Aldehyde oxidoreductases. Medical search

Oxidoreductases that are specific for ALDEHYDES.

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

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)

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.

An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.

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).

A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.

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.

Oxidoreductases that are specific for KETONES.

A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.

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).

Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.

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.

Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.

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.

A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.

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.

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.

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 flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.

A kingdom of hyperthermophilic ARCHAEA found in diverse environments.

A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.

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)

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

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

A 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

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

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

A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.

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

A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.

A 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.

Ecosystem and environmental activities, functions, or events.

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)

An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.

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

A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)

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.

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.

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 flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.

(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 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.

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.

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)

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.

The rate dynamics in chemical or physical systems.

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.

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 thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

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.

Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.

Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.

An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.

A photo-active pigment localized in prolamellar bodies occurring within the proplastids of dark-grown bean leaves. In the process of photoconversion, the highly fluorescent protochlorophyllide is converted to chlorophyll.

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

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

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.

Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.

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.

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)

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.

Proteins found in any species of bacterium.

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.

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

The space between the inner and outer membranes of a cell that is shared with the cell wall.

A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.

Compounds containing the -SH radical.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.

A low-molecular-weight (16,000) iron-free flavoprotein containing one molecule of flavin mononucleotide (FMN) and isolated from bacteria grown on an iron-deficient medium. It can replace ferredoxin in all the electron-transfer functions in which the latter is known to serve in bacterial cells.

Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.

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.

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

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

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.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

A 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.

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

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

Proteins found in the PERIPLASM of organisms with cell walls.

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.

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)

Proteins prepared by recombinant DNA technology.

One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.

Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.

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.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)

A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)

The functional hereditary units of BACTERIA.

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)

Compounds based on fumaric acid.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

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)

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

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

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.

One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.

A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.

The relationships of groups of organisms as reflected by their genetic makeup.

A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).

Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.

The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.

Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

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

Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).

A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.

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.

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

A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.

A species of gram-positive bacteria that is a common soil and water saprophyte.

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.

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

Proteins obtained from ESCHERICHIA COLI.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.

An autosomal recessive neurocutaneous disorder characterized by severe ichthyosis MENTAL RETARDATION; SPASTIC PARAPLEGIA; and congenital ICHTHYOSIS. It is caused by mutation of gene encoding microsomal fatty ALDEHYDE DEHYDROGENASE leading to defect in fatty alcohol metabolism.

Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

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

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

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.

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

The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.

An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.

An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.

The study of the structure, preparation, properties, and reactions of carbon compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

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.

A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)

A metallic element with the atomic symbol Ir, atomic number 77, and atomic weight 192.22.

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

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

Life or metabolic reactions occurring in an environment containing oxygen.

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

Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)

Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.

Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.

Proteins found in any species of fungus.

The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.

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

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

Nitrate-dependent regulation of acetate biosynthesis and nitrate respiration by Clostridium thermoaceticum. (1/1279)

Nitrate has been shown to shunt the electron flow in Clostridium thermoaceticum from CO2 to nitrate, but it did not influence the levels of enzymes involved in the Wood-Ljungdahl pathway (J. M. Frostl, C. Seifritz, and H. L. Drake, J. Bacteriol. 178:4597-4603, 1996). Here we show that under some growth conditions, nitrate does in fact repress proteins involved in the Wood-Ljungdahl pathway. The CO oxidation activity in crude extracts of nitrate (30 mM)-supplemented cultures was fivefold less than that of nitrate-free cultures, while the H2 oxidation activity was six- to sevenfold lower. The decrease in CO oxidation activity paralleled a decrease in CO dehydrogenase (CODH) protein level, as confirmed by Western blot analysis. Protein levels of CODH in nitrate-supplemented cultures were 50% lower than those in nitrate-free cultures. Western blots analyses showed that nitrate also decreased the levels of the corrinoid iron-sulfur protein (60%) and methyltransferase (70%). Surprisingly, the decrease in activity and protein levels upon nitrate supplementation was observed only when cultures were continuously sparged. Northern blot analysis indicates that the regulation of the proteins involved in the Wood-Ljungdahl pathway by nitrate is at the transcriptional level. At least a 10-fold decrease in levels of cytochrome b was observed with nitrate supplementation whether the cultures were sparged or stoppered. We also detected nitrate-inducible nitrate reductase activity (2 to 39 nmol min-1 mg-1) in crude extracts of C. thermoaceticum. Our results indicate that nitrate coordinately represses genes encoding enzymes and electron transport proteins in the Wood-Ljungdahl pathway and activates transcription of nitrate respiratory proteins. CO2 also appears to induce expression of the Wood-Ljungdahl pathway genes and repress nitrate reductase activity. (+info)

Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. (2/1279)

A marked difference in hepatic activity of aldehyde oxidase between rats and monkeys was found to be responsible for the previously reported marked species difference in the metabolism of Zaleplon in vivo. In the postmitochondrial fractions, S-9s, from liver homogenates of these animals, Zaleplon was transformed in the presence of NADPH into the side chain oxidation product, N-desethyl-Zaleplon, and the aromatic ring oxidation product, 5-oxo-Zaleplon. In the rat S-9, N-desethyl-Zaleplon and 5-oxo-Zaleplon were a major and a very minor metabolites, respectively. However, in the monkey S-9, Zaleplon was transformed into 5-oxo-Zaleplon at a much higher rate than that for N-desethyl-Zaleplon formation. N-Desethyl-Zaleplon was formed in the monkey S-9 at a rate almost equal to that in the rat S-9. N-Desethyl-5-oxo-Zaleplon was formed at a minor rate only in the monkey S-9 through N-desethyl-Zaleplon as an obligatory intermediate. The hepatic activity for the formation of 5-oxo-Zaleplon in the monkey and rat was localized in cytosol and did not require NADPH. Sensitivity to various inhibitors and requirement of water as oxygen source, using H218O, strongly suggested that the hepatic cytosolic formation of 5-oxo-Zaleplon was mediated by aldehyde oxidase. N-Desethyl-Zaleplon was formed in the presence of NADPH by microsomes from the liver of rats and monkeys, and its formation was strongly suggested using various cytochrome P-450 inhibitors to be mediated by a number of cytochrome P-450 isoforms, such as 3A, 2C, and 2D subfamilies. (+info)

A genetic linkage map of rat chromosome 9 with a new locus for variant activity of liver aldehyde oxidase. (3/1279)

A genetic linkage map of rat chromosome 9 consisting of five loci including a new biochemical marker representing a genetic variation of the activity of the liver aldehyde oxidase, (Aox) was constructed. Linkage analysis of the five loci among 92 backcross progeny of (WKS/Iar x IS/Iar)F1 x WKS/Iar revealed significant linkages between these loci. Minimizing crossover frequency resulted in the best gene order: Aox-D9Mit4-Gls-Cryg-Tp53l1. The homologues of the Cryg, Gls, and Aox genes have been mapped on mouse chromosome 1 and human chromosome 2q. The present findings provide further evidence for the conservation of synteny among these regions of rat, mouse, and human chromosomes. (+info)

Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. (4/1279)

Pseudomonas aeruginosa ATCC 17933 grown aerobically on ethanol produces a soluble cytochrome c550 together with a quinoprotein ethanol dehydrogenase. A 3.2 kb genomic DNA fragment containing the gene encoding cytochrome c550 was cloned and sequenced. Two other complete and two truncated ORFs were also identified. A truncated ORF encoding the quinoprotein ethanol dehydrogenase (exaA) was found upstream of the cytochrome c550 gene (exaB) and in reverse orientation. An ORF encoding a NAD(+)-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c550 gene and in the same orientation. Another ORF showed similarity to the pqqA gene and a truncated ORF similarity to the pqqB gene, both involved in the biosynthesis of the prosthetic group PQQ. The organization of these genes was found to be different from the well-studied methanol oxidation system in methylotrophic bacteria. The deduced amino acid sequence of cytochrome c550 from P. aeruginosa showed some similarity to cytochrome c6 of the alga Chlamydomonas reinhardtii and the haem domain of quinohaemoprotein alcohol dehydrogenases of acetic acid bacteria, but no similarity to the soluble cytochrome cL of the quinoprotein methanol oxidation system of methylotrophs could be detected. A mutant of P. aeruginosa with an interrupted cytochrome c550 gene was unable to grow on ethanol, which proves that cytochrome c550 is an essential component of the ethanol oxidation system in this organism. (+info)

Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (5/1279)

Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3. (+info)

Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver. (6/1279)

A barbiturate-sensitive aldehyde reductase was purified to homogeneity from rat liver and shown to metabolize the cancer-chemotherapeutic antibiotic daunorubicin. The aldehyde reductase may have important roles in the metabolism of exogeneous drugs as well as the aldehyde derivatives of the biogenic amines. (+info)

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (7/1279)

A Staphylococcus xylosus C2A gene cluster, which encodes enzymes in the pathway for choline uptake and dehydrogenation (cud), to form the osmoprotectant glycine betaine, was identified. The cud locus comprises four genes, three of which encode proteins with significant similarities to those known to be involved in choline transport and conversion in other organisms. The physiological role of the gene products was confirmed by analysis of cud deletion mutants. The fourth gene possibly codes for a regulator protein. Part of the gene cluster was shown to be transcriptionally regulated by choline and elevated NaCl concentrations as inducers. (+info)

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (8/1279)

In order to investigate the effects of trace elements on different metabolic pathways, the thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been cultivated on various carbon substrates in the presence and absence of molybdate. When grown on glucose (but neither on glutamate nor casein hydrolysate) as sole carbon source, the lack of molybdate results in serious growth inhibition. By analysing cytosolic fractions of glucose adapted cells for molybdenum containing compounds, an aldehyde oxidoreductase was detected that is present in the cytosol to at least 0.4% of the soluble protein. With Cl2Ind (2,6-dichlorophenolindophenol) as artificial electron acceptor, the enzyme exhibits oxidizing activity towards glyceraldehyde, glyceraldehyde-3-phosphate, isobutyraldehyde, formaldehyde, acetaldehyde and propionaldehyde. At its pH-optimum (6.7), close to the intracellular pH of Sulfolobus, the glyceraldehyde-oxidizing activity is predominant. The protein has an apparent molecular mass of 177 kDa and consists of three subunits of 80.5 kDa (alpha), 32 kDa (beta) and 19.5 kDa (gamma). It contains close to one Mo, four Fe, four acid-labile sulphides and four phosphates per protein molecule. Methanol extraction revealed the existence of 1 FAD per molecule and 1 molybdopterin per molecule, which was identified as molybdopterin guanine dinucleotide on the basis of perchloric acid cleavage and thin layer chromatography. EPR-spectra of the aerobically prepared enzyme exhibit the so-called 'desulpho-inhibited'-signal, known from chemically modified forms of molybdenum containing proteins. Anaerobically prepared samples show both, the signals arising from the active molybdenum-cofactor as well as from the two [2Fe-2S]-clusters. According to metal-, cofactor-, and subunit-composition, the enzyme resembles the members of the xanthine oxidase family. Nevertheless, the melting point and long-term thermostability of the protein are outstanding and perfectly in tune with the growth temperature of S. acidocaldarius (80 degrees C). The findings suggest the enzyme to function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylated Entner-Doudoroff pathway and thereby may attribute a new physiological role to this class of enzyme. (+info)

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an ... Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. Methods in Enzymology. ... The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use ... Mukund S, Adams MW (1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a ...

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

Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme ... catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes ...

https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(nicotinoprotein)

"Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry / FEBS. 271 (1): ...

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

Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme ... dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803)". Microbiology. 156 (Pt 2): 463-71. doi: ... dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and ...

https://en.wikipedia.org/wiki/Methanol_dehydrogenase_(nicotinoprotein)

The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... In enzymology, a carboxylate reductase (EC 1.2.99.6) is an enzyme that catalyzes the chemical reaction an aldehyde + acceptor ... oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, tungsten. White H, Strobl G, Feicht R ...

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

... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus,[18] and even cadmium in ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. doi:10.1126/science.7878465. PMID 7878465.. ...

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

... tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus, and even cadmium in the ... aldehyde ferredoxin oxidoreductase". Science. 267 (5203): 1463-9. Bibcode:1995Sci...267.1463C. doi:10.1126/science.7878465. ...

https://en.wikipedia.org/wiki/Cofactor_(biochemistry)

November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239 ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common ... H+ The 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP+, whereas its 3 products are long-chain acyl-CoA, ... is an enzyme that catalyzes the chemical reaction a long-chain aldehyde + CoA + NADP+ ⇌ {\displaystyle \rightleftharpoons } a ...

https://en.wikipedia.org/wiki/Long-chain-fatty-acyl-CoA_reductase

... the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin Oxidoreductase". ...

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

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Other names in common use include aldehyde dismutase, and cannizzanase. As of late 2007, only one structure has been solved for ... Kato N, Shirakawa K, Kobayashi H, Sakazawa C (1983). "The dismutation of aldehydes by a bacterial enzyme". Agric. Biol. Chem. ... The systematic name of this enzyme class is formaldehyde:formaldehyde oxidoreductase. ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include ... oxidoreductase. Aerobic carboxydotrophic bacteria utilize copper-molybdenum flavoenzymes. Anaerobic bacteria utilize nickel- ... clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]". European Journal of Biochemistry ...

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... The systematic name of this enzyme class is formylmethanofuran:acceptor oxidoreductase. This enzyme is also called ... formylmethanofuran:(acceptor) oxidoreductase. This enzyme participates in folate biosynthesis. It has 2 cofactors: molybdenum, ...

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

... these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, ... This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. Some proteins of this family contain a potassium ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". J. Biol. Chem. 264 (16): 9547-51. PMID 2498333 ... channel beta chain regulatory domain; these are reported to have oxidoreductase activity. AKR1 Steroidogenic enzyme Bohren KM, ...

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

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Mandal SK, Datta Chaudhuri B (1987). "Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental ... The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase. This ... Huang DY, Furukawa A, Ichikawa Y (1999). "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse ...

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

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... T; Akaba, S; Oritani, T; Delarue, M; Bellini, C; Caboche, M; Koshiba, T (1998). "Higher activity of an aldehyde oxidase in the ... The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include ... Marion-Poll A, Caboche M, Kamiya Y, Koshiba T (1998). "Molecular cloning and characterization of aldehyde oxidases in ...

https://en.wikipedia.org/wiki/Indole-3-acetaldehyde_oxidase

https://en.wikipedia.org/wiki/Pyruvate_oxidase_(CoA-acetylating)

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

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and ...

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(cytochrome)

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include ... formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate ...

https://en.wikipedia.org/wiki/Formate_dehydrogenase_(cytochrome)

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase. Yagi T (October 1969). "Formate: ... cytochrome oxidoreductase of Desulfovibrio vulgaris". Journal of Biochemistry. 66 (4): 473-8. doi:10.1093/oxfordjournals.jbchem ...

https://en.wikipedia.org/wiki/Formate_dehydrogenase_(cytochrome-c-553)

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ...

https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a ... The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use ... Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". J. Bacteriol. ... include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, ...

https://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(cytochrome_b-561)

Aldehyde ferredoxin oxidoreductase (AOR) in Thermococcus strain ES-1 Formaldehyde ferredoxin oxidoreductase (FOR) in ... Tungsten-using enzymes typically reduce carboxylic acids to aldehydes. The tungsten oxidoreductases may also catalyse ... For example, enzymes called oxidoreductases use tungsten similarly to molybdenum by using it in a tungsten-pterin complex with ... One of the enzymes in the oxidoreductase family which sometimes employ tungsten (bacterial formate dehydrogenase H) is known to ...

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

... and for being one of the few organisms identified as possessing aldehyde ferredoxin oxidoreductase enzymes containing tungsten ...

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

... aldehyde oxidoreductases MeSH D08.811.682.657.163.249 - aldehyde dehydrogenase MeSH D08.811.682.657.163.249.750 - omega- ... amino acid oxidoreductases MeSH D08.811.682.664.500.062 - alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid ... succinate cytochrome c oxidoreductase MeSH D08.811.600.250.875.249 - electron transport complex ii MeSH D08.811.600.250.875.249 ... aldehyde reductase MeSH D08.811.682.047.150.700.237 - d-xylulose reductase MeSH D08.811.682.047.150.700.400 - glycerolphosphate ...

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

The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H- ... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase. Structural studies[edit]. As of late 2007, ...

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

EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...

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

oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • pyruvate dehydrogenase (NAD+) ... oxidoreductase activity. • pyruvate dehydrogenase (acetyl-transferring) activity. • ...

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

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

oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... AR belongs to the aldehyde-keto reductase superfamily, with a widely expression in human organs including the kidney, lens, ... It also participates in glucose metabolism and osmoregulation and plays a protective role against toxic aldehydes derived from ...

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

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- ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...

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

4.1.2: Aldehyde-lyases. *Fructose-bisphosphate aldolase *Aldolase A. *Aldolase B. *Aldolase C ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...

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

cellular aldehyde metabolic process. • aldehyde catabolic process. • D-glucuronate catabolic process. • L-ascorbic acid ... alditol:NADP+ 1-oxidoreductase activity. • electron carrier activity. • oxidoreductase activity. • alcohol dehydrogenase (NADP+ ... "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

Enzymes that transfer aldehyde or ketone groups and included in EC 2.2. This category consists of various transketolases and ... hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. EC 2.1 includes enzymes that ... Transaldolase, the namesake of aldehyde transferases, is an important part of the pentose phosphate pathway. The reaction it ...

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

EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...

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

The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... The G6P is then converted to 6-phosphogluconolactone in the presence of enzyme glucose-6-phosphate dehydrogenase( an oxido- ... The G3P is converted to 1,3-bisphosphoglycerate int the presence of enzyme glyceraldehyde-3-phosphate dehydrogenase (an oxido- ...

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

The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...

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

Aldehyde/oxo oxidoreductases (EC 1.2). 1.2.1: NAD or NADP. *Aldehyde dehydrogenase *Acetaldehyde dehydrogenase ... Oxidoreductase. References[edit]. *^ a b PDB: 1NVM; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). "Crystal structure of a ... Wang X, Weiner H (Jan 1995). "Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde ... Crabb D, Xiao Q (Jun 1998). "Studies on the enzymology of aldehyde dehydrogenase-2 in genetically modified HeLa cells". ...

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

oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor. • protein binding. • metal ion ... oxidoreductase activity. • carboxy-lyase activity. • 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) ...

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

1qtn: CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...

https://en.wikipedia.org/wiki/CASP8

oxidoreductase activity. • aldehyde dehydrogenase [NAD(P)+ activity]. • aldehyde dehydrogenase (NAD) activity. • NAD binding. • ... oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor. • glyceraldehyde-3-phosphate ... Mitochondrial aldehyde dehydrogenase belongs to the aldehyde dehydrogenase family of enzymes that catalyze the chemical ... ALDH2, ALDH-E2, ALDHI, ALDM, aldehyde dehydrogenase 2 family (mitochondrial), aldehyde dehydrogenase 2 family member. ...

https://en.m.wikipedia.org/wiki/ALDH2

oxidoreductase activity. • aldehyde dehydrogenase (NAD) activity. • oxidoreductase activity, acting on the aldehyde or oxo ... Aldehyde dehydrogenase 16 family, member A1 also known as ALDH16A1 is an aldehyde dehydrogenase gene. ... "Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1". Neurogenetics. 10 (3): 217-28. doi ...

https://en.m.wikipedia.org/wiki/ALDH16A1

oxidoreductase activity, acting on the CH-CH group of donors. • acyl-CoA dehydrogenase activity. • identical protein binding. • ... oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase activity. • flavin adenine dinucleotide binding. ...

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

The aldehyde then departs as formic acid and a double bond is simultaneously introduced to yield the demethylated product.[7] ... Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14). 1.14.11: 2-oxoglutarate. *Prolyl hydroxylase ...

https://en.wikipedia.org/wiki/Lanosterol_14α-demethylase

The aldehyde groups of the triose sugars are oxidised, and inorganic phosphate is added to them, forming 1,3- ... an oxidoreductase D-1,3-bisphosphoglycerate (1,3BPG) NAD+ + Pi. NADH + H+. ...

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

... s are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ... a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde ...

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

1 Category:Oxidoreductases (EC 1) (Oxidoreductase) *1.1 Category:EC 1.1 (act on the CH-OH group of donors) ... 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 ... Category:EC 5.3 (intramolecular oxidoreductases)Edit. *Category:EC 5.3.3 *Enoyl CoA isomerase (EC 5.3.3.8) ...

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

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

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

Irreversible inhibitors often contain reactive functional groups such as nitrogen mustards, aldehydes, haloalkanes, alkenes, ... Oxidoreductase (EC 1). *1.1 Aldose reductase. *HMG-CoA reductase. *1.3 5α-Reductase ...

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

Oxidoreductases: CH-CH oxidoreductases (EC 1.3). 1.3.1: NAD/NADP acceptor. *Enoyl-acyl carrier protein reductase/Enoyl ACP ...

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

The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include ... In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...

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

oxidoreductase activity. • 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity] ...

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

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

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

In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin ... The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a ... Roy R, Dhawan IK, Johnson MK, Rees DC, Adams MW (2006-04-15). Handbook of Metalloproteins: Aldehyde Ferredoxin Oxidoreductase ( ...

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

Aldehyde ferredoxin oxidoreductase, N-terminal domain superfamily (IPR036503). Short name: Ald_Fedxn_OxRdtase_N_sf ... Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [PMID: 9242907] contain a tungsten cofactor and an 4Fe4S cluster ... Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.. Science 267 1463-9 1995 ... formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from ...

https://www.ebi.ac.uk/interpro/entry/IPR036503

It might play a role in the detoxification of aldehydes to avoid cell damage. ... Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. ... oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: EcoCycInferred from direct assayi*. Ref.5 ... Aldehyde oxidoreductase iron-sulfur-binding subunit PaoACurated (EC:1.2.99.6*Search proteins in UniProtKB for this EC number. ...

https://www.uniprot.org/uniprot/P77165

Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ... Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4- ...

http://www.biochemj.org/content/329/3/469

Three different types of tungsten-containing aldehyde oxidizing enzymes aldehyde ferredoxin oxidoreductase (AOR), formaldehyde ... Detailed kinetic analyses of FOR indicate that C4 - C6 dialdehyde or acid-substituted aldehyde may serve as the physiological ... ferredoxin oxidoreductase (FOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) have previously been isolated ...

https://athenaeum.libs.uga.edu/handle/10724/20424

eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (N) ... eco:b2455 eutE; aldehyde oxidoreductase, ethanolamine utilization protein; K04021 aldehyde dehydrogenase (A) ... aldehyde oxidoreductase, ethanolamine utilization protein (P77445). Identification. Name:. aldehyde oxidoreductase, ...

http://ecmdb.ca/proteins/P77445

Скачать презентацию Mo MOLYBDENUM TUNGSTEN Nitrogenase Xanthine oxidase Aldehyde Oxidoreductase MOP 19-Mo Ni Mn Со Биохимия ... Mo MOLYBDENUM/TUNGSTEN Nitrogenase Xanthine oxidase Aldehyde Oxidoreductase (MOP) Dimethylsulfoxide Reductase Trimethylamine N- ... Oxide Reductase Dissimilatory Nitrate Reductase Formaldehyde Ferredoxin Oxidoreductase Aldehyde Ferredoxin Oxidoreductase ...

https://present5.com/mo-molybdenum-tungsten-nitrogenase-xanthine-oxidase-aldehyde-oxidoreductase-mop/

ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. The identification of the gene from ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ... Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid. Author. Venkitasubramanian Padmesh, Daniels Lacy, Das ... Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ATP and NADPH dependent reduction of carboxylic acids ...

http://academic.naver.com/article.naver?doc_id=64814343

... the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase ... the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase ...

https://moh-it.pure.elsevier.com/en/publications/cloning-of-the-cdnas-coding-for-two-novel-molybdo-flavoproteins-s/fingerprints/

Aldehyde Oxidoreductases. LinkOut - more resources. Medical. *Genes and Gene Therapy - MedlinePlus Health Information ... Aldehyde oxidase as a cell marker for internal organs in Drosophila melanogaster.. Janning W. ...

https://www.ncbi.nlm.nih.gov/pubmed/4632933?dopt=Abstract

CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 ... CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774. Coordinates. PDB Format Method. X ... Rebelo, J. et al., Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC ...

https://swissmodel.expasy.org/templates/1dgj

New tasks for old enzymes: xanthine oxidase and aldehyde oxidoreductase. Maia, L. B. L. (Speaker) ...

https://novaresearch.unl.pt/en/activities/new-tasks-for-old-enzymes-xanthine-oxidase-and-aldehyde-oxidoredu

Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. By MK Chan, S Mukund, A Kletzin, MW ...

http://science.sciencemag.org/content/267/5203

Aldehyde Oxidoreductases / genetics * Aldehyde Oxidoreductases / metabolism* * Esters / metabolism* * Gene Fusion / physiology ...

https://pubmed.ncbi.nlm.nih.gov/26138876/

Aldehyde Oxidoreductases / genetics* * Aldehyde Oxidoreductases / metabolism * Arabidopsis / cytology * Arabidopsis / ...

https://pubmed.ncbi.nlm.nih.gov/12783329/?dopt=Abstract

Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1). ... Aldehyde ferredoxin oxidoreductase, domains 2 & 3 family protein. Escherichia coli 1-176-05_S3_C2. Loading... ... Tungsten-containing aldehyde ferredoxin oxidoreductase. Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC ...

http://www.ebi.ac.uk/interpro/ISignatureProteins?sig=SM00790&query=R

... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... aldehyde oxidoreductase; DHAK, dihydroxyacetone kinase; FHL, formate hydrogen lyase complex; FRD, fumarate reductase; GlyD, ... Zhang, Y.; Li, Y.; Du, C.; Liu, M.; Cao, Z. Inactivation of aldehyde dehydrogenase: A key factor for engineering 1,3- ... By inactivating aldehyde dehydrogenase (ADH), the enzyme responsible for ethanol formation in K. pneumoniae YMU2, less ethanol ...

https://www.mdpi.com/1996-1073/6/9/4739/htm

Maia, Luisa B. ; Moura, José J.G. / Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite ... Maia, L. B., & Moura, J. J. G. (2018). Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite ... Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes. / Maia, ... Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes. Redox ...

https://novaresearch.unl.pt/en/publications/putting-xanthine-oxidoreductase-and-aldehyde-oxidase-on-the-no-me

Alcohol Oxidoreductases); EC 1.1.- (glycolic acid dehydrogenase); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde ...

http://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=D08.811.520.224.600.700

Aldehyde Oxidoreductases); EC 1.2.99.2 (carbon monoxide dehydrogenase); P6YC3EG204 (Vitamin B 12). ... NADPH Oxidoreductases); EC 1.6.4.- (thioredoxin glutathione reductase); K848JZ4886 (Cysteine). ...

http://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=D05.500.562

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

Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the ... exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from ... exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from ... hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and ...

https://ri.conicet.gov.ar/handle/11336/12512

The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for ... Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and ...

https://ri.conicet.gov.ar/handle/11336/494

Classification: OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A)). *Organism(s): Escherichia coli (strain K12) ...

https://www.rcsb.org/structure/1GAD

Classification: OXIDOREDUCTASE (NAD(A)-ALDEHYDE(D)). *Organism(s): Homo sapiens. *Deposited: 1983-06-20 Released: 1983-10-27 ...

https://www.rcsb.org/structure/3GPD

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

Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With unknown physiological acceptors. ... Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the ... Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from ... Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. ...

https://www.genome.jp/dbget-bin/www_bget?ec:1.2.99.7

Oxidoreductases;. Acting on the aldehyde or oxo group of donors;. With NAD+ or NADP+ as acceptor. ... an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+ [RN:R01486]. ... The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit ...

https://www.genome.jp/dbget-bin/www_bget?ec:1.2.1.29

Other name(s): aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd. Systematic name: aldehyde:acceptor oxidoreductase (FAD- ... Other name(s): aldehyde:(acceptor) oxidoreductase. Systematic name: aldehyde:acceptor oxidoreductase. Comments: A tungsten ... Accepted name: aldehyde ferredoxin oxidoreductase. Reaction: an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ ... Systematic name: aldehyde:quinone oxidoreductase. Comments: Wide specificity; acts on straight-chain aldehydes up to C10, ...

https://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC1/0202p.html

Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray ...

https://www.mdpi.com/1422-0067/15/2/2794

Aldehyde oxidase as a cell marker for internal organs in Drosophila melanogaster. (nih.gov)
Herein, we will review the current knowledge on two of those "non-dedicated nitrite reductases", the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans. (unl.pt)
Maia, LB & Moura, JJG 2018, ' Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes ', Redox Biology , vol. 19, pp. 274-289. (unl.pt)
Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and heterocyclic compounds. (conicet.gov.ar)
Purification and characterization of an aldehyde oxidase from Pseudomonas sp. (genome.jp)
Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. (genome.jp)
2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. (qmul.ac.uk)
Aldehyde oxidase: a molybdoflavoprotein. (qmul.ac.uk)
6. Yoshihara, S. and Tatsumi, K. Purification and characterization of hepatic aldehyde oxidase in male and female mice. (qmul.ac.uk)
The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. (nature.com)
Other enzymes such as xanthine oxidoreductase or aldehyde oxidase may also be involved. (labome.org)
Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (uni-potsdam.de)
Aldehyde oxidase (AOX1) is an enzyme with broad substrate specificity, catalyzing the oxidation of a wide range of endogenous and exogenous aldehydes as well as N-heterocyclic aromatic compounds. (aspetjournals.org)
The enzymes xanthine oxidoreductase (XOR) and aldehyde oxidase (AO) catalyzed the oxidation of M1dG and M1G. (vanderbilt.edu)
Other names in common use include betaine aldehyde oxidase , BADH , betaine aldehyde dehydrogenase , and BetB . (academic.ru)
The molybdoflavoenzymes (MFEs), aldehyde oxidase (AOX) and xanthine oxidoreductase (XOR) catalyse the oxidation of many drugs, environmental pollutants and N-heterocyclic compounds. (hud.ac.uk)

In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O + 2 oxidized ferredoxin ⇌ an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)
The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. (wikipedia.org)
Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase. (wikipedia.org)
The main substrates for aldehyde ferredoxin oxidoreductase are acetaldehyde, phenylacetaldehyde, and isovalerdehyde, which is a metabolic product from common amino acids and glucose. (wikipedia.org)
thus, they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. (wikipedia.org)
Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [ PMID: 9242907 ] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [ PMID: 8672295 ]. (ebi.ac.uk)
Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. (ebi.ac.uk)
Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. (ebi.ac.uk)
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. (ebi.ac.uk)
Three different types of tungsten-containing aldehyde oxidizing enzymes aldehyde ferredoxin oxidoreductase (AOR), formaldehyde ferredoxin oxidoreductase (FOR) and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) have previously been isolated from this microorganism. (uga.edu)
The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. (wikipedia.org)
Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase. (wikipedia.org)
Consistently, most of the other active oxidoreductases rely on either reduced ferredoxin and/or NADPH as the electron donor. (asm.org)
Key to the understanding of this energy metabolism is the presence of membrane-associated reduced ferredoxin:NAD + oxidoreductase (Rnf), of electron-bifurcating and ferredoxin-dependent transhydrogenase (Nfn), and of acetaldehyde:ferredoxin oxidoreductase, which is present with very high specific activities in H 2 /CO 2 -grown cells. (asm.org)
In the case of substrate-level phosphorylation, acetyl-CoA reduction to ethanol proceeds via free acetic acid involving acetaldehyde:ferredoxin oxidoreductase (carboxylate reductase). (asm.org)

During an analysis of the C. bescii genome sequence for oxidoreductase-type enzymes, evidence was uncovered to suggest that the primary redox metabolism of C. bescii has a completely uncharacterized aspect involving tungsten, a rarely used element in biology. (asm.org)
[ 17 ] Schiff-base aldehyde adducts with other amino-containing molecules, including key membrane enzymes and proteins, may also be detrimental to their function. (medscape.com)
Aldehyde dehydrogenase enzymes oxidize aldehydes to generate carboxylic acids for use in the muscle and heart. (genecards.org)
Any of a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones. (thefreedictionary.com)
The two main enzymes involved in alcohol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). (thefreedictionary.com)

3. Schenkels, P. and Duine, J.A. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. (qmul.ac.uk)
The 3 substrates of this enzyme are betaine aldehyde , NAD + , and H 2 O , whereas its 3 products are betaine , NADH , and H + . (academic.ru)
Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. (yeastgenome.org)

The archaeons Pyrococcus ES-4 strain and Thermococcus ES-1 strain differ by their substrate specificity: AFOs show a broader size range of its aldehyde substrates. (wikipedia.org)

Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. (wikipedia.org)
However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated 2-ketoacids. (wikipedia.org)
The aim of this study was to identify the cardiac oxidoreductases involved in the metabolism of 4-hydroxy-2- trans -nonenal (HNE), an α,β unsaturated aldehyde generated during the peroxidation of ω-6 polyunsaturated fatty acids. (biochemj.org)
The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N- heterocycles and aldehydes and the reduction of N- oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6]. (qmul.ac.uk)
Two decades later, Sjögren-Larsson syndrome was shown to be an inborn error of lipid metabolism caused by deficient activity of fatty alcohol:NAD oxidoreductase. (medscape.com)
Therefore, patients with Sjögren-Larsson syndrome have deficient activity of FALDH and fatty alcohol:NAD oxidoreductase, which results in defective metabolism of both fatty aldehyde and fatty alcohol. (medscape.com)
Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. (genecards.org)
This gene encodes a member of the aldehyde dehydrogenase family, a group of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. (creativebiomart.net)

Here, we tested the removal of formaldehyde and aromatic aldehydes using effective microorganisms including yeast, lactic acid bacteria, and photosynthetic bacteria. (springer.com)
Other aldehydes were analyzed by GC-MS. Results show that effective microorganisms remove 70-100 % of formaldehyde, benzaldehyde, and 4-methylbenzaldehyde in about a week. (springer.com)

It might play a role in the detoxification of aldehydes to avoid cell damage. (uniprot.org)

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)

Reduction of aromatic acids to aldehydes and alcohols in the cell-free system. (naver.com)
Gröger H, Hummel W, Borchert S, Kraußer M (2011) Reduction of ketones and aldehydes to alcohols. (springer.com)
Sjögren-Larsson syndrome is a genetic disease characterized by ichthyosis, mental retardation, spasticity and mutations in the ALDH3A2 gene coding for fatty aldehyde dehydrogenase, an enzyme necessary for oxidation of fatty aldehydes and fatty alcohols. (pubmedcentralcanada.ca)
Fatty aldehydes and their precursor lipids, such as fatty alcohols [ 30 ] and leukotriene B4 [ 38 , 39 ], accumulate in tissues of SLS patients. (pubmedcentralcanada.ca)

Detailed kinetic analyses of FOR indicate that C4 - C6 dialdehyde or acid-substituted aldehyde may serve as the physiological substrate for this enzyme. (uga.edu)
Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. (freepatentsonline.com)

[ 9 ] FALDH is involved in the oxidation of fatty aldehydes produced by catabolism of ether glycerolipids (plasmalogens), which are prominent phospholipids in myelin. (medscape.com)

Carboxylate reductases (CARs, E.C. 1.2.1.30) generate aldehydes from their corresponding carboxylic acid with high selectivity. (frontiersin.org)

1. Purification and properties of aryl-aldehyde: NADP-oxidoreductase from Neurospora crassa. (naver.com)
Purification, Characterization, and Properties of an Aryl Aldehyde Oxidoreductase from Nocardia Sp. (naver.com)

Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774. (expasy.org)
Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and FeS 2. (conicet.gov.ar)
The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically competent form an equatorial oxo ligand instead of the sulfido ligand. (conicet.gov.ar)
Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774. (genome.jp)
Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the Mo site. (genome.jp)

and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum. (wikipedia.org)
and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum [ PMID: 8026480 ]. (ebi.ac.uk)
The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. (ebi.ac.uk)

Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. (ebi.ac.uk)
Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg 2+, ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. (naver.com)
carboxylic acid reductase: cloning, expression, and characterization of a new aldehyde oxidoreductase family. (naver.com)

Numerous aldehyde dehydrogenase genes exist, of which ALDH2 is best known for its role in alcohol oxidation. (genecards.org)

[ 3 ] Subsequent studies identified a defect in fatty aldehyde dehydrogenase (FALDH), a component of the fatty alcohol:NAD oxidoreductase enzyme complex. (medscape.com)
[ 9 ] FALDH is a component of the fatty alcohol:NAD oxidoreductase enzyme complex that catalyzes the sequential oxidation of fatty alcohol to aldehyde and fatty acid. (medscape.com)
Fatty alcohol and aldehyde may likewise alter the normal integrity of myelin membranes in the brain, leading to white-matter disease and spasticity. (medscape.com)
Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. (medscape.com)
Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. (medscape.com)
1. Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. (qmul.ac.uk)

Thus AR might constitute an antioxidative enzyme involved in myocardial protection against endogenous and exogenous cytotoxic aldehydes and against oxidative stress. (biochemj.org)

Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. (medscape.com)
Rizzo WB, Carney G. Sjogren-Larsson syndrome: diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2). (medscape.com)
ALDH2 (Aldehyde Dehydrogenase 2 Family (Mitochondrial)) is a Protein Coding gene. (genecards.org)
GO annotations related to this gene include oxidoreductase activity and aldehyde dehydrogenase (NAD) activity . (genecards.org)
Sjögren-Larsson syndrome (SLS) is caused by mutations in the ALDH3A2 gene that encodes fatty aldehyde dehydrogenase (FALDH) [ 2 ], an enzyme that catalyzes the oxidation of aliphatic aldehydes to fatty acids [ 17 , 29 ]. (pubmedcentralcanada.ca)

Sjogren-Larsson syndrome: molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency. (medscape.com)

The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit liver. (genome.jp)

Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes. (genome.jp)
FALDH acts on several aliphatic aldehydes, but no single lipid has been identified yet as central to the pathogenesis. (pubmedcentralcanada.ca)

Aldehyde Dehydrogenase, Yeast, CAS 9028-88-0, is a native aldehyde dehydrogenase from yeast that catalyzes the oxidation of acetaldehyde to acetic acid. (merckmillipore.com)
The genetic defect in Sjögren-Larsson syndrome results in deficient activity of FALDH, which catalyzes the oxidation of fatty aldehyde to fatty acid. (medscape.com)
Microsomal fatty aldehyde dehydrogenase catalyzes the oxidation of aliphatic aldehyde derived from ether glycerolipid catabolism: implications for Sjogren-Larsson syndrome. (medscape.com)

Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations. (genecards.org)
Vascular responses to nitrite are mediated by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase in the rat. (semanticscholar.org)

The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). (wikipedia.org)

This protein belongs to the aldehyde dehydrogenase family of proteins. (genecards.org)

AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases [ PMID: 9275170 ]. (ebi.ac.uk)

Anatomy4

Organisms11

Diseases1

Chemicals and Drugs85

Analytical, Diagnostic and Therapeutic Techniques and Equipment13

Phenomena and Processes37

Disciplines and Occupations1

Information Science4

Health Care1

Nitrate-dependent regulation of acetate biosynthesis and nitrate respiration by Clostridium thermoaceticum. (1/1279)

Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. (2/1279)

A genetic linkage map of rat chromosome 9 with a new locus for variant activity of liver aldehyde oxidase. (3/1279)

Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. (4/1279)

Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (5/1279)

Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver. (6/1279)

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (7/1279)

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (8/1279)

Aldehyde Oxidoreductases

Aldehydes

Oxidoreductases

Aldehyde Dehydrogenase

Protein Disulfide Reductase (Glutathione)

Alcohol Oxidoreductases

Pyruvate Synthase

NADH, NADPH Oxidoreductases

Ketone Oxidoreductases

Glutaredoxins

NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases

Oxidation-Reduction

Protein Disulfide-Isomerases

Aldehyde Reductase

Oxidoreductases Acting on Sulfur Group Donors

Flavoproteins

Thioredoxins

Oxidoreductases Acting on Aldehyde or Oxo Group Donors

Amino Acid Sequence

Molecular Sequence Data

Quinone Reductases

Electron Transport Complex II

Nanoarchaeota

Wolinella

NAD

Catalysis

NADP

Thioredoxin-Disulfide Reductase

Disulfides

Substrate Specificity

Succinate Dehydrogenase

Coenzymes

Acetaldehyde

Oxidoreductases Acting on CH-CH Group Donors

Ecological and Environmental Processes

Electron Transport

Glucose Oxidase

Acrolein

Benzaldehydes

Sequence Homology, Amino Acid

Pleurotus

NAD(P)H Dehydrogenase (Quinone)

Ferredoxin-NADP Reductase

Flavin-Adenine Dinucleotide

Electron Transport Complex I

15-Oxoprostaglandin 13-Reductase

Escherichia coli

Flavins

Stereoisomerism

Alcohol Dehydrogenase

Kinetics

Sequence Alignment

Iron-Sulfur Proteins

Cysteine

Disulfiram

Oxidoreductases Acting on CH-NH2 Group Donors

Prokaryotic Cells

Xanthine Dehydrogenase

Protochlorophyllide

Ketones

Binding Sites

Models, Molecular

Multienzyme Complexes

Electrons

Retinal Dehydrogenase

Alcohols

FMN Reductase

Bacterial Proteins

Molecular Structure

Alkadienes

Periplasm

Glucose 1-Dehydrogenase

Sulfhydryl Compounds

Isomerases

PQQ Cofactor

Flavodoxin

Rhodobacter capsulatus

Sugar Alcohol Dehydrogenases

Hydroxysteroid Dehydrogenases

Protein Folding