L-Iditol 2-Dehydrogenase: An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14L-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.Alcohol Dehydrogenase: 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.Glyceraldehyde-3-Phosphate Dehydrogenases: Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.Aldehyde Dehydrogenase: 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.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.Glucosephosphate DehydrogenaseMalate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.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.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).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.Carbohydrate Dehydrogenases: Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates 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 1.1.99.Succinate Dehydrogenase: 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.Glycerolphosphate DehydrogenaseNAD: 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)Glucose 1-Dehydrogenase: 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.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Ketoglutarate Dehydrogenase ComplexAldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Glucose Dehydrogenases: D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.Phosphogluconate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.NADH 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.IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Formate Dehydrogenases: Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.Acyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Xanthine Dehydrogenase: 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.3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.Hydroxybutyrate DehydrogenasePyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.11-beta-Hydroxysteroid Dehydrogenases: Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.Oxidoreductases: 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)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)Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Kinetics: The rate dynamics in chemical or physical systems.Glucosephosphate Dehydrogenase Deficiency: A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.11-beta-Hydroxysteroid Dehydrogenase Type 1: A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.Alanine Dehydrogenase: An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.Mannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.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.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Butyryl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Retinal Dehydrogenase: 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.20-Hydroxysteroid Dehydrogenases: A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).Amino 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.11-beta-Hydroxysteroid Dehydrogenase Type 2: An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.Acyl-CoA Dehydrogenase, Long-Chain: A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.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).Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Isovaleryl-CoA Dehydrogenase: A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).3-Isopropylmalate Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.Malate Dehydrogenase (NADP+)Pyruvate Dehydrogenase (Lipoamide)-Phosphatase: (Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.Leucine Dehydrogenase: An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.Phosphoglycerate Dehydrogenase: An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Estradiol Dehydrogenases: Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Glutamate Dehydrogenase (NADP+)Succinate-Semialdehyde Dehydrogenase: An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).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.Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating): An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Oxidoreductases Acting on CH-CH Group Donors: 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.Prephenate Dehydrogenase: An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Cloning, Molecular: 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.1-Pyrroline-5-Carboxylate Dehydrogenase: An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.Glutaryl-CoA Dehydrogenase: A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.PyruvatesCoenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.20-alpha-Hydroxysteroid Dehydrogenase: An enzymes that catalyzes the reversible reduction-oxidation reaction of 20-alpha-hydroxysteroids, such as from PROGESTERONE to 20-ALPHA-DIHYDROPROGESTERONE.Ketoglutaric Acids: A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)Oxidoreductases Acting on CH-NH Group Donors: Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.Glycerol-3-Phosphate Dehydrogenase (NAD+)Acetaldehyde: 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.Saccharopine Dehydrogenases: Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.Galactose Dehydrogenases: D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.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)Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.Dimethylglycine Dehydrogenase: A FLAVOPROTEIN enzyme that catalyzes the oxidative demethylation of dimethylglycine to SARCOSINE and FORMALDEHYDE.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)Aspartate-Semialdehyde Dehydrogenase: An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.Betaine-Aldehyde Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Mutation: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.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)Pyruvate Dehydrogenase Complex Deficiency Disease: An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.Mitochondria, Liver: Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)PQQ Cofactor: 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.Cortisone Reductase: An enzyme that catalyzes the interconversion of a ketone and hydroxy group at C-20 of cortisone and other 17,20,21-trihydroxy steroids. EC 1.1.1.53.IsocitratesProline Oxidase: The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Formates: Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.MalatesAspartokinase Homoserine Dehydrogenase: A bifunctional protein consisting of aspartokinase, and homoserine dehydrogenase activities. It is found primarily in BACTERIA and in PLANTS.Thioctic Acid: An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.Genes, Bacterial: The functional hereditary units of BACTERIA.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.Enzyme Stability: 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.Citrate (si)-Synthase: Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.Acetoin Dehydrogenase: An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.Sarcosine Dehydrogenase: A LIVER mitochondrial matrix flavoenzyme that catalyzes the oxidation of SARCOSINE to GLYCINE and FORMALDEHYDE. Mutation in the enzyme causes sarcosinemia, a rare autosomal metabolic defect characterized by elevated levels of SARCOSINE in BLOOD and URINE.Disulfiram: 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.Glycolysis: A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.GlutaratesPseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

*  Gentaur Molecular :BBridge \ Sorbitol Dehydrogenase, from Microorganism \ 199-12391
Sorbitol Dehydrogenase, from Microorganism \ 199-12391 for more molecular products just contact us ... Polyol dehydrogenase). [gutB BSU06150] Sorbitol dehydrogenase (EC 1.1.1.14) (Glucitol dehydrogenase) (L-iditol 2-dehydrogenase) ... Gluconate/polyol dehydrogenase large subunit). [tms1 SPBC1773.05c] Putative sorbitol dehydrogenase (EC 1.1.1.14) (L-iditol 2- ... Glucitol-6-phosphate dehydrogenase) (Ketosephosphate reductase). [SORD] Sorbitol dehydrogenase (EC 1.1.1.14) (L-iditol 2- ...
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Mouse Monoclonal Anti-Sorbitol Dehydrogenase Antibody (13G5). Validated: WB, IHC, IHC-P. Tested Reactivity: Human. 100% ... Additional Sorbitol Dehydrogenase Products. Sorbitol Dehydrogenase NBP2-02202 * Sorbitol Dehydrogenase Antibodies. * Sorbitol ... Blogs on Sorbitol Dehydrogenase. There are no specific blogs for Sorbitol Dehydrogenase, but you can read our latest blog posts ... PTMs for Sorbitol Dehydrogenase Antibody (NBP2-02202). Learn more about PTMs related to Sorbitol Dehydrogenase Antibody (NBP2- ...
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*  L-iditol 2-dehydrogenase - Wikipedia
... sorbitol dehydrogenase, L-iditol:NAD+ 5-oxidoreductase, L-iditol (sorbitol) dehydrogenase, glucitol dehydrogenase, L-iditol: ... NAD+-dependent sorbitol dehydrogenase, and NAD+-sorbitol dehydrogenase. This enzyme participates in fructose and mannose ... In enzymology, a L-iditol 2-dehydrogenase (EC 1.1.1.14) is an enzyme that catalyzes the chemical reaction L-iditol + NAD+ ⇌ L- ... The systematic name of this enzyme class is L-iditol:NAD+ 2-oxidoreductase. Other names in common use include polyol ...
  https://en.wikipedia.org/wiki/L-iditol_2-dehydrogenase
*  D-iditol 2-dehydrogenase - Wikipedia
Shaw DRD (1956). "Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase". Biochem. J. 64 (3): 394-405. ... In enzymology, a D-iditol 2-dehydrogenase (EC 1.1.1.15) is an enzyme that catalyzes the chemical reaction D-iditol + NAD+ ⇌ {\ ... The systematic name of this enzyme class is D-iditol:NAD+ 2-oxidoreductase. This enzyme is also called D-sorbitol dehydrogenase ... displaystyle \rightleftharpoons } D-sorbose + NADH + H+ Thus, the two substrates of this enzyme are D-iditol and NAD+, whereas ...
  https://en.wikipedia.org/wiki/D-iditol_2-dehydrogenase
*  KEGG SSDB Best Search Result: byi:BYI23 B014300
sdf:ACG33_11075 short-chain dehydrogenase K07234 414 103 ( -) 29 0.340 106 -, 1 sed:SeD_A4756 DNA mismatch repair protein MutL ... plim:PHILAsVB114_00185 L-iditol 2-dehydrogenase K00008 339 100 ( -) 29 0.315 111 -, 1 plj:VFPFJ_02451 secreted aspartic ... ssx:SACTE_1149 Aldehyde Dehydrogenase K00128 464 107 ( -) 30 0.301 136 -, 1 stre:GZL_02983 recombination regulator RecX K03565 ... ocm:CBP12_01810 D-amino acid dehydrogenase K00285 414 103 ( -) 29 0.325 83 -, 1 ovi:T265_14885 hypothetical protein 188 103 ...
  http://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=byi:BYI23_B014300
*  Sorbitol Dehydrogenase Antibody (2A10) (NBP1-47994): Novus Biologicals
Mouse Monoclonal Anti-Sorbitol Dehydrogenase Antibody (2A10). Validated: WB, IHC, IHC-P. Tested Reactivity: Human. 100% ... Additional Sorbitol Dehydrogenase Products. Sorbitol Dehydrogenase NBP1-47994 * Sorbitol Dehydrogenase Antibodies. * Sorbitol ... Blogs on Sorbitol Dehydrogenase. There are no specific blogs for Sorbitol Dehydrogenase, but you can read our latest blog posts ... PTMs for Sorbitol Dehydrogenase Antibody (NBP1-47994). Learn more about PTMs related to Sorbitol Dehydrogenase Antibody (NBP1- ...
  https://www.novusbio.com/products/sorbitol-dehydrogenase-antibody-2a10_nbp1-47994
*  MEDLINE - Resultado p gina 1
Co-expression of the recombined alcohol dehydrogenase and glucose dehydrogenase and cross-linked enzyme aggregates ... L-Iditol 2-Dehydrogenase); EC 1.1.1.47 (Glucose 1-Dehydrogenase). ... 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) were discovered ... Alcohol Dehydrogenase); EC 1.1.1.47 (Glucose 1-Dehydrogenase); ML9LGA7468 (Phenylethyl Alcohol); T3C89M417N (Glutaral). ...
  http://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&format=standard.pft&indexSearch=EX&exprSearch=D08.811.682.047.150.270.500&lang=p&base=MEDLINE
*  I2D - Interologous Interaction Database
Q64442: Sorbitol dehydrogenase; 1.1.1.14; L-iditol 2-dehydrogenase. Pubmed References: 1 Source. Type. Score. BioGrid Predicted ... P06151: L-lactate dehydrogenase A chain; LDH-A; 1.1.1.27; LDH muscle subunit; LDH-M. Pubmed References: 1 Source. Type. Score. ... Q8BVP2: L-lactate dehydrogenase {ECO:0000256,RuleBase:RU000496}; 1.1.1.27 {ECO:0000256,RuleBase:RU000496}. Pubmed References: 1 ... Pubmed References: 2 Source. Type. Score. IntAct_Rat Predicted - Domains-Sup. Gene-CoExp. GO-Similarity. GO-CoLocalization. ...
  http://128.100.137.135/ophidv2.204/ForwardingServlet?inputFormat=ENTREZGENE&outputFormat=htmlOutput&ophidOrganism=MOUSE&proteins=56174
*  Galactitol 2-dehydrogenase - Wikipedia
Shaw DRD (1956). "Polyol dehydrogenases. 3. Galactitol dehydrogenase and D-iditol dehydrogenase". Biochem. J. 64 (3): 394-405. ... This enzyme is also called dulcitol dehydrogenase. This enzyme participates in galactose metabolism. ... In enzymology, a galactitol 2-dehydrogenase (EC 1.1.1.16) is an enzyme that catalyzes the chemical reaction galactitol + NAD+ ... The systematic name of this enzyme class is galactitol:NAD+ 2-oxidoreductase. ...
  https://en.wikipedia.org/wiki/Galactitol_2-dehydrogenase
*  List of MeSH codes (D08) - Wikipedia
... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... l-iditol 2-dehydrogenase MeSH D08.811.682.047.150.700.649 --- mannitol dehydrogenase MeSH D08.811.682.047.150.900 --- uridine ... 11-beta-hydroxysteroid dehydrogenase type 1 MeSH D08.811.682.047.436.174.600 --- 11-beta-hydroxysteroid dehydrogenase type 2 ... l-lactate dehydrogenase MeSH D08.811.682.047.551.500 --- l-lactate dehydrogenase (cytochrome) MeSH D08.811.682.047.605 --- ...
  https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
*  List of EC numbers (EC 1) - Wikipedia
EC 1.1.1.1: alcohol dehydrogenase EC 1.1.1.2: alcohol dehydrogenase (NADP+) EC 1.1.1.3: homoserine dehydrogenase EC 1.1.1.4: (R ... L-iditol 2-dehydrogenase EC 1.1.1.15: D-iditol 2-dehydrogenase EC 1.1.1.16: galactitol 2-dehydrogenase EC 1.1.1.17: mannitol-1- ... glutaryl-CoA dehydrogenase EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase EC 1.3 ... butyryl-CoA dehydrogenase EC 1.3.99.3: acyl-CoA dehydrogenase EC 1.3.99.4: 3-oxosteroid 1-dehydrogenase EC 1.3.99.5: 3-oxo-5a- ...
  https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)
*  KEGG BRITE: KEGG Orthology (KO) - Mus musculus (mouse)
235033 Rdh8; retinol dehydrogenase 8 98711 Rdh10; retinol dehydrogenase 10 (all-trans) 17252 Rdh11; retinol dehydrogenase 11 ... L-iditol 2-dehydrogenase [EC:1.1.1.14] K00078 DHDH; dihydrodiol dehydrogenase / D-xylose 1-dehydrogenase (NADP) [EC:1.3.1.20 ... 77974 Rdh12; retinol dehydrogenase 12 19683 Rdh16; retinol dehydrogenase 16 103142 Rdh9; retinol dehydrogenase 9 107605 Rdh1; ... alcohol dehydrogenase 1/7 [EC:1.1.1.1] K13951 ADH1_7; alcohol dehydrogenase 1/7 [EC:1.1.1.1] K13980 ADH4; alcohol dehydrogenase ...
  http://www.genome.jp/kegg-bin/get_htext?mmu00001+394435
*  What does L-driver mean?
l-iditol 2-dehydrogenase. Alternative searches for L-driver:. *Search for Synonyms for L-driver ... l-aminoadipate-semialdehyde dehydrogenase. *l-bomb. *l-dopa. *l-dops. *l-estimator ...
  http://www.definitions.net/definition/L-driver
*  KEGG SSDB Best Search Result: paz:TIA2EST2 03385
tfu:Tfu_2481 glutamate dehydrogenase (NAD) K15371 1617 108 ( 7) 30 0.330 115 -, 2 thw:BMG03_06730 DNA polymerase I K02335 941 ... acy:Anacy_2584 L-iditol 2-dehydrogenase K00008 343 107 ( -) 30 0.361 61 -, 1 adl:AURDEDRAFT_182290 glycoside hydrolase K22277 ... ntp:CRH09_03140 acyl-CoA dehydrogenase 389 108 ( -) 30 0.304 102 -, 1 pba:PSEBR_a1633 putative Histidine kinase, Hybrid K20973 ... sro:Sros_6477 aldehyde dehydrogenase (NAD) family prote K22187 511 105 ( 1) 30 0.305 105 -, 2 strt:A8713_08890 sulfate ABC ...
  http://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=paz:TIA2EST2_03385
*  Identification of novel metabolic interactions controlling carbon flux from xylose to ethanol in natural and recombinant yeasts...
Rizzi M, Harwart K, Erlemann P, Bui-Thanh N-A, Dellweg H. Purification and properties of the NAD+-xylitol-dehydrogenase from ... Thermodynamics of reactions catalyzed by l-iditol 2-dehydrogenase: the xylose assimilation pathway. J Chem Thermodyn. 1996;28: ... Lunzer R, Mamnun Y, Haltrich D, Kulbe KD, Nidetzky B. Structural and functional properties of a yeast xylitol dehydrogenase, a ... Eliasson A, Hofmeyr J-HS, Pedler S, Hahn-Hägerdal B. The xylose reductase/xylitol dehydrogenase/xylulokinase ratio affects ...
  https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-015-0340-x
*  Safety of fenbendazole in swine. - Semantic Scholar
In the groups fed 75 or 125 mg, sorbitol dehydrogenase activity increased on day 3 but returned to base line on day 10. ... In the groups fed 75 or 125 mg, sorbitol dehydrogenase activity increased on day 3 but returned to base line… (More) ...
  https://www.semanticscholar.org/paper/Safety-of-fenbendazole-in-swine.-Hayes-Oehme/1d316e85a140244c7e0448ae7bf97d5b3230e934
*  PRODUCTION OF 1,4 BUTANEDIOL IN A MICROORGANISM - MICROBIA, INC.
... conversion of 5-hydroxy-L-norvaline to 5-hydroxy-2-oxopentanoate; (e) conversion of 5-hydroxy-2- oxopentanoate to 4- ... hydroxybutyrate dehydrogenase, a 1 ,3 propanediol dehydrogenase, cinnamyl-alcohol dehydrogenase, or an alcohol dehydrogenase. ... L-iditol 2-dehydrogenase, or a zinc-containing alcohol dehydrogenase.. 86. The recombinant microbial host of any of the ... 3 propanediol dehydrogenase, cinnamyl-alcohol dehydrogenase, or an alcohol dehydrogenase; the polypeptide that catalyzes the ...
  http://www.sumobrain.com/patents/wipo/Production-14-butanediol-in-microorganism/WO2010085731.html
*  Compositions and Methods for Modeling Saccharomyces cerevisiae Metabolism - Patent application
YJR159W 1.1.1.14 SOR1 sorbitol dehydrogenase (L-iditol 2- SOT + NAD -, FRU + NADH sor1 dehydrogenase) Galactose metabolism ... dehydrogenase (IMP YLR432W 1.1.1.205 IMD3 probable inosine-5'-monophosphate IMP + NAD -, NADH + XMP prm4 dehydrogenase (IMP ... Aspartate semialdehyde dehydrogenase YJR139C 1.1.1.3 hom6 Homoserine dehydrogenase I ASPSA + NADH -, NAD + HSER hom6_1 YJR139C ... histidinol dehydrogenase YCL030C 3.5.4.19 his4 histidinol dehydrogenase PRBAMP -, PRFP his4_2 YIL020C 5.3.1.16 his6 ...
  http://www.patentsencyclopedia.com/app/20100280803
*  A Role for Sorbitol in Desiccation Tolerance of Developing Maize Kernels: Inference from the Properties of Maize Sorbitol...
Jeffery J, Chesters J, Mills C, Sadler PJ, Jornvall H (1984) Sorbitol dehydrogenase is a zinc enzyme. EMBO J. 3: 357-360.PubMed ... L-Iditol:Nad Oxidoreductases] from four mammalian species. Comp.Biochem.Physiol. 59B: 213-218.CrossRefGoogle Scholar ... The zinccontaining long-chain alcohol dehydrogenases. Eur.J.Biochem. 167: 195-201.PubMedCrossRefGoogle Scholar ... Jeffery J, Jornvall H (1988) Sorbitol dehydrogenase. Adv.Enzymol.Relat. Areas Mol.Biol. 61: 47-106.PubMedGoogle Scholar ...
  https://rd.springer.com/chapter/10.1007/978-3-642-79133-8_22
*  Genetic variability of Prochilodus lineatus (Characiformes, Prochilodontidae) in the upper Paraná river
3-Hydroxybutyrate dehydrogenase (HBDH 3.1.1.30) L-Iditol dehydrogenase (IDDH 1.1.1.14) ... I. Lactate dehydrogenase. Comp. Biochem. Physiol. 97: 235-246. [ Links ]. Fenerich-Verani, N., Schwants, M.L.B. and Schwants, A ... Soluble malate dehydrogenase. Comp. Biochem. Physiol. 97: 247-255. [ Links ]. Foresti, F., Toledo-Filho, S.A. and Almeida- ... According to Fenerich-Verani et al. (1990), the least anodal isozyme may correspond to alcohol dehydrogenase (ADH) expression ( ...
  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84551997000300005&lng=es&nrm=iso
*  Alcohol metabolism | definition of Alcohol metabolism by Medical dictionary
l-iditol dehydrogenase (ID). a liver specific enzyme; serum determinations have been used in the horse to detect hepatocellular ... See also: alcohol dehydrogenase (acceptor), alcohol dehydrogenase (NADP+). alcohol dehydrogenase. /al·co·hol de·hy·dro·gen·ase ... lactate dehydrogenase (LDH), lactic acid dehydrogenase. an enzyme that catalyzes the interconversion of lactate and pyruvate. ... glutamate dehydrogenase (GD), glutamic dehydrogenase. an enzyme that catalyzes the reversible reaction of glutamic acid into 2- ...
  http://medical-dictionary.thefreedictionary.com/Alcohol+metabolism
*  L-leucine | definition of L-leucine by Medical dictionary
l-iditol dehydrogenase (ID). *l-iditol dehydrogenase (ID). *l-iditol dehydrogenase (ID) ... Isovaleryl CoA dehydrogenase, which is located in the mitochondria, is important for metabolism of L-leucine.. Acute metabolic ... 2-Amino-4-methylvaleric acid; the l-isomer is one of the amino acids found in proteins; a nutritionally essential amino acid. ... organic acids in which one or more of the hydrogen atoms is replaced by the amino group, NH2. They are the end-products of ...
  http://medical-dictionary.thefreedictionary.com/L-leucine
*  Lide | definition of Lide by Medical dictionary
l-iditol dehydrogenase. *lidless. *Lidneria clavata. *lidocaine. *lidocaine HCl. *lidocaine hydrochloride. *lidocaine ... Each eyelid consists of the following layers, starting anteriorly: (1) skin, (2) a layer of subcutaneous connective tissue, (3 ... the CanoScan LiDE 35 scanner boosts performance and functionality by upgrading the connection to USB 2.. Canon's Three New ...
  https://medical-dictionary.thefreedictionary.com/Lide
*  Lick arse | definition of lick arse by Medical dictionary
l-iditol dehydrogenase. *lidless. *Lidneria clavata. *lidocaine. *lidocaine HCl. *lidocaine hydrochloride. *lidocaine ... 2. a mixture of salt plus other macro-elements, especially phosphorus, trace elements, vitamins and other feed additives, fed ...
  https://medical-dictionary.thefreedictionary.com/lick+arse

Sorbitol dehydrogenase: Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene.Lactate dehydrogenase elevating virus: Lactate dehydrogenase elevating virus, or LDV for short, belongs to part of the arteriviridae family and the nidovirales order. Also included in the nidovirales order are the coronaviridae.Alcohol dehydrogenaseDehydrogenase: A dehydrogenase (also called DHO in the literature) is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by a reduction reaction that transfers one or more hydrides (H−) to an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN.Long-chain-aldehyde dehydrogenase: Fatty aldehyde dehydrogenase (or Long-chain-aldehyde dehydrogenase) is an aldehyde dehydrogenase enzyme that in human is encoded in the ALDH3A2 gene on chromosome 17.Glutamate dehydrogenase: Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle.Isocitric acidDihydrolipoamideSuccinate dehydrogenase subunit E: In molecular biology, the protein domain named Sdh5 is also named SdhE which stands for succinate dehydrogenase protein E. In the past, it has also been named YgfY and DUF339.Glycerol phosphate shuttle: 380px|thumb|Glycerol Phosphate ShuttleHydroxysteroid dehydrogenaseSucA RNA motifSoluble quinoprotein glucose dehydrogenase: Soluble quinoprotein glucose dehydrogenase (, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with system name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionPhosphogluconate dehydrogenaseNADH dehydrogenase: NADH dehydrogenase (, cytochrome c reductase, type 1 dehydrogenase, beta-NADH dehydrogenase dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH diaphorase, NADH diaphorase, NADH hydrogenase, NADH oxidoreductase, NADH-menadione oxidoreductase, reduced diphosphopyridine nucleotide diaphorase) is an enzyme with systematic name NADH:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionIMP dehydrogenaseFormate dehydrogenase (acceptor): Formate dehydrogenase (acceptor) (, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with system name formate:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionMedium-chain acyl-coenzyme A dehydrogenase deficiencyXanthinuriaDehydratase: Dehydratase is an enzyme that catalyzes the removal of oxygen and hydrogen from organic compounds in the form of water. This process is also known as dehydration reaction.Glucose-methanol-choline oxidoreductase family: In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.FluorouracilA-1,4-glucan-protein synthase (UDP-forming): Alpha-1,4-glucan-protein synthase (UDP-forming) (, UDP-glucose:protein glucosyltransferase, glycogen initiator synthase, UDPGlc:protein transglucosylase, UPTG, uridine diphosphoglucose protein transglucosylase I, proglycogen synthase, uridine diphosphoglucose-protein 4-alpha-glucosyltransferase, uridine diphosphoglucose-protein glucosyltransferase, UDP-glucose protein transglucosylase, UDP-glucose-protein glucosyltransferase, uridine diphosphate glucose-protein transglucosylase I) is an enzyme with system name UDP-glucose:protein 4-alpha-glucosyltransferase. This enzyme catalyses the following chemical reactionBurst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".MannitolColes PhillipsProstamide/prostaglandin F2alpha synthase: Prostamide/prostaglandin F2alpha synthase (, prostamide/PGF synthase, prostamide F synthase, prostamide/prostaglandin F synthase, tPGF synthase) is an enzyme with system name thioredoxin:(5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate oxidoreductase . This enzyme catalyses the following chemical reactionACADSB: ACADSB is a human gene that encodes short/branched chain specific acyl-CoA dehydrogenase (SBCAD), an enzyme in the acyl CoA dehydrogenase family.Protein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Long-chain acyl-CoA dehydrogenase: Long-chain acyl-CoA dehydrogenase (, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with system name long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.Table of standard reduction potentials for half-reactions important in biochemistry: The values below are standard reduction potentials for half-reactions measured at 25°C, 1 atmosphere and a pH of 7 in aqueous solution.Isocitrate/isopropylmalate dehydrogenase family: In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary related enzymes isocitrate dehydrogenase, 3-isopropylmalate dehydrogenase and tartrate dehydrogenase.Peroxynitric acidSRG1 RNA: SRG1 RNA (SER3 regulatory gene 1) is a non-coding RNA which represses the expression of SER3 (YER081W). SER3 is a gene which codes for a phosphoglycerate dehydrogenase involved in the biosynthesis of serine.Isozyme: Isozymes (also known as isoenzymes or more generally as Multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters (e.Specificity constant: In the field of biochemistry, the specificity constant (also called kinetic efficiency or k_{cat}/K_{M}), is a measure of how efficiently an enzyme converts substrates into products. A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.HypotoniaList of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.Liver sinusoid: A liver sinusoid is a type of sinusoidal blood vessel (with fenestrated, discontinuous endothelium) that serves as a location for the oxygen-rich blood from the hepatic artery and the nutrient-rich blood from the portal vein.SIU SOM Histology GISymmetry element: A symmetry element is a point of reference about which symmetry operations can take place. In particular, symmetry elements can be centers of inversion, axes of rotation and mirror planes.Ligation-independent cloning: Ligation-independent cloning (LIC) is a form of molecular cloning that is able to be performed without the use of restriction endonucleases or DNA ligase. This allows genes that have restriction sites to be cloned without worry of chopping up the insert.Glutaryl-CoA dehydrogenase: Glutaryl-CoA dehydrogenase (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA dehydrogenase family (ACD).Cofactor Engineering: Cofactor engineering, a subset of metabolic engineering, is defined as the manipulation of the use of cofactors in an organism’s metabolic pathways. In cofactor engineering, the concentrations of cofactors are changed in order to maximize or minimize metabolic fluxes.Acetonedicarboxylic acidN1-acetylpolyamine oxidase: N1-acetylpolyamine oxidase (, hPAO-1, mPAO, hPAO) is an enzyme with system name N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming). This enzyme catalyses the following chemical reactionProkaryotic acetaldehyde dehydrogenase dimerisation domain: In molecular biology, prokaryotic acetaldehyde dehydrogenase dimerisation domain is a protein domain found at the C-terminus of prokaryotic acetaldehyde dehydrogenases, it adopts a structure consisting of an alpha-beta-alpha-beta(3) core, which mediates dimerisation of the protein.Saccharopine dehydrogenase: In molecular biology, the protein domain Saccharopine dehydrogenase (SDH), also named Saccharopine reductase, is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The Saccharopine dehydrogenase enzyme can be classified under , , , and .L-galactose 1-dehydrogenase: L-galactose 1-dehydrogenase (, L-GalDH, L-galactose dehydrogenase) is an enzyme with system name L-galactose:NAD+ 1-oxidoreductase. This enzyme catalyses the following chemical reactionAlkaliphile: Alkaliphiles are a class of extremophilic microbes capable of survival in alkaline (pH roughly 8.5-11) environments, growing optimally around a pH of 10.Tether (cell biology): Biological cells which form bonds with a substrate and are at the same time subject to a flow can form long thin membrane cylinders called tethers, which connect the adherent area to the main body of the cell. Under physiological conditions, neutrophil tethers can extend to several micrometers.DimethylglycineMitochondrion: The mitochondrion (plural mitochondria) is a double membrane-bound organelle found in most eukaryotic cells. The word mitochondrion comes from the Greek , , i.LysineGlycine betaine aldehydeDNA binding site: DNA binding sites are a type of binding site found in DNA where other molecules may bind. DNA binding sites are distinct from other binding sites in that (1) they are part of a DNA sequence (e.Silent mutation: Silent mutations are mutations in DNA that do not significantly alter the phenotype of the organism in which they occur. Silent mutations can occur in non-coding regions (outside of genes or within introns), or they may occur within exons.Molar mass distribution: In linear polymers the individual polymer chains rarely have exactly the same degree of polymerization and molar mass, and there is always a distribution around an average value. The molar mass distribution (or molecular weight distribution) in a polymer describes the relationship between the number of moles of each polymer species (Ni) and the molar mass (Mi) of that species.Reverse Krebs cycle: The reverse Krebs cycle (also known as the reverse tricarboxylic acid cycle, the reverse TCA cycle, or the reverse citric acid cycle)Oxidoreductase FAD-binding domain: B:7-104 B:7-104 B:7-104

(1/156) Polyol formation and NADPH-dependent reductases in dog retinal capillary pericytes and endothelial cells.

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

(2/156) Hypertonicity-induced accumulation of organic osmolytes in papillary interstitial cells.

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

(3/156) Identification of a ubiquitous family of membrane proteins and their expression in mouse brain.

A family of genes encoding membrane proteins with a unique structure has been identified in DNA and cDNA clones of various eukaryotes ranging from yeast to human. The nucleotide sequences of three novel cDNAs from Drosophila melanogaster and mouse were determined. The amino acid sequences of the two mouse proteins have human homologs. The gene (TMS1) encoding the yeast member of this family was disrupted, and the resulting mutant showed no significant phenotype under several stress conditions. The expression of the mouse genes TMS-1 and TMS-2 was examined by in situ hybridization of sections from brain, liver, kidney, heart and testis of an adult mouse as well as in a 1-day-old whole mouse. While the expression of TMS-2 was found to be restricted to the central nervous system, TMS-1 was also expressed in kidney and testis. The expression of TMS-1 and TMS-2 in the brain overlapped and was localized to areas associated with glutamatergic excitatory neurons, such as the hippocampus and cerebral cortex. High-magnification analysis indicated that both mRNAs are expressed in neurons. Semiquantitative analysis of mRNA expression was performed in various parts of the brain. The conservation, unique structure and localization in the mammalian brain of this novel protein family suggest an important biological role.  (+info)

(4/156) Selective disruption of protein aggregation by cyclodextrin dimers.

Beta-cyclodextrin (CD) dimers (n = 11) were synthesized and tested against eight enzymes, seven of which were dimeric or tetrameric, for inhibitor activity. Initial screening showed that only L-lactate dehydrogenase and citrate synthase were inhibited but only by two specific CD dimers in which two beta-CDs were linked on the secondary face by a pyridine-2,6-dicarboxylic group. Further investigation suggested that these CD dimers inhibit the activity of L-lactate dehydrogenase and citrate synthase at least in part by disruption of protein-protein aggregation.  (+info)

(5/156) Clofibrate-induced in vitro hepatoprotection against acetaminophen is not due to altered glutathione homeostasis.

Prior induction of peroxisome proliferation protects mice against the in vivo hepatotoxicity of acetaminophen and various other bioactivation-dependent toxicants. The mechanisms underlying such chemoresistance are poorly understood, although they have been suggested to involve alterations in glutathione homeostasis. To clarify the role of glutathione in this phenomenon, we isolated hepatocytes from mice in which hepatic peroxisome proliferation had been induced with clofibrate. The cells were incubated with a range of acetaminophen concentrations and the extent of cell killing after up to 8 h was assessed by measuring lactate dehydrogenase leakage from the cells. Hepatocytes from clofibrate-pretreated mice were much less susceptible to acetaminophen than cells from vehicle-treated controls. However, the extent of glutathione depletion during exposure to acetaminophen was similar in both cell types, as were rates of excretion of the product of glutathione-mediated detoxication of acetaminophen's quinoneimine metabolite, 3-glutathionyl-acetaminophen. The glutathione-replenishing ability of clofibrate-pretreated cells after a brief exposure to diethyl maleate also resembled that of control cells. More importantly, prior depletion of glutathione by diethyl maleate did not abolish the resistance of clofibrate-pretreated cells to acetaminophen. Taken together, these findings indicate that although glutathione-dependent pathways may contribute to hepatoprotection during peroxisome proliferation, the resistance phenomenon is not due exclusively to this mechanism.  (+info)

(6/156) Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress.

Sorbitol dehydrogenase (l-iditol:NAD(+) 2-oxidoreductase, E.C. 1.1.1. 14) (SDH) was significantly protected from thermally induced inactivation and aggregation by bovine lens alpha-crystallin. An alpha-crystallin/SDH ratio as low as 1:2 in weight was sufficient to preserve the transparency of the enzyme solution kept for at least 2 h at 55 degrees C. Moreover, an alpha-crystallin/SDH ratio of 5:1 (w/w) was sufficient to preserve the enzyme activity fully at 55 degrees C for at least 40 min. The protection by alpha-crystallin of SDH activity was essentially unaffected by high ionic strength (i.e. 0.5 m NaCl). On the other hand, the transparency of the protein solution was lost at a high salt concentration because of the precipitation of the alpha-crystallin/SDH adduct. Magnesium and calcium ions present at millimolar concentrations antagonized the protective action exerted by alpha-crystallin against the thermally induced inactivation and aggregation of SDH. The lack of protection of alpha-crystallin against the inactivation of SDH induced at 55 degrees C by thiol blocking agents or EDTA together with the additive effect of NADH in stabilizing the enzyme in the presence of alpha-crystallin suggest that functional groups involved in catalysis are freely accessible in SDH while interacting with alpha-crystallin. Two different adducts between alpha-crystallin and SDH were isolated by gel filtration chromatography. One adduct was characterized by a high M(r) of approximately 800,000 and carried exclusively inactive SDH. A second adduct, carrying active SDH, had a size consistent with an interaction of the enzyme with monomers or low M(r) aggregates of alpha-crystallin. Even though it had a reduced efficiency with respect to alpha-crystallin, bovine serum albumin was shown to mimic the chaperone-like activity of alpha-crystallin in protecting SDH from thermal denaturation. These findings suggest that the multimeric structural organization of alpha-crystallin may not be a necessary requirement for the stabilization of the enzyme activity.  (+info)

(7/156) Peroxisome proliferator-activated receptor alpha-null mice lack resistance to acetaminophen hepatotoxicity following clofibrate exposure.

The purpose of this study was to investigate whether activation of the nuclear receptor PPARalpha is needed for protection from acetaminophen (APAP) hepatotoxicity produced by repeated administration of the peroxisome proliferator clofibrate (CFB). Female wild-type and PPARalpha-null mice received corn oil vehicle or 500 mg CFB/kg, ip, daily for 10 days. They were then fasted overnight (18 h) and either killed at 4 or 24 h after challenge with 400 mg APAP/kg. Controls received 50% propylene glycol vehicle only. In this model of CFB hepatoprotection, liver injury was assessed by measuring plasma sorbitol dehydrogenase activity and by histopathology at 24 h after APAP challenge. Significant hepatocellular necrosis was evident in both corn oil-pretreated PPARalpha-null and wild-type mice at 24 h after APAP challenge. In agreement with previous studies, CFB-pretreated wild-type mice showed marked protection against APAP toxicity. In contrast, CFB did not provide protection against APAP hepatotoxicity in the PPARalpha-null mice. Similarly, at 4 h after APAP challenge, hepatic glutathione depletion and selective arylation of cytosolic proteins were reduced significantly in CFB-pretreated wild-type mice, but not in PPARalpha-null mice. The lack of changes in APAP binding and NPSH depletion in CFB-pretreated, PPARalpha-null mice is consistent with the presence of significant liver injury at 24 h in this treatment group. These findings demonstrate that the protection against APAP hepatotoxicity by peroxisome proliferator treatment is mediated by the activation of PPARalpha.  (+info)

(8/156) Mannitol-1-phosphate dehydrogenase from Cryptococcus neoformans is a zinc-containing long-chain alcohol/polyol dehydrogenase.

Cryptococcus neoformans, the causative agent of cryptococcosis, produces large amounts of mannitol in culture and in infected mammalian hosts. Although there is considerable indirect evidence that mannitol synthesis may be required for wild-type stress tolerance and virulence in C. neoformans, this hypothesis has not been tested directly. It has been proposed that mannitol-1-phosphate dehydrogenase (MPD) is required for fungal mannitol synthesis, but no MPD-deficient fungal mutants or cDNAs or genes encoding fungal MPDs have been described. Therefore, C. neoformans was purified from a 148 kDa homotetramer of 36 kDa subunits that catalysed the reaction mannitol1-phosphate+NAD--><--fructose 6-phosphate+NADH. Partial peptide sequences were used to isolate the corresponding cDNA and gene, and the deduced MPD protein was found to be homologous to the zinc-containing long-chain alcohol/polyol dehydrogenases. Lysates of Saccharomyces cerevisiae transformed with the cDNA of interest (but not vector-transformed controls) contained MPD catalytic activity. Lastly, Northern analyses demonstrated MPD mRNA in glucose- and mannitol-grown C. neoformans cells. Thus, MPD has been purified and characterized from C. neoformans, and the corresponding cDNA and gene (MPD1) cloned and sequenced. Availability of C. neoformans MPD1 should permit direct testing of the hypotheses that (i) MPD is required for mannitol biosynthesis and (ii) the ability to synthesize mannitol is essential for wild-type stress tolerance and virulence.  (+info)




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  • protein
  • An essential amino acid, C 6 H 13 NO 2 , obtained by the hydrolysis of protein by pancreatic enzymes during digestion and necessary for optimal growth in children and for the maintenance of nitrogen balance in adults. (thefreedictionary.com)
  • catalyzes
  • f) a nucleic acid molecule encoding a polypeptide that catalyzes the conversion of 4-hydroxybutanal to 1 ,4-butanediol, wherein the cell produces at least one of 5-hydroxy-L-norvaline, 5-hydroxy-2- oxopentanoate, 4-hydroxybutanal and 1,4-butanediol. (sumobrain.com)
  • liver
  • Samples of liver and muscle were removed from fresh fish, frozen in liquid nitrogen, and stored at -20 o C. The tissues were homogenized in Eppendorf tubes with CCl 4 and 0.02 M Tris/HCl buffer, pH 7.5 at 1:1:2 concentrations, respectively, using plastic sticks. (scielo.br)
  • Tissue
  • Each eyelid consists of the following layers, starting anteriorly: (1) skin, (2) a layer of subcutaneous connective tissue, (3) a layer of striated muscle fibres of the orbicularis muscle, (4) a layer of submuscular connective tissue, (5) a fibrous layer, including the tarsal plates, (6) a layer of smooth muscle, (7) the palpebral conjunctiva. (thefreedictionary.com)
  • important
  • 4S)-3-[(5S)-5-(4-Fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one ((S)-ET-5) is an important chiral intermediate in the synthesis of chiral side chain of ezetimibe. (bireme.br)