Aldehyde dehydrogenase. Medical search

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.

Organic compounds containing a carbonyl group in the form -CHO.

Oxidoreductases that are specific for ALDEHYDES.

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.

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.

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.

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.

An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.

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.

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

A 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).

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.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

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.

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.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

A group of nitrogen mustard compounds which are substituted with a phosphoramide group or its derivatives. They are usually cytotoxic and used as antineoplastic agents.

The rate dynamics in chemical or physical systems.

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)

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

A hypnotic and sedative used in the treatment of INSOMNIA.

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 1.1.1.14

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.

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.

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.

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 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)

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

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.

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.

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).

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.

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.

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).

A transient reddening of the face that may be due to fever, certain drugs, exertion, stress, or a disease process.

Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.

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.

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.

Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.

Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

Used in the form of its salts as a dye and as an intermediate in manufacture of Acid Yellow, diazo dyes, and indulines.

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.

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.

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.

Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.

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)

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.

An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.

Alcohol oxidoreductases with substrate specificity for LACTIC ACID.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Acyclic branched or unbranched hydrocarbons having two carbon-carbon double bonds.

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.

A reagent used for the determination of iron.

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.

A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

Highly proliferative, self-renewing, and colony-forming stem cells which give rise to NEOPLASMS.

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)

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

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.

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.

Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.

A volatile vasodilator which relieves ANGINA PECTORIS by stimulating GUANYLATE CYCLASE and lowering cytosolic calcium. It is also sometimes used for TOCOLYSIS and explosives.

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.

Oxidoreductases that are specific for KETONES.

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).

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.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

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.

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.

A vasodilator with general properties similar to NITROGLYCERIN but with a more prolonged duration of action. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1025)

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

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)

The sum of the weight of all the atoms in a molecule.

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.

An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.

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)

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)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

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.

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.

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.

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.

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.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

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)

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.

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.

Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.

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)

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.

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.

The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.

A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

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).

Proteins prepared by recombinant DNA technology.

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.

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)

Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.

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.

Compounds based on benzene fused to oxole. They can be formed from methylated CATECHOLS such as EUGENOL.

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.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

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.

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).

The functional hereditary units of BACTERIA.

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.

An enzyme bound to the inner mitochondrial membrane that catalyzes the oxidation of CHOLINE to BETAINE.

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).

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.

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 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.

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.

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.

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))-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.

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+.

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.

An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.

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.

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.

A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.

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 1.1.1.62

Behaviors associated with the ingesting of alcoholic beverages, including social drinking.

The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.

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)

Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.

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)

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.

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)

* Intellectual disability: Individuals with Sjogren-Larsson syndrome typically have mild to moderate intellectual disability, which can range from mild cognitive impairment to more severe developmental delays.
* Seizures: Seizures are a common feature of Sjogren-Larsson syndrome, and they can be difficult to control with medication.
* Physical abnormalities: Individuals with Sjogren-Larsson syndrome may have distinctive physical features, such as short stature, thinning of the hair on the scalp, and thin, brittle skin. They may also have joint deformities, such as clubfoot or scoliosis.
* Vision problems: Sjogren-Larsson syndrome can cause vision problems, including nearsightedness, farsightedness, and astigmatism.
* Hearing loss: Some individuals with Sjogren-Larsson syndrome may experience hearing loss or auditory processing disorders.

There is no cure for Sjogren-Larsson syndrome, but various treatments can help manage the symptoms. These may include medications to control seizures, physical therapy to improve joint mobility and strength, and occupational therapy to develop daily living skills. In addition, speech and language therapy may be helpful for individuals with hearing loss or communication difficulties.

Early diagnosis of Sjogren-Larsson syndrome is important to ensure that children receive appropriate interventions and support as early as possible. Diagnosis typically involves a combination of clinical evaluation, genetic testing, and imaging studies, such as MRI or CT scans. Genetic counseling can also be helpful for families who have a history of the condition.

Overall, Sjogren-Larsson syndrome is a rare and complex disorder that requires careful management and support. With appropriate interventions and resources, individuals with this condition can lead fulfilling lives.

Flushing can also be a side effect of certain medications, such as beta-blockers, aspirin, and some antidepressants. In addition, flushing can be a sign of an underlying condition that affects blood flow or blood vessels, such as Raynaud's disease or lupus.

Treatment for flushing will depend on the underlying cause. For example, if flushing is caused by an allergic reaction, medications such as antihistamines may be prescribed. If the flushing is caused by a medical condition, treatment will focus on managing that condition. In some cases, lifestyle changes such as avoiding triggers, wearing protective clothing, and using cool compresses can help reduce flushing.

It is important to seek medical attention if flushing is severe, persistent, or accompanied by other symptoms such as fever, chest pain, or difficulty breathing. Your healthcare provider can diagnose the underlying cause of flushing and recommend appropriate treatment.

The condition is inherited in an X-linked recessive pattern, meaning that the gene for G6PD deficiency is located on the X chromosome and affects males more frequently than females. Females may also be affected but typically have milder symptoms or may be carriers of the condition without experiencing any symptoms themselves.

G6PD deficiency can be caused by mutations in the G6PD gene, which can lead to a reduction in the amount of functional enzyme produced. The severity of the condition depends on the specific nature of the mutation and the degree to which it reduces the activity of the enzyme.

Symptoms of G6PD deficiency may include jaundice (yellowing of the skin and eyes), fatigue, weakness, and shortness of breath. In severe cases, the condition can lead to hemolytic anemia, which is characterized by the premature destruction of red blood cells. This can be triggered by certain drugs, infections, or foods that contain high levels of oxalic acid or other oxidizing agents.

Diagnosis of G6PD deficiency typically involves a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment is focused on managing symptoms and preventing complications through dietary modifications, medications, and avoidance of triggers such as certain drugs or infections.

Overall, G6PD deficiency is a relatively common genetic disorder that can have significant health implications if left untreated. Understanding the causes, symptoms, and treatment options for this condition is important for ensuring appropriate care and management for individuals affected by it.

Aldehyde dehydrogenases (EC 1.2.1.3) are a group of enzymes that catalyse the oxidation of aldehydes. They convert aldehydes (R ... Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the ... The active site of a human mitochondrial aldehyde dehydrogenase 2. Cys302 and Glu268 interact with the aldehyde substrate. The ... Marchitti SA, Brocker C, Stagos D, Vasiliou V (June 2008). "Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase ...

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

https://en.wikipedia.org/wiki/Betaine-aldehyde_dehydrogenase

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 (February 1949). "Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme" (PDF). The Journal of ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD )

... 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. ...

https://en.wikipedia.org/wiki/Coniferyl-aldehyde_dehydrogenase

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 + ... Adachi O, Matsushita K, Shinagawa E, Ameyama M (1980). "Crystallization and properties of NADP-dependent aldehyde dehydrogenase ... SEEGMILLER JE (1953). "Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast". J. Biol. Chem. 201 (2): 629-37 ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NADP )

... 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 ...

https://en.wikipedia.org/wiki/Aryl-aldehyde_dehydrogenase

... 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 ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(FAD-independent)

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. ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(pyrroloquinoline-quinone)

... 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 ...

https://en.wikipedia.org/wiki/Aryl-aldehyde_dehydrogenase_(NADP )

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): ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P) )

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) Portal: Biology v t e ... The ALDH3A2 belongs to the aldehyde dehydrogenase superfamily and is a membrane-associated protein typically containing 485 ...

https://en.wikipedia.org/wiki/Long-chain-aldehyde_dehydrogenase

"Entrez Gene: ALDH18A1 aldehyde dehydrogenase 18 family, member A1". Fischer-Zirnsak B, Escande-Beillard N, Ganesh J, Tan YX, Al ... 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 ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_18_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 ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_6_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 ( ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_4_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 ... Aldehyde dehydrogenase, dimeric NADP-preferring) at the PDBe-KB. Yoshida A (1993). "Molecular genetics of human aldehyde ... "Entrez Gene: ALDH3A1 aldehyde dehydrogenase 3 family, memberA1". Estey T, Piatigorsky J, Lassen N, Vasiliou V (January 2007). " ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_3_family,_member_A1

"Entrez Gene: ALDH9A1 aldehyde dehydrogenase 9 family, member A1". Human ALDH9A1 genome location and ALDH9A1 gene details page ... This protein belongs to the aldehyde dehydrogenase family of proteins. It has a high activity for oxidation of gamma- ... Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R (December 1993). "Human aldehyde dehydrogenase. cDNA cloning ... McPherson JD, Wasmuth JJ, Kurys G, Pietruszko R (February 1994). "Human aldehyde dehydrogenase: chromosomal assignment of the ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_9_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. ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_5_family,_member_A1

Jakoby WB (1963). "Aldehyde dehydrogenase". In Boyer PD, Lardy H, Myrback K (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... Yamada EW, Jakoby WB (March 1960). "Aldehyde oxidation. V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The ... In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical ...

https://en.wikipedia.org/wiki/Malonate-semialdehyde_dehydrogenase_(acetylating)

"aldehyde dehydrogenase - Homo sapiens". BRENDA. Technische Universität Braunschweig. January 2015. Retrieved 13 April 2015. ... and then aldehyde dehydrogenase (ALDH), which converts 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 ...

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

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 (Dec 1994). "Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase ...

https://en.wikipedia.org/wiki/ALDH3B1

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. ...

https://en.wikipedia.org/wiki/ALDH1A3

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". ...

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

Aldehyde dehydrogenases (ALDH) are NAD+ dependent enzymes that function to remove toxic aldehydes from the body, functioning ... acetaldehyde dehydrogenase alcohol dehydrogenase Delta12-fatty acid dehydrogenase glutamate dehydrogenase (an enzyme that can ... alpha-ketoglutarate dehydrogenase (uses NAD+) succinate dehydrogenase (uses FAD) malate dehydrogenase (uses NAD+) An IUPAC ... Deactivation of aldehyde dehydrogenases has been shown to be instrumental in the mechanisms of many cancers. ALDHs function in ...

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

Some aldehydes are substrates for aldehyde dehydrogenase enzymes which metabolize aldehydes in the body. There are toxicities ... the aldehyde may be named by replacing the suffix -ic acid or -oic acid in this trivial name by -aldehyde. The word aldehyde ... The aldehyde group is somewhat polar. The C=O bond length is about 120-122 picometers. Aldehydes have properties that are ... Aldehydes are common and play important roles in the technology and biological spheres. Aldehydes feature a carbon center that ...

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

Dyck, Lillian E. (1993). "Absence of the atypical mitochondrial aldehyde dehydrogenase (ALDH2) isozyme in Saskatchewan Cree ... Dyck, Lillian E. (1990). "Isoenzymes of aldehyde dehydrogenase in human lymphocytes". Alcoholism: Clinical and Experimental ...

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

... is the first known aldehyde dehydrogenase activator. Ma X, Luo Q, Zhu H, Liu X, Dong Z, Zhang K, et al. (May 2018). " ... Chen CH, Budas GR, Churchill EN, Disatnik MH, Hurley TD, Mochly-Rosen D (September 2008). "Activation of aldehyde dehydrogenase ... Chen CH, Ferreira JC, Gross ER, Mochly-Rosen D (January 2014). "Targeting aldehyde dehydrogenase 2: new therapeutic ... "Aldehyde dehydrogenase 2 activation ameliorates CCl4 -induced chronic liver fibrosis in mice by up-regulating Nrf2/HO-1 ...

https://en.wikipedia.org/wiki/Alda-1

DOPAL is detoxified mainly by aldehyde dehydrogenase. DOPAL is a metabolite of dopamine by monoamine oxidase activity, or MAO, ... Li, W., Spaziano, V.T., Burke, WJ., "Synthesis of a biochemically important aldehyde - 3,4-dihydroxyphenylacetaldehyde", Bio- ... Aldehydes, Catechols, All stub articles, Biochemistry stubs, Aromatic compound stubs). ...

https://en.wikipedia.org/wiki/3,4-Dihydroxyphenylacetaldehyde

Alcohol metabolism depends on the enzymes alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Genetic variants of ... Edenberg HJ, McClintick JN (December 2018). "Alcohol Dehydrogenases, Aldehyde Dehydrogenases, and Alcohol Use Disorders: A ... "Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related ... July 2012). "Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate ...

https://en.wikipedia.org/wiki/Short-term_effects_of_alcohol_consumption

... of aldehydes catalyzed by alcohol dehydrogenase Access to lactone building blocks via horse liver alcohol dehydrogenase- ... "Enantioselective Oxidation of Aldehydes Catalyzed by Alcohol Dehydrogenase". Angewandte Chemie International Edition. 51 (39): ... "Access to Lactone Building Blocks via Horse Liver Alcohol Dehydrogenase-Catalyzed Oxidative Lactonization". ACS Catalysis. 3 ( ...

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

This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... In enzymology, a glycolaldehyde dehydrogenase (EC 1.2.1.21) is an enzyme that catalyzes the chemical reaction glycolaldehyde + ... Davies DD (1960). "The purification and properties of glycolaldehyde dehydrogenase". J. Exp. Bot. 11 (3): 289-295. doi:10.1093/ ...

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

... 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-molybdopterin and also ... Schräder T, Rienhöfer A, Andreesen JR (September 1999). "Selenium-containing xanthine dehydrogenase from Eubacterium barkeri". ...

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

Carbohydrates are aldehydes or ketones, with many hydroxyl groups attached, that can exist as straight chains or rings. ... Hundreds of separate types of dehydrogenases remove electrons from their substrates and reduce NAD+ into NADH. This reduced ... In anaerobic conditions, glycolysis produces lactate, through the enzyme lactate dehydrogenase re-oxidizing NADH to NAD+ for re ...

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

Upon forming the aldehyde in the ring opening step, it is oxidized to form the carboxylic acid and subsequently a ... Averantin is converted to averufin via a two different enzymes, a hydroxylase and an alcohol dehydrogenase. This will oxygenate ...

https://en.wikipedia.org/wiki/Aflatoxin_B1

In addition, it has been found to inhibit aldehyde dehydrogenase and estrogen sulfotransferase in vitro (Ki = 35 μM and 1-3 μM ... Le Bail JC, Laroche T, Marre-Fournier F, Habrioux G (November 1998). "Aromatase and 17beta-hydroxysteroid dehydrogenase ... Unlike many other flavonoids, tropoflavin does not show any inhibitory activity on 17β-hydroxysteroid dehydrogenase. ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... In enzymology, an oxoglutarate dehydrogenase (NADP+) (EC 1.2.1.52) is an enzyme that catalyzes the chemical reaction 2- ... NADP+-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis". J. Biochem. Tokyo. 96 (3): 931-4. doi:10.1093/ ... This enzyme is also called oxoglutarate dehydrogenase (NADP+). Inui H, Miyatake K, Nakano Y, Kitaoka S (September 1984). " ...

https://en.wikipedia.org/wiki/Oxoglutarate_dehydrogenase_(NADP )

... releasing HCl and ammonia to form an aldehyde. The aldehyde group can further react with another amino group to form a Schiff ... found that succinic dehydrogenase was inhibited in vitro by HClO, which led to the investigation of the possibility that ... Succinate dehydrogenase was also inhibited by HClO, stopping the flow of electrons to oxygen. Later studies revealed that ... Rakita, RM; Michel, BR; Rosen, H (1990). "Differential inactivation of Escherichia coli membrane dehydrogenases by a ...

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

The list of ingredients includes the enzymes quinoprotein alcohol dehydrogenase (QADH) and quinoprotein aldehyde dehydrogenase ...

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

Human ALDH1A1 aldehyde dehydrogenase is capable of oxidizing malondialdehyde. Malondialdehyde and other thiobarbituric reactive ... This compound is a reactive aldehyde and is one of the many reactive electrophile species that cause toxic stress in cells and ... The production of this aldehyde is used as a biomarker to measure the level of oxidative stress in an organism. Malondialdehyde ...

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

In both species, it is subsequently metabolized into 4-hydroxyphenylacetate by aldehyde dehydrogenase (ALDH) enzymes in humans ... 4-hydroxyphenyl)acetaldehyde is an alpha-CH2-containing aldehyde and a member of phenylacetaldehydes. It has a role as a human ... Aldehydes, Phenolic human metabolites, All stub articles, Molecular and cellular biology stubs). ... and the phenylacetaldehyde dehydrogenase (feaB) enzyme in E. coli. The condensation of 4-hydroxyphenylacetaldehyde and dopamine ...

https://en.wikipedia.org/wiki/4-Hydroxyphenylacetaldehyde

... is reduced to coniferyl alcohol by the action of dehydrogenase enzymes. It is found in Senra incana ( ... coniferyl aldehyde is a precursor to sinapaldehyde via hydroxylation mediated by coniferyl aldehyde 5-hydroxylase. ... Coniferyl aldehyde is an organic compound with the formula HO(CH3O)C6H3CH=CHCHO. It is a derivative of cinnamaldehyde, ... "Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms". Proceedings of the ...

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

Although the structure of glyoxylic acid is described as having an aldehyde functional group, the aldehyde is only a minor ... It has also been reported that the pyruvate dehydrogenase complex may play a role in glycolate and glyoxylate metabolism. ... the aldehyde structure has as a major conformer a cyclic hydrogen-bonded structure with the aldehyde carbonyl in close ... They are generally formed from reactive aldehydes, such as those present on reducing sugars and alpha-oxoaldehydes. In a study ...

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

Brocker C, Cantore M, Failli P, Vasiliou V (May 2011). "Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and ... Aldehyde dehydrogenase 7 family, member A1, also known as ALDH7A1 or antiquitin, is an enzyme that in humans is encoded by the ... The protein encoded by this gene is a member of subfamily 7 in the aldehyde dehydrogenase gene family. These enzymes are ... As a member of subfamily 7 of the aldehyde dehydrogenase gene family, antiquitin performs NAD(P)+-dependent oxidation of ...

https://en.wikipedia.org/wiki/ALDH7A1

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Other names in common use include aero-oxalo dehydrogenase, and oxalic acid oxidase. This enzyme participates in glyoxylate and ...

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

This sequential pathway first produces alcohols, then alcohol and aldehyde dehydrogenases, and ultimately aldehydes and fatty ...

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

Methylglyoxal reductase and aldehyde dehydrogenase convert methylglyoxal into lactaldehyde and, eventually, L-lactate. If ... Methylglyoxal is, however, a reactive aldehyde that is very toxic to cells, it can inhibit growth in E. coli at milimolar ... The usual pathway converting GAP to pyruvate starts with the enzyme glyceraldehyde 3-phosphate dehydrogenase (Weber 711-13). ... "Structural Anayysis of Glyeraldehyde 3-Phosphate Dehydrogenase from Escherichia coli: Direct Evidence for Substrate Binding and ...

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

In an α,β-unsaturated enal, the alkene is conjugated to the carbonyl group of the aldehyde (formyl group). The simplest enal is ... Two prominent examples are coumaroyl-coenzyme A and crotonyl-coenzyme A. They arise by the action of acyl-CoA dehydrogenases. ... Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718-25 ... Traditional methods for regioselective enolate formation use either electronic activating groups (e.g. aldehydes) or steric ...

https://en.wikipedia.org/wiki/Α,β-Unsaturated_carbonyl_compound

... a new class of NADP+-specific aldehyde dehydrogenase". Biochemical Journal. 397 (1): 131-8. doi:10.1042/BJ20051763. ISSN 0264- ... "Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: ...

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

The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... Glyceraldehyde-3-phosphate dehydrogenase NAD++ Pi NADH + H+ NAD++ Pi NADH + H+ 2 × 1,3-Bisphosphoglycerate 2 × Phosphoglycerate ...

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

... but it can be converted to formaldehyde by alcohol dehydrogenase and then converted to formic acid by aldehyde dehydrogenase, ... glyoxylic acid and oxalic acid by aldehyde dehydrogenase, lactate dehydrogenase (LDH) and glycolate oxidase in mammalian ...

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

... is then oxidized to lactic acid by aldehyde dehydrogenase. Lactaldehyde is a three-carbon atom species with a ... Methylglyoxal is converted to D-lactaldehyde by glycerol dehydrogenase (gldA). ... carbonyl group on the first carbon atom (making it an aldehyde), and a hydroxy group on the second carbon atom, making it a ...

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

"Social factors", despite claims made by social constructionists, have no impact on a genetic aldehyde dehydrogenase deficiency ... and then metabolize acetaldehyde primarily by NAD2-dependent aldehyde dehydrogenase 2 (ALDH2) to acetic acid. East Asians have ... Humans metabolize ethanol to acetaldehyde primarily through NAD+-dependent alcohol dehydrogenase (ADH) class I enzymes (i.e. ...

https://en.wikipedia.org/wiki/Alcohol-induced_respiratory_reactions

... which is in turn converted by aldehyde dehydrogenase into guanidinobutyrate and secreted by the kidneys. Agmatine was found to ... An alternative pathway, mainly in peripheral tissues, is by diamine oxidase-catalyzed oxidation into agmatine-aldehyde, ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ...

https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(ferredoxin)

These include cytochrome P450 2E1 (CYP2E1), quinine oxidoreductase (NQ01 or DT-diaphorase or NAD(P)H dehydrogenase (quinone 1 ... On some condensation products of aldehydes), Liebig's Annalen der Chemie und Pharmacie, 162(1): 77-124, 309-320. From p. 89: " ...

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

Murphy CD, Moss SJ, O'Hagan D (2001). "Isolation of an aldehyde dehydrogenase involved in the oxidation of fluoroacetaldehyde ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... In enzymology, a fluoroacetaldehyde dehydrogenase (EC 1.2.1.69) is an enzyme that catalyzes the chemical reaction ...

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

It is also an allosteric inhibitor of human liver aldehyde dehydrogenase. Prunetin can lower blood pressure of spontaneously ... Sheikh, S.; Weiner, H. (1997). "Allosteric inhibition of human liver aldehyde dehydrogenase by the isoflavone prunetin". ...

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

Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ...

https://www.medscape.com/answers/285913-41586/how-is-alcohol-withdrawal-treated

SEARCH RESULTS for: Aldehyde Dehydrogenase Inhibitor [Drug Class] (9 results) *Share : JavaScript needed for Sharing tools. ...

https://dailymed.nlm.nih.gov/dailymed/search.cfm?query=Aldehyde%20Dehydrogenase%20Inhibitor&searchdb=class

Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ...

http://emedicine.medscape.com/article/285913-medication

View Mouse Monoclonal anti-Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) (NBP2-02483). Validated Applications: WB, Flow ... Home » Aldehyde Dehydrogenase 3-A1/ALDH3A1 » Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibodies » Aldehyde Dehydrogenase 3-A1/ ... Blogs on Aldehyde Dehydrogenase 3-A1/ALDH3A1. There are no specific blogs for Aldehyde Dehydrogenase 3-A1/ALDH3A1, but you can ... Additional Aldehyde Dehydrogenase 3-A1/ALDH3A1 Products. Array NBP2-02483 * Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibodies ...

https://www.novusbio.com/products/aldehyde-dehydrogenase-3-a1-aldh3a1-antibody-oti1b6_nbp2-02483

... profiling to contribute to the delineation of the range of expression and subcellular localization of aldehyde dehydrogenases ( ...

https://edrn.nci.nih.gov/data-and-resources/publications/22110949-2014-comprehensive-proteomic-profiling-of-aldehyde-dehydrogenases-in-lung-adenocarcinoma-cell-lines/

Carney, G., Wei, S., & Rizzo, W. B. (2004). Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase ... Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase gene ALDH3A2. Human mutation. 2004 Aug;24(2 ... Carney, G, Wei, S & Rizzo, WB 2004, Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase gene ... Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase gene ALDH3A2. / Carney, Gael; Wei, Shu; ...

https://experts.nebraska.edu/en/publications/sj%C3%B6gren-larsson-syndrome-seven-novel-mutations-in-the-fatty-aldeh

... and tissue distribution of the zebrafish aldehyde dehydrogenase 2. ... Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2.. Title. Molecular ... Aldehyde Dehydrogenase, Amino Acid Sequence, Animals, Baculoviridae, Blotting, Western, Brain Chemistry, Central Nervous System ... Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2. ...

https://bpp.oregonstate.edu/biblio/molecular-cloning-baculovirus-expression-and-tissue-distribution-zebrafish-aldehyde-1

SEARCH RESULTS for: Aldehyde Dehydrogenase Inhibitor [Drug Class] (9 results) *Share : JavaScript needed for Sharing tools. ...

https://www.dailymed.nlm.nih.gov/dailymed/search.cfm?query=Aldehyde%20Dehydrogenase%20Inhibitor&searchdb=class

Aldehyde dehydrogenase enzymes (ALDHs) have a broad spectrum of biological activities through the oxidation of both endogenous ... Discovery of NCT-501, a Potent and Selective Theophylline-Based Inhibitor of Aldehyde Dehydrogenase 1A1 (ALDH1A1). J Med Chem. ... Compounds and compositions that inhibit aldehyde dehydrogenases, may be used for the treatment of various conditions such as ... Discovery of Orally Bioavailable, Quinoline-based Aldehyde Dehydrogenase 1A1 (ALDH1A1) Inhibitors with Potent Cellular Activity ...

http://www.techtransfer.nih.gov/tech/tab-3244

Human ALDM(Aldehyde Dehydrogenase, Mitochondrial) ELISA Kit. Human ALDM(Aldehyde Dehydrogenase, Mitochondrial) ELISA Kit ... Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) ELISA Kit. SEC024Hu-10x96wellstestplate Cloud-Clone 10x96-wells test plate. ... Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) ELISA Kit. SEC024Hu-1x48wellstestplate Cloud-Clone 1x48-wells test plate. ... Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) ELISA Kit. SEC024Hu-1x96wellstestplate Cloud-Clone 1x96-wells test plate. ...

https://jsce-ip.com/human-aldmaldehyde-dehydrogenase-mitochondrial-elisa-kit/

Mitochondrial aldehyde dehydrogenase 2 alleviates septic liver injury by inhibiting ferro [Mitochondrial aldehyde dehydrogenase ... and to investigate whether mitochondrial aldehyde dehydrogenase 2 (ALDH2) can alleviate sepsis-induced liver injury by ...

https://pesquisa.bvsalud.org/portal/resource/pt/mdl-37545443

Aldehyde Dehydrogenase, Aldehyde Dehydrogenase, Mitochondrial, Animals, Heart Failure, Male, Mitochondria, Mitochondrial ...

https://www.rdm.ox.ac.uk/publications/478063

Aldehyde Dehydrogenase 1. Aldehyde Dehydrogenase 1 Family. Bonding, Human-Pet. Human-Animal Bond. ... Pyruvate Dehydrogenase (Acetyl-Transferring) Kinase. Pyruvate Dehydrogenase Acetyl-Transferring Kinase. Respiratory Distress ...

https://www.nlm.nih.gov/pubs/techbull/nd20/nd20_medline_data_changes_2021.html

AND TISSUE DISTRIBUTION OF THE ZEBRAFISH ALDEHYDE DEHYDROGENASE 2 ... AND TISSUE DISTRIBUTION OF THE ZEBRAFISH ALDEHYDE DEHYDROGENASE ... MOLECULAR CLONING, BACULOVIRUS EXPRESSION, AND TISSUE DISTRIBUTION OF THE ZEBRAFISH ALDEHYDE DEHYDROGENASE 2. Title. MOLECULAR ... AND TISSUE DISTRIBUTION OF THE ZEBRAFISH ALDEHYDE DEHYDROGENASE 2. ...

https://seafood.oregonstate.edu/biblio/molecular-cloning-baculovirus-expression-and-tissue-distribution-zebrafish-aldehyde-0

Our most recent studies suggest that this may reflect downregulation of aldehyde dehydrogenase 1A1 (ALDH1A1) in the diabetic ... Pyruvate dehydrogenase kinase/lactate axis: a therapeutic target for neovascular age-related macular degeneration identified by ... Arai T, Koyama R, Yuasa M, Kitamura D, Mizuta R (2014) Acrolein, a highly toxic aldehyde generated under oxidative stress in ... Oxidative stress results in the formation of lipid aldehydes, which covalently bind to nucleophilic amino-acid residues to form ...

https://link.springer.com/article/10.1007/s00125-018-4707-y

Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism. Journal ... Recent studies on a bacterial version of an enzyme of this pathway, 2-aminomuconate semialdehyde (2-AMS) dehydrogenase (AMSDH ...

https://www.jbc.org/Enzymology?ContribAuthorRaw=Liu%2C+Aimin&KeywordRaw=NAD+biosynthesis&KeywordRaw=biodegradation&startPage=&KeywordRaw=2-aminomuconate%20semialdehyde%20dehydrogenase

Interests: molecular physiology/pharmacology; oxidative stress; cell death pathways; aldehyde dehydrogenases; cancer stem cells ...

https://www.mdpi.com/journal/life/sectioneditors/Cell_and_Tissue

alcohol dehydrogenase. ALDH. aldehyde dehydrogenase. CYP2E1. cytochrome P4502E1. MDI. Mental Developmental Index. ANOVA. ... Alcohol Dehydrogenase-2*3 Allele Protects Against Alcohol-Related Birth Defects Among African Americans. D. G. McCarver, H. R. ... Alcohol Dehydrogenase-2*3 Allele Protects Against Alcohol-Related Birth Defects Among African Americans. D. G. McCarver, H. R. ... Alcohol Dehydrogenase-2*3 Allele Protects Against Alcohol-Related Birth Defects Among African Americans. D. G. McCarver, H. R. ...

https://jpet.aspetjournals.org/content/283/3/1095

Fatty aldehyde dehydrogenase deficiency, see Sjögren-Larsson syndrome. *Fatty liver, see Non-alcoholic fatty liver disease ... Familial pyrimidemia, see Dihydropyrimidine dehydrogenase deficiency. *Familial rectal pain, see Paroxysmal extreme pain ...

https://medlineplus.gov/genetics/condition-f/

Liu SY, Zheng PS . High aldehyde dehydrogenase activity identifies cancer stem cells in human cervical cancer. Oncotarget 2013 ... Our previous studies have demonstrated that high aldehyde dehydrogenase activity may be used to identify CSCs in human cervical ...

https://www.nature.com/articles/cddis2017393?error=cookies_not_supported&code=690749c9-8c76-4f13-b6b9-c388c17deced

Aldehyde dehydrogenase (ALDH) activity. Cells labeled with H33342 were resuspended at 106 cells per milliliter in Aldefluor ... Cell viability were assessed using Lactate dehydrogenase (LDH) release test according to the vendors instructions. The results ...

https://www.oncotarget.com/article/14066/text/

Alcohol and aldehyde dehydrogenase polymorphisms and alcoholism. Behav Genet. 1993 Mar;23(2):131-136. PMID: 8512527 ... such as aldehyde dehydrogenase (see Core article on the basics).181-184 These variants lead to a buildup of acetaldehyde, a ... Implications for global susceptibility to aldehydes toxicity. EBioMedicine. 2020 May 8;55:102753. PMCID: PMC7218264 ...

https://www.niaaa.nih.gov/health-professionals-communities/core-resource-on-alcohol/medical-complications-common-alcohol-related-concerns

Alcohol Dehydrogenase; Aldehyde dehydrogenase; Carbamates; Cytochrome P450; CYP; Flavin-Containing Monooxygenase; FMO; Human ... Alcohols; Aldehydes; Carbamates; Cytochemistry; Cytotoxins; Humans; Metabolism; Metabolites; Pesticide-industry; Pesticide- ...

http://www2a.cdc.gov/nioshtic-2/BuildQyr.asp?s1=agricultur%2A+or+farm%2A&f1=%2A&Adv=0&terms=1&PageNo=474&RecNo=4731&View=f&

The role of endogenous aldehydes and aldehyde dehydrogenases (ALDH) in DNA damage, cancer, and development (e.g. FAS) ... Acetaldehyde in turn is further converted to acetate by aldehyde dehydrogenases (ALDH). In addition to generating acetaldehyde ... Aldehyde dehydrogenase 2 (ALDH2) also provides cardioprotection. Consequently, genetic deficiencies in ALDH2 activities, and ... The primary enzymes of alcohol metabolism are alcohol dehydrogenase (ADH), cytochrome p450 (CYP2E1) and, to a lesser extent, ...

https://grants.nih.gov/grants/guide/pa-files/PA-12-235.html

Symbols: ALDH2, ALDH2B4 , ALDH2B4 (ALDEHYDE DEHYDROGENASE 2); 3-chloroallyl aldehyde dehydroge…. swissprot. blastx. Q9SU63. 241 ... Aldehyde dehydrogenase family 2 member B4, mitochondrial OS=Arabidopsis thaliana GN=ALDH2B4 PE=…. ...

https://www.sgn.cornell.edu/search/unigene.pl?unigene_id=584018

aldehyde dehydrogenase 2 family member. involved_in. ISS. ISO. GO_REF:0000024. (MGI:6827320,PMID:26711020). UniProt. RGD. PMID: ...

https://rgd.mcw.edu/rgdweb/ontology/annot.html?acc_id=GO:0042435

Name: aldehyde dehydrogenase family 7, member A1. Synonyms: Atq1, D18Wsu181e. Type: Gene ...

https://www.mmrrc.org/catalog/sds.php?mmrrc_id=38662

Acetaldehyde, which is responsible for some of the deleterious effects of ethanol, is further oxidized to acetic acid by aldehyde dehydrogenases (ALDHs), of which mitochondrial ALDH2 is the most efficient. (oregonstate.edu)
This chemotype demonstrated a high degree of selectivity over other ALDH isozymes (ALDH1B1, ALDH3A1, and ALDH2) and other dehydrogenases (HPGD and HSD17ß4). (nih.gov)
To observe the ferroptosis triggered by in different pathways during cecal ligation and puncture (CLP)-induced liver injury in septic mice , and to investigate whether mitochondrial aldehyde dehydrogenase 2 (ALDH2) can alleviate sepsis -induced liver injury by inhibiting ferroptosis . (bvsalud.org)

Sjögren-Larsson syndrome (SLS) is an inherited neurocutaneous disease caused by mutations in the ALDH3A2 gene that codes for fatty aldehyde dehydrogenase (FALDH), an enzyme involved in lipid metabolism. (nebraska.edu)
abstract = "Sj{\"o}gren-Larsson syndrome (SLS) is an inherited neurocutaneous disease caused by mutations in the ALDH3A2 gene that codes for fatty aldehyde dehydrogenase (FALDH), an enzyme involved in lipid metabolism. (nebraska.edu)
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) in Tissue homogenates, cell lysates and other biological fluids. (jsce-ip.com)
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (jsce-ip.com)
Recent studies on a bacterial version of an enzyme of this pathway, 2-aminomuconate semialdehyde (2-AMS) dehydrogenase (AMSDH), have provided a detailed understanding of the catalytic mechanism and identified residues conserved for muconate semialdehyde recognition and activation. (jbc.org)
Here, we show that in advanced ovarian cancers NFκB signaling via the RelB transcription factor supports TIC populations by directly regulating the cancer stem-like associated enzyme aldehyde dehydrogenase (ALDH). (nih.gov)
In humans, molybdenum is a cofactor for three enzyme classes-sulfiteoxidase, aldehyde dehydrogenase, and xanthine oxidase (Kisker et al. (cdc.gov)
Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) ( EC 1.2.1.12) is an enzyme that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. (bionity.com)
Doing so is a multi-step process: First, a liver enzyme called alcohol dehydrogenase transforms the alcohol you've ingested into a compound called acetaldehyde. (thecut.com)
Next, another enzyme called aldehyde dehydrogenase breaks that down into acetate, which then becomes carbon dioxide and water. (thecut.com)

Mitochondrial aldehyde dehydrogenase 2 alleviates septic liver injury by inhibiting ferroptosis in mouse model]. (bvsalud.org)
Potentiating mitochondrial aldehyde dehydrogenase 2 to treat post-infarction heart failure. (ox.ac.uk)

The conversion of 6-deoxy penciclovir to penciclovir is catalyzed by aldehyde oxidase. (medscape.com)
Raloxifene, a potent aldehyde oxidase inhibitor in vitro, could decrease the formation of penciclovir. (medscape.com)

The primary enzymes of alcohol metabolism are alcohol dehydrogenase (ADH), cytochrome p450 (CYP2E1) and, to a lesser extent, catalase, enzymes that primarily reside in the cytoplasm, the endoplasmic reticulum (ER) and the peroxisome, respectively. (nih.gov)

Ethanol is metabolized to acetaldehyde mainly by the alcohol dehydrogenase pathway and, to a lesser extent, through microsomal oxidation (CYP2E1) and the catalase-H(2)O(2) system. (oregonstate.edu)
6. Effects of Gene Polymorphisms, Metabolic Activity, and Content of Alcohol Dehydrogenase and Acetaldehyde Dehydrogenases on prognosis of Hepatocellular Carcinoma Patients. (nih.gov)

Aldehyde dehydrogenase 1 (ALDH1A1) is specifically expressed by a subpopulation of nigral DA neurons located in the ventrolateral(VL) tier of rodent SNpc. (nih.gov)

In a PD mouse model, scientists targeted dehydrogenase 1A1-positive (ALDH1A1+) nigrostriatal dopaminergic neurons (nDANs)-the dopamine-producing brain cells that experience the most loss in PD, causing severe impairments in motor skill learning and modest reduction in high-speed walking. (nih.gov)

Aldehyde dehydrogenase enzymes (ALDHs) have a broad spectrum of biological activities through the oxidation of both endogenous and exogenous aldehydes. (nih.gov)

Western Blot: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Analysis of extracts (10ug) from 2 different cell lines by using anti-ALDH3A1 monoclonal antibody at 1:200 dilution. (novusbio.com)
Immunocytochemistry/ Immunofluorescence: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Staining of COS7 cells transiently transfected by pCMV6-ENTRY ALDH3A1. (novusbio.com)
Immunohistochemistry-Paraffin: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Staining of paraffin-embedded prostate tissue using anti-ALDH3A1 mouse monoclonal antibody. (novusbio.com)
Flow Cytometry: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - HEK293T cells transfected with either pCMV6-ENTRY ALDH3A1. (novusbio.com)
Western Blot: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY ALDH3A1 (Right lane) cDNA for 48 hrs and lysed. (novusbio.com)

We used activity-based protein profiling to discover that the primary target of DKM 3-42 was the catalytic cysteine in aldehyde dehydrogenase 3A1 (ALDH3A1). (nih.gov)

Isolated cancer cells with relatively high aldehyde dehydrogenase 1 (ALDH1) activity display in vitro features of CSCs, including capacities for proliferation, self-renewal, and differentiation, resistance to chemotherapy, and expressing CSC surface marker CD133. (nih.gov)

Aldehyde dehydrogenase variation enhances effect of pesticides associated with Parkinson's disease . (snpedia.com)

Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2. (oregonstate.edu)

Aldehyde dehydrogenase 1 is a tumor stem cell-associated marker in lung cancer. (nih.gov)

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate as the name indicates. (bionity.com)

The primary enzymes of alcohol metabolism are alcohol dehydrogenase (ADH), cytochrome p450 (CYP2E1) and, to a lesser extent, catalase, enzymes that primarily reside in the cytoplasm, the endoplasmic reticulum (ER) and the peroxisome, respectively. (nih.gov)
3. Effects of Gene Polymorphisms, Metabolic Activity, and Content of Alcohol Dehydrogenase and Acetaldehyde Dehydrogenases on Prognosis of Hepatocellular Carcinoma Patients. (nih.gov)

Twelve aldehyde dehydrogenase (ALDH) genes have been identified in humans. (nih.gov)
This chemotype demonstrated a high degree of selectivity over other ALDH isozymes (ALDH1B1, ALDH3A1, and ALDH2) and other dehydrogenases (HPGD and HSD17ß4). (nih.gov)
The ALDH7A1 gene is a member of the aldehyde dehydrogenase (ALDH) gene family. (medlineplus.gov)
10. Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human large bowel: association of the functional polymorphisms of ADH and ALDH genes with hemorrhoids and colorectal cancer. (nih.gov)

Aldehyde dehydrogenase gene superfamily: the 2000 update. (nih.gov)
Antiquitin, a relatively unexplored member in the superfamily of aldehyde dehydrogenases with diversified physiological functions. (medlineplus.gov)

These genes, located on different chromosomes, encode a group of enzymes which oxidizes varieties of aliphatic and aromatic aldehydes. (nih.gov)
Aldehyde dehydrogenase enzymes (ALDHs) have a broad spectrum of biological activities through the oxidation of both endogenous and exogenous aldehydes. (nih.gov)
These genes provide instructions for producing enzymes that alter molecules called aldehydes. (medlineplus.gov)

Low Km aldehyde dehydrogenase (ALDH2) polymorphism, alcohol-drinking behavior, and chromosome alterations in peripheral lymphocytes. (nih.gov)
11. Genetic polymorphisms of aldehyde dehydrogenase 2, cytochrome p450 2E1 for liver cancer risk in HCV antibody-positive japanese patients and the variations of CYP2E1 mRNA expression levels in the liver due to its polymorphism. (nih.gov)
19. Polymorphism of alcohol and aldehyde dehydrogenase genes and alcoholic cirrhosis in Chinese patients. (nih.gov)

8. Pharmacological recruitment of aldehyde dehydrogenase 3A1 (ALDH3A1) to assist ALDH2 in acetaldehyde and ethanol metabolism in vivo. (nih.gov)
17. Ethanol and acetaldehyde metabolism in chinese with different aldehyde dehydrogenase-2 genotypes. (nih.gov)

We used activity-based protein profiling to discover that the primary target of DKM 3-42 was the catalytic cysteine in aldehyde dehydrogenase 3A1 (ALDH3A1). (nih.gov)
6. Use of an "acetaldehyde clamp" in the determination of low-KM aldehyde dehydrogenase activity in H4-II-E-C3 rat hepatoma cells. (nih.gov)

Comprehensive proteomic profiling of aldehyde dehydrogenases in lung adenocarcinoma cell lines. (nih.gov)

Anatomy6

Organisms5

Diseases3

Chemicals and Drugs106

Analytical, Diagnostic and Therapeutic Techniques and Equipment7

Psychiatry and Psychology1

Phenomena and Processes21

Disciplines and Occupations1

Information Science3

Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (1/1111)

Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (2/1111)

Stimulation of premature retinoic acid synthesis in Xenopus embryos following premature expression of aldehyde dehydrogenase ALDH1. (3/1111)

The negative regulation of the rat aldehyde dehydrogenase 3 gene by glucocorticoids: involvement of a single imperfect palindromic glucocorticoid responsive element. (4/1111)

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)

Relationships within the aldehyde dehydrogenase extended family. (6/1111)

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)

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)

Aldehyde Dehydrogenase

Aldehydes

Aldehyde Oxidoreductases

Disulfiram

Acetaldehyde

Retinal Dehydrogenase

Alcohol Dehydrogenase

Betaine-Aldehyde Dehydrogenase

Cyanamide

NAD

L-Lactate Dehydrogenase

Alcohol Oxidoreductases

Glyceraldehyde-3-Phosphate Dehydrogenases

Isoenzymes

Benzaldehydes

Glutamate Dehydrogenase

Glucosephosphate Dehydrogenase

Sjogren-Larsson Syndrome

Malate Dehydrogenase

Isocitrate Dehydrogenase

Phosphoramide Mustards

Kinetics

NADP

Liver

Chloral Hydrate

L-Iditol 2-Dehydrogenase

Dihydrolipoamide Dehydrogenase

Molecular Sequence Data

Carbohydrate Dehydrogenases

Succinate Dehydrogenase

Mitochondria, Liver

Substrate Specificity

Ethanol

Amino Acid Sequence

Oxidation-Reduction

Glycerolphosphate Dehydrogenase

Aldehyde Reductase

Methylmalonate-Semialdehyde Dehydrogenase (Acylating)

Succinate-Semialdehyde Dehydrogenase

Flushing

Hydroxysteroid Dehydrogenases

Glucose 1-Dehydrogenase

Sugar Alcohol Dehydrogenases

Ketoglutarate Dehydrogenase Complex

Acrolein

Coenzymes

3-Hydroxysteroid Dehydrogenases

p-Aminoazobenzene

Xanthine Dehydrogenase

Glucose Dehydrogenases

Phosphogluconate Dehydrogenase

Acyl-CoA Dehydrogenases

Oxidoreductases

NADH Dehydrogenase

IMP Dehydrogenase

Lactate Dehydrogenases

Base Sequence

Alkadienes

Formate Dehydrogenases

2,2'-Dipyridyl

Acyl-CoA Dehydrogenase

17-Hydroxysteroid Dehydrogenases

Neoplastic Stem Cells

Alcohols

Catalysis

Hydroxybutyrate Dehydrogenase

Cloning, Molecular

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)

Oxidoreductases Acting on CH-NH Group Donors

Nitroglycerin

Ditiocarb

Ketone Oxidoreductases

Pyruvate Dehydrogenase (Lipoamide)

3-Hydroxyacyl CoA Dehydrogenases

Sequence Homology, Amino Acid

Escherichia coli

11-beta-Hydroxysteroid Dehydrogenases

Pentaerythritol Tetranitrate

Cytosol

Uridine Diphosphate Glucose Dehydrogenase