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)

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

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

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

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

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 ( ...
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 ...
"Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry. 271 (1): 212-219 ...
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 ...
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 ...
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 ...
... 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. ...
November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239 ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, and aldehyde ... The systematic name of this enzyme class is aldehyde:NAD+ oxidoreductase. Other names in common use include CoA-independent ... In enzymology, an aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) is an enzyme that catalyzes the chemical reaction an aldehyde + ...
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 aldehyde:NADP+ oxidoreductase. Other names in common use include NADP+-acetaldehyde ... In enzymology, an aldehyde dehydrogenase (NADP+) (EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction an aldehyde + ... Adachi O, Matsushita K, Shinagawa E, Ameyama M (1980). "Crystallization and properties of NADP-dependent aldehyde dehydrogenase ...
NAD+ oxidoreductase. Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde ... ROTHSCHILD HA, BARRON ES (1954). "The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase". J. Biol. Chem. 209 (2 ...
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 aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called ... In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical ... Patel RN, Hou CT, Derelanko P, Felix A (1980). "Purification and properties of a heme-containing aldehyde dehydrogenase from ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is aryl-aldehyde:NADP+ oxidoreductase (ATP-forming). Other names in common use include ... 1. Purification and properties of aryl-aldehyde: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. 8 (3): 413-9. ... "Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa". Eur. J. ...
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 aryl-aldehyde:oxygen oxidoreductase. Crawford DL, Sutherland JB, Pometto AL, Miller ... In enzymology, an aryl-aldehyde oxidase (EC 1.2.3.9) is an enzyme that catalyzes the chemical reaction an aromatic aldehyde + ... H2O2 The 3 substrates of this enzyme are aromatic aldehyde, O2, and H2O, whereas its two products are aromatic carboxylic acid ...
The systematic name of this enzyme class is aldehyde:NAD(P)+ oxidoreductase. Other names in common use include aldehyde ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction an aldehyde ... Black S (1951). "Yeast aldehyde dehydrogenase". Arch. Biochem. Biophys. 34 (1): 86-97. doi:10.1016/S0003-9861(51)80013-4. PMID ...
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 abscisic-aldehyde:oxygen oxidoreductase. Other names in common use include abscisic ... In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction abscisic aldehyde ... Seo M, Koiwai H, Akaba S, Komano T, Oritani T, Kamiya Y, Koshiba T (2000). "Abscisic aldehyde oxidase in leaves of Arabidopsis ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is aryl-aldehyde:NAD+ oxidoreductase. This enzyme participates in tyrosine metabolism ... In enzymology, an aryl-aldehyde dehydrogenase (EC 1.2.1.29) is an enzyme that catalyzes the chemical reaction an aromatic ... H+ The 3 substrates of this enzyme are aromatic aldehyde, NAD+, and H2O, whereas its 3 products are aromatic acid, NADH, and H+ ...
... acceptor oxidoreductase (FAD-independent). Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with ... Andrade SL, Brondino CD, Feio MJ, Moura I, Moura JJ (2000). "Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB ... "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239): 1170-6. Bibcode ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ ... The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase. Achterholt S, Priefert H, Steinbuchel A ... In enzymology, a coniferyl-aldehyde dehydrogenase (EC 1.2.1.68) is an enzyme that catalyzes the chemical reaction coniferyl ... 2 H+ The 4 substrates of this enzyme are coniferyl aldehyde, H2O, NAD+, and NADP+, whereas its 4 products are ferulate, NADH, ...
Another oxidoreductase is formaldehyde ferredoxin oxidoreductase, or FOR, which catalyzes the oxidation of aldehydes into ... The next oxidoreductase, WOR4, does not help oxidize aldehydes, but rather has a role in the reduction of elemental sulfur (S0 ... The fifth and final oxidoreductase is named WOR5, and it has a broad specificity for aromatic and aliphatic aldehyde species. ... These enzymes function optimally above 90 °C. The first to be discovered was aldehyde ferredoxin oxidoreductase, or AOR, which ...
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 ...
... the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin Oxidoreductase". ...
NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction (11R)-dihydroartemisinic aldehyde + NADP+ ⇌ {\ ... Artemisinic aldehyde Delta11(13)-reductase (EC 1.3.1.92, Dbr2) is an enzyme with systematic name artemisinic aldehyde: ... Artemisinic+aldehyde+Delta11(13)-reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... displaystyle \rightleftharpoons } artemisinic aldehyde + NADPH + H+ This enzyme i present in Artemisia annua. Bertea CM, Freije ...
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. ...
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. CODH are a rather diverse group of enzymes, containing two unrelated types of CODH. Aerobic carboxydotrophic ... clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]". European Journal of Biochemistry ...
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, ...
... 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, ...
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 oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo ...
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 ...
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 glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and ...
... glyceraldehyde-3-phosphate ferredoxin oxidoreductase, respiratory arsenate reductase, carbon monoxide dehydrogenase, aldehyde ... Some bacterial oxidoreductases use tungsten in a similar manner as molybdenum by using it in a tungsten-pterin complex, with ... Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. The first tungsten-requiring enzyme to be ...
Upon forming the aldehyde in the ring opening step, it is oxidized to form the carboxylic acid and subsequently a ... an oxidoreductase. Then a final recyclization occurs to form aflatoxin B1. Aflatoxin B1 is a potent genotoxic hepatocarcinogen ...
All luciferases are classified as oxidoreductases (EC 1.13.12.-), meaning they act on single donors with incorporation of ... molecular oxygen oxidizes flavin mononucleotide and a long-chain aliphatic aldehyde to an aliphatic carboxylic acid. The ...
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+ ... 2002). "The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals ...
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 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating). This enzyme is also ...
Oxidoreductases are enzymes that catalyze the reactions that involve the transfer of electrons. Methanol in itself is toxic due ... Ethylene glycol (common antifreeze) can be converted into toxic glycolic acid, glyoxylic acid and oxalic acid by aldehyde ... but it can be converted to formaldehyde by alcohol dehydrogenase and then converted to formic acid by aldehyde dehydrogenase, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl ... The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include ...
These include cytochrome P450 2E1 (CYP2E1), quinine oxidoreductase (NQ01 or DT-diaphorase or NAD(P)H dehydrogenase (quinone 1 ... On some condensation products of aldehydes), Liebig's Annalen der Chemie und Pharmacie, 162(1): 77-124, 309-320. From p. 89: " ... Individuals carrying variant of NAD(P)H:quinone oxidoreductase 1 (NQO1), microsomal epoxide hydrolase (EPHX) and deletion of ...
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 fluoroacetaldehyde:NAD+ oxidoreductase. Murphy CD, Moss SJ, O'Hagan D (2001). " ... "Isolation of an aldehyde dehydrogenase involved in the oxidation of fluoroacetaldehyde to fluoroacetate in Streptomyces ...
The mechanism for the reduction of the CoA thioester to the aldehyde involves a hydride transfer to the carbonyl carbon from ... Cinnamoyl-CoA reductase (EC 1.2.1.44), systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but ... The tetrahedral intermediate then collapses, kicking out the CoA and forming an aldehyde as the final product. The thiolate of ... As can be seen in the diagram shown to the right, these monolignols are derived directly from their corresponding aldehydes, ...
... whereas its 3 products are coniferyl aldehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, ... The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD. Mansell RL ... coniferyl aldehyde + NADPH + H+ Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, ...
... whereas its 3 products are abscisic aldehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically ... The systematic name of this enzyme class is xanthoxin:NAD+ oxidoreductase. Other names in common use include xanthoxin oxidase ... abscisic aldehyde + NADH + H+ Thus, the two substrates of this enzyme are xanthoxin and NAD+, ... "The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde". Plant Cell. 14 (8): ...
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 2-methyl-3-oxopropanoate:NAD+ 3-oxidoreductase (CoA-propanoylating). Other names in ...
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 phenylglyoxylate:NAD+ oxidoreductase. It has 3 cofactors: FAD, Thiamin diphosphate ... Hirsch W, Schagger H, Fuchs G (1998). "Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic ...
Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... The systematic name of this enzyme class is long-chain-alcohol:oxygen oxidoreductase. Other names in common use include long- ... Yeast have low levels of fatty alcohol dehydrogenase.) The long-chain alcohol is then oxidized by long-chain fatty aldehyde ...
... whereas its two products are betaine aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, ... The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline ... oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase. This ... betaine aldehyde + reduced acceptor Thus, the two substrates of this enzyme are choline and acceptor, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of a donor with ... The systematic name of this enzyme class is L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). Other names in ... NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. This enzyme ...
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 5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD+ oxidoreductase. This enzyme is ...
... converting amines to aldehydes and NH3 by the reaction: amine + H2O + O2 ⇌ aldehyde + NH3 + H2O2 In humans, the pyridoxine 5′- ... Pyridoxine 5′-phosphate oxidase is a member of the enzyme class oxidases, or more specifically, oxidoreductases. These enzymes ...
... whereas its 4 products are aldehyde, ketone, nitrite, and H2O2. This enzyme belongs to the family of oxidoreductases, ... The systematic name of this enzyme class is nitroalkane:oxygen oxidoreductase. Other names in common use include nitroethane ... an aldehyde or ketone + nitrite + H2O2 The 3 substrates of this enzyme are nitroalkane, H2O, and O2, ... oxidase, NAO, and nitroethane:oxygen oxidoreductase. This enzyme participates in nitrogen metabolism. LITTLE HN (1951). " ...
oxidoreductase activity, acting on the aldehyde or oxo group of donors. 0.216422278300306. bayes_pls_golite062009. ... oxidoreductase activity [IEA. ] NAD or NADH binding [IEA. ] 3-hydroxybutyrate dehydrogenase activity [IEA. ] 2-deoxy-D- ... oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor ... oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor ...
Oxidoreductases Acting on Aldehyde or Oxo Group Donors [D08.811.682.657] Oxidoreductases Acting on Aldehyde or Oxo Group Donors ... Aldehyde Oxidoreductases (1978-2005). Public MeSH Note:. 2006; GLUTAMATE-5-SEMIALDEHYDE DEHYDROGENASE was indexed under ...
Cardiopulmonary resuscitation; Heart arrest; Nitric oxide; S-Nitrosoglutathione; Aldehyde Oxidoreductases; Animals; Benzoates; ...
Aldehyde Oxidoreductases (2) * Bacterial Proteins (2) * Biomass (2) * Biomass yield (2) * Catabolic pathway (2) ...
tungsten-containing aldehyde:ferredoxin oxidoreductase 157, 348. DVU1491. hypothetical protein DVU1491 134, 156. ...
Oxidoreductases, especially aldehyde dehydrogenases and aldo-keto reductases, are the first barrier against aldehyde compounds ... Characterization of human oxidoreductases involved in aldehyde odorant metabolism. Boichot, Valentin; Menetrier, Franck; Saliou ... Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the ... Glutathione S-Transferase Highly Expressed in Holotrichia parallela Antennae Inactivates the Odorant Unsaturated Aldehyde ...
Aldehyde/oxo oxidoreductases (EC 1.2). 1.2.1 - NAD or NADP acceptor. Aldehyde dehydrogenase - Acetaldehyde dehydrogenase (ALDH2 ... in which an aldehyde is converted into a carboxylic acid (ΔG°=-50 kJ/mol (-12kcal/mol)). The energy released by this highly ... Glyceraldehyde 3-phosphate dehydrogenase - Long-chain-aldehyde dehydrogenase. 1.2.4 - disulfide acceptor. Oxoglutarate ...
Tailoring Clostridium ljungdahlii for Improved Ethanol Production by Genetic Engineering of the Aldehyde:Ferredoxin ... Oxidoreductase (AOR) and Chemostat Fermentation Schulz, Sarah (2024-10-10); Dissertation * A Tale of Two Barrels: Import of β- ...
1 oxidoreductases.EC_1.2 oxidoreductase acting on aldehyde or oxo group of donor(50.1.2 : 625.6)","protein_coding" " ... 1 oxidoreductases.EC_1.3 oxidoreductase acting on CH-CH group of donor(50.1.3 : 207.1)","protein_coding" "Solyc07g055050.3.1"," ... 1 oxidoreductases.EC_1.14 oxidoreductase acting on paired donor with incorporation or reduction of molecular oxygen(50.1.13 : ... 1 oxidoreductases.EC_1.14 oxidoreductase acting on paired donor with incorporation or reduction of molecular oxygen(50.1.13 : ...
... and for being one of the few organisms identified as possessing aldehyde ferredoxin oxidoreductase enzymes containing tungsten ...
Quinone Oxidoreductase in Rat Liver. Kelly, V. P., Ellis, E. M., Manson, M. M., Chanas, S. A., Moffat, G. J., McLeod, R., Judah ... a Natural Benzopyrone That Is a Potent Inducer of Aflatoxin B1-Aldehyde Reductase, the Glutathione S-Transferase A5 and P1 ...
Combined deficiency of xanthine dehydrogenase and aldehyde oxidase, see Hereditary xanthinuria. *Combined immunodeficiency due ... Congenital adrenal hyperplasia due to apparent combined p450c17 and p450c21 deficiency, see Cytochrome P450 oxidoreductase ... Combined deficiency of sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase, see Molybdenum cofactor deficiency ... Combined xanthine oxidase and sulfite oxidase and aldehyde oxidase deficiency, see Molybdenum cofactor deficiency ...
For example, in the case of EC 1.2.3.4, the digits indicate that the enzyme is an oxidoreductase (class 1), that it acts on the ... aldehyde or oxo group of donors (subclass 2), that oxygen is an acceptor (sub-subclass 3) and that it was the fourth enzyme ... Clicking on the class or subclass title (e.g. "Oxidoreductases") will open a separate window with information describing the ... At the time of writing (June 2007), ExplorEnz holds 1108 class-1 entries (oxidoreductases), 1162 class-2 entries (transferases ...
Oxidoreductases 100% * Aldehydes 95% * Stem cells 93% * Aldehyde Dehydrogenase 85% * Biomarkers 82% ...
Bienzymatic Cascade Combining a Peroxygenase with an Oxidase for the Synthesis of Aromatic Aldehydes from Benzyl Alcohols. Ma, ... Oxidoreductases Engineering & Materials Science 90% * peroxygenase Medicine & Life Sciences 86% * Biocatalysts Engineering & ...
hexadecanol:NAD+ oxidoreductase. Comments:. The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme ... also oxidizes the corresponding aldehydes to fatty acids.. Links to other databases:. BRENDA, EXPASY, KEGG, MetaCyc, CAS ...
Broad specificity nadph-dependent aldehyde reductase, zn-containing; Catalyzes the reduction of a wide range of aldehydes into ... Putative nadh-binding oxidoreductase; Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides ... Broad specificity nadph-dependent aldehyde reductase, zn-containing; Catalyzes the reduction of a wide range of aldehydes into ... Broad specificity nadph-dependent aldehyde reductase, zn-containing; Catalyzes the reduction of a wide range of aldehydes into ...
Such enzymes are part of the aldo-keto reductase super family and represent monomeric NADPH-dependant oxidoreductases that have ... that sorbitol is being produced by alternate glycolysis pathways in the tumors and that our observation of decreased aldehyde ...
Oxidoreductases Acting on Aldehyde or Oxo Group Donors [D08.811.682.657] Oxidoreductases Acting on Aldehyde or Oxo Group Donors ... Oxidoreductases - Preferred Concept UI. M0015649. Scope note. The class of all enzymes catalyzing oxidoreduction reactions. The ... entry terms OXIDASES; REDUCTASES, and DEHYDROGENASES are GEN only: see Tree D8 under OXIDOREDUCTASES for all indentions and ... The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is ...
Oxidoreductases Acting on Aldehyde or Oxo Group Donors Oxidoreductases Acting on CH-CH Group Donors ...
1 Oxidoreductases. 1.2 Acting on the aldehyde or oxo group of donors ... 4,4-diapolycopene aldehyde oxidase, ALD, CrtN2, CrtNb, crtNc. ECTree. ...
2002-2005: 14 BI3 - Study of biochemical and physiological properties of plant amine oxidases and aldehyde oxidases ( ... 2008-2012: 522/08/0555 Structure-functional characterization of oxidoreductases acting on nitrogenous regulatory compounds in ... 2011-2013: PP501/11/1591 Structure-functional characterization of several plant aldehyde dehydrogenase families (coordinator ...
We conclude that Tyr-48 acts as the proton donor in the reduction of aldehydes by aldose reductase, while the neutral His-110 ... Aldose reductase, an NADPH dependent oxidoreductase, has received considerable attention due to its possible link to diabetic ...
aldehyde dehydrogenase (NAD );Aldehyde dehydrogenase family. 0.01. OF. AOA69117. No alias. Aldehyde dehydrogenase domain. 0.02 ... oxidoreductase activity. IEA. Interproscan. BP. GO:0055114. oxidation-reduction process. IEA. Interproscan. ... aldehyde dehydrogenase Atd3 (predicted).... 0.03. OF. YMR170C. No alias. Cytoplasmic aldehyde dehydrogenase; involved in ... aldehyde dehydrogenase (predicted).... 0.03. OF. SPCC550.10.1. No alias. ...
... betaine-aldehyde dehydrogenase to synthesize GB or/and As-GB. Both opuC and betB were distributed in various class-level clades ... most of which serve oxidoreductase functions [70]. Biosynthesis of Sec is not a common trait of prokaryotes [71]. Considering ...
3D Structure of chain 5OUJ_A - CRYSTAL STRUCTURE OF HUMAN AKR1B1 COMPLEXED WITH NADP+ AND COMPOUND 39 - 5OUJ | canSARS
1.-.-.- Oxidoreductases. *1.1.1.42 Isocitrate dehydrogenases. *1.2.3.1 Aldehyde oxidase. *1.4.3.13 Lysyl oxidases ...
... and aldehyde deformylating oxygenase (ADO) convert C16 acyl-ACP to the C15 pentadecane through an aldehyde (hexadecanal) ... oxidoreductase (FNR) to produce molecular hydrogen. Reprinted from Liu and co-workers [93]. (D) PduA*, a variant of the PduA ... oxidoreductase (FNR) to produce molecular hydrogen. Reprinted from Liu and co-workers [93]. (D) PduA*, a variant of the PduA ... and recognition that aldehyde intermediates such as 4-HPAA are channeled away by the yeasts endogenous enzymes [2,20,70]. The ...
  • Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. (string-db.org)
  • Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. (string-db.org)
  • For example, in the case of EC 1.2.3.4, the digits indicate that the enzyme is an oxidoreductase (class 1), that it acts on the aldehyde or oxo group of donors (subclass 2), that oxygen is an acceptor (sub-subclass 3) and that it was the fourth enzyme classified in this sub-subclass (serial number 4). (biomedcentral.com)
  • The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. (enzyme-database.org)
  • We conclude that Tyr-48 acts as the proton donor in the reduction of aldehydes by aldose reductase, while the neutral His-110 has a role in substrate binding during the catalysis. (sussex.ac.uk)

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