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)

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

long-chain-fatty-acyl-CoA reductase Ja 1.2.3.1 aldehyde oxidase Ja ... L-xylulose reductase Ja 1.1.1.11 D-arabitol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-xylulose + NADH + H+ D-arabitol 4- ... Aldehyde of keton + NADH + H+ Alcoholdehydrogenase (NAD+) Ja 1.1.1.2 Alcohol + NADP+ ⇌. {\displaystyle \rightleftharpoons }. ... Aldehyde + NADPH + H+ Alcoholdehydrogenase (NADP+) Ja 1.1.1.3 L-Homoserine + NAD(P)+ ⇌. {\displaystyle \rightleftharpoons }. L- ...

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

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

Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase ... NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) ...

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

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

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 ... Aldose reductase inhibitors, which are substances that prevent or slow the action of aldose reductase, are currently being ...

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

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

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

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

von Wartburg, J.P. and Wermoth, B. (1980). "Aldehyde reductase". u: Jakoby, W.B.. Enzymatic Basis of Detoxication. 1. New York ...

https://sh.wikipedia.org/wiki/L-glukuronat_reduktaza

Bosron, W.F. & Prairie, R.L. (1972). „Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties ... Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain ...

https://sr.wikipedia.org/wiki/Alkohol_dehidrogenaza_

Aldehyde-based and carboxylate inhibitors are effective but toxic because the functional activity of aldehyde reductase is ... halogen bond that contributes to the large potency of this inhibitor for human aldose reductase rather than aldehyde reductase ... Carboxylate and aldehyde inhibitors were shown to hydrogen bond with Trp 111, Tyr 48, and His 110. The "specificity pocket," ... An example of this assertion in drug design is the substrate specificity for the binding of IDD 594 to human aldose reductase. ...

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

Within this group are the glutathione S-transferases (GSTs) such as hGSTA4-4 and hGST5.8, aldose reductase, and aldehyde ... 4-HNE has 3 reactive groups: an aldehyde, a double-bond at carbon 2, and a hydroxy group at carbon 4. It is found throughout ... 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) )

... function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase ... Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and ... This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. ... These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH ...

https://en.wikipedia.org/wiki/AKR1C1

... aldo-keto reductase family 1, member A1 (aldehyde reductase), aldo-keto reductase family 1 member A1. ... aldo-keto reductase (NADP) activity. • L-glucuronate reductase activity. • glucuronolactone reductase activity. • retinol ... "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

... 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

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)

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

... 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

The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor ...

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

Dihydroflavonol 4-reductase uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl alcohol or ... Coniferyl-aldehyde dehydrogenase uses coniferyl aldehyde, H2O, NAD+, and NADP+ to produce ferulate, NADH, NADPH, and H+. ... Coniferyl aldehyde is a low molecular weight phenolic compound susceptible to be extracted from cork stoppers into wine. ... Coniferyl-alcohol dehydrogenase uses coniferyl alcohol and NADP+ to produce coniferyl aldehyde, NADPH, and H+. ...

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

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

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

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

... 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)

... 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 ... A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase". J. Biol. Chem. 276 (44): 40803-10. doi ... Retrieved from "https://en.wikipedia.org/w/index.php?title=2-alkenal_reductase&oldid=950717434" ...

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

Β-Ketoacyl ACP reductase. *3-Hydroxyacyl ACP dehydrase. *Enoyl ACP reductase. Fatty acid desaturases. *Stearoyl-CoA desaturase- ...

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

The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... an oxido-reductase) with the presence of co-enzyme nicotinamide adenine dinucleotide phosphate (NADP+). which will be reduced ...

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

... reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier ... 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme ... 3-oxoacyl-(acyl-carrier-protein) reductase. From Wikipedia, the free encyclopedia. (Redirected from Beta-Ketoacyl ACP reductase ... Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP ...

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

oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • protein binding. • metal ion ... Dephospho-(reductase kinase) kinase (EC 2.7.11.3). *AMP-activated protein kinase α *PRKAA1 ...

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

... is an inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase), an enzyme that catalyzes the ... The silyl ether on hydrogenolysis followed by Collins oxidation gave the aldehyde. Stereoselective preparation of (E,E)-diene ... HMG CoA reductase occurs early in the biosynthetic pathway and is among the first committed steps to cholesterol formulation. ... This inhibition of reductase would lead to accumulation of lipophylic intermediates with a formal sterol ring. ...

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

... then attacks the free aldehyde to form a carbocation that is quenched by electrons from the methyl-phenol ring. This is done in ... Halogenated/ribonucleotide reductase inhibitors (Cladribine. *Clofarabine. *Fludarabine). *Nelarabine. *Thiopurine (Tioguanine# ...

https://en.wikipedia.org/wiki/Ecteinascidin_743

With regards to the activity of GSH reductase (GRx), there was higher activity in the group pretreated with WPC than in the ... Reactive oxygen free radical species in the heart were quantified by the cytotoxic aldehydes malondialdehyde (MDA), 4-hydroxy- ... Whey Protein Concentrate Promotes the Production of Glutathione (GSH) by GSH Reductase in the PC12 Cell Line After Acute ... Mice receiving iron treatments with whey supplementation had significantly lower concentrations of cytotoxic aldehydes and ...

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

In the second reaction, biliverdin is converted to bilirubin by biliverdin reductase (BVR):[citation needed] ... In two sequential reactions a 17-hydroxyethylfarnesyl moiety is added at the 2-position and an aldehyde is added at the 8- ...

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

talk)‎ (→‎IUPAC names for aldehydes) (Tags: Mobile edit, Mobile web edit). *(diff , hist) . . Aldehyde‎; 15:51 . . (-1)‎ . . ‎ ... 2,4 Dienoyl-CoA reductase‎; 15:07 . . (0)‎ . . ‎. 77.87.224.99. (talk)‎ (changed Tyr199 to Tyr166, please refer to reference # ... Aldehyde‎; 09:44 . . (+10)‎ . . ‎. 2405:205:1001:97f3:b315:5de1:8a9c:30cc. (talk)‎ (→‎Structure and bonding) (Tags: Mobile edit ... m Aldehyde‎; 16:01 . . (+1)‎ . . ‎. Edgar181. (talk , contribs)‎ (Reverted edits by 2405:205:2190:4836:E3B8:A17E:CB4C:348A ( ...

https://en.wikipedia.org/wiki/Special:RecentChangesLinked/Acyl_CoA_dehydrogenase

This reduced cofactor is then a substrate for any of the reductases in the cell that require electrons to reduce their ... Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC (March 1995). "Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ... Hanukoglu I (December 2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A ... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus,[18] and even cadmium in ...

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

Subsequently, tropinone reductase I (EC 1.1.1.206) converts tropinone to tropine which condenses with phenylalanine-derived ... A cytochrome P450 classified as Cyp80F1[4] oxidizes and rearranges littorine to hyoscyamine aldehyde. ...

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

These oxidation products are further reduced by the enzyme dihydroflavonol 4-reductase to the corresponding colorless ... significant portions of ingested anthocyanins are likely to degrade to phenolic acids and aldehyde in vivo, following ... dihydroflavonol 4-reductase (DFR), anthocyanidin synthase (ANS), UDP-glucoside: flavonoid glucosyltransferase (UFGT), and ... ring hydroxylation status and pH have been shown to mediate the degradation of anthocyanins to their phenolic acid and aldehyde ...

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

... reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier ... 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme ... Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP ... In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction ...

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

Bifunctional aldehydes are reactive chemicals that are formed endogenously via lipid peroxidation and prostoglandin ... Halogenated/ribonucleotide reductase inhibitors (Cladribine. *Clofarabine. *Fludarabine). *Nelarabine. *Thiopurine (Tioguanine# ... Malondialdehyde is a prototypical example that can crosslink DNA via two exocylcic guanine amino groups.[13] Other aldehydes, ... Often found within pesticides, tobacco smoke, and automotive exhaust, α,β unsaturated aldehydes, such as acrolein and ...

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

The conversion changes the sugar (xylose, an aldehyde) into the primary alcohol, xylitol. Impurities are then removed.[5] The ... L-Xylulose reductase. *Xylonic acid. References[edit]. *^ Safety data sheet for xylitol from Fisher Scientific. Retrieved 2014- ...

https://en.wikipedia.org/wiki/E967

His4 catalyzes the oxidation of L-histidinol to form L-histidinal, an amino aldehyde. In the last step, L-histidinal is ... HMG-CoA reductase. *Isovaleryl coenzyme A dehydrogenase. *α-Ketoisocaproate dioxygenase. *Leucine 2,3-aminomutase ...

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

... a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde ... Beta-Ketoacyl ACP reductase. *Carbohydrate dehydrogenases. *Carnitine dehydrogenase. *D-malate dehydrogenase (decarboxylating) ...

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

DMSO reductase. Category:EC 1.1 (act on the CH-OH group of donors)Edit. *Category:EC 1.1.1 (with NAD+ or NADP+ as acceptor) * ... Category:EC 1.2 (act on the aldehyde or oxo group of donors)Edit. *Category:EC 1.2.1 (with NAD+ or NADP+ as acceptor) * ... Category:EC 2.2 (transfer aldehyde or ketone groups)Edit. *Category:EC 2.2.1 *Transketolase EC 2.2.1.1 ... 1.2 Category:EC 1.2 (act on the aldehyde or oxo group of donors) ... D-xylulose reductase EC 1.1.1.9. *L-xylulose reductase EC 1.1. ...

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

Dihydrofolate reductase is inhibited by methotrexate which prevents binding of its substrate, folic acid. Binding site in blue ... Irreversible inhibitors often contain reactive functional groups such as nitrogen mustards, aldehydes, haloalkanes, alkenes, ... Trypanothione reductase with the lower molecule of an inhibitor bound irreversibly and the upper one reversibly. Created from ... For example, in the figure showing trypanothione reductase from the human protozoan parasite Trypanosoma cruzi, two molecules ...

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

... (or ENR) (EC 1.3.1.9), is a key enzyme of the type II fatty acid synthesis (FAS) system.[1 ... NADH-Enoyl+ACP+Reductase at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Identification and characterization of inhibitors of bacterial enoyl-acyl carrier protein reductase". Antimicrobial Agents and ... "Atromentin and leucomelone, the first inhibitors specific to enoyl-ACP reductase (FabK) of Streptococcus pneumoniae". The ...

https://en.wikipedia.org/wiki/Enoyl-acyl_carrier_protein_reductase

Aldehyde oxidase (~70%), CYP3A4 (~30%);[1] UGT1A4 (minor). Metabolites. GS-563117 (inactive in vitro). ... Halogenated/ribonucleotide reductase inhibitors (Cladribine. *Clofarabine. *Fludarabine). *Nelarabine. *Thiopurine (Tioguanine# ...

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

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 ... Dihydroflavonol 4-reductase is an enzyme part of the lignin biosynthesis pathway. ...

https://en.wikipedia.org/wiki/Dihydroflavonol_4-reductase

Artemisinic aldehyde Delta11(13)-reductase (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) Biology ... "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

Crystal structure of porcine aldehyde reductase at 2.0 angstrom resolution: Modeling an inhibitor in the active site of the ...

http://www.rcsb.org/pdb/explore/materialsAndMethods.do?structureId=1CWN

3H4G: Structure Of Aldehyde Reductase Holoenzyme In Complex With Potent Aldose Reductase Inhibitor Fidarestat: Implications For ...

https://www.ncbi.nlm.nih.gov/Structure/pdb/3H4G

High levels of NADPH-dependent reductase activity against pterin-6-aldehyde and its dihydro form were detected in Arabidopsis, ... releasing a pterin aldehyde fragment that can be re-used in folate synthesis if the aldehyde group is reduced. ... Folate salvage in plants: pterin aldehyde reduction is mediated by multiple non-specific aldehyde reductases Plant J. 2007 Aug; ... encoding a pterin aldehyde reductase was identified by searching the short-chain dehydrogenase/reductase family for proteins ...

https://pubmed.ncbi.nlm.nih.gov/17550420/?dopt=Abstract

Inhibition of rat kidney aldehyde reductase at 0.1 mM after 20 mins by spectrometric analysis. ...

https://pubchem.ncbi.nlm.nih.gov/bioassay/462443

Category: Aldehyde Reductase. Posted on June 20, 2017. Targeted toxins, referred to as immunotoxins or cytotoxins also, are ...

http://www.woofahs.com/category/aldehyde-reductase/

Recent studies recommend that glucose may be an incidental substrate of aldehyde reductase, which seems to be more adept in ... Additionally, aldehyde reductase inhibition has been demonstrated to increase vascular oxidative stress induced by inflammation ... The reduction of glucose by the aldehyde reductase-catalyzed polyol pathway has been related to the secondary diabetic ... Based on these studies, aldehyde reductase has been ascribed an important antioxidant role. Because of its significant in ...

https://www.biocatalogue.org/services/4274

admin January 19, 2018 Aldehyde Reductase hSNF2b, Probucol supplier Maintenance of genome honesty via repair of DNA damage is a ... admin January 6, 2018 Aldehyde Reductase Felypressin Acetate, RG7112 CLEC14a (C-type lectin website family 14 member) is a ... admin September 4, 2017 Aldehyde Reductase a member of the integrin a chain family with 165 kDa MW. which is expressed on NK ... admin February 16, 2018 Aldehyde Reductase 856866-72-3, DNM1 We present optimum perfusion conditions for the growth of ...

http://www.bioinf.org/index.php/category/aldehyde-reductase/page/2/

... reductase promoter is important for artemisinin yield in different chemotypes of Artemisia annua L., Plant Molecular Biology" ... Artemisinic aldehyde is reduced into dihydroartemisinic aldehyde by DBR2. Artemisinic aldehyde can also be oxidized by amorpha- ... Overexpression of artemisinic aldehyde Δ11(13) reductase gene-enhanced artemisinin and its relative metabolite biosynthesis in ... The activity of the artemisinic aldehyde Δ11(13) reductase promoter is important for artemisinin... Yang, Ke; Monafared, ...

https://www.deepdyve.com/lp/springer_journal/the-activity-of-the-artemisinic-aldehyde-11-13-reductase-promoter-is-a5MAjvHwQh

Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis. Peter ... Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis ... Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis ... Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis ...

http://www.biochemj.org/content/366/3/889

At least 24 aldehyde reductases from Saccharomyces cerevisiae have been characterized and most function in in situ ... Functions of aldehyde reductases from Saccharomyces cerevisiae in detoxification of aldehyde inhibitors and their ... GRE2 from Scheffersomyces stipitis as an aldehyde reductase contributes tolerance to aldehyde inhibitors derived from ... cerevisiae as aldehyde reductases provides a guideline for their practical applications in in situ detoxification of aldehyde ...

https://rd.springer.com/article/10.1007/s00253-020-10722-9?error=cookies_not_supported&code=d315a475-abea-4a16-8fa5-af88b1189da5

Aldehyde reductases - sub set of CESK-6000 (standard format) - We offer a range of biocatalysts in easy-to-use kits. Click here ...

https://www.almacgroup.com/api-chemical-development/biocatalyst_product/aldehyde-reductases-sub-set-of-cesk-6000-standard-format/

What is aldehyde reductase class-I alcohol dehydrogenase, beta subunit? Meaning of aldehyde reductase class-I alcohol ... What does aldehyde reductase class-I alcohol dehydrogenase, beta subunit mean? ... aldehyde reductase class-I alcohol dehydrogenase, beta subunit explanation free. ... Looking for online definition of aldehyde reductase class-I alcohol dehydrogenase, beta subunit in the Medical Dictionary? ...

https://medical-dictionary.thefreedictionary.com/aldehyde+reductase+class-I+alcohol+dehydrogenase%2C+beta+subunit

Aflatoxin B1 aldehyde reductase member 2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma- ... Aflatoxin B1 aldehyde reductase member 2 from Human, Recombinant. Aflatoxin B1 aldehyde reductase member 2 from Human, ... Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in ... AFB1 aldehyde reductase 1; AFB1-AR 1; Aldoketoreductase 7; Succinic semialdehyde reductase ...

https://www.creative-enzymes.com/product/Aflatoxin-B1-Aldehyde-Reductase-Member-2-From-Human-Recombinant_3383.html

SpecificityC TerminusStorage/StabilityAliquot and store at -20°C Minimize freezing and thawing More InformationImmunogenThe immunogen was a 13-residue peptide matching a sequence from the C Terminus of Human AKR1A1 See Accession Number s NP_006057 1 NP_697021 1 Formulation 0 5 mg/ml in TBS

https://www.raybiotech.com/goat-anti-human-aldehyde-reductase-c-terminus/

Aldose reductase, Aldose Reductase like protein 1 and Aldehyde Reductase are homologous proteins that are overexpressed in ... Aldose reductase, Aldose Reductase like protein 1 and Aldehyde Reductase are homologous proteins that are overexpressed in ... Conclusion: New molecules targeting Aldose reductase, Aldose Reductase like protein 1 and Aldehyde Reductase have been designed ... Conclusion: New molecules targeting Aldose reductase, Aldose Reductase like protein 1 and Aldehyde Reductase have been designed ...

https://www.eurekaselect.com/175676/article

... Basal cell carcinoma (BCC) of your skin may be the most Basal cell carcinoma (BCC) of your skin may be the ... Aldehyde Reductase Open in another window The molecular chaperone Hsp90 requires the help Open in another window The molecular ... Aldehyde Reductase Although caspase-2 is thought to be involved with death receptor-mediated apoptosis, Although caspase-2 is ... Aldehyde Reductase Goal: To investigate whether the conjugation of magainin II (MG2), an Goal: To investigate whether the ...

https://www.brain-tumor-cancer-information.com/category/aldehyde-reductase/

Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in ... Aflatoxin B(1) aldehyde reductase (AKR7A2) was confirmed to be only highly expressed in pancreatic cancer, not in normal ... The protein encoded by this gene belongs to the aldo/keto reductase (AKR) superfamily and AKR7 family, which are involved in ... The human aldo-keto reductase AKR7A2 has been proposed previously to catalyze the NADPH-dependent reduction of succinic ...

https://pharos.nih.gov/idg/targets/O43488

Category: Aldehyde Reductase. In response to tension cells must reprogram gene expression to adjust and survive quickly ...

https://paccon2016.com/category/aldehyde-reductase/

Category: Aldehyde Reductase. Posted on June 16, 2017. IMPORTANCE Obtained neuromyotonia is regarded as an autoimmune disorder ...

http://health-e-nc.org/category/aldehyde-reductase/

Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor ... Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor ... Aldo-keto reductase family 1 member A1. > Aldo/keto reductase * Occurring in:. *Aldo-keto reductase family 1 member A1. > ... Aldo/keto reductase, conserved site * Occurring in:. *Aldo-keto reductase family 1 member A1. > NADP-dependent oxidoreductase ...

https://www.ebi.ac.uk/pdbe/entry/pdb/3cv7

Aldehyde Reductase Supplementary MaterialsAdditional file 1: Figure S1 LKB1 kinase activity was unaffected by Tax kinase assay ...

https://woodgreenoutreach.org/category/aldehyde-reductase/

... versus rat lens aldose reductase (EC 1.1.1.21). All aldose reductase. inhibitors examined inhibited aldehyde reductase to some ... versus rat lens aldose reductase (EC 1.1.1.21). All aldose reductase. inhibitors examined inhibited aldehyde reductase to some ... versus rat lens aldose reductase (EC 1.1.1.21). All aldose reductase. inhibitors examined inhibited aldehyde reductase to some ... versus rat lens aldose reductase (EC 1.1.1.21). All aldose reductase. inhibitors examined inhibited aldehyde reductase to some ...

https://nebraska.pure.elsevier.com/en/publications/inhibition-of-aldehyde-reductase-by-aldose-reductase-inhibitors

Category: Aldehyde Reductase. The transforming growth factor isoforms, TGF-1, -2, and -3, are small. Published on March 25, ...

http://www.globaltechbiz.com/category/aldehyde-reductase/

Bovine kidney aldose reductase (ALR2) displays substrate inhibition by aldehyde substrates that is uncompetitive versus NADPH ... Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase. ... The practical implications of these results for kinetics studies of aldose reductase are discussed. ... Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reducta ...

https://pesquisa.bvsalud.org/portal/resource/pt/mdl-2125486

Reactivity of enzyme modification reagents with aldose reductase and aldehyde reductase. / Mizoguchi, T.; Itabe, H.; Kador, P. ... Reactivity of enzyme modification reagents with aldose reductase and aldehyde reductase. Advances in experimental medicine and ... title = "Reactivity of enzyme modification reagents with aldose reductase and aldehyde reductase", ... T1 - Reactivity of enzyme modification reagents with aldose reductase and aldehyde reductase ...

https://experts.nebraska.edu/en/publications/reactivity-of-enzyme-modification-reagents-with-aldose-reductase-

Crystal structure and biophysical analysis of furfural detoxifying aldehyde reductase from clostridium beijerinkii. Applied and ... Crystal structure and biophysical analysis of furfural detoxifying aldehyde reductase from clostridium beijerinkii ... Many aldehydes such as furfural are present in high quantities in lignocellulose lysates and are fermentation inhibitors that ... Cbei_3974 has recently been identified as an aldo-keto reductase responsible for partial furfural resistance in Clostridium ...

http://orca-mwe.cf.ac.uk/122822/

Herein, we demonstrated that an aldo/keto reductase PYC7 is responsible for the reduction of aldehyde to alcohol congeners. The ... Herein, we demonstrated that an aldo/keto reductase PYC7 is responsible for the reduction of aldehyde to alcohol congeners. The ... Herein, we demonstrated that an aldo/keto reductase PYC7 is responsible for the reduction of aldehyde to alcohol congeners. The ... Herein, we demonstrated that an aldo/keto reductase PYC7 is responsible for the reduction of aldehyde to alcohol congeners. The ...

https://okayama.pure.elsevier.com/en/publications/controlling-the-production-of-phytotoxin-pyriculol-in-pyricularia

aldehyde reductase DEFINITION: An enzyme of the oxidoreductase class that catalyzes the reduction of aldoses to form alditols, ... In galactosemia due to galactokinase deficiency, catalysis of the reduction of galactose to galactitol by aldehyde reductase in ... aldehyde reductase 6 and p8 were decreased in the AQP1 null mice. Uroplakin 1A, carboxylesterase 3, matrilin 2 and lipocalin 2 ... aldehyde reductase 6 and p8 were decreased in the AQP1 null mice. Uroplakin 1A, carboxylesterase 3, matrilin 2 and lipocalin 2 ...

http://www.ndif.org/proceedings/147-Renal_medullary_gene_expression_in_aquaporin1_null_mice/abstract

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

Reactive aldehyde species Dihydrofolate reductase Inhibitor

RASP (reactive aldehyde species) are elevated in ocular and systemic inflammatory disease, and they are targets of ADX-629 and reproxalap, two of the ALDX's lead investigational compounds. (marketglobalist.com)
and reactive aldehyde species that are pro-inflammatory (RASP) scavengers, such as ADX-629 for treating autoimmune diseases, allergy, and covid-19, as well as ADX-103 for the treatment of retinal diseases. (stocksignalslive.com)

ALDX's clinical pipeline also includes ADX-2191, an inhibitor of dihydrofolate reductase in Phase 3 trials for proliferative vitreoretinopathy. (marketglobalist.com)
It also develops ADX-2191, a dihydrofolate reductase inhibitor which is in phase 3 for the prevention of proliferative vitreoretinopathy, and phase II clinical trial for the treatment of primary vitreoretinal lymphoma. (stocksignalslive.com)

Pitavastatin calcium, a novel member of the medication class of statins , is a calcium salt formulation of pitavastatin which is a highly effective HMG-CoA reductase inhibitor. (biz.pl)
Disulfiram is a specific inhibitor of aldehyde-dehydrogenase (ALDH1) , used for the treatment of chronic alcoholism by producing an acute sensitivity to alcohol. (biz.pl)

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