containing at least one HN | group (3) an aliphatic aldehyde, and (4) an aliphatic acid containing at least six carbon atoms, in the respective reactant molar ratio of 1:0.1-10:1-10:0.014-1.0 and further reacting such modified condensation product with from about 2 to about 6 moles of an aliphatic aldehyde per mole of the alkyl-substituted hydroxy aromatic compound.
Define propionaldehyde. propionaldehyde synonyms, propionaldehyde pronunciation, propionaldehyde translation, English dictionary definition of propionaldehyde. n. A flammable liquid, C3H6O, with a suffocating odor, used in the manufacture of plastics and rubber chemicals, and as a preservative and disinfectant....
TY - JOUR. T1 - Sodium hypochlorite as oxidant in phase transfer catalytic systems. Part I. Oxidation of aromatic aldehydes. AU - Abramovici, Sara. AU - Neumann, Ronny. AU - Sasson, Yoel. PY - 1985. Y1 - 1985. N2 - Aromatic aldehydes were oxidized to carboxylic acids in high yields and selectivity under mild conditions. The reactions were performed using aqueous sodium hypochlorite as oxidant in a liquid-liquid phase transfer catalytic system using quaternary ammonium salts as catalysts. The reaction was strongly pH-dependent, with maximum reaction rates at pH 9-11. Similarly, extraction of the hypochlorite ion was maximal at these pHs. The maxima are attributed to coextraction of hypochlorous acid together with the hypochlorite anion into the organic phase, the former significantly increasing the reaction rate.. AB - Aromatic aldehydes were oxidized to carboxylic acids in high yields and selectivity under mild conditions. The reactions were performed using aqueous sodium hypochlorite as oxidant ...

Fatty aldehyde dehydrogenase deficiency. Causes, symptoms, treatment Fatty aldehyde dehydrogenase deficiencyFatty aldehyde dehydrogenase deficiency. Causes, symptoms, treatment Fatty aldehyde dehydrogenase deficiency

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 ...
more infohttp://drugster.info/medic/term/fatty-aldehyde-dehydrogenase-deficiency/

Potassium in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa (pdb...Potassium in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa (pdb...

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 ...
more infohttp://potassium.atomistry.com/pdb2wme.html

Cyanamide
      - Calcium Carbimide
     Summary Report | CureHunterCyanamide - Calcium Carbimide Summary Report | CureHunter

Aldehyde Dehydrogenase 8. Messenger RNA (mRNA) 9. Hydrogen 10. Urea (Carbamide) Related Therapies and Procedures. 1. Oral ...
more infohttp://www.curehunter.com/public/keywordSummaryD003484-Cyanamide-Calcium-Carbimide.do

Aldehyde dehydrogenase - Everything2.comAldehyde dehydrogenase - Everything2.com

... 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 ...
more infohttps://everything2.com/title/Aldehyde+dehydrogenase

NAD/NADP-dependent betaine aldehyde dehydrogenase (A3NKP8) | InterPro | EMBL-EBINAD/NADP-dependent betaine aldehyde dehydrogenase (A3NKP8) | InterPro | EMBL-EBI

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 ...
more infohttp://www.ebi.ac.uk/interpro/protein/A3NKP8

LOC542567 aldehyde dehydrogenase 2 [Zea mays] - Gene - NCBILOC542567 aldehyde dehydrogenase 2 [Zea mays] - Gene - NCBI

aldehyde dehydrogenase 2. Names. ALDH2B6. aldehyde dehydrogenase 2-2. aldehyde dehydrogenase2. mitochondrial aldehyde ... PLN02466; aldehyde dehydrogenase family 2 member. cl11961. Location:67 → 542. ALDH-SF; NAD(P)+-dependent aldehyde dehydrogenase ... aldehyde dehydrogenase 2. Gene type. protein coding. RefSeq status. PROVISIONAL. Organism. Zea mays Lineage. Eukaryota; ... Characterization of the aldehyde dehydrogenase gene families of Zea mays and Arabidopsis. Skibbe DS, et al. Plant Mol Biol, ...
more infohttps://www.ncbi.nlm.nih.gov/gene?amp=&cmd=Retrieve&dopt=Graphics&list_uids=542567

DailyMed - Search Results for Acetyl Aldehyde Dehydrogenase InhibitorsDailyMed - Search Results for Acetyl Aldehyde Dehydrogenase Inhibitors

SEARCH RESULTS for: Acetyl Aldehyde Dehydrogenase Inhibitors [Drug Class] (10 results) * Share : JavaScript needed for Sharing ...
more infohttps://dailymed.nlm.nih.gov/dailymed/search.cfm?query=Acetyl%20Aldehyde%20Dehydrogenase%20Inhibitors&searchdb=class

Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes...: Ingenta ConnectNovel ABA- and dehydration-inducible aldehyde dehydrogenase genes...: Ingenta Connect

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- ...
more infohttps://www.ingentaconnect.com/content/bsc/tpj/2001/00000028/00000005/art00006

Alcoholism Medication: Glutamate receptor blockers, Aldehyde dehydrogenase inhibitors, Opiate antagonistsAlcoholism Medication: Glutamate receptor blockers, Aldehyde dehydrogenase inhibitors, Opiate antagonists

Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ...
more infohttps://emedicine.medscape.com/article/285913-medication

ALDH7A1 aldehyde dehydrogenase 7 family member A1 [Homo sapiens (human)] - Gene - NCBIALDH7A1 aldehyde dehydrogenase 7 family member A1 [Homo sapiens (human)] - Gene - NCBI

ALDH7A1 aldehyde dehydrogenase 7 family member A1 [Homo sapiens] ALDH7A1 aldehyde dehydrogenase 7 family member A1 [Homo ... P6c dehydrogenase. alpha-AASA dehydrogenase. antiquitin-1. betaine aldehyde dehydrogenase. delta1-piperideine-6-carboxylate ... aldehyde dehydrogenase 7 family member A1provided by HGNC. Primary source. HGNC:HGNC:877 See related. Ensembl:ENSG00000164904 ... ALDH7A1 aldehyde dehydrogenase 7 family member A1 [ Homo sapiens (human) ] Gene ID: 501, updated on 13-Jan-2020 ...
more infohttps://www.ncbi.nlm.nih.gov/gene/501

CLAH10 - Aldehyde dehydrogenase - Davidiella tassiana (Mycosphaerella tassiana) - CLAH10 gene & proteinCLAH10 - Aldehyde dehydrogenase - Davidiella tassiana (Mycosphaerella tassiana) - CLAH10 gene & protein

Belongs to the aldehyde dehydrogenase family.Curated. Family and domain databases. Gene3D Structural and Functional Annotation ... sp,P40108,ALDH_DAVTA Aldehyde dehydrogenase OS=Davidiella tassiana OX=29918 GN=CLAH10 PE=1 SV=2 ... PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. ... PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. ...
more infohttp://www.uniprot.org/uniprot/P40108

Aldh3a2 - Fatty aldehyde dehydrogenase - Mus musculus (Mouse) - Aldh3a2 gene & proteinAldh3a2 - Fatty aldehyde dehydrogenase - Mus musculus (Mouse) - Aldh3a2 gene & protein

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 ...
more infohttp://www.uniprot.org/uniprot/P47740

aldehyde dehydrogenase 1 family member L1 ELISA Kits | Biocompare.comaldehyde dehydrogenase 1 family member L1 ELISA Kits | Biocompare.com

Compare aldehyde dehydrogenase 1 family member L1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices ... aldehyde dehydrogenase 1 family member L1 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established ... Your search returned 21 aldehyde dehydrogenase 1 family member L1 ELISA ELISA Kit across 3 suppliers. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-2266136/ELISA_Kit/ELISA_aldehyde_dehydrogenase_1_family_member_L1

Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs: Novus BiologicalsAldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs: Novus Biologicals

Browse our Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pair catalog backed by our Guarantee+. ... Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs available through Novus Biologicals. ... Aldehyde dehydrogenase 3 antibody pair, aldehyde dehydrogenase 3 family, member A1 antibody pair, Aldehyde dehydrogenase family ... aldehyde dehydrogenase isozyme 3 antibody pair, aldehyde dehydrogenase type III antibody pair, ALDH3aldehyde dehydrogenase, ...
more infohttps://www.novusbio.com/antibody-pairs/aldehyde-dehydrogenase-3-a1-aldh3a1

Immunohistochemical analysis of aldehyde dehydrogenase isoforms and th | BCTTImmunohistochemical analysis of aldehyde dehydrogenase isoforms and th | BCTT

... aldehyde dehydrogenase (ALDH) activity has been used to identify cancer stem-like cells within the tumor. The presence and ... Immunohistochemical analysis of aldehyde dehydrogenase isoforms and their association with estrogen-receptor status and disease ... Immunohistochemical analysis of aldehyde dehydrogenase isoforms and their association with estrogen-receptor status and disease ... Abstract: In many types of tumors, especially breast tumors, aldehyde dehydrogenase (ALDH) activity has been used to identify ...
more infohttps://www.dovepress.com/immunohistochemical-analysis-of-aldehyde-dehydrogenase-isoforms-and-th-peer-reviewed-article-BCTT

RCSB PDB - Protein Feature View 









 - Aldehyde dehydrogenase, dimeric NADP-preferring - P11883 (AL3A1 RAT)RCSB PDB - Protein Feature View - Aldehyde dehydrogenase, dimeric NADP-preferring - P11883 (AL3A1 RAT)

Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:2831537). Preferentially oxidizes aromatic aldehyde ... An aldehyde + NADP+ + H2O = a carboxylate + NADPH. UniProt ... Aldehyde dehydrogenase, dimeric NADP-preferring - P11883 (AL3A1 ...
more infohttp://www.rcsb.org/pdb/protein/P11883

Aldehyde dehydrogenase 3B1 | definition of aldehyde dehydrogenase 3B1 by Medical dictionaryAldehyde dehydrogenase 3B1 | definition of aldehyde dehydrogenase 3B1 by Medical dictionary

What is aldehyde dehydrogenase 3B1? Meaning of aldehyde dehydrogenase 3B1 medical term. What does aldehyde dehydrogenase 3B1 ... Looking for online definition of aldehyde dehydrogenase 3B1 in the Medical Dictionary? aldehyde dehydrogenase 3B1 explanation ... redirected from aldehyde dehydrogenase 3B1) ALDH3B1. A gene on chromosome 11q13 that encodes an aldehyde dehydrogenase that ... Aldehyde dehydrogenase 3B1 , definition of aldehyde dehydrogenase 3B1 by Medical dictionary https://medical-dictionary. ...
more infohttps://medical-dictionary.thefreedictionary.com/aldehyde+dehydrogenase+3B1

Nutrients | Free Full-Text | Aldehyde Dehydrogenase 1A1: Friend or Foe to  Female Metabolism?Nutrients | Free Full-Text | Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?

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. ...
more infohttp://mdpi.com/2072-6643/6/3/950

Mesenchymal glioma stem cells are maintained by activated glycolytic metabolism involving aldehyde dehydrogenase 1A3 | PNASMesenchymal glioma stem cells are maintained by activated glycolytic metabolism involving aldehyde dehydrogenase 1A3 | PNAS

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 ...
more infohttps://www.pnas.org/content/110/21/8644?ijkey=bda1811a857330f68ac1726a35cad417d825ae9c&keytype2=tf_ipsecsha

Aldh16a1 MGI Mouse Gene Detail - MGI:1916998 - aldehyde dehydrogenase 16 family, member A1Aldh16a1 MGI Mouse Gene Detail - MGI:1916998 - aldehyde dehydrogenase 16 family, member A1

IPR016163 Aldehyde dehydrogenase, C-terminal. IPR015590 Aldehyde dehydrogenase domain. IPR016162 Aldehyde dehydrogenase, N- ...
more infohttp://www.informatics.jax.org/marker/MGI:1916998

Aldh7a1 MGI Mouse Gene Detail - MGI:108186 - aldehyde dehydrogenase family 7, member A1Aldh7a1 MGI Mouse Gene Detail - MGI:108186 - aldehyde dehydrogenase family 7, member A1

IPR015590 Aldehyde dehydrogenase domain. IPR029510 Aldehyde dehydrogenase, glutamic acid active site. IPR016162 Aldehyde ...
more infohttp://www.informatics.jax.org/marker/MGI:108186

Aldehyde Dehydrogenase | Lymphatic & Endocrine system articles | Body & Health Conditions center | SteadyHealth.comAldehyde Dehydrogenase | Lymphatic & Endocrine system articles | Body & Health Conditions center | SteadyHealth.com

Aldehyde dehydrogenase and Alcohol dehydrogenase. Experts are saying that Aldehyde dehydrogenase (ALDH) is functioning often in ... Function of Aldehyde Dehydrogenases. Several researches done in the past have proven that Aldehyde Dehydrogenases are able to ... The famous aldehyde dehydrogenase inhibitor is called Disulfiram! This drug inhibits the enzyme aldehyde dehydrogenase, ... Experts are saying that aldehyde dehydrogenase detoxifies this to acetic acid.. *It is also proven that aldehyde dehydrogenase ...
more infohttps://www.steadyhealth.com/articles/aldehyde-dehydrogenase

Human Metabolome Database: Showing Protein Aldehyde dehydrogenase X, mitochondrial (HMDBP00297)Human Metabolome Database: Showing Protein Aldehyde dehydrogenase X, mitochondrial (HMDBP00297)

Showing Protein Aldehyde dehydrogenase X, mitochondrial (HMDBP00297). IdentificationBiological propertiesGene propertiesProtein ... Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5; ... Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5 ... Aldehyde + NAD + Water → Fatty acid + NADH + Hydrogen Ion. details Acetaldehyde + NAD + Water → Acetic acid + NADH + Hydrogen ...
more infohttp://www.hmdb.ca/proteins/HMDBP00297

TraeALDH7B1- 5A, encoding aldehyde dehydrogenase 7 in wheat, confers improved drought tolerance in Arabidopsis | SpringerLinkTraeALDH7B1- 5A, encoding aldehyde dehydrogenase 7 in wheat, confers improved drought tolerance in Arabidopsis | SpringerLink

... encoding aldehyde dehydrogenase 7 in wheat, conferred significant drought tolerance to Arabidopsis , supported by molecular ... Aldehyde dehydrogenase (ALDH) is a family of enzymes catalyzing the irreversible conversion of aldehydes into acids to decrease ... Lindahl R (1992) Aldehyde dehydrogenases and their role in Carcinogenesis. Crit Rev Biochem Mol Biol 27:283-335PubMedCrossRef ... Yoshida A, Rzhetsky A, Hsu LC, Chang C (1998) Human aldehyde dehydrogenase gene family. Eur J Biochem 251:549-557PubMedCrossRef ...
more infohttps://link.springer.com/article/10.1007%2Fs00425-015-2290-8

Glu504Lys Single Nucleotide Polymorphism of Aldehyde Dehydrogenase 2 Gene and the Risk of Human DiseasesGlu504Lys Single Nucleotide Polymorphism of Aldehyde Dehydrogenase 2 Gene and the Risk of Human Diseases

"Distribution of messenger RNAs for aldehyde dehydrogenase 1, aldehyde dehydrogenase 2, and aldehyde dehydrogenase 5 in human ... M.-K. Chern and R. Pietruszko, "Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase," Biochemical and ... G.-S. Peng and S.-J. Yin, "Effect of the allelic variants of aldehyde dehydrogenase ALDH2∗2 and alcohol dehydrogenase ADH1B∗2 ... "Aldehyde dehydrogenase 2 (ALDH2) rescues myocardial ischaemia/reperfusion injury: role of autophagy paradox and toxic aldehyde ...
more infohttps://www.hindawi.com/journals/bmri/2015/174050/
  • 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)
  • Here we found that the opportunistic pathogen Pseudomonas aeruginosa PAO1 produced NAD + - or NADP + -dependent hydrazone dehydrogenase (HDH), which converts hydrazones to the corresponding hydrazides and acids rather than to the simple hydrolytic product aldehydes. (asm.org)
  • The active site binds to one molecule of an aldehyde and an NAD(P)+ that functions as a cofactor. (wikipedia.org)
  • Nilsson GE, Tottmar O: Biogenic aldehydes in brain: on their preparation and reactions with rat brain tissue. (springer.com)
  • Inoue K, Lindros KO: Subcellular distribution of human brain aldehyde dehydrogenase. (springer.com)