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)

3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... long-chain-3-hydroxyacyl-CoA dehydrogenase activity. • GO:0001948 protein binding. • catalytic activity. • transferase activity ... HADHB, ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ...

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

Hydroxyacyl-Coenzyme A dehydrogenase. To acetyl-CoA. *Malonyl-CoA decarboxylase. Aldehydes. *Long-chain-aldehyde dehydrogenase ...

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

acyl-CoA dehydrogenase activity. • identical protein binding. • oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase ... ACADM, acyl-CoA dehydrogenase, C-4 to C-12 straight chain, ACAD1, MCAD, MCADH, acyl-CoA dehydrogenase medium chain. ... "Mitochondrially encoded NADH dehydrogenase 1". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).. *^ Matsubara Y, Kraus ... ACADM (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ...

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

2cg5: STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL ... "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1-3): 94- ...

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

"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

doi:10.1016/0006-2952(93)90285-5. Dyck, Lillian E. (1993). "Absence of the atypical mitochondrial aldehyde dehydrogenase (ALDH2 ... doi:10.1016/0024-3205(93)90442-6. Dyck, Lillian E. (1990). "Isoenzymes of aldehyde dehydrogenase in human lymphocytes". ...

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. "3,4-dihydroxyphenylacetaldehyde - Compound Summary". PubChem Compound. ... Li, W., Spaziano, V.T., Burke, WJ., "Synthesis of a biochemically important aldehyde - 3,4-dihydroxyphenylacetaldehyde", Bio- ...

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

Gama-Castro S.; Núñez C.; Segura D.; Moreno S.; Guzmán J. & Espín G. (2001). "Azotobacter vinelandii Aldehyde Dehydrogenase ... it is also affected by aldehyde dehydrogenase[13] and the response regulator AlgR.[14] ...

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

NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ ... alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD- ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; ...

https://id.wikipedia.org/wiki/Oksidoreduktase_alkohol:NAD+

2006;42(1):8-16 Crabb DW (2004). "Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants ... Alcohol metabolism depends on the enzymes alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). Genetic variants of ... Edenberg HJ, McClintick JN (2018). "Alcohol Dehydrogenases, Aldehyde Dehydrogenases, and Alcohol Use Disorders: A Critical ... Koppaka V (2012). "Aldehyde Dehydrogenase Inhibitors: a Comprehensive Review of the Pharmacology, Mechanism of Action, ...

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

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

"Entrez Gene: ALDH18A1 aldehyde dehydrogenase 18 family, member A1". Liu, Li-Kai; Becker, Donald F.; Tanner, John J. (2017-10-15 ... In many prokaryotes, proline dehydrogenase and P5C dehydrogenase form a bifunctional enzyme that prevents the release of P5C ... the enzyme proline dehydrogenase produces P5C from proline, and the enzyme 1-pyrroline-5-carboxylate dehydrogenase converts GSA ...

https://en.wikipedia.org/wiki/1-Pyrroline-5-carboxylic_acid

Betaine aldehyde is further oxidised in the mitochondria in mice to betaine by the enzyme betaine aldehyde dehydrogenase (EC ... In humans betaine aldehyde activity is performed by a nonspecific cystosolic aldehyde dehydrogenase enzyme (EC 1.2.1.3) TMG is ... "BRENDA - Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase". Brenda-enzymes.org. Retrieved 2016-07-07. Chern, M. K.; ... Pietruszko, R. (1999). "Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, ...

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

"Aldehyde dehydrogenases in cellular responses to oxidative/electrophilic stress". Free Radical Biology and Medicine. 56: 89-101 ...

https://en.wikipedia.org/wiki/Stem-cell_niche

Other studies have suggested that reduced activity by the enzyme aldehyde dehydrogenase may be responsible for a build-up of ... March 1993). "Analysis of corneal aldehyde dehydrogenase patterns in pathologic corneas". Cornea. 12 (2): 146-54. doi:10.1097/ ...

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

"Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1". Human ALDH1L1 genome location and ALDH1L1 gene details page ... The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies ... 10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene. The protein encoded by this ... Krupenko SA, Oleinik NV (2002). "10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in ...

https://en.wikipedia.org/wiki/ALDH1L1

Aldehyde dehydrogenase family 3 member B2 is an enzyme that in humans is encoded by the ALDH3B2 gene. This gene encodes a ... "Entrez Gene: ALDH3B2 aldehyde dehydrogenase 3 family, member B2". Human ALDH3B2 genome location and ALDH3B2 gene details page ... Hsu LC, Chang WC (Dec 1996). "Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase ... member of the aldehyde dehydrogenase family, a group of isozymes that may play a major role in the detoxification of aldehydes ...

https://en.wikipedia.org/wiki/ALDH3B2

Aldehyde dehydrogenase 1 family, member A2, also known as ALDH1A2 or retinaldehyde dehydrogenase 2 (RALDH2), is an enzyme that ... "Entrez Gene: ALDH1A2 aldehyde dehydrogenase 1 family, member A2". CS1 maint: discouraged parameter (link) Duester G (September ... This protein belongs to the aldehyde dehydrogenase family of proteins. The product of this gene is an enzyme that catalyzes the ... Wang X, Penzes P, Napoli JL (1996). "Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia ...

https://en.wikipedia.org/wiki/ALDH1A2

Sládek NE (August 1999). "Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines". Current ...

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

"Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation". The Biochemical Journal. 329 ... Adh: Alcohol dehydrogenase- Drosophila melanogaster can express the alcohol dehydrogenase (ADH) mutation, thereby preventing ... "Alpha-ketoglutarate reduces ethanol toxicity in Drosophila melanogaster by enhancing alcohol dehydrogenase activity and ... the breakdown of toxic levels of alcohols into aldehydes and ketones.[40] While ethanol produced by decaying fruit is a natural ...

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

These agents all exert their effect by being converted to nitric oxide in the body by mitochondrial aldehyde dehydrogenase ( ... the enzyme for this conversion was not discovered to be mitochondrial aldehyde dehydrogenase (ALDH2) until 2002.[4] ... "An essential role for mitochondrial aldehyde dehydrogenase in nitroglycerin bioactivation". Proceedings of the National Academy ...

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

... 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

This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... Aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1 or retinaldehyde dehydrogenase 1 (RALDH1), is an enzyme that ... Ma S, Chan KW, Lee TK, Tang KH, Wo JY, Zheng BJ, Guan XY (July 2008). "Aldehyde dehydrogenase discriminates the CD133 liver ... Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A (June 1985). "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2". ...

https://en.wikipedia.org/wiki/ALDH1A1

Aldehyde dehydrogenase 8 family, member A1 also known as ALDH8A1 is an enzyme that in humans is encoded by the ALDH8A1 gene. ... This protein belongs to the aldehyde dehydrogenase family of enzymes. It was originally thought to play a role in a pathway of ... Davis I, Yang Y, Wherritt D, Liu A (June 2018). "Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the ... Lin M, Napoli JL (December 2000). "cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis- ...

https://en.wikipedia.org/wiki/ALDH8A1

Algar EM, Abedinia M, VandeBerg JL, Holmes RS (1991). "Purification and properties of baboon corneal aldehyde dehydrogenase: ... King G, Holmes RS (Sep 1993). "Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic ... PDB: 1K87; Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ (Feb 2003). "Structure of the proline dehydrogenase domain of the ... In the case of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), in addition to the large number of ...

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

... alcohol dehydrogenase converts 1-butanol to butyraldehyde; this is then converted to butyric acid by aldehyde dehydrogenase. ... possibly because of its slower transformation by alcohol dehydrogenase. Liquid 1-butanol, as is common with most organic ...

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

... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... Glutaryl-CoA dehydrogenase. *Isovaleryl coenzyme A dehydrogenase. *3-oxo-5beta-steroid 4-dehydrogenase ...

https://en.wikipedia.org/wiki/2-alkenal_reductase

The oxidases xanthine oxidase, aldehyde oxidase, and sulfite oxidase[31] Legumes, whole grains, nuts[25] molybdenum deficiency ... Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ...

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

pyruvate dehydrogenase (acetyl-transferring) activity. • oxidoreductase activity, acting on the aldehyde or oxo group of donors ... PDHA2, PDHAL, Pyruvate dehydrogenase (lipoamide) alpha 2, pyruvate dehydrogenase alpha 2, pyruvate dehydrogenase E1 alpha 2 ... Pyruvate dehydrogenase (lipoamide) alpha 2, also known as pyruvate dehydrogenase E1 component subunit alpha, testis-specific ... Mutations in the PDHA2 gene have been known to cause one form of pyruvate dehydrogenase deficiency. Pyruvate dehydrogenase ...

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

l-galactonolactone dehydrogenase.[131] to produce ascorbic acid.[122] l-Ascorbic acid has a negative feedback on l-galactose ... The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor ... l-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between the carbonyl on C1 and hydroxyl ... UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ...

https://en.wikipedia.org/wiki/L-ascorbic_acid

The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor ... UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ... Leferink, N. G.; van den Berg, W. A.; van Berkel, W. J. (2008). "L-Galactono-γ-lactone Dehydrogenase from Arabidopsis thaliana ... L-Galactose reacts with the enzyme L-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between ...

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

Furthermore, alcohol dehydrogenase is present in the stomach lining. After absorption, the alcohol passes to the liver through ... but reach lower aldehyde concentrations and have milder hangovers. Rate of detoxification of alcohol can also be slowed by ... Alcohol is metabolized mainly by the group of six enzymes collectively called alcohol dehydrogenase. These convert the ethanol ... Such persons have impaired acetaldehyde dehydrogenase, which causes acetaldehyde levels to peak higher, producing more severe ...

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

pyruvate dehydrogenase (acetyl-transferring) activity. • oxidoreductase activity, acting on the aldehyde or oxo group of donors ... pyruvate dehydrogenase alpha 1, pyruvate dehydrogenase E1 alpha 1 subunit, pyruvate dehydrogenase E1 subunit alpha 1. ... pyruvate dehydrogenase complex. • mitochondrial matrix. • هسته یاخته. • هستک. • میتوکندری. فرایند زیستی. • mitochondrial acetyl ... pyruvate dehydrogenase (NAD+) activity. • GO:0001948 پیوند پروتئینی. ترکیبات سلولی. • intracellular membrane-bounded organelle ...

https://fa.m.wikipedia.org/wiki/پیرووات_دهیدروژناز_

alcohol dehydrogenase (NADP+) activity. • retinal dehydrogenase activity. • allyl-alcohol dehydrogenase activity. • NADP- ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... AR belongs to the aldehyde-keto reductase superfamily, with a widely expression in human organs including the kidney, lens, ... It also participates in glucose metabolism and osmoregulation and plays a protective role against toxic aldehydes derived from ...

https://en.wikipedia.org/wiki/AKR1B1

catalyzed by retinol dehydrogenases (RDHs)[9] and alcohol dehydrogenases (ADHs).[10] Retinol is called vitamin A alcohol, or ... It was originally called retinene,[2] and renamed[3] after it was discovered to be vitamin A aldehyde.[4][5] Retinal is one of ... catalyzed by retinal dehydrogenases[11] also known as retinaldehyde dehydrogenases (RALDHs)[10] as well as retinal oxidases.[12 ... BALL, S; GOODWIN, TW; MORTON, RA (1946). "Retinene1-vitamin A aldehyde". The Biochemical Journal. 40 (5-6): lix. PMID 20341217. ...

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

"aldehyde dehydrogenase - Homo sapiens". BRENDA. Technische Universität Braunschweig. January 2015. Retrieved 13 April 2015.. ... and then aldehyde dehydrogenase (ALDH), which convert it to phenylacetic acid.[5] This means that for significant ... 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.m.wikipedia.org/wiki/Phenethylamine

... class 3 aldehyde dehydrogenase, glucose-6-phosphate isomerase, and tissue kallikrein (function unknown)[5] ... Minor enzymes include salivary acid phosphatases A+B, N-acetylmuramoyl-L-alanine amidase, NAD(P)H dehydrogenase (quinone), ...

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

aldehyde dehydrogenase NAD(P)+ Ja 1.2.1.8 betaine-aldehyde dehydrogenase Ja 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase ( ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ... Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja 1.1.1.2 Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. ...

https://nl.wikipedia.org/wiki/Oxidoreductase

... of aldehyde dehydrogenase deficiency or chronic fatigue syndrome. Severe pain after drinking alcohol may indicate a more ... Alcohol intolerance is due to a genetic polymorphism of the enzyme alcohol dehydrogenase, the enzyme that metabolises ingested ... together with other substances to the accumulation of harmful Acetaldehyde by inhibiting the enzyme acetaldehyde dehydrogenase ...

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

retinol dehydrogenase activity. • allyl-alcohol dehydrogenase activity. Cydrannau o'r gell. • cytosol. • extracellular exosome ... cellular aldehyde metabolic process. • aldehyde catabolic process. • D-glucuronate catabolic process. • L-ascorbic acid ... "The role of aldehyde reductase AKR1A1 in the metabolism of Î³-hydroxybutyrate in 1321N1 human astrocytoma cells. ". Chem Biol ... "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. ". Acta Crystallogr D Biol ...

https://cy.wikipedia.org/wiki/AKR1A1

In bacteria, carbon monoxide is produced via the reduction of carbon dioxide by the enzyme carbon monoxide dehydrogenase, an Fe ... Carbon monoxide is, along with aldehydes, part of the series of cycles of chemical reactions that form photochemical smog. It ... Large quantities of aldehydes are produced by the hydroformylation reaction of alkenes, carbon monoxide, and H2. ...

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

Genetics: alleles associated with aldehyde dehydrogenase (ALDH) and flushing phenotypes (alcohol flush reaction) in Asians are ... "Alcohol metabolism in Asian-American men with genetic polymorphisms of aldehyde dehydrogenase". Annals of Internal Medicine. ... "The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases ... For example, some people (predominantly East Asians) have a mutation in their alcohol dehydrogenase gene that makes this enzyme ...

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

Most of the aldophosphamide is then oxidised by the enzyme aldehyde dehydrogenase (ALDH) to make carboxycyclophosphamide. A ... Kohn FR, Sladek NE (1985). "Aldehyde dehydrogenase activity as the basis for the relative insensitivity of murine pluripotent ...

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

Enzymes that transfer aldehyde or ketone groups and included in EC 2.2. This category consists of various transketolases and ... Herbst EA, MacPherson RE, LeBlanc PJ, Roy BD, Jeoung NH, Harris RA, Peters SJ (Jan 2014). "Pyruvate dehydrogenase kinase-4 ... Transaldolase, the namesake of aldehyde transferases, is an important part of the pentose phosphate pathway. The reaction it ... and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA. Transferases are also utilized ...

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

Mechanism of oxidation of primary alcohols to carboxylic acids via aldehydes and aldehyde hydrates ... which has a higher affinity for liver alcohol dehydrogenase. In this way methanol will be excreted intact in urine.[21][22][23] ... If a higher priority group is present (such as an aldehyde, ketone, or carboxylic acid), then the prefix hydroxy-is used,[14] e ... Aldehydes or ketones are reduced with sodium borohydride or lithium aluminium hydride (after an acidic workup). Another ...

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

The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... The G6P is then converted to 6-phosphogluconolactone in the presence of enzyme glucose-6-phosphate dehydrogenase( an oxido- ... From here, GA is oxidized via GA dehydrogenase into glycerate. The glycerate is phosphorylated by glycerate kinase into 2PG. ... The G3P is converted to 1,3-bisphosphoglycerate int the presence of enzyme glyceraldehyde-3-phosphate dehydrogenase (an oxido- ...

https://en.m.wikipedia.org/wiki/Entner–Doudoroff_pathway

Hydroxyacyl-Coenzyme A dehydrogenase. To acetyl-CoA. *Malonyl-CoA decarboxylase. Aldehydes. *Long-chain-aldehyde dehydrogenase ...

https://en.wikipedia.org/wiki/Beta-Ketoacyl_ACP_reductase

Crabb D, Xiao Q (Jun 1998). "Studies on the enzymology of aldehyde dehydrogenase-2 in genetically modified HeLa cells". ... Acetaldehyde dehydrogenase. (acetylating). Crystallographic structure of the acetaldehyde dehydrogenase from Pseudomonas sp.[1] ... Acetaldehyde dehydrogenases (EC 1.2.1.10) are dehydrogenase enzymes which catalyze the conversion of acetaldehyde into acetic ... Hempel J, von Bahr-Lindström H, Jörnvall H (May 1984). "Aldehyde dehydrogenase from human liver. Primary structure of the ...

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

Protein yìí wà ní ẹbí aldehyde dehydrogenase ti àwọn protein. Gene yìí máa ń kóòdù fún succinic semialdehyde dehydrogenase tí ó ... "Entrez Gene: ALDH5A1 aldehyde dehydrogenase 5 family, member A1 (succinate-semialdehyde dehydrogenase)".. ... "A functional polymorphism in the succinate-semialdehyde dehydrogenase (aldehyde dehydrogenase 5 family, member A1) gene is ... Aldehyde dehydrogenase 5 family, member A1. Lát'ọwọ́ Wikipedia, ìwé ìmọ̀ ọ̀fẹ́ ...

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

2007.urtean, "methanol dehydrogenase" nobela batekanlantanoideak entzimen kofaktore bezala aurkituak izan ziren " ... New Anhydrous Lithium Lanthanide Binaphtholates and Their Use in Enantioselective Alkyl Addition to Aldehydes»] Organometallics ...

https://eu.wikipedia.org/wiki/Lantanoide

GABA can also be synthesized from putrescine[48][49] by diamine oxidase and aldehyde dehydrogenase.[48] ... Succinic semialdehyde is then oxidized into succinic acid by succinic semialdehyde dehydrogenase and as such enters the citric ...

https://en.wikipedia.org/wiki/Gamma-Aminobutyric_acid

... releasing HCl and ammonia to form an aldehyde.[35] The aldehyde group can further react with another amino group to form a ... Venkobachar et al.[46] found that succinic dehydrogenase was inhibited in vitro by HOCl, which led to the investigation of the ... Succinate dehydrogenase was also inhibited by HOCl, stopping the flow of electrons to oxygen. Later studies[38] revealed that ... Rakita, RM; Michel, BR; Rosen, H (1990). "Differential inactivation of Escherichia coli membrane dehydrogenases by a ...

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

Aldehyde/oxo oxidoreductases (EC 1.2). 1.2.1: NAD or NADP. *Aldehyde dehydrogenase *Acetaldehyde dehydrogenase ... alpha-ketoacid dehydrogenase activity. Cellular component. • mitochondrial alpha-ketoglutarate dehydrogenase complex. • ... 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial is an enzyme that in humans is encoded by the BCKDHA gene.[5] ... oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • protein binding. • metal ion ...

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

... aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ultimately oxidized to carbon ... Other articles where Aldehyde dehydrogenase is discussed: alcohol consumption: Processing in the liver: …acted upon by another ... acted upon by another enzyme, aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ...

https://www.britannica.com/science/aldehyde-dehydrogenase

... this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ethanal ... Or ALDH, this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ...

https://everything2.com/title/Aldehyde+dehydrogenase

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

Aldehyde dehydrogenaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p ... tr,Q7M053,Q7M053_RAT Aldehyde dehydrogenase OS=Rattus norvegicus OX=10116 PE=1 SV=1 BSGZPTAVMYILFHKR Align. Format. Add to ...

https://www.uniprot.org/uniprot/Q7M053

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

GO:0008802 betaine-aldehyde dehydrogenase activity GO:0016491 oxidoreductase activity GO:0016620 oxidoreductase activity, ... acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor GO:0046872 metal ion binding ...

http://www.ebi.ac.uk/interpro/protein/A3NKP8

Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead (IPR000674). Short name: Ald_Oxase/Xan_DH_a/b ... The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [PMID: ... Aldehyde oxidase (EC:1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and ... Xanthine dehydrogenase (EC:1.1.1.204) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and ...

http://www.ebi.ac.uk/interpro/entry/IPR000674

NAD-dependent aldehyde dehydrogenase activity, NAD-linked aldehyde dehydrogenase activity, aldehyde dehydrogenase (NAD+), ... aldehyde dehydrogenase (NAD+), aldehyde:NAD+ oxidoreductase activity, CoA-independent aldehyde dehydrogenase activity, m- ... propionaldehyde dehydrogenase activity, CoA-independent aldehyde dehydrogenase activity, NAD-aldehyde dehydrogenase activity, ... NAD-aldehyde dehydrogenase activity, NAD-dependent 4-hydroxynonenal dehydrogenase activity, NAD-dependent aldehyde ...

https://www.yeastgenome.org/go/GO:0004029

aldehyde dehydrogenase X, mitochondrial. Names. ALDH class 2. acetaldehyde dehydrogenase 5. aldehyde dehydrogenase 5. ... ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo sapiens] ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo ... This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... aldehyde dehydrogenase 1 family member B1provided by HGNC. Primary source. HGNC:HGNC:407 See related. Ensembl:ENSG00000137124 ...

https://www.ncbi.nlm.nih.gov/gene/219

Aldehyde dehydrogenase activity promotes survival of human muscle precursor cells.. Jean E1, Laoudj-Chenivesse D, Notarnicola C ... Aldehyde dehydrogenases (ALDH) are a family of enzymes that efficiently detoxify aldehydic products generated by reactive ...

https://www.ncbi.nlm.nih.gov/pubmed/19840193?dopt=Abstract

Keywords: Arabidopsis thaliana; Craterostigma plantagineum; abscisic acid; aldehyde dehydrogenase; dehydration; enzyme activity ... Phylogenetically, the Cp- and Ath-ALDH3 and -ALDH4 proteins are closely related to aldehyde dehydrogenases from bacteria and ... Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma ... a gene was isolated with homology to class 3 variable substrate aldehyde dehydrogenases (ALDH). The C. plantagineum gene Cp- ...

https://www.ingentaconnect.com/content/bsc/tpj/2001/00000028/00000005/art00006

tr,A0A658YN00,A0A658YN00_CAMCO Aldehyde dehydrogenase OS=Campylobacter coli OX=195 GN=aldA PE=4 SV=1 ... Aldehyde dehydrogenase. Lacticaseibacillus paracasei subsp. tolerans. 488. Aldehyde dehydrogenase. Lactobacillus sp. HMSC25A02 ...

https://www.uniprot.org/uniprot/A0A658YN00

SEARCH RESULTS for: Acetyl Aldehyde Dehydrogenase Inhibitors [Drug Class] (10 results) * Share : JavaScript needed for Sharing ...

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

Aldehyde dehydrogenases (ALDHs) are highly expressed in the chemotherapy- and radiotherapy-resistant cell subpopulations of ... Aldehyde Dehydrogenase Inhibitors for Cancer Therapeutics Trends Pharmacol Sci. 2019 Oct;40(10):774-789. doi: 10.1016/j.tips. ... Aldehyde dehydrogenases (ALDHs) are highly expressed in the chemotherapy- and radiotherapy-resistant cell subpopulations of ... Keywords: aldehyde dehydrogenase; cancer pharmacology; cancer resistance; cancer stem cells; cancer therapy; targeted ...

https://pubmed.ncbi.nlm.nih.gov/31515079/

BETAINE ALDEHYDE DEHYDROGENASE. A, B, D, F, G, H. 490. Pseudomonas aeruginosa. Mutation(s): 0 EC: 1.2.1.8. ... BETAINE ALDEHYDE DEHYDROGENASE. C, E. 490. Pseudomonas aeruginosa. Mutation(s): 0 EC: 1.2.1.8. ... In the human pathogen Pseudomonas aeruginosa, the NAD(P)(+)-dependent betaine aldehyde dehydrogenase (PaBADH) may play the dual ... In the human pathogen Pseudomonas aeruginosa, the NAD(P)(+)-dependent betaine aldehyde dehydrogenase (PaBADH) may play the dual ...

https://www.rcsb.org/structure/2WME

2011) Aldehyde dehydrogenase: Its role as a cancer stem cell marker comes down to the specific isoform. Cell Cycle 10(9):1378- ... Aldehyde Dehydrogenase 1A3 Activity Is Markedly Elevated in Mes GSCs Compared with Mes Non-GSCs and PN GSCs.. Based on the ... 2009) Aldehyde dehydrogenase 1 is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation ... 2011) Aldehyde dehydrogenase activity of breast cancer stem cells is primarily due to isoform ALDH1A3 and its expression is ...

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

We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze ... Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?. Jennifer M. Petrosino. ... Petrosino, J.M.; DiSilvestro, D.; Ziouzenkova, O. Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism? Nutrients ... "Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?" Nutrients 6, no. 3: 950-973. ...

http://mdpi.com/2072-6643/6/3/950

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

http://www.rcsb.org/pdb/protein/P11883

Inhibition of aldehyde dehydrogenase and retinoid signaling induces the expansion of human hematopoietic stem cells. John P. ... Aldehyde dehydrogenase (ALDH) is an enzyme that is expressed in the liver and is required for the conversion of retinol ( ... Inhibition of aldehyde dehydrogenase and retinoid signaling induces the expansion of human hematopoietic stem cells ... Inhibition of aldehyde dehydrogenase and retinoid signaling induces the expansion of human hematopoietic stem cells ...

https://www.pnas.org/content/103/31/11707

Compare aldehyde dehydrogenase 1 family member L1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices ... aldehyde dehydrogenase 1 family member L1 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established ... Your search returned 21 aldehyde dehydrogenase 1 family member L1 ELISA ELISA Kit across 3 suppliers. ...

https://www.biocompare.com/pfu/110627/soids/2-2266136/ELISA_Kit/ELISA_aldehyde_dehydrogenase_1_family_member_L1

Compare Anti-aldehyde dehydrogenase 5 family member A1 Antibody Products from leading suppliers on Biocompare. View ... Anti-aldehyde dehydrogenase 5 family member A1 Antibody Products. Anti-Aldehyde dehydrogenase 5 family member A1 antibodies are ... Your search returned 192 aldehyde dehydrogenase 5 family member A1 Antibodies across 28 suppliers. ... The protein may also be known as SSADH, SSDH, succinate-semialdehyde dehydrogenase, mitochondrial, and NAD(+)-dependent ...

https://www.biocompare.com/pfu/110447/soids/2269678/Antibodies/aldehyde_dehydrogenase_5_family_member_A1

"Distribution of messenger RNAs for aldehyde dehydrogenase 1, aldehyde dehydrogenase 2, and aldehyde dehydrogenase 5 in human ... M.-K. Chern and R. Pietruszko, "Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase," Biochemical and ... G.-S. Peng and S.-J. Yin, "Effect of the allelic variants of aldehyde dehydrogenase ALDH2∗2 and alcohol dehydrogenase ADH1B∗2 ... "Aldehyde dehydrogenase 2 (ALDH2) rescues myocardial ischaemia/reperfusion injury: role of autophagy paradox and toxic aldehyde ...

https://www.hindawi.com/journals/bmri/2015/174050/

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

https://link.springer.com/article/10.1007%2Fs00425-015-2290-8

AcrR and Rex Control Mannitol and Sorbitol Utilization through Their Cross-Regulation of Aldehyde-Alcohol Dehydrogenase (AdhE) ...

https://aem.asm.org/keyword/aldehyde-alcohol-dehydrogenase-adhe

ALDH, aldehyde dehydrogenase; BALDH, betaine aldehyde dehydrogenase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GGSALDH, ... Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes. ... Hydrazone dehydrogenase, which belongs to the aldehyde dehydrogenase (ALDH) superfamily, attacked the C=N double bond of ... Group X Aldehyde Dehydrogenases of Pseudomonas aeruginosa PAO1 Degrade Hydrazones. Kosuke Taniyama, Hideomi Itoh, Atsushi ...

https://jb.asm.org/content/194/6/1447

Vascular bioactivation of nitroglycerin is catalyzed by cytosolic aldehyde dehydrogenase-2. Download Prime PubMed App to iPhone ... AdenoviridaeAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialAnimalsAortaBiotransformationCell LineCytosolDNAHumans ... Bioactivation of pentaerythrityl tetranitrate by mitochondrial aldehyde dehydrogenase.. *Potent inhibition of aldehyde ... Changes in aldehyde dehydrogenase 2 expression in rat blood vessels during glyceryl trinitrate tolerance development and ...

https://www.unboundmedicine.com/medline/citation/22207712/Vascular_bioactivation_of_nitroglycerin_is_catalyzed_by_cytosolic_aldehyde_dehydrogenase_2_

IPR015590 Aldehyde dehydrogenase domain. IPR029510 Aldehyde dehydrogenase, glutamic acid active site. IPR016162 Aldehyde ...

http://www.informatics.jax.org/marker/MGI:108186

IPR016163 Aldehyde dehydrogenase, C-terminal. IPR015590 Aldehyde dehydrogenase domain. IPR016162 Aldehyde dehydrogenase, N- ...

http://www.informatics.jax.org/marker/MGI:1916998

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

https://medical-dictionary.thefreedictionary.com/aldehyde+dehydrogenase+3B1

... we investigated the genotype of aldehyde dehydrogenase (ALDH) 2 and alcohol dehydrogenase 2 (ADH2) in DM-Mt3243. ... Mitochondrial Aldehyde Dehydrogenase in Diabetes Associated With Mitochondrial tRNALeu(UUR) Mutation at Position 3243. ... Mitochondrial Aldehyde Dehydrogenase in Diabetes Associated With Mitochondrial tRNALeu(UUR) Mutation at Position 3243 ... Mitochondrial Aldehyde Dehydrogenase in Diabetes Associated With Mitochondrial tRNALeu(UUR) Mutation at Position 3243 ...

https://care.diabetesjournals.org/content/19/12/1423

Or ALDH, this breaks down various aldehyde s into the corresponding carboxylic acid s. (everything2.com)
Aldehyde dehydrogenases (ALDH) are a family of enzymes that efficiently detoxify aldehydic products generated by reactive oxygen species and might therefore participate in cell survival. (nih.gov)
In order to identify genes that are critical for the ABA-dependent stress response in the resurrection plant Craterostigma plantagineum , a gene was isolated with homology to class 3 variable substrate aldehyde dehydrogenases (ALDH). (ingentaconnect.com)
Aldehyde dehydrogenase (ALDH) is an enzyme that is expressed in the liver and is required for the conversion of retinol (vitamin A) to retinoic acids. (pnas.org)
9 , 10 ) demonstrated that the intracellular enzyme, aldehyde dehydrogenase (ALDH), protected BM progenitors from the cytotoxic effects of cyclophosphamide by deactivation of its metabolite, 4-hydroxycyclophosphamide ( 9 , 10 ). (pnas.org)
Aldehyde dehydrogenase (ALDH) 2 is a mitochondrial enzyme that is known for its important role in oxidation and detoxification of ethanol metabolite acetaldehyde. (hindawi.com)
Aldehyde dehydrogenase (ALDH) 2 is a mitochondrial enzyme that catalyzes the oxidation of acetaldehyde, an intermediate of ethanol metabolism [ 1 ]. (hindawi.com)
Aldehyde dehydrogenase (ALDH) is a family of enzymes catalyzing the irreversible conversion of aldehydes into acids to decrease the damage caused by abiotic stresses. (springer.com)
Gene cloning indicated that the HDH is part of the group X aldehyde dehydrogenase (ALDH) family, which is distributed among bacteria, although the physiological roles of the ALDH family remain unknown. (asm.org)
OBJECTIVE To ascertain why alcohol is prone to manifest unpleasant effects in diabetes associated with mitochondrial tRNA Leu(UUR) mutation at position 3243 (DM-Mt3243), we investigated the genotype of aldehyde dehydrogenase (ALDH) 2 and alcohol dehydrogenase 2 (ADH2) in DM-Mt3243. (diabetesjournals.org)
In many types of tumors, especially breast tumors, aldehyde dehydrogenase (ALDH) activity has been used to identify cancer stem-like cells within the tumor. (dovepress.com)
ALDH activity measured fluorimetrically using a high concentration of aliphatic aldehyde as substrate was studied in human glioblastomas grafted in nude mice. (springer.com)
In view of previous works, these results suggest a relationship between alterations in ALDH iso-enzymes activities and cytosolic aldehyde concentrations with respect to normal or tumoral cell growth. (springer.com)
Important thing to know is that ALDH oxidizes aldehydes to carboxylic acids. (steadyhealth.com)
Experts are saying that Aldehyde dehydrogenase (ALDH) is functioning often in tandem with Alcohol dehydrogenase. (steadyhealth.com)
Using a rat model, we then showed that nociception tightly correlated with ALDH activity ( R 2 = 0.90) and that reduced nociception was associated with less early growth response protein 1 (EGR1) in the spinal cord and less reactive aldehyde accumulation at the insult site (including acetaldehyde and 4-hydroxynonenal). (sciencemag.org)
Background and Objectives Primitive human hematopoietic cells contain higher levels of aldehyde dehydrogenase (ALDH) activity than their terminally differentiating progeny but the particular stages at which ALDH levels change have not been well defined. (haematologica.org)
A complementary strategy for the functional identification and characterization of normal stem cells and their malignant counterparts involves the measurement of aldehyde dehydrogenase (ALDH) activity. (aacrjournals.org)
Aldehyde dehydrogenase (ALDH) 1A enzymes produce retinoic acid (RA), a transcription induction molecule. (ovid.com)
High aldehyde dehydrogenase (ALDH hi ) activity has been reported in normal and cancer stem cells. (frontiersin.org)
A widely used universal stem cell marker is aldehyde dehydrogenase (ALDH) ( 6 - 8 ). (frontiersin.org)
ALDH is a generic designation for a superfamily of NAD-dependent enzymes that catalyze the oxidation of aldehydes to acids. (frontiersin.org)
In the course of engineering these strains, a number of mutations have been discovered in their adhE genes, which encode both alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes. (asm.org)
Aldehyde dehydrogenase (ALDH) enzymes catalyze the NAD(P)+-dependent oxidation of a wide variety of endogenous and exogenous aldehydes to their corresponding acids. (ovid.com)
Here, we isolated by fluorescence activated cell sorting technique, two populations of Wharton's jelly (WJ)-MSCs based on their aldehyde dehydrogenase (ALDH) activity. (springer.com)
This reaction could take place by two different methods: via an acylating aldehyde dehydrogenase (ALDH) that could catalyze the reaction to yield pimeloyl-CoA in one step or via the oxidation of pimelic semialdehyde to pimelic acid by a nonacylating ALDH, including its subsequent activation by a CoA-ligase or a CoA-transferase. (pubmedcentralcanada.ca)
Before determining the IC50's for the Aldehyde Dehydrogenase (ALDH) inhibitor, we performed some initial experiments to establish appropriate assay conditions. (bioassaysys.com)
The IC50 determination required two steps: 1) 20 min pre-incubation of 45 µL ALDH (1.3 U/rxn) with 5 µL disulfiram in 100% DMSO, and 2) aldehyde dehydrogenase reaction with 900 µM final [acetaldehyde] for 30 min at 25°C. We titrated disulfiram from 0-50 µM and computed the ΔOD for each inhibitor concentration. (bioassaysys.com)
CSCs were isolated from SUM149 and MARY-X, an IBC cell line and primary xenograft, by virtue of increased aldehyde dehydrogenase (ALDH) activity as assessed by the ALDEFLUOR assay. (aacrjournals.org)
Lung cancer stem cells (CSC) with elevated aldehyde dehydrogenase (ALDH) activity are self-renewing, clonogenic, and tumorigenic. (aacrjournals.org)
This ELISA kit is based on the principle of double-antibody sandwich technique to detect Rat aldehyde dehydrogenase,ALDH ELISA Kit Be used only for research purposes, not be used for medical diagnosis. (ttnet.net)
BACKGROUND/OBJECTIVES: Heavy alcohol drinking is a risk factor of colorectal cancer (CRC), but little is known on the effect of polymorphisms in the alcohol-metabolizing enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) on the alcohol-related risk of CRC in Caucasian populations. (lu.se)
article{01d9c5b7-1e40-4ebf-9258-6769f39c0b13, abstract = {BACKGROUND/OBJECTIVES: Heavy alcohol drinking is a risk factor of colorectal cancer (CRC), but little is known on the effect of polymorphisms in the alcohol-metabolizing enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) on the alcohol-related risk of CRC in Caucasian populations. (lu.se)
Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes that are responsible for clearance of aldehydes in the body. (eurekaselect.com)
Among the isoenzymes of ALDH, ALDH2 is believed to play a major role in clearance of toxic aldehydes. (eurekaselect.com)
After transplantation into β-glucuronidase (GUSB)-deficient NOD/SCID/mucopolysaccharidosis type VII mice, we characterized the distribution of lineage-depleted human umbilical cord blood-derived cells purified by selection using high aldehyde dehydrogenase (ALDH) activity with CD133 coexpression. (elsevier.com)
Aldehyde dehydrogenase (ALDH) activity is commonly used as a marker to identify cancer stem-like cells. (iupui.edu)
The second step of RA synthesis is controlled by members of the aldehyde dehydrogenase (ALDH) family also known as retinaldehyde dehydrogenase (RALDH) that further oxidize retinaldehyde to produce RA. (ozgene.com)
The purpose of this comprehensive meta-analysis was to assess the association of aldehyde dehydrogenase (ALDH) expression with overall survival (OS) and disease-free survival (DFS)/progression-free survival (PFS) in ovarian cancer patients. (biomedcentral.com)
Many ALDH isozymes are important in oxidizing reactive aldehydes derived from lipid peroxidation and thereby help maintain cellular homeostasis. (medchemexpress.com)
NCT-501 is a potent and selective theophylline-based inhibitor of aldehyde dehydrogenase 1A1 (ALDH1A1) , inhibits hALDH1A1 with IC 50 of 40 nM, typically shows better selectivity over other ALDH isozymes and other dehydrogenases (hALDH1B1, hALDH3A1, and hALDH2, IC 50 >57 μM). (medchemexpress.com)
CVT-10216 is a highly selective, reversible aldehyde dehydrogenase-2 (ALDH-2) inhibitor with an IC 50 of 29 nM. (medchemexpress.com)

ALDH1 and ALDH2 are the most important enzymes for aldehyde oxidation, and both are tetrameric enzymes composed of 54 kDa subunits. (wikipedia.org)
There is a mutant form of aldehyde dehydrogenase, termed ALDH2*2, wherein a lysine residue replaces a glutamate in the active site at position 487 of ALDH2. (wikipedia.org)
ALDH2 also metabolizes other reactive aldehydes such as 4-hydroxy-2-nonenal and acrolein. (hindawi.com)
In addition, ALDH2 is important for the detoxification of reactive aldehydes such as 4-HNE and acrolein [ 2 ]. (hindawi.com)
ALDH2 may be one of the essential mechanisms for the removal of these reactive aldehydes and protecting cells and organs from these toxic aldehydes. (hindawi.com)
According to general view, aldehyde dehydrogenase-2 (ALDH2) catalyzes the high-affinity pathway of vascular nitroglycerin (GTN) bioactivation in smooth muscle mitochondria. (unboundmedicine.com)
To be more precise - two acetaldehyde dehydrogenase isozymes, cytosolic (ALDH1) and mitochondrial (ALDH2), catalyze this reaction. (steadyhealth.com)
Exogenous aldehydes can cause pain in animal models, suggesting that aldehyde dehydrogenase-2 (ALDH2), which metabolizes many aldehydes, may regulate nociception. (sciencemag.org)
The atypical genotypes of low K m aldehyde dehydrogenase (ALDH2) have higher blood concentrations of free acetaldehyde after drinking alcohol. (aacrjournals.org)
To elucidate the mechanism underlying reduction of nitroglycerin (GTN) to nitric oxide (NO) by mitochondrial aldehyde dehydrogenase (ALDH2), we generated mutants of the enzyme lacking the cysteines adjacent to reactive Cys302 (C301S and C303S), the glutamate that participates as a general base in aldehyde oxidation (E268Q) or combinations of these residues. (aspetjournals.org)
Mitochondrial aldehyde dehydrogenase (ALDH2) displays some promise in the protection against cardiovascular diseases although its role in diabetes has not been elucidated. (biomedcentral.com)
Reactive aldehydes contribute to pain pathologies and cardiac injury, suggesting that aldehyde dehydrogenase (ALDH2), which detoxifies aldehydes, may regulate chronic pain related MI/R injury. (onlinejacc.org)
However, treatment of CCD-WT mice with ALDH2-selective activator (Alda-1) significantly reduced chronic neuropathic pain-induced SIRT1 carbonylative inactivation and decreased MI/R injury (minor infarct size, less apoptosis, and elevated cardiac function) likely as a result of prevented aldehyde overload and carbonyl stress. (onlinejacc.org)
ALDH2 activation blocked reactive aldehyde overproduction induced carbonyl stress and attenuated ischemic vulnerability in chronic pain individual. (onlinejacc.org)
Aldehyde dehydrogenase 2 (ALDH2) is an anti-apoptotic enzyme whose activity decline associates with myocardial injury. (eurekaselect.com)
Genetic variation in alcohol dehydrogenase (ADH1A, ADH1B, ADH1C, ADH7) and aldehyde dehydrogenase (ALDH2), alcohol consumption and gastric cancer risk in the European Prospective Investigation into Cancer and Nutrition (EPIC) cohort. (environment-health.ac.uk)
ADH7 and aldehyde dehydrogenase, ALDH2), alcohol intake and GC risk. (environment-health.ac.uk)
Acetaldehyde dehydrogenase 2 (ALDH2) is the key enzyme responsible for metabolism of the alcohol metabolite acetaldehyde in the liver. (ijbs.com)
4-Hydroxynonenal is a substrate and an inhibitor of acetaldehyde dehydrogenase 2 (ALDH2) . (medchemexpress.com)

acted upon by another enzyme, aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ultimately oxidized to carbon dioxide and water. (britannica.com)
Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the liver and are metabolized by the body's muscle and heart. (wikipedia.org)
The active site of the aldehyde dehydrogenase enzyme is largely conserved throughout the different classes of the enzyme and, although the number of amino acids present in a subunit can change, the overall function of the site changes little. (wikipedia.org)
A magnesium may be used to help the enzyme function, although the amount it helps the enzyme can vary between different classes of aldehydes. (wikipedia.org)
The overall reaction catalysed by the aldehyde dehydrogenases is: RCHO + NAD+ + H2O → RCOOH + NADH + H+ In this NAD(P)+-dependent reaction, the aldehyde enters the active site through a channel extending from the surface of the enzyme. (wikipedia.org)
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde + NAD+ + H2O ⇌ {\displaystyle \rightleftharpoons } betaine + NADH + 2 H+ The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, NADH, and H+. (wikipedia.org)
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. (wikipedia.org)
The systematic name of this enzyme class is betaine-aldehyde:NAD+ oxidoreductase. (wikipedia.org)
The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups. (ebi.ac.uk)
Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. (nih.gov)
[1] [2] This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP - and NADPH -dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities. (wikidoc.org)
Succinate-semialdehyde dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH5A1 gene . (wikidoc.org)
Low-autocrine RA generation by the cytosolic aldehyde dehydrogenase 1 (Aldh1a1, -a2, and -a3) enzyme family ( 14 ) stimulates adipogenesis via mechanisms dependent on transcription factors ZFP423 and PPARγ ( 15 ). (diabetesjournals.org)
The 3 substrates of this enzyme are betaine aldehyde , NAD + , and H 2 O , whereas its 3 products are betaine , NADH , and H + . (academic.ru)
Aldehyde dehydrogenase is the next enzyme after alcohol dehydrogenase in the major pathway of alcohol metabolism. (creative-biogene.com)
Lack of the cysteines did not affect dehydrogenase activity but impeded GTN denitration, aggravated GTN-induced enzyme inactivation, and increased NO formation. (aspetjournals.org)
Gene expression studies indicate that the RF2C gene, which is strongly expressed in all organs, appears essential, suggesting that the crucial role of the enzyme would certainly be linked to the cell wall formation using aldehydes from phenylpropanoid pathway as substrates. (biochemj.org)
The kinetic properties of the mitochondrial enzyme, compared with those reported for the cytoplasmic aldehyde dehydrogenase from sheep liver, show significant differences, which may be important in the oxidation of aldehydes in vivo. (biochemj.org)
There is a deficiency of an enzyme called fatty aldehyde dehydrogenase 10 (FALDH10)in the Sjogren-Larsson syndrome. (drugster.info)

The topic of this work is of major importance since we show that invasion and metastasis in IBC are mediated by a cellular subcomponent with stem cell characteristics expressing the stem cell marker aldehyde dehydrogenase 1 (ALDH1). (aacrjournals.org)
To determine the differences in response following the use of aldehyde dehydrogenase 1 (ALDH1) and Raf kinase inhibitor protein (RKIP) as cervical cancer stem cell markers. (ajol.info)
In models of triple-negative breast cancer (TNBC), it has recently been shown that the epidermal growth factor receptor (EGFR) pathway is up-regulated in the aldehyde dehydrogenase 1 (ALDH1)-positive cancer stem cell fraction. (uzh.ch)
SR-T100 downregulated the expression of stem cell markers, including aldehyde dehydrogenase 1 (ALDH1), Notch1, and FoxM1, and reduced sphere formation in ovarian cancer cells. (jcancer.org)
The present study is to determine the expression of aldehyde dehydrogenase 1 (ALDH1) and ATPbinding cassette superfamily G member 2 (ABCG2) in patients with triple-negative breast cancer, and to understand the relationship of ALDH1 and ABCG2 with triple-negative breast cancer. (alliedacademies.org)
Disulfiram (Tetraethylthiuram disulfide) is a specific inhibitor of aldehyde-dehydrogenase (ALDH1) , used for the treatment of chronic alcoholism by producing an acute sensitivity to alcohol. (medchemexpress.com)
4-Diethylaminobenzaldehyde is a reversible aldehyde dehydrogenases (ALDHs) inhibitor, with a K i of 4 nM for ALDH1. (medchemexpress.com)

The active site of a human mitochondrial aldehyde dehydrogenase 2. (wikipedia.org)
Kinetic studies were carried out on mitochondrial aldehyde dehydrogenase (EC 1.2.1.3) isolated from sheep liver. (biochemj.org)
Xiu-Ju Luo, Bin Liu, Qi-Lin Ma and Jun Peng, "Mitochondrial Aldehyde Dehydrogenase, A Potential Drug Target for Protection of Heart and Brain from Ischemia/Reperfusion Injury", Current Drug Targets (2014) 15: 948. (eurekaselect.com)

A gene on chromosome 11q13 that encodes an aldehyde dehydrogenase that plays a major role in detoxifying aldehydes generated by alcohol metabolism and lipid peroxidation. (thefreedictionary.com)
This gene encodes a mitochondrial NAD + -dependent succinic semialdehyde dehydrogenase . (wikidoc.org)
Gene expression profiling revealed that Aldehyde dehydrogenase 1 family, member A3 (ALDH1A3) is up regulated in OcMMP. (bl.uk)
The gene products are similar to nonacylating aldehyde dehydrogenases (ThnG) and to proteins representing a complete beta-oxidation pathway (ThnH to ThnP). (sigmaaldrich.com)
A gene on chromosome 17p11.2 that encodes an aldehyde dehydrogenase that plays a major role in detoxifying alcohol-derived acetaldehyde, metabolising corticosteroids, biogenic amines, neurotransmitters and in lipid peroxidation. (thefreedictionary.com)
The ALDH3A1 gene product forms a homodimer that preferentially oxidises aromatic and medium-chain (6 carbons or more) saturated and unsaturated aldehyde substrates. (thefreedictionary.com)
The qualitative change requires the derepression of a gene for an aldehyde dehydrogenase expressed in normal liver only after exposure to potentially harmful xenobiotics. (portlandpress.com)
Holmes, R. S., 1977, The genetics of a-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3, Genetics 87:709. (springer.com)
Holmes, R. S., 1979a, Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse - evidence for a cis-acting regulator gene (Adh-3-t) controlling C 2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adh-3-t on chromosome 3, Biochem. (springer.com)
The protein encoded by this gene belongs to the aldehyde dehydrogenase family. (creative-biogene.com)
The ABA2 gene product belongs to the family of short-chain dehydrogenases/reductases, which are known to be NAD- or NADP-dependent oxidoreductases. (plantcell.org)

Hellström E, Tottmar O: Effects of aldehyde dehydrogenase inhibitors on enzymes involved in the metabolism of biogenic aldehydes in rat liver and brain. (springer.com)

Aldehyde dehydrogenases (ALDHs) constitute a superfamily of NAD(P) + -dependent enzymes that catalyse irreversible oxidation of aldehydes to the corresponding carboxylic acids. (biochemj.org)
Aldehyde Dehydrogenases (ALDHs) are a superfamily of NADP + -dependent enzymes that metabolize endogenous and exogenous aldehydes to corresponding carboxylic acids. (medchemexpress.com)

We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze conversion of retinaldehyde to retinoic acid. (mdpi.com)
We investigated the role of retinoic acid (RA) production by aldehyde dehydrogenase 1 (Aldh1a1, -a2, and -a3), the major RA-producing enzymes on sex-specific fat depot formation. (diabetesjournals.org)
CM10 is a potent and selective aldehyde dehydrogenase 1A (ALDH1A) family inhibitor, with IC 50 s of 1700, 740, and 640 nM for ALDH1A1, ALDH1A2, and ALDH1A3, respectively. (medchemexpress.com)

Conversely, aldehyde dehydrogenase activation using retinoic acid added to control conjunctival fibroblasts cultures promoted OcMMP-like phenotype in the scarring assays. (bl.uk)
Finally, the three retinaldehyde dehydrogenases cooperatively mediate retinoic acid signaling during the eye development. (ovid.com)

The protein may also be known as SSADH, SSDH, succinate-semialdehyde dehydrogenase, mitochondrial, and NAD(+)-dependent succinic semialdehyde dehydrogenase. (biocompare.com)
aldh5a1 has several biochemical functions, for example, aldehyde dehydrogenase (NAD) activity, protein homodimerization activity, succinate-semialdehyde dehydrogenase (NAD+) activity. (creativebiomart.net)

A fluorimetric assay of aldehyde dehydrogenase isozymes, based on naphthaldehyde oxidation, is compared with Western Blotting analysis on several clinical samples obtained from surgery. (mdpi.com)
Characterization of aldehyde dehydrogenase isozymes in ovarian cancer tissues and sphere cultures. (harvard.edu)
Holmes, R.S., 1978b, Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: localization of Ahd-1 encoding the mitochondrial isozymes on chromosome 4, Biochem. (springer.com)
Holmes, R. S., 1979b, Genetics, ontogeny and testosterone inducibility of aldehyde oxidase isozymes in the mouse: evidence for two genetic loci (Aox-1 and Aox-2) closely linked on chromosome 1, Biochem. (springer.com)
There are two major aldehyde dehydrogenase isozymes in the liver, cytosolic and mitochondrial, which are encoded by distinct genes, and can be distinguished by their electrophoretic mobility, kinetic properties, and subcellular localization. (creative-biogene.com)

Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. (wikipedia.org)
Aldehyde oxidase ( EC:1.2.3.1 ) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. (ebi.ac.uk)
The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [ PMID: 7502041 , PMID: 10430865 ]. (ebi.ac.uk)
Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. (ebi.ac.uk)
Ahd-1 (encoding AHD-A 2 ) was found on chromosome 4 near Gpd-1 (encoding the liver isozyme of glucose-6-phosphate dehydrogenase), whereas the aldehyde oxidase loci (Aox-1, Aox-2) were closely linked on chromosome 1 near Id-1 (encoding isocitrate dehydrogenase). (springer.com)
Here we describe the immobilisation of two biocatalytically relevant co-factor recycling enzymes, glucose dehydrogenase (GDH) and NADH oxidase (NOD) on aldehyde functional ReSynTM polymer microspheres with varying functional group densities. (csir.co.za)

Disulfiram labeled with carbon-14 reacts specifically with human liver aldehyde dehydrogenase E1 with loss of catalytic activity and no incorporation of label. (sciencemag.org)
The subcellular distribution and properties of four aldehyde dehydrogenase isoenzymes (I-IV) identified in 2-acetylaminofluorene-induced rat hepatomas and three aldehyde dehydrogenases (I-III) identified in normal rat liver are compared. (portlandpress.com)
In normal liver, mitochondria (50%) and microsomal fraction (27%) possess the majority of the aldehyde dehydrogenase, with cytosol possessing little, if any, activity. (portlandpress.com)
The quantitative change involves both an increase in activity and a change in subcellular location of a basal normal-liver aldehyde dehydrogenase isoenzyme. (portlandpress.com)
Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. (biochemj.org)
Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations. (mybiosource.com)

4-HNE is an α , β -unsaturated aldehyde formed during lipid peroxidation in vivo [ 17 ]. (hindawi.com)
Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. (biochemj.org)

Several researches done in the past have proven that Aldehyde Dehydrogenases are able to oxidize a wide range of endogenous and exogenous aldehydes. (steadyhealth.com)

They convert aldehydes (R-C(=O)-H) to carboxylic acids (R-C(=O)-O-H). The oxygen comes from a water molecule. (wikipedia.org)

We offer Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs for use in common research applications: Immunoprecipitation, Sandwich ELISA, Western Blot. (novusbio.com)
Each Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pair is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
Our Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs can be used in a variety of model species: Human. (novusbio.com)
Choose from our Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody Pairs. (novusbio.com)

Enzymatic activity analysis showed that TraeALDH7B1-5A had acetaldehyde dehydrogenase activity. (springer.com)

A cysteine and a glutamate will interact with the aldehyde substrate. (wikipedia.org)
Cys302 and Glu268 interact with the aldehyde substrate. (wikipedia.org)
There is no doubt- aldehyde dehydrogenases have broad substrate specificity. (steadyhealth.com)
Isoenzymes I-III can be identified in both fractions and differ from each other on the basis of substrate and coenzyme specificity, substrate K m , inhibition by disulfiram and anti-(hepatoma aldehyde dehydrogenase) sera, and/or isoelectric point. (portlandpress.com)

Oxidation of aldehydes is considered to be generally a detoxification reaction because it is based on removing the electrophilic products of alcohol oxidation. (steadyhealth.com)
It is proven that alcohol dehydrogenase oxidizes ethanol to acetaldehyde, which is responsible for some hangover symptoms. (steadyhealth.com)
There is a single major alcohol dehydrogenase (ADH) and a single major aldehyde dehydrogenase (AldDH) in Aspergillus nidulans . (royalsocietypublishing.org)
Below are the list of possible Aldehyde-alcohol dehydrogenase products. (mybiosource.com)
Alcohol and aldehyde dehydrogenases: Retinoid metabolic effects in mouse knockout models. (ozgene.com)
The first step of RA synthesis is controlled by enzymes of the alcohol dehydrogenase (ADH) and retinol dehydrogenase (RDH) families that catalyze oxidation of retinol to retinaldehyde. (ozgene.com)

Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism? (mdpi.com)
Endogenous aldehydes are generated during the metabolism of amino acids, carbohydrates, lipids, and vitamins as well as the biotransformation of many drugs and environmental chemicals [ 10 , 13 - 15 ]. (hindawi.com)
It is important to know that aldehydes are substances formed during the metabolism of amino acids, carbohydrates, lipids, biogenic amines, vitamins, and steroids. (steadyhealth.com)
Glutaryl-CoA dehydrogenase (ThnN) would catalyze the oxidation and decarboxylation of glutaryl-CoA and yield crotonyl-CoA, which enters the central metabolism via acetyl-CoA. (sigmaaldrich.com)

Phylogenetically, the Cp- and Ath-ALDH3 and -ALDH4 proteins are closely related to aldehyde dehydrogenases from bacteria and mammalian species and are separated from known plant ALDHs and betaine-aldehyde dehydrogenases (BADH). (ingentaconnect.com)

Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. (yeastgenome.org)

Aldehyde dehydrogenases (ALDHs) are highly expressed in the chemotherapy- and radiotherapy-resistant cell subpopulations of many different cancer types. (nih.gov)
Thus, the detoxification of harmful aldehydes generated endogenously or ingested from environment and foods is an important role of ALDHs. (hindawi.com)
Therefore, ALDHs play a crucial role in detoxifying aldehydes produced by various metabolic pathways. (biochemj.org)

Addition of disulfiram, a selective aldehyde dehydrogenase inhibitor restored phenotype and function of OcMMP fibroblasts to control cell levels. (bl.uk)
The data indicate that the tumour-specific aldehyde dehydrogenase phenotype is explainable by qualitative and quantitative changes involving primarily cytosolic and microsomal aldehyde dehydrogenase. (portlandpress.com)

This protein belongs to the aldehyde dehydrogenases family of proteins. (nih.gov)
On the other hand, aldehydes are highly reactive compounds, which can form adducts with proteins, DNA, and lipids, affecting the function of these biomolecules and leading to cell toxicity. (hindawi.com)
Down-regulation of aldehyde dehydrogenase 1A1 in Clone #3 CM and gelsolin levels in Clone #8 CM by siRNA transfection revealed an important involvement of these proteins in promoting and inhibiting invasion in these pancreatic cancer cell lines. (dcu.ie)

Ogier G, Chantepie J, Quash G, Doutheau A, Gord J, Marion C: The effect of a novel inhibitor of aldehyde dehydrogenase on viral replication. (springer.com)

It is also important in metabolizing other toxic aldehydes such as 4-hydroxy-2-nonenal (4-HNE) and acrolein [ 2 ]. (hindawi.com)
In animal myocardial or cerebral ischemia/ reperfusion (I/R) models, accumulation of toxic aldehydes, such as 4-hydroxy-2-nonenal and malondialdehyde, is thought to be an important mechanism for myocardial and cerebral I/R injury. (eurekaselect.com)

Aldehyde dehydrogenase activity promotes survival of human muscle precursor cells. (nih.gov)
Aldehyde dehydrogenase activity in xenografted human brain tumor in nude mice. (springer.com)
Koivula T, Turner AJ, Huttunen M, Koivusalo M: Subcellular and perisynaptic distribution of rat brain aldehyde dehydrogenase activity. (springer.com)
Harvey WK, Lindahl R: Activity of various aldehyde-metabolizing enzymes in chemically-induced rat hepatomas. (springer.com)
Perin A, Sessa A, Ciaranfi E: Carcinostatic effect of aliphatic aldehydes and aldehyde dehydrogenase activity in Ehrlich carcinoma, Sarcoma 180, and Yoshida AH 130 hepatoma. (springer.com)
ThnG has a nonacylating NAD-dependent pimelic semialdehyde dehydrogenase activity that renders pimelic acid a seven-carbon dicarboxylic acid. (sigmaaldrich.com)
Mutagenesis studies have shown that these genes are not essential for growth on tetralin or fatty acids, although a thnG disruption mutant showed threefold less pimelic semialdehyde dehydrogenase activity. (sigmaaldrich.com)
Hepatomas possess considerable cytosolic aldehyde dehydrogenase (20%), in addition to mitochondrial (23%) and microsomal (35%) activity. (portlandpress.com)
Nolta, Jan A. / Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase activity . (elsevier.com)

Inoue K, Lindros KO: Subcellular distribution of human brain aldehyde dehydrogenase. (springer.com)
Canuto RA, Garcea R, Biocca M, Pascale R, Pirisi L, Feo F: The subcellular distribution and properties of aldehyde dehydrogenase of hepatoma AH-130. (springer.com)

This fatty aldehyde dehydrogenase deficiency is in fact a genetic disease. (steadyhealth.com)
Restoration of fatty aldehyde dehydrogenase deficiency in SjÃ¶gren-Larsson syndrome. (drugster.info)

Aldehyde dehydrogenases (EC 1.2.1.3) are a group of enzymes that catalyse the oxidation of aldehydes. (wikipedia.org)
Well, it is very important to know that aldehyde dehydrogenases are also a group of enzymes that catalyse the oxidation or dehydrogenation of aldehydes. (steadyhealth.com)

One theory is that a certain type of stem cell, aldehyde dehydrogenase bright stem cells, may stimulate the growth of new vessels. (clinicaltrials.gov)

Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. (wikidoc.org)
Human succinic semialdehyde dehydrogenase. (wikidoc.org)

Your search returned 21 aldehyde dehydrogenase 1 family member L1 ELISA ELISA Kit across 3 suppliers. (biocompare.com)
Anti-Aldehyde dehydrogenase 5 family member A1 antibodies are available from several suppliers. (biocompare.com)
Your search returned 192 aldehyde dehydrogenase 5 family member A1 Antibodies across 28 suppliers. (biocompare.com)

Recombinant ABA2 protein produced in Escherichia coli exhibits a K m value for xanthoxin of 19 μM and catalyzes in a NAD-dependent manner the conversion of xanthoxin to abscisic aldehyde, as determined by HPLC-mass spectrometry. (plantcell.org)
Aldehyde Dehydrogenase, Yeast, CAS 9028-88-0, is a native aldehyde dehydrogenase from yeast that catalyzes the oxidation of acetaldehyde to acetic acid. (merckmillipore.com)

Aldehydes, which are highly reactive molecules, are toxic at high concentrations. (biochemj.org)

These results strongly suggest that elevated reactive aldehyde concentration, like that observed in the presence of chronic pain, may render cardiomyocytes more susceptible to I/R injury by SIRT1 carbonylative inactivation and impairment the cardioprotection of LKB1-mediated AMPK activation. (onlinejacc.org)

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