Aldehyde reductase. Medical search

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.

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

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).

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.

Oxidoreductases that are specific for ALDEHYDES.

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)

Antioxidant; also a post-harvest dip to prevent scald on apples and pears.

Alcohol analog of NICOTINIC ACID which is a direct-acting peripheral vasodilator that causes flushing and may decrease blood pressure. It is used in vasospasm and threatened GANGRENE.

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.

Compounds based on imidazolidine dione. Some derivatives are ANTICONVULSANTS.

A long-acting barbiturate that depresses most metabolic processes at high doses. It is used as a hypnotic and sedative and may induce dependence. Barbital is also used in veterinary practice for central nervous system depression.

A potent hepatotoxic and hepatocarcinogenic mycotoxin produced by the Aspergillus flavus group of fungi. It is also mutagenic, teratogenic, and causes immunosuppression in animals. It is found as a contaminant in peanuts, cottonseed meal, corn, and other grains. The mycotoxin requires epoxidation to aflatoxin B1 2,3-oxide for activation. Microsomal monooxygenases biotransform the toxin to the less toxic metabolites aflatoxin M1 and Q1.

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

Oxidoreductases that are specific for the reduction of NITRATES.

A group of corticosteroids carrying hydroxy groups, usually in the 11- or 17-positions. They comprise the bulk of the corticosteroids used systemically. As they are relatively insoluble in water, salts of various esterified forms are often used for injections or solutions.

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)

Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.

The rate dynamics in chemical or physical systems.

The only family of the buckwheat order (Polygonales) of dicotyledonous flowering plants. It has 40 genera of herbs, shrubs, and trees.

A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.

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

A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.

A polyhydric alcohol with about half the sweetness of sucrose. Sorbitol occurs naturally and is also produced synthetically from glucose. It was formerly used as a diuretic and may still be used as a laxative and in irrigating solutions for some surgical procedures. It is also used in many manufacturing processes, as a pharmaceutical aid, and in several research applications.

A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.

An organic compound used often as a reagent in organic synthesis, as a flavoring agent, and in tanning. It has been demonstrated as an intermediate in the metabolism of acetone and its derivatives in isolated cell preparations, in various culture media, and in vivo in certain animals.

Compounds based on reduced IMIDAZOLINES which contain no double bonds in the ring.

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)

Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.

An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.

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

A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5

A flavoprotein that catalyzes the reduction of heme-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. EC 1.6.2.4.

Precursors in the biosynthesis of prostaglandins and thromboxanes from arachidonic acid. They are physiologically active compounds, having effect on vascular and airway smooth muscles, platelet aggregation, etc.

3-Carbamoyl-1-beta-D-ribofuranosyl pyridinium hydroxide-5'phosphate, inner salt. A nucleotide in which the nitrogenous base, nicotinamide, is in beta-N-glycosidic linkage with the C-1 position of D-ribose. Synonyms: Nicotinamide Ribonucleotide; NMN.

Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

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 enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

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).

A cyclic endoperoxide intermediate produced by the action of CYCLOOXYGENASE on ARACHIDONIC ACID. It is further converted by a series of specific enzymes to the series 2 prostaglandins.

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

A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.

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.

Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.

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

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.

Carrier of aroma of butter, vinegar, coffee, and other foods.

A group of physiologically active prostaglandin endoperoxides. They are precursors in the biosynthesis of prostaglandins and thromboxanes. The most frequently encountered member of this group is the prostaglandin H2.

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

A large and heterogenous group of fungi whose common characteristic is the absence of a sexual state. Many of the pathogenic fungi in humans belong to this group.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.

An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

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 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.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

A flavoprotein amine oxidoreductase that catalyzes the reversible conversion of 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. This enzyme was formerly classified as EC 1.1.1.171.

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

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

The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.

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.

A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.

An NAD-dependent enzyme that catalyzes the oxidation of nitrite to nitrate. It is a FLAVOPROTEIN that contains IRON and MOLYBDENUM and is involved in the first step of nitrate assimilation in PLANTS; FUNGI; and BACTERIA. It was formerly classified as EC 1.6.6.1.

Reductases that catalyze the reaction of peptide-L-methionine -S-oxide + thioredoxin to produce peptide-L-methionine + thioredoxin disulfide + H(2)O.

An enzyme of the oxidoreductase class that catalyzes the formation of 2'-deoxyribonucleotides from the corresponding ribonucleotides using NADPH as the ultimate electron donor. The deoxyribonucleoside diphosphates are used in DNA synthesis. (From Dorland, 27th ed) EC 1.17.4.1.

Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.

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.

NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.

A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.

An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC 1.6.99.7.

A subtype of thioredoxin reductase found primarily in the CYTOSOL.

A microanalytical technique combining mass spectrometry and gas chromatography for the qualitative as well as quantitative determinations of compounds.

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

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)

An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.

Proteins prepared by recombinant DNA technology.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

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.

The chemical and physical integrity of a pharmaceutical product.

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)

Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.

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.

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.

A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.

A 3-oxoacyl reductase that has specificity for ACYL CARRIER PROTEIN-derived FATTY ACIDS.

Oxidoreductases that specifically reduce arsenate ion to arsenite ion. Reduction of arsenate is a critical step for its biotransformation into a form that can be transported by ARSENITE TRANSPORTING ATPASES or complexed by specific sulfhydryl-containing proteins for the purpose of detoxification (METABOLIC DETOXIFICATION, DRUG). Arsenate reductases require reducing equivalents such as GLUTAREDOXIN or AZURIN.

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.

The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.

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

A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)

A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE along with molybdoferredoxin and is active in nitrogen fixation.

A metallic element with the atomic symbol Mo, atomic number 42, and atomic weight 95.94. It is an essential trace element, being a component of the enzymes xanthine oxidase, aldehyde oxidase, and nitrate reductase. (From Dorland, 27th ed)

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

Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.

A NADPH-dependent oxidase that reduces hydrogen sulfite to HYDROGEN SULFIDE. It is found in many microoganisms.

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 for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.

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

An enzyme found primarily in SULFUR-REDUCING BACTERIA where it plays an important role in the anaerobic carbon oxidation pathway.

Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.

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

Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.

An enzyme that catalyzes the oxidation of D-glycerate to hydroxypyruvate in the presence of NADP.

Inhibitors of the enzyme, dihydrofolate reductase (TETRAHYDROFOLATE DEHYDROGENASE), which converts dihydrofolate (FH2) to tetrahydrofolate (FH4). They are frequently used in cancer chemotherapy. (From AMA, Drug Evaluations Annual, 1994, p2033)

Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.

An FAD-dependent oxidoreductase found primarily in BACTERIA. It is specific for the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. This enzyme was formerly listed as EC 1.1.1.68 and 1.1.99.15.

Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.

A subtype of thioredoxin reductase found primarily in MITOCHONDRIA.

An iron-sulfur and MOLYBDENUM containing FLAVOPROTEIN that catalyzes the oxidation of nitrite to nitrate. This enzyme can use either NAD or NADP as cofactors. It is a key enzyme that is involved in the first step of nitrate assimilation in PLANTS; FUNGI; and BACTERIA. This enzyme was formerly classified as EC 1.6.6.2.

A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.

Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.

The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)

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.

A FERREDOXIN-dependent oxidoreductase that is primarily found in PLANTS where it plays an important role in the assimilation of SULFUR atoms for the production of CYSTEINE and METHIONINE.

The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.

Tungsten. A metallic element with the atomic symbol W, atomic number 74, and atomic weight 183.85. It is used in many manufacturing applications, including increasing the hardness, toughness, and tensile strength of steel; manufacture of filaments for incandescent light bulbs; and in contact points for automotive and electrical apparatus.

Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

(5Z)-(15S)-11 alpha-Hydroxy-9,15-dioxoprostanoate:NAD(P)+ delta(13)-oxidoreductase. An enzyme active in prostaglandin E and F catabolism. It catalyzes the reduction of the double bond at the 13-14 position of the 15-ketoprostaglandins and uses NADPH as cofactor. EC 1.3.1.48.

A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.

An IRON-containing protein that uses siroheme and 4Fe-4S iron-sulfur centers as prosthetic groups. It catalyzes the six-electron oxidation of AMMONIA to nitrite.

A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.

A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.

Proteins found in any species of bacterium.

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

An enzyme that catalyzes the reversible oxidation of inosine 5'-phosphate (IMP) to guanosine 5'-phosphate (GMP) in the presence of AMMONIA and NADP+. This enzyme was formerly classified as EC 1.6.6.8.

A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

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

Unsaturated hydrocarbons of the type Cn-H2n, indicated by the suffix -ene. (Grant & Hackh's Chemical Dictionary, 5th ed, p408)

Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)

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.

An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the fatty acid biosynthesis pathway. It has a preference for acyl derivatives with carbon chain length from 4 to 16.

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.

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.

An enzyme found primarily in BACTERIA and FUNGI that catalyzes the oxidation of ammonium hydroxide to nitrite. It is an iron-sulfur HEME; FLAVOPROTEIN containing siroheme and can utilize both NAD and NADP as cofactors. This enzyme was formerly classified as EC 1.6.6.4.

Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.

Salts of nitrous acid or compounds containing the group NO2-. The inorganic nitrites of the type MNO2 (where M=metal) are all insoluble, except the alkali nitrites. The organic nitrites may be isomeric, but not identical with the corresponding nitro compounds. (Grant & Hackh's Chemical Dictionary, 5th ed)

Screening of Korean forest plants for rat lens aldose reductase inhibition. (1/765)

Naturally occurring substances which can prevent and treat diabetic complications were sought by examining ethanol extracts prepared from Korean forest plants for their inhibitory effects on rat lens aldose reductase activity in vitro. Among the plants examined, Acer ginnala, Illicium religiosum and Cornus macrophylla exerted the most strong inhibitory activity on aldose reductase. (+info)

Polyol formation and NADPH-dependent reductases in dog retinal capillary pericytes and endothelial cells. (2/765)

PURPOSE: Dogs fed a diet containing 30% galactose experience retinal vascular changes similar to those in human diabetic retinopathy, with selective pericyte loss as an initial lesion. In the present study the relationship among reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reductases, polyol formation, and flux through the polyol pathway in cultured dog retinal capillary cells were investigated. METHODS: Pericytes and endothelial cells were cultured from retina of beagle dogs. NADPH-dependent reductases were characterized by chromatofocusing after gel filtration. Sugars in cultured cells were analyzed by gas chromatography, and flux through the polyol pathway was investigated by 19F nuclear magnetic resonance (NMR) with 3-fluoro-3-deoxy-D-glucose (3FG) as a substrate. The presence of aldose reductase and sorbitol dehydrogenase in these cells was examined by northern blot analysis. RESULTS: Two distinct peaks corresponding to aldose reductase and aldehyde reductase, the latter being dominant, were observed in pericytes by chromatofocusing. Culture in medium containing either 10 mM D-galactose or 30 mM D-glucose resulted in the accumulation of sugar alcohol in pericytes that was markedly reduced by aldose reductase inhibitors. 19F NMR spectra obtained from pericytes cultured for 5 days in medium containing 2 mM 3FG displayed the marked accumulation of 3-fluoro-deoxysorbitol but not 3-fluoro-deoxyfructose. No 3FG metabolism was observed in similarly cultured endothelial cells. With northern blot analysis, aldose reductase was detected in pericytes but not in endothelial cells. Sorbitol dehydrogenase was below the detectable limit in pericytes and endothelial cells. CONCLUSIONS: Aldose, aldehyde, and glyceraldehyde reductases are present in dog retinal capillary pericytes, with aldehyde reductase being the major reductase present. Polyol accumulation easily occurs in pericytes but not in endothelial cells. (+info)

Functional consensus for mammalian osmotic response elements. (3/765)

The molecular mechanisms underlying adaptation to hyperosmotic stress through the accumulation of organic osmolytes are largely unknown. Yet, among organisms, this is an almost universal phenomenon. In mammals, the cells of the renal medulla are uniquely exposed to high and variable salt concentrations; in response, renal cells accumulate the osmolyte sorbitol through increased transcription of the aldose reductase (AR) gene. In cloning the rabbit AR gene, we found the first evidence of an osmotic response region in a eukaryotic gene. More recently, we functionally defined a minimal essential osmotic response element (ORE) having the sequence CGGAAAATCAC(C) (bp -1105 to -1094). In the present study, we systematically replaced each base with every other possible nucleotide and tested the resulting sequences individually in reporter gene constructs. Additionally, we categorized hyperosmotic response by electrophoretic mobility shift assays of a 17-bp sequence (-1108 to -1092) containing the native ORE as a probe against which the test constructs would compete for binding. In this manner, binding activity was assessed for the full range of osmotic responses obtained. Thus we have arrived at a functional consensus for the mammalian ORE, NGGAAAWDHMC(N). This finding should accelerate the discovery of genes previously unrecognized as being osmotically regulated. (+info)

Maleic acid and succinic acid in fermented alcoholic beverages are the stimulants of gastric acid secretion. (4/765)

Alcoholic beverages produced by fermentation (e.g., beer and wine) are powerful stimulants of gastric acid output and gastrin release in humans. The aim of this study was to separate and specify the gastric acid stimulatory ingredients in alcoholic beverages produced by fermentation. Yeast-fermented glucose was used as a simple model of fermented alcoholic beverages; it was stepwise separated by different methods of liquid chromatography, and each separated solution was tested in human volunteers for its stimulatory action on gastric acid output and gastrin release. Five substances were detected by high-performance liquid chromatography and were analyzed by mass spectrometry and 1H-13C nuclear magnetic resonance spectroscopy. At the end of the separation process of the five identified substances, only the two dicarboxylic acids, maleic acid and succinic acid, had a significant (P < 0.05) stimulatory action on gastric acid output (76% and 70% of fermented glucose, respectively), but not on gastrin release. When given together, they increased gastric acid output by 100% of fermented glucose and by 95% of maximal acid output. We therefore conclude that maleic acid and succinic acid are the powerful stimulants of gastric acid output in fermented glucose and alcoholic beverages produced by fermentation, and that gastrin is not their mediator of action. (+info)

Osmotic response element is required for the induction of aldose reductase by tumor necrosis factor-alpha. (5/765)

Induction of aldose reductase (AR) was observed in human cells treated with tumor necrosis factor-alpha (TNF-alpha). AR protein expression increased severalfold in human liver cells after 1 day of exposure to 100 units/ml TNF-alpha. An increase in AR transcripts was also observed in human liver cells after 3 h of TNF-alpha treatment, reaching a maximum level of 11-fold at 48 h. Among the three inflammatory cytokines: TNF-alpha, interleukin-1, and interferon-gamma, TNF-alpha (100 units/ml) gave the most induction of AR. Differences in the pattern of AR induction were observed in human liver, lens, and retinal pigment epithelial cells with increasing concentrations of TNF-alpha. A similar pattern of AR promoter response was observed between TNF-alpha and osmotically stressed human liver cells. The deletion of the osmotic response element (ORE) abolished the induction by TNF-alpha and osmotic stress. A point mutation that converts ORE to a nuclear factor-kappaB (NF-kappaB) sequence abolished the osmotic response but maintained the TNF-alpha response. Electrophoretic gel mobility shift assays showed two NF-kappaB proteins, p50 and p52, capable of binding ORE sequence, and gel shift Western assay detected NF-kappaB proteins p50 and p65 in the ORE complex. Inhibitors of NF-kappaB signaling, lactacystin, and MG132 abolished the AR promoter response to TNF-alpha. (+info)

Comparisons of genomic structures and chromosomal locations of the mouse aldose reductase and aldose reductase-like genes. (6/765)

Aldose reductase (AR), best known as the first enzyme in the polyol pathway of sugar metabolism, has been implicated in a wide variety of physiological functions and in the etiology of diabetic complications. We have determined the structures and chromosomal locations of the mouse AR gene (Aldor1) and of two genes highly homologous to Aldor1: the fibroblast growth factor regulated protein gene (Fgfrp) and the androgen regulated vas deferens protein gene (Avdp). The number of introns and their locations in the mouse Aldor1 gene are identical to those of rat and human AR genes and also to those of Fgfrp and Avdp. Mouse Aldor1 gene was found to be located near the Cald1 (Caldesmon) and Ptn (Pleiotropin) loci at the proximal end of chromosome 6. The closely related genes Fgfrp and Avdp were also mapped in this region of the chromosome, suggesting that these three genes may have arisen by a gene duplication event. (+info)

Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis. (7/765)

Giant cell arteritis (GCA) is a systemic vasculitis preferentially affecting large and medium-sized arteries. Inflammatory infiltrates in the arterial wall induce luminal occlusion with subsequent ischemia and degradation of the elastic membranes, allowing aneurysm formation. To identify pathways relevant to the disease process, differential display-PCR was used. The enzyme aldose reductase (AR), which is implicated in the regulation of tissue osmolarity, was found to be upregulated in the arteritic lesions. Upregulated AR expression was limited to areas of tissue destruction in inflamed arteries, where it was detected in T cells, macrophages, and smooth muscle cells. The production of AR was highly correlated with the presence of 4-hydroxynonenal (HNE), a toxic aldehyde and downstream product of lipid peroxidation. In vitro exposure of mononuclear cells to HNE was sufficient to induce AR production. The in vivo relationship of AR and HNE was explored by treating human GCA temporal artery-severe combined immunodeficiency (SCID) mouse chimeras with the AR inhibitors Sorbinil and Zopolrestat. Inhibition of AR increased HNE adducts twofold and the number of apoptotic cells in the arterial wall threefold. These data demonstrate that AR has a tissue-protective function by preventing damage from lipid peroxidation. We propose that AR is an oxidative defense mechanism able to neutralize the toxic effects of lipid peroxidation and has a role in limiting the arterial wall injury mediated by reactive oxygen species. (+info)

Hypertonicity-induced accumulation of organic osmolytes in papillary interstitial cells. (8/765)

BACKGROUND: Medullary cells of the concentrating kidney are exposed to high extracellular solute concentrations. It is well established that epithelial cells in this kidney region adapt osmotically to hypertonic stress by accumulating organic osmolytes. Little is known, however, of the adaptive mechanisms of a further medullary cell type, the papillary interstitial cell [renal papillary fibroblast (RPF)]. We therefore compared the responses of primary cultures of RPFs and papillary collecting duct (PCD) cells exposed to hypertonic medium. METHODS: In RPFs and PCD cells, organic osmolytes were determined by high-performance liquid chromatography; mRNA expression for organic osmolyte transporters [Na+/Cl(-)-dependent betaine transporter (BGT), Na(+)-dependent myo-inositol transporter (SMIT)], and the sorbitol synthetic and degrading enzymes [aldose reductase (AR) and sorbitol dehydrogenase (SDH), respectively] was determined by Northern blot analysis. RESULTS: Exposure to hypertonic medium (600 mOsm/kg by NaCl addition) caused intracellular contents of glycerophosphorylcholine, betaine, myo-inositol, and sorbitol, but not free amino acids, to increase significantly in both RPFs and PCD cells. The rise in intracellular contents of these organic osmolytes was accompanied by enhanced expression of mRNAs coding for BGT, SMIT, and AR in both RPFs and PCD cells. SDH mRNA abundance, however, was unchanged. Nonradioactive in situ hybridization studies on sections from formalin-fixed and paraffin-embedded, normally concentrating kidneys showed strong expression of BGT, SMIT, and AR mRNAs in interstitial and collecting duct cells of the papilla, whereas expression of SDH mRNA was much weaker in both cell types. CONCLUSIONS: These results suggest that both RPFs and PCD cells use similar strategies to adapt osmotically to the high interstitial NaCl concentrations characteristic for the inner medulla and papilla of the concentrating kidney. (+info)

... (EC 1.3.1.92, Dbr2) is an enzyme with systematic name artemisinic aldehyde:NADP+ ... Artemisinic+aldehyde+Delta11(13)-reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... "The molecular cloning of artemisinic aldehyde Delta11(13) reductase and its role in glandular trichome-dependent biosynthesis ... This enzyme catalyses the following chemical reaction (11R)-dihydroartemisinic aldehyde + NADP+ ⇌ {\displaystyle \ ...

https://en.wikipedia.org/wiki/Artemisinic_aldehyde_Delta11(13)-reductase

3DG inactivates aldehyde reductase. Aldehyde reductase is the cellular enzyme that protects the body from 3DG. Detoxification ... Takahashi M, Lu YB, Myint T, Fujii J, Wada Y, Taniguchi N (January 1995). "In vivo glycation of aldehyde reductase, a major 3- ... Suzuki K, Koh YH, Mizuno H, Hamaoka R, Taniguchi N (February 1998). "Overexpression of aldehyde reductase protects PC12 cells ... "Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes". Biochemical Pharmacology. 53 (8): ...

https://en.wikipedia.org/wiki/3-Deoxyglucosone

Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in ... "Entrez Gene: AKR1A1 aldo-keto reductase family 1, member A1 (aldehyde reductase)". Palackal NT, Burczynski ME, Harvey RG, ... by mammalian aldose reductase and aldehyde reductase". Biochimica et Biophysica Acta (BBA) - General Subjects. 1244 (1): 10-6. ... Takahashi M, Lu YB, Myint T, Fujii J, Wada Y, Taniguchi N (January 1995). "In vivo glycation of aldehyde reductase, a major 3- ...

https://en.wikipedia.org/wiki/Aldo-keto_reductase_family_1,_member_A1

In enzymology, aldose reductase (or aldehyde reductase) (EC 1.1.1.21) is a cytosolic NADPH-dependent oxidoreductase that ... The reaction mechanism of aldose reductase in the direction of aldehyde reduction follows a sequential ordered path where NADPH ... Barski OA, Gabbay KH, Bohren KM (September 1999). "Characterization of the human aldehyde reductase gene and promoter". ... AKR1B1 Aldo-keto reductase Petrash JM (April 2004). "All in the family: aldose reductase and closely related aldo-keto ...

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

Turner, A. J.; Hick, P. E. (15 September 1975). "Inhibition of aldehyde reductase by acidic metabolites of the biogenic amines ...

https://en.wikipedia.org/wiki/Jordan_O'Doherty

Turner, A. J.; Hick, P. E. (1975-09-15). "Inhibition of aldehyde reductase by acidic metabolites of the biogenic amines". ...

https://en.wikipedia.org/wiki/Sherilyn_Williams-Stroud

... such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others. All ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547-51. PMID 2498333 ... The aldo-keto reductase family is a family of proteins that are subdivided into 16 categories; these include a number of ... Borhani DW, Harter TM, Petrash JM (December 1992). "The crystal structure of the aldose reductase.NADPH binary complex". J. ...

https://en.wikipedia.org/wiki/Aldo-keto_reductase

November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239 ... McEwan AG, Ridge JP, McDevitt CA, Hugenholtz P (2002). "The DMSO Reductase Family of Microbial Molybdenum Enzymes; Molecular ...

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

Methylglyoxal reductase and aldehyde dehydrogenase convert methylglyoxal into lactaldehyde and, eventually, L-lactate. If ... Methylglyoxal is, however, a reactive aldehyde that is very toxic to cells, it can inhibit growth in E. coli at milimolar ...

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

"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239): 1170-6. Bibcode ... Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd. As of late 2007, only one ... In enzymology, an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction an ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ...

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

The role of aldehyde reductase tyrosine phenol group is to serve as a general acid to provide proton to the reduced aldehyde ... The mechanism involves a tyrosine residue in the active site of aldehyde reductase. The hydrogen atom on NADH is transferred to ... Aldose reductase is the first enzyme in the sorbitol-aldose reductase pathway responsible for the reduction of glucose to ... The reaction requires NADH and is catalyzed by aldose reductase. Glucose reduction is the first step of the polyol pathway of ...

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

Aflatoxin B1 aldehyde reductase member 2 is an enzyme that in humans is encoded by the AKR7A2 gene. Aldo-keto reductases, such ... "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)". Human AKR7A2 genome location and ... evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase ... Praml C, Savelyeva L, Perri P, Schwab M (1998). "Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a ...

https://en.wikipedia.org/wiki/AKR7A2

AR belongs to the aldehyde-keto reductase superfamily, with a widely expression in human organs including the kidney, lens, ... Aldo-keto reductase family 1, member B1 (AKR1B1), also known as aldose reductase, is an enzyme that is encoded by the AKR1B1 ... Robinson B, Hunsaker LA, Stangebye LA, Vander Jagt DL (December 1993). "Aldose and aldehyde reductases from human kidney cortex ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ...

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

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

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

... aldehyde dehydrogenase and aldehyde reductase. The end product of epinephrine and norepinephrine is vanillylmandelic acid (VMA ...

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

Within this group are the glutathione S-transferases (GSTs) such as hGSTA4-4 and hGST5.8, aldose reductase, and aldehyde ... 4-HNE has two reactive groups: the conjugated aldehyde and the C=C double-bond, and the hydroxy group at carbon 4. The α,β- ... Although they are the most studied ones, in the same process other oxygenated α,β-unsaturated aldehydes (OαβUAs) are generated ... Increased activity of the mitochondrial enzyme aldehyde dehydrogenase 2 (ALDH2) has been shown to have a protective effect ...

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

The chanoclavine intermediate is then oxidized to chanoclavine-l-aldehyde, catalyzed by the short-chain dehydrogenase/reductase ... in which agroclavine is produced following the formation of chanoclavine-l-aldehyde, catalyzed by EasA through a keto-enol ... tautomerization to facilitate rotation about the C-C bond, followed by tautomerization back to the aldehyde and condensation ...

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

Other names in common use include retinal reductase, aldehyde reductase (NADPH/NADH), and alcohol dehydrogenase [NAD(P)]. This ... an aldehyde + NAD(P)H + H+ The 3 substrates of this enzyme are alcohol, NAD+, and NADP+, whereas its 4 products are aldehyde, ...

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

The short contact between Br and Thr 113 OG explains the selectivity of IDD 594 towards AR, because in aldehyde reductase the ... The molecules fail to bind to each other if similar aldehyde reductase replaces the enzyme, or chlorine replaces the drug ... For example, inhibitor IDD 594 binds to human aldose reductase through a bromine halogen bond, as shown in the figure. ... June 2004). "Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A ...

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

RASP are metabolized by aldehyde dehydrogenases or aldehyde reductases. Due to the toxicity of RASP, only a small number of ... Reactive aldehyde species (RASP), also known as reactive aldehydes, refer to a class of electrophilic organic aldehyde ... Wood, Paul L.; Khan, M. Amin; Moskal, Joseph R. (2007-05-11). "The concept of "aldehyde load" in neurodegenerative mechanisms: ... Fritz, Kristofer S.; Petersen, Dennis R. (2013-06-01). "An overview of the chemistry and biology of reactive aldehydes". Free ...

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

... respiratory arsenate reductase, carbon monoxide dehydrogenase, aldehyde oxidase. Prosthetic group of: formate dehydrogenase, ... Molybdopterin is a: Cofactor of: xanthine oxidase, DMSO reductase, sulfite oxidase, nitrate reductase, ethylbenzene ... Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. The first tungsten-requiring enzyme to be ... Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate ...

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

... carbonyl reductase, nonspecific NADPH-dependent carbonyl reductase, aldehyde reductase 1, and carbonyl reductase (NADPH). This ... Other names in common use include aldehyde reductase 1, prostaglandin 9-ketoreductase, xenobiotic ketone reductase, NADPH- ... In enzymology, a carbonyl reductase (NADPH) (EC 1.1.1.184) is an enzyme that catalyzes the chemical reaction R-CO-R' + NADPH + ... Wermuth B (1981). "Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to ...

https://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH)

Aldo-keto reductases, such as AKR7A3, are involved in the detoxification of aldehydes and ketones.[supplied by OMIM, Apr 2004 ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Aflatoxin B1 aldehyde reductase ... Aldo-keto reductase family 7 member A3 is a protein that in humans is encoded by the AKR7A3 gene. ... "Entrez Gene: Aldo-keto reductase family 7 member A3". Retrieved 2018-04-13. ...

https://en.wikipedia.org/wiki/AKR7A3

... ferredoxin-nitrite reductase MeSH D08.811.682.655.750.500 - nitrite reductase (NAD(P)H) MeSH D08.811.682.657.163 - aldehyde ... aldehyde reductase MeSH D08.811.682.047.150.700.237 - d-xylulose reductase MeSH D08.811.682.047.150.700.400 - glycerolphosphate ... gmp reductase MeSH D08.811.682.655.500 - nitrate reductases MeSH D08.811.682.655.500.124 - nitrate reductase MeSH D08.811. ... testosterone 5-alpha-Reductase MeSH D08.811.682.662.162 - dihydropteridine reductase MeSH D08.811.682.662.171 - FMN reductase ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

... artemisinic aldehyde Δ11(13)-reductase EC 1.3.1.93: very-long-chain enoyl-CoA reductase EC 1.3.1.94: polyprenol reductase EC ... flavin reductase (NADH) EC 1.5.1.37: FAD reductase (NADH) EC 1.5.1.38: FMN reductase (NADPH) EC 1.5.1.39: FMN reductase (NAD(P) ... zeatin reductase EC 1.3.1.70: Δ14-sterol reductase EC 1.3.1.71: Δ24(241)-sterol reductase EC 1.3.1.72: Δ24-sterol reductase EC ... nitrite reductase (NAD(P)H) EC 1.7.1.5: hyponitrite reductase EC 1.7.1.6: azobenzene reductase EC 1.7.1.7: GMP reductase EC 1.7 ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)

Other names in common use include aldehyde reductase, L-hexonate:NADP dehydrogenase, TPN-L-gulonate dehydrogenase, aldehyde ... reductase II, NADP-L-gulonate dehydrogenase, D-glucuronate dehydrogenase, D-glucuronate reductase, and L-glucuronate reductase ... In enzymology, a glucuronate reductase (EC 1.1.1.19) is an enzyme that catalyzes the chemical reaction L-gulonate + NADP+ ⇌ {\ ...

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

White H, Strobl G, Feicht R, Simon H (September 1989). "Carboxylic acid reductase: a new tungsten enzyme catalyses the ... In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. Aldehyde Ferredoxin ... AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid ...

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

LuxAB codes for luciferase while luxCDE codes for a fatty-acid reductase complex that is responsible for synthesizing aldehydes ... With the exception of the Photorhabdus operon type, all variants of the lux operon contain the flavin reductase-encoding luxG ... Nevertheless, all bio-luminescent bacteria share a common gene sequence: the enzymatic oxidation of Aldehyde and reduced Flavin ... For bacterial bio-luminescence specifically, the biochemical reaction involves the oxidation of an aliphatic aldehyde by a ...

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

... and then the gamma-glutamyl phosphate is the made into gamma-glutamic semi-aldehyde in the gamma-glutamyl phosphate reductase ... "Entrez Gene: ALDH18A1 aldehyde dehydrogenase 18 family, member A1". Fischer-Zirnsak B, Escande-Beillard N, Ganesh J, Tan YX, Al ... P5CS consists of two domains: gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, each of which are used to complete ... This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial ...

https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_18_family,_member_A1

... aldehyde oxidase, and mitochondrial amidoxime reductase. People severely deficient in molybdenum have poorly functioning ... Those enzymes include aldehyde oxidase, sulfite oxidase and xanthine oxidase. With one exception, Mo in proteins is bound by ...

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

Carbohydrates are aldehydes or ketones, with many hydroxyl groups attached, that can exist as straight chains or rings. ... This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to transfer hydrogen ...

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

A reductase then catalyzes the reduction of the ketone on the norsolorinic acid side-chain to yield averantin. Averantin is ... Upon forming the aldehyde in the ring opening step, it is oxidized to form the carboxylic acid and subsequently a ... a reductase. These enzymes use both molecular oxygen and two NADPH's to dehydrate one of the hydroxyl groups on the ...

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

The general scheme is a condensation and oxidation process starting with pyrrole and an aldehyde. Porphyrins have been ... The enzymes involved in this pathway are glutamyl-tRNA synthetase, glutamyl-tRNA reductase, and glutamate-1-semialdehyde 2,1- ... Rothemund P (1935). "Formation of Porphyrins from Pyrrole and Aldehydes". J. Am. Chem. Soc. 57 (10): 2010-2011. doi:10.1021/ ... the highly reduced porphyrin coordinated to nickel that binds the Cofactor F430 active site in methyl coenzyme M reductase (MCR ...

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

Inhibitors of dihydrofolate reductase (DHFR) are prominent examples. Other examples of these substrate mimics are the protease ... Irreversible inhibitors often contain reactive functional groups such as nitrogen mustards, aldehydes, haloalkanes, alkenes, ... Folic acid is the oxidised form of the substrate of dihydrofolate reductase, an enzyme that is potently inhibited by ... For example, in the figure showing trypanothione reductase from the human protozoan parasite Trypanosoma cruzi, two molecules ...

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

... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... In enzymology, a 2-alkenal reductase (EC 1.3.1.74) is an enzyme that catalyzes the chemical reaction n-alkanal + NAD(P)+ ⇌ {\ ... A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase". J. Biol. Chem. 276 (44): 40803-10. doi ...

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

... of ketones and aldehyde.: Milder methylating agents include tetramethyltin, dimethylzinc, and trimethylaluminium. Chemistry ... "Methylenetetrahydrofolate reductase gene promoter hypermethylation in semen samples of infertile couples correlates with ... "Aromatic Hydrocarbons from aromatic ketones and aldehydes: 1,1-Diphenylethane". Organic Syntheses. 55: 7. doi:10.15227/orgsyn. ... "Methylation loss at H19 imprinted gene correlates with methylenetetrahydrofolate reductase gene promoter hypermethylation in ...

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

Although the structure of glyoxylic acid is described as having an aldehyde functional group, the aldehyde is only a minor ... In the mitochondria, glyoxylate is converted into glycine by AGT2 or into glycolate by glyoxylate reductase. A small amount of ... the aldehyde structure has as a major conformer a cyclic hydrogen-bonded structure with the aldehyde carbonyl in close ... They are generally formed from reactive aldehydes, such as those present on reducing sugars and alpha-oxoaldehydes. In a study ...

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

In an α,β-unsaturated enal, the alkene is conjugated to the carbonyl group of the aldehyde (formyl group). The simplest enal is ... 2-alkenal reductase Enol Smith, Michael B.; March, Jerry (2007), Advanced Organic Chemistry: Reactions, Mechanisms, and ... Traditional methods for regioselective enolate formation use either electronic activating groups (e.g. aldehydes) or steric ... An enal (or alkenal) is an organic compound containing both alkene and aldehyde functional groups. ...

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

... a new class of NADP+-specific aldehyde dehydrogenase". Biochemical Journal. 397 (1): 131-8. doi:10.1042/BJ20051763. ISSN 0264- ... "Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum". Archives ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... and glyceraldehyde-3-phosphate ferredoxin reductase. Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ...

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

In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl ... dihydromyricetin reductase, NADPH-dihydromyricetin reductase, and dihydroquercetin reductase. This enzyme participates in ... In enzymology, a dihydrokaempferol 4-reductase (EC 1.1.1.219) is an enzyme that catalyzes the chemical reaction cis-3,4- ... Dihydroflavonol 4-reductase is an enzyme part of the lignin biosynthesis pathway. ...

https://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase

The mechanism for the reduction of the CoA thioester to the aldehyde involves a hydride transfer to the carbonyl carbon from ... "Comparative and phylogenomic analyses of cinnamoyl-CoA reductase and cinnamoyl-CoA-reductase-like gene family in land plants". ... The tetrahedral intermediate then collapses, kicking out the CoA and forming an aldehyde as the final product. The thiolate of ... As can be seen in the diagram shown to the right, these monolignols are derived directly from their corresponding aldehydes, ...

https://en.wikipedia.org/wiki/Cinnamoyl-CoA_reductase

... has been shown to interact with GroES, ALDH2, Caspase 3 and Dihydrofolate reductase. The genes of bacteriophage (phage) ... "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". ...

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

R-COOH is reduced by a two-enzyme system to an aldehyde. The reaction is: R-COOH + ATP + NADPH → R-CHO + AMP + PP + NADP+. One ... luxC codes for the enzyme acyl-reductase, luxD codes for acyl-transferase, and luxE makes the proteins needed for the enzyme ... In A. fischeri, it is directly next to luxE (giving luxCDABE-fre) from 1042306 to 1048745 [1] To generate the aldehyde needed ... Luciferase produces blue/green light through the oxidation of reduced flavin mononucleotide and a long-chain aldehyde by ...

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

"Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry. 271 (1): 212-219 ... "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". ...

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

In enzymology, a carboxylate reductase (EC 1.2.99.6) is an enzyme that catalyzes the chemical reaction an aldehyde + acceptor ... The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) ... White H, Strobl G, Feicht R, Simon H (1989). "Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ...

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

... likely due to inhibition of the enzyme vitamin K epoxide reductase) and a reaction with ethanol similar to that produced by ... disulfiram (Antabuse), due to inhibition of aldehyde dehydrogenase. Cefotetan has a broad spectrum of activity and has been ...

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

Messner KR, Imlay JA (November 2002). "Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate ... and aldehyde dehydrogenases. The amino acid methionine is prone to oxidation, but oxidized methionine can be reversible. ... "Oxidative stress and covalent modification of protein with bioactive aldehydes". The Journal of Biological Chemistry. 283 (32 ...

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

Other names in common use include choline oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and ... betaine aldehyde + reduced acceptor Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products ... are betaine aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of a donor with ... which is cleaved into the enzymes N-acetyl-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also ...

https://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase

... and serve to replenish NADP+ by using the NADPH produced by fermentation to reduce aldehydes to alcohols. The aldehydes are ... By introducing the superoxide reductases of P. furiosus into plants, the levels of O2 can be rapidly reduced.[citation needed] ... P. furiosus ADHs typically have a broad range of aldehyde substrates they can use, and they can also catalyze the reverse ... The next oxidoreductase, WOR4, does not help oxidize aldehydes, but rather has a role in the reduction of elemental sulfur (S0 ...

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

... catalyzed by glutamyl-tRNA reductase. It is isomerized by glutamate-1-semialdehyde 2,1-aminomutase to give aminolevulinic acid ... Aldehydes, All stub articles, Biochemistry stubs). ...

https://en.wikipedia.org/wiki/Glutamate-1-semialdehyde

In the acyl reduction pathway, a reductase converts VLCFAs into primary alcohols, which can then be converted to wax esters ... In the decarbonylation pathway, aldehydes are produced and decarbonylated to form alkanes, and can be subsequently oxidized to ... such as aldehydes, alcohols, alkanes, ketones, and esters. Also present are other compounds in cuticular wax which are not ...

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

In accordance with finasteride being a potent 5α-reductase inhibitor but a weak inhibitor of 5β-reductase, the medication ... Finasteride is extensively metabolized in the liver, first by hydroxylation via CYP3A4 and then by aldehyde dehydrogenase. It ... its affinity for the enzyme is substantially less than for 5α-reductase (an order of magnitude less than for 5α-reductase type ... In addition to inhibiting 5α-reductase, finasteride has also been found to competitively inhibit 5β-reductase (AKR1D1). However ...

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

Aldehyde dehydrogenases (ALDH) are NAD+ dependent enzymes that function to remove toxic aldehydes from the body, functioning ... Any of these may be called dehydrogenases, especially those in which NAD+ is the electron acceptor (oxidant), but reductase is ... Build-up of aldehydes in the brain and pericardium can be detrimental to a person's health, as they can form adducts with ... Aldehydes are the natural by-product of many physiological processes, as well as being the consequence of many industrial ...

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

... Scheller PN, Lenz M, Hammer S, Hauer B, ... Imine Reductase-Catalyzed Intermolecular Reductive Amination of Aldehydes and Ketones. ChemCatChem, 7(20), p 3239-3242. ... Imine Reductase-Catalyzed Intermolecular Reductive Amination of Aldehydes and Ketones. ChemCatChem. 2015;7(20):3239-3242. ... "Imine Reductase-Catalyzed Intermolecular Reductive Amination of Aldehydes and Ketones". ChemCatChem 7 (20): 3239-3242. ...

https://pub.uni-bielefeld.de/record/2949723

Aldose reductase is a monomer of α subunits, aldehyde reductase I is a dimer of α and β subunits and aldehyde reductase II is a ... Aldose reductase is a monomer of α subunits, aldehyde reductase I is a dimer of α and β subunits and aldehyde reductase II is a ... Aldose reductase is a monomer of α subunits, aldehyde reductase I is a dimer of α and β subunits and aldehyde reductase II is a ... Aldose reductase is a monomer of α subunits, aldehyde reductase I is a dimer of α and β subunits and aldehyde reductase II is a ...

https://researchexperts.utmb.edu/en/publications/aldose-and-aldehyde-reductases-in-human-tissues

... H. Guo;DEL CORSO, ANTONELLA;L. Q. Huang;MURA, UMBERTO;P. ... In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH- ... In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH- ... We expressed one of these proteins of H. armigera, aldo-keto reductase (AKR), which bears 56% identity to bovine aldose ...

https://arpi.unipi.it/handle/11568/454267

Developmental retardation in neonates of aldehyde reductase (AKR1A)-deficient mice is associated with low ascorbic acid and ...

http://bukka.phar.kyushu-u.ac.jp/publication/developmental-retardation-in-neonates-of-aldehyde-reductase-akr1a-deficient-mice-is-associated-with-low-ascorbic-acid-and-high-corticosterone-levels/

Aldehyde Reductase. en. dc.subject.mesh. Human Growth Hormone. en. dc.subject.mesh. Ivermectin. en. ...

https://extranet.who.int/iris/restricted/handle/10665/54579?show=full

e) Aldehyde reductase and (f) Alcohol oxidase (EC:1.1.1.2). Whether aldehyde reductases first produce aldehydes which are then ... because aldehyde reductases can also catalyze the reduction of the fatty aldehyde to the alcohol, so alcohols and not aldehydes ... mevaldate reductase (EC 1.1.1.33) and lactaldehyde reductase (EC 1.1.1.55). Two contigs were named aldehyde reductase in ... For example, the question of whether aldehyde reductases first produce aldehydes which are then converted to alcohols, or vice ...

https://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-11-29

Western blotting; adulthood; aldehyde reductase; angiogenesis; blood pressure; cardiovascular diseases; children; cluster ...

https://pubag.nal.usda.gov/?f%5Bjournal_facet%5D%5B%5D=Journal+of+proteomics&f%5Bjournal_name%5D%5B%5D=Journal+of+proteomics&f%5Bsubject_term%5D%5B%5D=cardiovascular+diseases&per_page=100&sort=title

Arroyo-Sandoval, J. A., Marin-Bravo, M. J., Arroyo-Acevedo, J. L., Justil-Guerrero, H. J., Chavez-Asmat, R. J., Pari-Olarte, J. B., Chavez-Espinoza, J. H., Torres-Levano, J. D., Loyola-Gonzales, E., Almeida-Galindo, J. S. & Herrera-Calderon, O., May 2022, In: Pharmacognosy Journal. 14, 3, p. 622-628 7 p.. Research output: Contribution to journal › Article › peer-review ...

https://cris.unica.edu.pe/en/organisations/farmacia-y-bioquimica/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=title&descending=false

Mammalian metalloproteins and enzymes that have nitrate reductase activity include aldehyde oxidase, heme proteins, ... The action of bacterial nitrate reductases on the tongue and mammalian enzymes that have nitrate reductase activity in tissues ... Enterosalivary circulation pathway (nitrate reductase activity of bacteria on the tongue generates nitrite and nitrite which is ... are noted by the number 1. Bacterial nitrate reductases are noted by the number 2. Mammalian enzymes with nitrite reductase ...

https://www.atsdr.cdc.gov/csem/nitrate-nitrite/biologic_fate.html

Influence of Interindividual Variability of Aldose Reductase Protein Content on Polyol-Pathway Metabolites and Redox State in ... aldehyde reductase (1) * erythrocytes (1) * metabolites (1) * oxidation-reduction (1) Issue Section ...

https://diabetesjournals.org/care/search-results?f_AllAuthors=Chihiro+Nishimura%2C+MD

The role of aldehyde reductase tyrosine phenol group is to serve as a general acid to provide proton to the reduced aldehyde ... The mechanism involves a tyrosine residue in the active site of aldehyde reductase. The hydrogen atom on NADH is transferred to ... Aldose reductase is the first enzyme in the sorbitol-aldose reductase pathway[27] responsible for the reduction of glucose to ... It can be obtained by reduction of glucose, which changes the converted aldehyde group (−CHO) to a primary alcohol group (−CH2 ...

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

ADH1B , Alcohol dehydrogenase 1B , ADH, beta subunit , Aldehyde reductase , ADH2. See All ADH2 / ADH1B Antibodies ...

https://www.lsbio.com/antibodies/adh2-antibody-adh1b-antibody-clone-oti1c3-if-immunofluorescence-ihc-wb-western-ls-c337334/347945

Moreover, two enzymes involved in retinoic acid metabolism have been identified: Dehydrogenase reductase 7 and aldehyde ... However, blocking of retinoic acid receptor and aldehyde dehydrogenase led to a decrease in proliferative activity of coelomic ... glutathione reductase, glutathione S-transferase, and glutathione peroxidase, is activated to provide protection against ROS [ ... glutathione reductase, and glutathione S-transferase [126]. With various damaging effects, including cutaneous wound, the ...

https://www.mdpi.com/2073-4425/12/2/250

ZEP, zeaxanthin epoxidase; NCED, 9-cisepoxycarotenoid dioxygenase; SDR, short-chain dehydrogenase/reductase; AAO, aldehyde ... abscisic aldehyde is oxidized to ABA by aldehyde oxidase 3 (encoded by AAO3) in the presence of a molybdenum cofactor (MOCO) ( ... 2000). The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves ... 2002). The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde. Plant Cell 14, ...

https://www.frontiersin.org/articles/10.3389/fpls.2015.01248/full

AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3. ... AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of ...

https://www.prospecbio.com/akr7a3_antibody

p53+Aldehyde Dehydrogenase+Gli3+Glutathione Reductase+Nrf2 (1). * p53+Aldehyde Dehydrogenase+PLK1+Tau+XIAP+CYP2D6+CYP2C9+Pin1+ ... Aldehyde dehydrogenase 10 (4). * Aldehyde Dehydrogenase+ADRA2B+alpha 2a Adrenergic Receptor+alpha 2C Adrenergic Receptor/ADRA2C ... Aldehyde Dehydrogenase+Vitamin D Receptor (1). * Aldehyde Dehydrogenase+Vitamin D Receptor+Estrogen Receptor+TDP1+DNA ... Aldehyde Dehydrogenase+Interferon beta+HDAC1+HDAC2+HDAC3+HDAC4+HDAC5+HDAC6+HDAC7+HDAC11/HD11+Nuclear (1). ...

https://www.abcam.com/products?selected.researchAreas=Metabolism--Pathways+and+Processes--Metabolic+signaling+pathways--Alcohol+metabolism

Aldose reductase has a bunch of jobs. Aldehydes which can get into the cell can be toxic and aldose reductase transforms them ... Aldose reductase also takes a little bit of the glucose that comes into the cell and converts it to sorbitol for several ... This state of affairs probably has to do with the need of aldose reductase to make some sorbitol. The factor floor of ... When glucose enters the cell, it is met by two enzymes; hexokinase and aldose reductase. Hexokinase has one main job - get ...

https://asweetlife.org/dangers-from-without-and-within/

... including aliphatic and aromatic aldehydes and ketones, ketoprostaglan-dins, ketosteroids and xenobiotics. In so doing they ... Aldo-keto reductases (AKRs) are phase I metabolising enzymes that catalyse the reduced nicotinamide adenine dinucleotide ( ... Table 1 Systematic and trivial names of human Aldo-keto reductases (AKRs). From: Aldo-keto reductase (AKR) superfamily: ... Aldo-keto reductase family I, member C-like 2; AKRICL2 AKR6A3 KCNAB I; hKvbeta3; potassium voltage-gated channel, shaker- ...

https://humgenomics.biomedcentral.com/articles/10.1186/1479-7364-3-4-362/tables/1

Aldehyde Reductase / antagonists & inhibitors * Animals * Antioxidants / therapeutic use * Diabetes Mellitus / pathology * ...

https://pubmed.ncbi.nlm.nih.gov/18654858/

Bombyx mori-derived aldo-keto reductase AKR2E8 detoxifies aldehydes present in mulberry leaves. Yamamoto, K. & Endo, S., Jan 5 ...

https://kyushu-u.pure.elsevier.com/en/publications/?indexableKeyword=%2Fdk%2Fatira%2Fpure%2Fsustainabledevelopmentgoals%2Fresponsible_consumption_and_production&format=&page=11

Engineering the isobutanol biosynthetic pathway in Escherichia coli by comparison of three aldehyde reductase/alcohol ...

https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-020-1654-x

The Novel Roles of Aldose Reductase (AR) in Collagen GPVI- and Thrombin PAR4-Mediated Platelet Activation and Apoptosis: ...

https://tmu.pure.elsevier.com/en/organisations/school-of-medicine-2/projects/?status=FINISHED&ordering=type&descending=true&page=26

Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis. ... Dive into the research topics of Aldose reductase functions as a detoxification system for lipid peroxidation products in ...

https://mayoclinic.pure.elsevier.com/en/publications/aldose-reductase-functions-as-a-detoxification-system-for-lipid-p/fingerprints/

HUMAN ALDOSE REDUCTASE COMPLEXED WITH HALOGENATED IDD-TYPE INHIBITOR - 2IKI , canSARS ...

https://corona-1.cansar.icr.ac.uk/structure/2IKI/3d/2IKI_A

Reduction of tertiary amine N-oxides by liver preparations: function of aldehyde oxidase as a major N-oxide reductase ... The periplasmic nitrate reductase and trimethylamine N-oxide reductase of the photosynthetic bacterium Rhodobacter capsulatus ... The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural ... Classification of fumarate reductases and succinate dehydrogenases based upon their contrasting behavior in the reduced ...

https://www.brenda-enzymes.org/ligand.php?brenda_ligand_id=992

Aldose reductase and aldehyde reductase accounted for 94 and 6%, respectively, of total placental pyridine nucleotide-dependent ... The Km values for aldose reductase- and aldehyde reductase-catalyzed reduction of aldophosphamide to alcophosphamide were 0.15 ... Oxazaphosphorine-specific resistance in human MCF-7 breast carcinoma cell lines expressing transfected rat class 3 aldehyde ... Protection by transfected rat or human class 3 aldehyde dehydrogenase against the cytotoxic effects of oxazaphosphorine ...

https://www.wikigenes.org/e/chem/e/107744.html

C25.775.100.250 Aldehyde Reductase D8.811.682.47.820.275 Alexander Disease C10.228.518.625.312 alpha-2-Antiplasmin D12.776. ... E2.831.200 Cortisone Reductase D8.811.682.47.436.400.150 D8.811.682.47.820.125.150 Coxa Valga C5.550.338 Coxa Vara C5.550.353 ... K1.559.411.768 Progesterone Reductase D8.811.682.47.820.500 Propranolol D2.33.100.624.836 D2.33.755.624.836 Psychoses, ... D27.505.954.329.30.500 D-Xylulose Reductase D8.811.682.47.820.800 Dementia, Vascular C10.228.518.500 Demyelinating Autoimmune ...

https://decs.bvs.br/P/mnchg2014.txt

aldehyde reductase Agriculture & Biology 84% * retinal diseases Agriculture & Biology 66% * mouth Agriculture & Biology 46% ... Oral sorbinil, an aldose reductase inhibitor, was administered in a double-masked randomized trial to diabetics with no or ...

https://www.researchwithrutgers.com/en/projects/sorbinil-retinopathy-trial-2

Three reductases have been purified from human liver cytosol: two aldehyde reductases, which can reduce aliphatic aldehydes, ... ii) Oxidation of alcohols and aldehydes (a) Primary alcohols and aldehydes Primary aliphatic alcohols (attached to linear, ... Ambroziak, W. & Pietruszko, R. (1991) Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines ... aldehyde and ketone substrates (Nakayama et al., 1985). Carbonyl reductase activity in human liver shows limited ...

https://inchem.org/documents/jecfa/jecmono/v042je14.htm

... it a very important enzyme for the regulation of not only the cellular redox state by detoxifying the reactive lipid-aldehydes ... title = "Understanding the role of aldose reductase in ocular inflammation",. abstract = "Aldose reductase, although identified ... Yadav, U. C.S. ; Srivastava, S. K. ; Ramana, K. V. / Understanding the role of aldose reductase in ocular inflammation. In: ... N2 - Aldose reductase, although identified initially as a glucose-reducing enzyme via polyol pathway, is believed to be an ...

https://researchexperts.utmb.edu/en/publications/understanding-the-role-of-aldose-reductase-in-ocular-inflammation

Immunochemical characterizations of aldose reductase and aldehyde reductases I and II, partially purified by DEAE-cellulose (DE-52) column chromatography from human tissues, were carried out by immunotitration, using antisera raised against the homogenous preparations of human and bovine lens aldose reductase and human placenta aldehyde reductase I and aldehyde reductase II. (utmb.edu)
Anti-aldose reductase antiserum cross-reacted with aldehyde reductase I, anti-aldehyde reductase I antiserum cross-reacted with aldose reductase and anti-aldehyde reductase II antiserum precipitated aldehyde reductase II, but did not cross-react with aldose reductase or aldehyde reductase I from all the tissues examined. (utmb.edu)
Anti-α antiserum precipitated both aldehyde reductase I and aldose reductase, whereas anti-β antibodies cross-reacted with only aldehyde reductase I. Based on these studies, a three gene loci model is proposed to explain the genetic interrelationships among these enzymes. (utmb.edu)
Aldose reductase is a monomer of α subunits, aldehyde reductase I is a dimer of α and β subunits and aldehyde reductase II is a monomer of δ subunits. (utmb.edu)
We expressed one of these proteins of H. armigera, aldo-keto reductase (AKR), which bears 56% identity to bovine aldose reductase, displays a NADPH-dependent activity and is mainly expressed in the antennae of adults. (unipi.it)
The reaction requires NADH and is catalyzed by aldose reductase . (wikipedia.org)
Oral sorbinil, an aldose reductase inhibitor, was administered in a double-masked randomized trial to diabetics with no or minimal diabetic retinopathy. (researchwithrutgers.com)
Aldose reductase, although identified initially as a glucose-reducing enzyme via polyol pathway, is believed to be an important component of antioxidant defense system as well as a key mediator of oxidative stress-induced molecular signaling. (utmb.edu)
Ramana, K. V. / Understanding the role of aldose reductase in ocular inflammation . (utmb.edu)

RNA interference technology, colony formation, and MTT assays were used to investigate the role of aldo-keto reductase family 1, member C3 (AKR1C3) in MTX resistance in choriocarcinoma cells. (medsci.org)

ABSTRACT Serum levels of glutathione reductase (GR), glutathione S-transferase-α (GST-α) and malondialdehyde (MDA) were determined to evaluate their use in diagnosing hepatocellular damage in 75 children with liver disease. (who.int)

The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen transdihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation. (keepautomation.com)

Other enzymes in claim 1 include a fatty acyl-ACP thioesterase, which hydrolyzes a fatty acyl-ACP substrate, a fatty acyl-CoA aldehyde reductase, which reduces a fatty acyl-CoA molecule to a primary alcohol, a fatty acyl-CoA reductase, which reduces a fatty acyl-CoA molecule to an aldehyde, and a fatty aldehyde decarbonylase, which converts a fatty aldehyde to an alkane or alkene. (cleantechies.com)
Key example enzymes are carbohydrate active enzymes, carboxylic acid reductases and prolyl-peptidyl isomerases. (exeter.ac.uk)

As shown in our earlier works, ethanol has a dose-dependent protective effects against endothelial cellular senescence by activating aldehyde dehydrogenase 2 ( ALDH2 ) in vitro. (transhumanist.ru)

In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. (rcsb.org)

Current main projects for the group are the biosynthesis of the Coxiella burnetii O-antigen, and enzyme cascades based around carboxylic acid reductases. (exeter.ac.uk)

AKR7A3, takes part in the detoxification of aldehydes and ketones. (prospecbio.com)
ALDH2 represents the single most gene with the greatest number of human genetic polymorphism and is deemed an important enzyme for detoxification of reactive aldehydes. (transhumanist.ru)

The best substrates are linear aliphatic aldehydes of 8-10 carbon atoms, but not hydroxyaldehydes. (unipi.it)
Both pheromone components of H. armigera, which are unsaturated aldehydes of 16 carbons, are very poor substrates. (unipi.it)

The dual role played by AR has made it a very important enzyme for the regulation of not only the cellular redox state by detoxifying the reactive lipid-aldehydes generated by lipid peroxidation which is crucial in the cellular homeostasis, but also in the regulation of molecular signaling cascade that may regulate oxidative stress-induced cytotoxic events. (utmb.edu)
it inhibits the enzyme dihydrofolate reductase, which is essential for purine and pyrimidine synthesis. (medscape.com)

It is becoming increasingly clear that human aldo-keto reductases (AKRs) of the AKR1C family are intimately linked with cancer biology. (medsci.org)

Aldehyde Dehydrogenase 2 ( ALDH2 ) and Aging: Is There a Sensible Link? (transhumanist.ru)
Recent evidence from our group and others also revealed a tie between genetic mutation of mitochondrial aldehyde dehydrogenase ( ALDH2 ) and life span as well as cardiovascular aging. (transhumanist.ru)
Significant findings in Japanese were found for 1) gene-environment interaction for esophageal cancer between heavy drinking and aldehyde dehydrogenase 2 (ALDH2), 2) malignant lymphoma risk with methylenetetrahydrofalate reductase (MTHFR) and methionine synthase (MS), 3) interactions between smoking and two polymorphisms, interleukin 1B (IL-1B) and myeloperoxidase (MPO) for Helicobacter pylori infection, and 4) smoking habits with dopamine receptor D2 (DRD2) and IL-1B. (who.int)

It is not known whether aging alters the enzymatic reactive aldehyde- and lipid hydroperoxide-detoxifying capacity of the human arterial tissue favoring vascular oxidative stress. (transhumanist.ru)

Impaired enzymatic reactive aldehyde-detoxifying capacity and glutathione peroxidase activity in the aged human arterial tissue. (transhumanist.ru)
Thus, aging impairs the enzymatic reactive aldehyde-detoxifying capacity and GSH-Px activity of the human arterial tissue eventually favoring vascular oxidative stress. (transhumanist.ru)

1984), stimu- by aldehyde dehydrogenase to acrylic acid (Patel et al. (cdc.gov)

unsaturated aldehyde, is used as a water although other metabolites are also produced (Beauchamp et al. (cdc.gov)

In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH-dependent activity. (unipi.it)

It can be obtained by reduction of glucose , which changes the converted aldehyde group (−CHO) to a primary alcohol group (−CH 2 OH). (wikipedia.org)
Genetic polymorphisms of methylenetetrahydrofolate reductase and aldehyde dehydrogenase 2, alcohol use and risk of colorectal adenomas: Self-Defense Forces Health Study. (cdc.gov)

Aldehyde dehydrogenase family [Interproscan]. (ntu.edu.sg)

Sorbitol may be synthesised via a glucose reduction reaction [6] in which the converted aldehyde group is converted into a hydroxyl group. (wikipedia.org)

Aldo-keto reductase- and cytochrome P450-dependent formation of benzo[a]pyrene-derived DNA adducts in human bronchoalveolar cells. (keepautomation.com)

electrons on the aldehyde carbon-oxygen double bond are transferred to the oxygen that abstracts the proton on tyrosine side chain to form the hydroxyl group. (wikipedia.org)

The role of aldehyde reductase tyrosine phenol group is to serve as a general acid to provide proton to the reduced aldehyde oxygen on glucose. (wikipedia.org)

Enterosalivary circulation pathway (nitrate reductase activity of bacteria on the tongue generates nitrite and nitrite which is metabolized to NO in the stomach and circulation) [Hord 2011]. (cdc.gov)

The mechanism involves a tyrosine residue in the active site of aldehyde reductase. (wikipedia.org)

Anatomy5

Organisms6

Chemicals and Drugs107

Analytical, Diagnostic and Therapeutic Techniques and Equipment12

Phenomena and Processes18

Information Science3

Screening of Korean forest plants for rat lens aldose reductase inhibition. (1/765)

Polyol formation and NADPH-dependent reductases in dog retinal capillary pericytes and endothelial cells. (2/765)

Functional consensus for mammalian osmotic response elements. (3/765)

Maleic acid and succinic acid in fermented alcoholic beverages are the stimulants of gastric acid secretion. (4/765)

Osmotic response element is required for the induction of aldose reductase by tumor necrosis factor-alpha. (5/765)

Comparisons of genomic structures and chromosomal locations of the mouse aldose reductase and aldose reductase-like genes. (6/765)

Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis. (7/765)

Hypertonicity-induced accumulation of organic osmolytes in papillary interstitial cells. (8/765)

Aldehyde Reductase

Aldehydes

Alcohol Oxidoreductases

Aldehyde Dehydrogenase

Glyceraldehyde

Aldehyde Oxidoreductases

NADP

Ethoxyquin

Nicotinyl Alcohol

Sugar Alcohol Dehydrogenases

Hydantoins

Barbital

Benzaldehydes

Aflatoxin B1

Substrate Specificity

Nitrate Reductases

Hydroxycorticosteroids

Oxidoreductases

Hydroxymethylglutaryl CoA Reductases

Kinetics

Ribonucleotide Reductases

Polygonaceae

Cytochrome-B(5) Reductase

Liver

Hydroxybutyrate Dehydrogenase

Nitrite Reductases

Furaldehyde

Sorbitol

Oxidoreductases Acting on CH-CH Group Donors

Pyruvaldehyde

Imidazolidines

Alcohols

Glutathione Reductase

FMN Reductase

Molecular Weight

Thioredoxin-Disulfide Reductase

NADPH-Ferrihemoprotein Reductase

Prostaglandin Endoperoxides

Nicotinamide Mononucleotide

Hydroxyprostaglandin Dehydrogenases

Alcohol Dehydrogenase

Ferredoxin-NADP Reductase

Swine

Oxidation-Reduction

Prostaglandin H2

Cytochrome Reductases

Catalysis

Lens, Crystalline

Molecular Sequence Data

Immunodiffusion

Coenzymes

Amino Acid Sequence

Diacetyl

Prostaglandins H

Isoenzymes

Mitosporic Fungi

Amino Acids

Kidney

Tetrahydrofolate Dehydrogenase

Hydrogen-Ion Concentration

Cloning, Molecular

Chromatography, Gel

Methylenetetrahydrofolate Reductase (NADPH2)

Base Sequence

Electrophoresis, Polyacrylamide Gel

Isoelectric Point

Escherichia coli

Phenobarbital

Nitrate Reductase (NADH)

Methionine Sulfoxide Reductases

Ribonucleoside Diphosphate Reductase

Hydroxymethylglutaryl-CoA Reductase Inhibitors

Acetaldehyde

Quinone Reductases

Acrolein

NADH, NADPH Oxidoreductases

Rats, Inbred F344

Dihydropteridine Reductase

Thioredoxin Reductase 1

Gas Chromatography-Mass Spectrometry