NADPH Dehydrogenase: A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1.NADH, NADPH Oxidoreductases: 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.NADPH Oxidase: A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.Superoxides: Highly reactive compounds produced when oxygen is reduced by a single electron. In biological systems, they may be generated during the normal catalytic function of a number of enzymes and during the oxidation of hemoglobin to METHEMOGLOBIN. In living organisms, SUPEROXIDE DISMUTASE protects the cell from the deleterious effects of superoxides.Membrane Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.PhosphoproteinsNADH Dehydrogenase: A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.NAD: 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)NADP: 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)Oxidation-Reduction: 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).Nitrate Reductase (NADH): An NAD-dependent enzyme that catalyzes the oxidation of nitrite to nitrate. It is a FLAVOPROTEIN that contains IRON and MOLYBDENUM and is involved in the first step of nitrate assimilation in PLANTS; FUNGI; and BACTERIA. It was formerly classified as EC 1.6.6.1.Reactive Oxygen Species: Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.Electron Transport Complex I: 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.Kinetics: The rate dynamics in chemical or physical systems.Onium Compounds: Ions with the suffix -onium, indicating cations with coordination number 4 of the type RxA+ which are analogous to QUATERNARY AMMONIUM COMPOUNDS (H4N+). Ions include phosphonium R4P+, oxonium R3O+, sulfonium R3S+, chloronium R2Cl+Cytochrome ReductasesAcetophenonesOxidoreductases: 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)Quinone Reductases: 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.Electron Transport: 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)Flavin Mononucleotide: A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.Cytochrome b Group: Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.Hydrogen Peroxide: A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.Cytochrome-B(5) Reductase: A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.NADP Transhydrogenases: Enzymes that catalyze the reversible reduction of NAD by NADPH to yield NADP and NADH. This reaction permits the utilization of the reducing properties of NADPH by the respiratory chain and in the reverse direction it allows the reduction of NADP for biosynthetic purposes.Multienzyme Complexes: 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.Flavin-Adenine Dinucleotide: 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)Alcohol Oxidoreductases: 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).Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Rotenone: A botanical insecticide that is an inhibitor of mitochondrial electron transport.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Oxidative Stress: 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).Neutrophils: Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Hydrogen-Ion Concentration: 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)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Oxygen Consumption: The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)Molecular Sequence Data: 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.Mitochondria, Heart: The mitochondria of the myocardium.FMN Reductase: 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.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Oxygen: 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.Phagocytes: Cells that can carry out the process of PHAGOCYTOSIS.FlavoproteinsGlucosephosphate DehydrogenaseAmino Acid Sequence: 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.2,6-Dichloroindophenol: A dye used as a reagent in the determination of vitamin C.Ferredoxin-NADP Reductase: 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.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Pentose Phosphate Pathway: An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Ferricyanides: Inorganic salts of the hypothetical acid, H3Fe(CN)6.Respiratory Burst: A large increase in oxygen uptake by neutrophils and most types of tissue macrophages through activation of an NADPH-cytochrome b-dependent oxidase that reduces oxygen to a superoxide. Individuals with an inherited defect in which the oxidase that reduces oxygen to superoxide is decreased or absent (GRANULOMATOUS DISEASE, CHRONIC) often die as a result of recurrent bacterial infections.Escherichia coli: 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.Ubiquinone: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Submitochondrial Particles: The various filaments, granules, tubules or other inclusions within mitochondria.Mixed Function Oxygenases: Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.Flavins: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.L-Lactate Dehydrogenase: A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.NADH Tetrazolium Reductase: Catalyzes the reduction of tetrazolium compounds in the presence of NADH.Dihydrolipoamide Dehydrogenase: 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.MalatesSuccinates: Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.Glycerolphosphate Dehydrogenaserac1 GTP-Binding Protein: A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.Cattle: 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.Xanthine Oxidase: An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria.PyruvatesMembrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Electron Spin Resonance Spectroscopy: 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.Isocitrate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.Dicumarol: An oral anticoagulant that interferes with the metabolism of vitamin K. It is also used in biochemical experiments as an inhibitor of reductases.Superoxide Dismutase: An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1.Cell-Free System: A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)Pyruvic Acid: An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Molecular Weight: The sum of the weight of all the atoms in a molecule.Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Cytochrome P-450 Enzyme System: A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Spectrophotometry, Ultraviolet: Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Oxygenases: Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.Sulfite Reductase (NADPH): A NADPH-dependent oxidase that reduces hydrogen sulfite to HYDROGEN SULFIDE. It is found in many microoganisms.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Cyanides: Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Catalase: An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.rac GTP-Binding Proteins: A sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. This enzyme was formerly listed as EC 3.6.1.47.Dithionite: Dithionite. The dithionous acid ion and its salts.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Cytochromes: Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.Sugar Alcohol Dehydrogenases: 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.Imidazolines: Compounds based on reduced IMIDAZOLES containing a single double bond.Enoyl-(Acyl-Carrier-Protein) Reductase (NADH): An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.Protein Binding: 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.Antioxidants: Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.Glutathione: 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.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Cytochromes b5: Cytochromes of the b group that are found bound to cytoplasmic side of ENDOPLASMIC RETICULUM. They serve as electron carrier proteins for a variety of membrane-bound OXYGENASES. They are reduced by the enzyme CYTOCHROME-B(5) REDUCTASE.Glutathione Reductase: 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.
Reaction catalyzed: NADPH + NAD+ = NADP+ + NADH. NAD(P) transhydrogenase, mitochondrial abundance may be associated with human ... the enzyme uses energy from the mitochondrial proton gradient to produce high concentrations of NADPH. The resulting NADPH is ... In failing hearts, a partial loss of NAD(P) transhydrogenase's mitochondrial activity negatively impacts the NADPH-dependent ... Sheeran FL, Rydström J, Shakhparonov MI, Pestov NB, Pepe S (2010). "Diminished NADPH transhydrogenase activity and ...
Examples include NADPH, NADH, and FADH. The main role of these is to transport hydrogen atom to electron transport chain which ...
Category:EC 1.6 (act on NADH or NADPH)Edit. *Category:EC 1.6.1 (with NAD+ or NADP+ as acceptor) ...
Either NADH or NADPH can be used; in the model plant species Arabidopsis thaliana C-5 sterol desaturase catalyzes the reaction ... twice as fast with NADH while in S. cerevisiae the enzyme has little preference. The precise details of the reaction have been ...
Thus NADPH is also required for the synthesis of cholesterol from acetyl-CoA; while NADH is generated during glycolysis.) The ... When malate is oxidatively decarboxylated by "NADP+-linked malic enzyme" to form pyruvate, CO2 and NADPH are formed. NADPH is ... This difference exemplifies a general principle that NADPH is consumed during biosynthetic reactions, whereas NADH is generated ... Fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the action of enzymes called fatty acid ...
It has 3 cofactors: NADH, NADPH, and Heme. Lynn, W.S.; Brown, R.H. (1958). "The conversion of progesterone to androgens by ...
Thus NADPH is also required for the synthesis of cholesterol from acetyl-CoA; while NADH is generated during glycolysis.) The ... When malate is oxidatively decarboxylated by "NADP+-linked malic enzyme" pyruvate, CO2 and NADPH are formed. NADPH is also ... This difference exemplifies a general principle that NADPH is consumed during biosynthetic reactions, whereas NADH is generated ... D. L. Vander Jagt; B. Robinson; K. K. Taylor; L. A. Hunsaker (1992). "Reduction of trioses by NADPH-dependent aldo-keto ...
EC 1.6 (delujejo na NADH ali NADPH)[uredi , uredi kodo]. *EC 1.6.1 (NAD+ ali NADP+ kot akceptor) ...
They transfer electrons from NADH or NADPH to nitrate. Prokaryotic nitrate reductases belong to the DMSO reductase family of ...
Either NADH or NADPH can be used as cofactor. The most active substrate at pH 5.0 is aminoethylcysteine ketimine (AECK), ... This gene encodes a taxon-specific crystallin protein that binds NADPH and has sequence similarity to bacterial ornithine ...
... and ethanol via NADH- and NADPH-linked alcohol dehydrogenase. By its side, the acidogenic activity was found in the early 20th ...
NADPH is the preferred cofactor, but NADH is also used. Octopine dehydrogenase is involved in the reductive condensation of ...
... is an essential component of the membrane-associated enzyme phagocyte NADPH-oxidase This enzyme uses NADH or NADPH as the ... "Expression of NADH/NADPH oxidase p22phox in human coronary arteries." Circulation. October 5, 1999; 100(14): 1494-8. Fortuna A ... "p22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II induced ...
XR is reducing D-xylose to xylitol using NADH or NADPH. Xylitol is then oxidized to D-xylulose by XDH, using the cofactor NAD. ... Since the pentose phosphate pathway produces additional NADPH during metabolism, limiting this step will help to correct the ...
Additionally, NADPH can take the place of NADH in this reaction. This enzyme belongs to the family of oxidoreductases, ... As mentioned earlier, these enzymes have the ability to use either NADH or NADPH as the coenzyme. This gives them an advantage ... However, due to the relatively large concentration of NADPH compared to NADH under normal cellular concentration, the GRHPR ... NADH + H+ Thus, the two substrates of this enzyme are (R)-glycerate and NAD+, whereas its 3 products are hydroxypyruvate, NADH ...
NADH-dihydropteridine reductase, NADPH-dihydropteridine reductase, NADPH-specific dihydropteridine reductase, dihydropteridine ... NADH/NADPH cytochrome c reductase activity mediated with 6,7-dimethyltetrahydropterin". Insect Biochem. 2 (8): 385-399. doi: ... NADH, NADPH, and H+. This enzyme participates in folate biosynthesis. This enzyme belongs to the family of oxidoreductases, ... Nakanishi N, Hasegawa H, Watabe S (March 1977). "A new enzyme, NADPH-dihydropteridine reductase in bovine liver". Journal of ...
Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases EC 1.1.1.- (genes adh1, bdhA and bdhB), enzymes ... It catalyzes the oxidation of ethanol to acetaldehyde (ethanal): CH3CH2OH + NAD+ → CH3CHO + NADH + H+ This allows the ... leading to NADH and a zinc bound aldehyde or ketone Release of the product aldehyde. The mechanism in yeast and bacteria is the ... NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also ...
NADH, NADPH. Reduction. Ovary, endometrium, breast, brain, prostate, placenta. Strongly restricted. Breast cancer, prostate ... NADPH. Reduction. Testis, ovary, blood, saliva, skin, adipose tissue, brain, bone. Strongly restricted. 17β-HSD3 deficiency, ... NADH/NAD+. Reduction / oxidation. Retina, liver, adipose tissue, blood, others. ?. Fundus albipunctatus ... NADPH. Reduction. Prostate, mammary gland, liver, kidney, lung, heart, small intestine, colon, uterus, testis, brain, skeletal ...
... it is activated by NAD but inhibited noncompetitively by NADH and NADPH. Tabuchi T; Satoh T (1976). "Distinction between ...
... e.g.NADH, NADPH). These elements create monomers, the building blocks for macromolecules. Some important biological ... "The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6- ... These may be metal ions, vitamin derivatives such as NADH and acetyl CoA, or non-vitamin derivatives such as ATP. In the case ... Aspartate semialdehyde dehydrogenase catalyzes the NADPH-dependent reduction of aspartyl phosphate to yield aspartate ...
This reaction oxidizes NADPH to NADP+. Sorbitol dehydrogenase can then oxidize sorbitol to fructose, which produces NADH from ... and using much more NADPH, leaving less NADPH for other processes of cellular metabolism. This change of affinity is what is ... NADPH acts to promote nitric oxide and glutathione production, and its deficiency will cause glutathione deficiency as well. A ... Therefore, NADPH prevents reactive oxygen species from accumulating and damaging cells. Excessive activation of the polyol ...
Bacterial NADK is shown to be inhibited allosterically by both NADPH and NADH. NADK is also reportedly stimulated by calcium/ ... Due to the essential role of NADPH in lipid and DNA biosynthesis and the hyperproliferative nature of most cancers, NADK is an ... Tedeschi PM, Lin H, Gounder M, Kerrigan JE, Abali EE, Scotto K, Bertino JR (Oct 2015). "Suppression of Cytosolic NADPH Pool by ... While the role of NADK in increasing the NADPH pool appears to offer protection against apoptosis, there are also cases where ...
It can use both NADPH and NADH as a cofactor, but prefers NADPH. The enzyme substrate, glyoxylate, is a metabolite in plant ... Kleczkowski LA, Randall DD, Blevins DG (July 1987). "Inhibition of Spinach Leaf NADPH(NADH)-Glyoxylate Reductase by ... Other names in common use include NADH-glyoxylate reductase, glyoxylic acid reductase, and NADH-dependent glyoxylate reductase ... using the cofactor NADH or NADPH. The systematic name of this enzyme class is glycolate:NAD+ oxidoreductase. ...
The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen ... Fujii T, Kaneda T (1985). "Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from ... NADH, NADPH, H+, and O2, whereas its 4 products are 3,4-dihydroxybenzoate, NAD+, NADP+, and H2O. This enzyme belongs to the ...
The reactions related to the urea cycle produce NADH), and NADH can be produced in two different ways. One of these uses ... Another part of the cycle requires NADPH for the synthesis of fatty acids. Part of this reducing power is generated when the ... NADH reduces oxaloacetate to malate. This transformation is needed to transport the molecule out of the mitochondria. Once in ... Firstly the oxaloacetate is reduced to malate using NADH. Then the malate is decarboxylated to pyruvate. Now this pyruvate can ...
NADH and NADPH. The NAD+/NADH form is more important in catabolic reactions, while NADP+/NADPH is used in anabolic reactions. ... Although some more ATP is generated in the citric acid cycle, the most important product is NADH, which is made from NAD+ as ... This process uses the ATP and NADPH produced by the photosynthetic reaction centres, as described above, to convert CO2 into ... These proteins use the energy released from passing electrons from reduced molecules like NADH onto oxygen to pump protons ...
NADPH redox, special tRNA synthetases, etc.. You can help by adding to it. (January 2013) ... which is similar to the NADH dehydrogenase found in mitochondria.[22][25] ... "Multistep assembly of chloroplast NADH dehydrogenase-like subcomplex A requires several nucleus-encoded proteins, including ...
Kleczkowski LA, Randall DD, Blevins DG (1986). "Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate ... NADPH + H+ Thus, the two substrates of this enzyme are glycolate and NADP+, whereas its 3 products are glyoxylate, NADPH, and ... Other names in common use include NADPH-glyoxylate reductase, and glyoxylate reductase (NADP+). This enzyme participates in ...
The oxidation of NADH to NAD+ is critical for cold growth. Then, we examined whether changes in the NADH/NAD+ ratio might also ... Recombinant strains of S. cerevisiae modified for increased NADPH- and NADH-dependent Gdh1 and Gdh2 activity were tested for ... Schematic representation of some yeast NADH- and NADPH-dependent reactions and pathways cited in the text. Adh1-3 alcohol ... Redox engineering by ectopic expression of glutamate dehydrogenase genes links NADPH availability and NADH oxidation with cold ...
... to NADH, which can enter the respiratory chain for energy generation. ... Conversion of NADPH, generated by peripheral catabolic pathways, ... NADPH + NAD+ = NADP+ + NADH.. ,p>This subsection of the ... Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy ...
Finally, the fact that NADH, NAD+, and ADP all bind to the same site requires a re-analysis of the previous models for NADH ... As expected, since NADPH does not bind well to the second coenzyme site, no evidence of a bound molecule is observed at the ... Finally, the fact that NADH, NAD+, and ADP all bind to the same site requires a re-analysis of the previous models for NADH ... Finally, the fact that NADH, NAD+, and ADP all bind to the same site requires a re-analysis of the previous models for NADH ...
The mutations increased the KM for NADPH 880-fold, but only 2.5-fold for NADH. Overall, the catalytic efficiency for NADH ... twofold for NADH and threefold for NADPH) (Table S2) but also decreased the kcat on NADH (fourfold), thereby reducing the 46- ... Se_KARIDD (Table 1) had an eightfold decreased kcat with NADPH (from 0.8 to 0.1 s−1), whereas the kcat with NADH increased from ... Catalytic efficiency NADH/catalytic efficiency NADPH, on log scale, for six wild-type KARIs (light gray) and their cofactor- ...
Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase ... Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase ... activated by angiotensin II infusion is an NADH/NADPH-dependent, membrane-bound oxidase. Angiotensin II-, but not NE-, induced ...
NADH/NADPH Oxidase Activity. Aortic homogenates were prepared on ice in lysis buffer containing 1 mmol/L EGTA, 20 mmol/L ... and 1 mmol/L NADH or NADPH. Luminescence was calculated as the rate of counts per mg protein after deduction of the counts ... Antioxidant effects of vitamins C and E are associated with altered activation of vascular NADPH oxidase and superoxide ... NADPH (1 mmol/L), H4B (5 μmol/L), Ca2+ (2 mmol/L), L-valine (50 mmol/L), and a mixture of unlabeled (0 to 5 μmol/L) and L-[3H]- ...
Intracellular NADH and NADPH Determination. Intracellular levels of NADH and NADPH were determined with the PicoProbe NADH ... Bar charts show mean concentrations (±SEM) of n = 6 (ATP, AMP, NADPH) or n = 3 (NADH). Statistical analysis was performed using ... Concentrations of NADH and NADPH were calculated using standard curves and normalized to total protein concentration of the ... B) Intracellular TCA metabolites were generated as in panel (A). (C) Intracellular ATP, AMP, NADH, and NADPH concentrations ...
NAD+ and NADH, respectively) and determining their ratio in biological samples or in defined enzyme reactions. ... The NAD/NADH-Glo Assay is a bioluminescent, homogeneous single-reagent-addition assay for detecting total oxidized and reduced ... NAD/NADH-Glo™ Assay and NADP/NADPH-Glo™ Assays. The NAD/NADH-Glo and NADP/NADPH-Glo Assays are bioluminescent, homogeneous, ... allowing detection of total cellular NAD+ and NADH or NADP+ and NADPH. For the NAD/NADH-Glo™ Assay, an accessory protocol is ...
Direct transfer of NADH. 2 NAD in Skin. 2 NADH the energizing coenzyme. 1 Ca2-controls-slow-NADPH-oscillations-in-glucose- ... NAD and NADH in cellular functions and cell death. 1 NADH supplementation decreases pinacidil-primed. 1 NADH_NAD redox state of ... Ca2-controls-slow-NADPH-oscillations-in-glucose-stimulated-mouse-pancreatic-islets Ca2-controls-slow-NADPH-oscillations-in- ... Angiotensin II Stimulates NADH and NADPH Oxidase Activity in Cultured Vascular Smooth Muscle Cells ...
nadh / nadph. in Cell Biology Started by waddle, 26 Aug 2004 *0 replies ...
NADH. Nicotinamide adenine dinucleotide. NADPH. Nicotinamide adenosine dinucleotide phosphate. PHB. Poly-3-hydroxybutyrate ...
Enhanced NADH/NADPH oxidase-dependent *O(2)(-) production may contribute to endothelial dysfunction and vascular hypertrophy in ... Vascular NADH/NADPH oxidase is involved in enhanced superoxide production in spontaneously hypertensive rats. Hypertension 2000 ... Treated SHR had similar NADH/NADPH oxidase activity and p22phox expression as the WKY(30) group. The vascular functional and ... Vascular NADH/NADPH oxidase is involved in enhanced superoxide production in spontaneously hypertensive rats ...
Within this food set, the only possible route for the de novo synthesis of NADH depends on a reaction where PRPP reacts with ... In E. coli, PRPP is involved in many metabolic pathways being the precursor of histidine and NADH. ... Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenasee/Etf complex ... dxyl5p + nad + phthr → co 2 + pi + pdx5p + nadh + h 2o + h 2o + h ...
NADH), variation in metal dependence and the differences in the oligomeric state. In our study we investigated evolutionary ... However, global analysis of these enzymes unveiled significant functional diversity in the preference for cofactors (NADPH vs. ... NADH), variation in metal dependence and the differences in the oligomeric state. In our study we investigated evolutionary ... However, global analysis of these enzymes unveiled significant functional diversity in the preference for cofactors (NADPH vs. ...
NADPH), flavine adenine dinucleotide (FAD) and flavine mononucleotide (FMN). The 2D-spectrum of NADH (340/460 nm) is depicted ... Figure 15. 2-D fluorescence spectrum (A) nicotineamide dinucleotide (NADH) (pH = 7) and (B) Sacharomyces cerevisiae SP4 ... Figure 15. 2-D fluorescence spectrum (A) nicotineamide dinucleotide (NADH) (pH = 7) and (B) Sacharomyces cerevisiae SP4 ...
NADH. nicotinamide adenine dinucleotide. NADPH. nicotinamide adenine dinucleotide phosphate. Nrf1. nuclear respiratory factor 1 ... 8,17,35] It can enter the citric acid cycle to reduce NAD+ to NADH and can be used as a carbon source even in the presence of ... NADH)/nicotinamide adenine dinucleotide (NAD+) ratio due to increased lipid oxidation [13]. β-hydroxybutyric acid is the ketone ... NADPH), amino acids, nucleotides and fatty acids. Additionally, stimulation of lymphocyte B causes upregulation of glycolysis ...
NADH. +CoASH. Citrate. Acetyl CoA. ADP. CoA. OAA. ATP-citrate. Lyase. (Fed state). Malate. Malic Enzyme. NADP+. NADPH. CO2. ... NADH. NAD+. CO2. CO2. NADH. NAD+. ATP, NADH. ADP, Ca 2+. ATP, GTP, NADH, Succinyl CoA. Ca 2+. GDP. TPP. FAD. FADH2. Malonate, ... 14 NADPH. 14 NADP+. Chain elongaton. (adding malonyl CoA) / desaturtion (5,6,9 C). 1. Cytochrome b5. 2. Desaturase. 3. NADPH- ... NADH. NAD+. ADP. Glyceraldehyde 3-phosphate. Dihydroxyacetone Phosphate. Glycerol 3 Phosphate. NADH. NAD+. Glycerol 3 phosphate ...
... and NADH/NADPH oxidase.8,9⇓ Recent evidences suggest that among them, NADH/NADPH oxidase plays a crucial role in the generation ... Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ Res. 1994; 74: 1141- ... Phagocytic NADH/NADPH oxidase is composed of at least 6 components: plasma membrane spanning cytochrome b558 composed of gp91 ... These results suggest that the ROS derived from p22phox-based NADH/NADPH oxidase play an important role in the instability of ...
Category:EC 1.6 (act on NADH or NADPH)Edit. *Category:EC 1.6.1 (with NAD+ or NADP+ as acceptor) ...
NADH. PHOSPHATASE. GLUCOSE. NADPH. ALLYL ALCOHOL. GLUCOSE-6-PHOSPHATE. NITROETHANE. ALTRONOLACTONE. GLUCOSIDASE. OCTYLAMINE. ...
NADH and A-Ketoglutarate in P Flourescens Exposed to Oxidative Stress Introduction Oxygen and Life The metabolic processes su ... The Modulation of NADPH, NADH and A-Ketoglutarate in P Flourescens Exposed to Oxidative Stress. The Modulation of NADPH, NADH ... and uncoupled PC and PEPCK help transform NADH into NADPH, and increased direct enzymatic conversion of NAD+ and NADH to NADP+ ... IV: Conversion of NADH to NADPH. METABOLIC NETWORKS EVOKED BY ROS. A: The Glyxoylate Shunt. As citrate was the sole source of ...
NADH-dependent enzymes‎ (2 C). *. ► NADPH-dependent enzymes‎ (4 C). *. ► Neuraminidase‎ (2 C, 20 F) ...
Klingerberg M. (1985) NADH/NADPH. UV-methods, inMethods of Enzymatic Analysis, Vol. 7 (Bergmeyer J. and Graß1 M., eds), pp. 251 ... Wulff K. (1985) NADH/NADPH. Luminometric method, inMethods of Enzymatic Analysis, Vol. 7 (Bergmeyer J. and Graß1 M., eds), pp. ... NADH-CoQ1 reductase (nmol/min/mg of protein). Succinate-cytochrome c reductase (nmol/min/mg of protein). Cytochrome c oxidase ( ... NADPH concentrations were measured as previously reported (García-Nogales et al., 1999). In brief, neurons plated in 4-cm2 ...
Genetic variation of NADPH/NADH oxidase and susceptibility to diffuse panbronchiolitis (DPB) and chronic obstructive pulmonary ... Genetic variation of NADPH/NADH oxidase and susceptibility to diffuse panbronchiolitis (DPB) and chronic obstructive pulmonary ... a critical subunit of superoxide-generating NADH/NADPH oxidase, and susceptibility to DPB and COPD. Blood samples obtained from ...
The C242T-polymorphism of the NADPH/NADH oxidase gene p22phox subunit is not associated with pre-eclampsia.. Raijmakers MT1, ... Therefore we studied the prevalence of the C242T polymorphism in the NADPH/NADH oxidase gene in women with pre-eclampsia and/or ... Blood pressure is partly controlled by O(-)(2) production by NADPH/NADH oxidase and recently it was shown that a C242T ... In conclusion the C242T polymorphism in the p22phox subunit of the NADPH/NADH oxidase gene is not associated with pre-eclampsia ...
  • We also demonstrated that decreased capacity of glycerol production impairs growth at 15 but not at 30°C and that 15°C-grown baker's yeast cells display higher fermentative capacity than those cultivated at 30°C. Thus, increasing NADH oxidation by overexpression of GDH2 would help to avoid perturbations in the redox metabolism induced by a higher fermentative/oxidative balance at low temperature. (biomedcentral.com)
  • However, a major limitation is the increased need of oxidation of NADH to NAD + at low temperature. (biomedcentral.com)
  • However, increased or reduced NADPH availability by knock-out or overexpression of GRE3 , the NADPH-dependent aldose reductase gene, eliminated or exacerbated the cold-growth defect observed in YEpGDH1 cells. (biomedcentral.com)
  • The boGDH·NADPH·GLU·GTP complex shows the location of the additional phosphate on the active site coenzyme molecule and the GTP molecule bound to the GTP inhibitory site. (utmb.edu)
  • As expected, since NADPH does not bind well to the second coenzyme site, no evidence of a bound molecule is observed at the second coenzyme site under the pivot helix. (utmb.edu)
  • An adequate supply of NAD(P) precursors as well as a proper level of reducing equivalents in the form of NADPH are required for cold growth. (biomedcentral.com)
  • Here we present a straightforward recipe for altering the cofactor specificity of a class of NADPH-dependent oxidoreductases, the ketol-acid reductoisomerases (KARIs). (pnas.org)
  • Efforts to switch the cofactor specificity of oxidoreductases from NADPH to NADH have been made with varying degrees of success ( 8 ⇓ ⇓ ⇓ ⇓ ⇓ ⇓ ⇓ ⇓ - 17 ). (pnas.org)
  • Studies using various enzyme inhibitors and vascular homogenates suggested that the predominant source of .O2- activated by angiotensin II infusion is an NADH/NADPH-dependent, membrane-bound oxidase. (jci.org)
  • In particular, the C terminus functions as a toggle switch, which affects access of the NADPH substrate to the enzyme. (pnas.org)
  • The NADPH-oxidases (NOXs) form the only known enzyme family whose sole function is reactive oxygen species (ROS) generation ( 1 , 2 ). (pnas.org)
  • Campylobacter jejuni encodes 12 of the 14 subunits that make up the respiratory enzyme NADH:ubiquinone oxidoreductase (also called complex I). The two nuo genes not present in C. jejuni encode the NADH dehydrogenase, and in their place in the operon are the novel genes designated Cj1575c and Cj1574c. (asm.org)
  • This complex (also called NADH:ubiquinone oxidoreductase) is the first enzyme in many respiratory chains and catalyzes the transfer of electrons from NADH to the quinone pool, coupled with the translocation of protons across a membrane ( 12 ). (asm.org)
  • Under most physiological conditions, the enzyme uses energy from the mitochondrial proton gradient to produce high concentrations of NADPH. (wikipedia.org)
  • In failing hearts, a partial loss of NAD(P) transhydrogenase's mitochondrial activity negatively impacts the NADPH-dependent enzyme activities in the mitochondria and the capacity of mitochondria to maintain proton gradients, which may adversely impact energy production and oxidative stress defense in heart failure and exacerbate oxidative damage to cellular proteins. (wikipedia.org)
  • The progress curves obtained with preactivated enzyme are approximately exponential even at saturating concentrations of NADPH ( K m = 0.4 μM at 25°C, pH 7.3) and Hg 2+ ( K m = 3.2 μM in the presence of 1 mM cysteine). (wiley.com)
  • For hereditary methemoglobinemias, reduced enzyme activity is seen with NADH-methemoglobin reductase deficiency, but normal in HbM disease. (cdc.gov)
  • The enzyme-NADH complex is dissociated to be rate determining. (wikibooks.org)
  • To remove the effect of NADH or NADPH background, a blank sample may be set up for each sample by omitting the Glucose-6-Phosphate Enzyme Mix. (sigmaaldrich.com)
  • In our previous studies we have shown that the NADH dehydrogenase catalyzed electron transfer phenomenon is correlated with the affinity of anthraquinone drugs to the enzyme. (cognizantcommunication.com)
  • Enhanced NADH/NADPH oxidase-dependent *O(2)(-) production may contribute to endothelial dysfunction and vascular hypertrophy in this genetic model of hypertension. (unav.edu)
  • Furthermore, thrombin stimulated the phosphorylation of the PI 3-kinase target protein kinase B/Akt in a redox-sensitive and NADPH oxidase-dependent manner. (ahajournals.org)
  • This response is mediated by NADPH oxidase-dependent activation of p38 MAP kinase and the PI 3-kinase/protein kinase B/Akt pathway. (ahajournals.org)
  • These findings reveal the existence of slow oscillations in NAD(P)H autofluorescence in intact pancreatic islets, and suggest that they are shaped by Ca2+ concentration in a dynamic balance between activation of NADH -generating mitochondrial dehydrogenases and a Ca2+-induced decrease in NADH . (nadh.wiki)
  • The vascular functional and morphological parameters were improved in SHR(30)-I. These findings suggest that an association exists between p22phox gene overexpression and NADH/NADPH overactivity in the aortas of adult SHR. (unav.edu)
  • In SHR(30) compared with WKY(30), we found significantly greater p22phox mRNA level, NADH/NADPH-driven *O(2)(-) production, media thickness, and cross-sectional area and an impaired vasodilation in response to acetylcholine. (unav.edu)
  • Treated SHR had similar NADH/NADPH oxidase activity and p22phox expression as the WKY(30) group. (unav.edu)
  • In the presence of 1 mM cysteine only one equivalent of NADPH per FAD seems to be required for full activation which occurs after an incubation time of about 10 min. (wiley.com)
  • Our results suggest that NADPH production from D-glucose accounts for glutathione regeneration and protection from mitochondrial dysfunction. (wiley.com)
  • The effect of NADH and reduced ferredoxin on hydrogen production by Hyd1ABC. (asm.org)
  • Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. (uniprot.org)
  • Further implication of cytosolic NADPH in insulin secretion," The Journal of Biological Chemistry , vol. 270, no. 34, pp. 20051-20058, 1995. (hindawi.com)
  • The absorption of the NADPH probe is directly proportional to the concentration of NADPH in the solution. (abcam.com)
  • One approach to overcoming the cofactor imbalance is to engineer KARI to use NADH generated in glycolysis, thereby enabling anaerobic production of BCAA pathway products ( 7 , 8 ). (pnas.org)
  • Under the anaerobic conditions preferred for large-scale fermentations, biosynthesis of BCAAs and other products that use this pathway is limited by the pathway's cofactor imbalance and reduced cellular production of NADPH ( 7 , 8 ). (pnas.org)
  • We are going to need a biological reducing agent, like NADH, to carry out the second. (csbsju.edu)
  • That biological reducing agent, closely related to NADH, will be used to help reduce carbon dioxide. (csbsju.edu)