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.Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Carbohydrate Metabolism: Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.Dietary Carbohydrates: Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)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.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.Glucosephosphate DehydrogenaseAldehyde 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.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.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.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.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.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 1.1.1.14Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.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.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.Carbohydrate Conformation: The characteristic 3-dimensional shape of a carbohydrate.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.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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.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.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.Kinetics: The rate dynamics in chemical or physical systems.Hydroxybutyrate Dehydrogenase3-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 1.2.4.3.3-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.Pyruvate 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).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.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)Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.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.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)Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.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.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).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.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.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)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.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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).Oligosaccharides: Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.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.Antigens, Tumor-Associated, Carbohydrate: Carbohydrate antigens expressed by malignant tissue. They are useful as tumor markers and are measured in the serum by means of a radioimmunoassay employing monoclonal antibodies.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.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Starch: Any of a group of polysaccharides of the general formula (C6-H10-O5)n, composed of a long-chain polymer of glucose in the form of amylose and amylopectin. It is the chief storage form of energy reserve (carbohydrates) in plants.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.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+.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.Phosphoglycerate Dehydrogenase: An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.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 1.1.1.62Hydrogen-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)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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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.PolysaccharidesGlutamate 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).Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.PyruvatesGlyceraldehyde-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.Monosaccharides: Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)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.Fermentation: Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.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.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.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.Dietary Fats: Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)Fructose: A monosaccharide in sweet fruits and honey that is soluble in water, alcohol, or ether. It is used as a preservative and an intravenous infusion in parenteral feeding.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.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.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.Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.Galactose: An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.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)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.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.Blood Glucose: Glucose in blood.Glycerol-3-Phosphate Dehydrogenase (NAD+)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.

The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase. (1/380)

D-3-Phosphoglycerate dehydrogenase (PGDH) from Escherichia coli is allosterically inhibited by L-serine, the end product of its metabolic pathway. Previous results have shown that inhibition by serine has a large effect on Vmax and only a small or negligible effect on Km. PGDH is thus classified as a V-type allosteric enzyme. In this study, the active site of PGDH has been studied by site-directed mutagenesis to assess the role of certain residues in substrate binding and catalysis. These consist of a group of cationic residues (Arg-240, Arg-60, Arg-62, Lys-39, and Lys-141') that potentially form an electrostatic environment for the binding of the negatively charged substrate, as well as the only tryptophan residue found in PGDH and which fits into a hydrophobic pocket immediately adjacent to the active site histidine residue. Interestingly, Trp-139' and Lys-141' are part of the polypeptide chain of the subunit that is adjacent to the active site. The results of mutating these residues show that Arg-240, Arg-60, Arg-62, and Lys-141' play distinct roles in the binding of the substrate to the active site. Mutants of Trp-139' show that this residue may play a role in stabilizing the catalytic center of the enzyme. Furthermore, these mutants appear to have a significant effect on the cooperativity of serine inhibition and suggest a possible role for Trp-139' in the cooperative interactions between subunits.  (+info)

Molecular characterization of a flagellar export locus of Helicobacter pylori. (2/380)

Motility of Helicobacter species has been shown to be essential for successful colonization of the host. We have investigated the organization of a flagellar export locus in Helicobacter pylori. A 7-kb fragment of the H. pylori CCUG 17874 genome was cloned and sequenced, revealing an operon comprising an open reading frame of unknown function (ORF03), essential housekeeping genes (ileS and murB), flagellar export genes (fliI and fliQ), and a homolog to a gene implicated in virulence factor transport in other pathogens (virB11). A promoter for this operon, showing similarity to the Escherichia coli sigma70 consensus, was identified by primer extension. Cotranscription of the genes in the operon was demonstrated by reverse transcription-PCR, and transcription of virB11, fliI, fliQ, and murB was detected in human or mouse biopsies obtained from infected hosts. The genetic organization of this locus was conserved in a panel of H. pylori clinical isolates. Engineered fliI and fliQ mutant strains were completely aflagellate and nonmotile, whereas a virB11 mutant still produced flagella. The fliI and fliQ mutant strains produced reduced levels of flagellin and the hook protein FlgE. Production of OMP4, a member of the outer membrane protein family identified in H. pylori 26695, was reduced in both the virB11 mutant and the fliI mutant, suggesting related functions of the virulence factor export protein (VirB11) and the flagellar export component (FliI).  (+info)

Regulation of alginate biosynthesis in Pseudomonas syringae pv. syringae. (3/380)

Both Pseudomonas aeruginosa and the phytopathogen P. syringae produce the exopolysaccharide alginate. However, the environmental signals that trigger alginate gene expression in P. syringae are different from those in P. aeruginosa with copper being a major signal in P. syringae. In P. aeruginosa, the alternate sigma factor encoded by algT (sigma22) and the response regulator AlgR1 are required for transcription of algD, a gene which encodes a key enzyme in the alginate biosynthetic pathway. In the present study, we cloned and characterized the gene encoding AlgR1 from P. syringae. The deduced amino acid sequence of AlgR1 from P. syringae showed 86% identity to its P. aeruginosa counterpart. Sequence analysis of the region flanking algR1 in P. syringae revealed the presence of argH, algZ, and hemC in an arrangement virtually identical to that reported in P. aeruginosa. An algR1 mutant, P. syringae FF5.32, was defective in alginate production but could be complemented when algR1 was expressed in trans. The algD promoter region in P. syringae (PsalgD) was also characterized and shown to diverge significantly from the algD promoter in P. aeruginosa. Unlike P. aeruginosa, algR1 was not required for the transcription of algD in P. syringae, and PsalgD lacked the consensus sequence recognized by AlgR1. However, both the algD and algR1 upstream regions in P. syringae contained the consensus sequence recognized by sigma22, suggesting that algT is required for transcription of both genes.  (+info)

A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. (4/380)

The serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b) consists of D-fucose and L-rhamnose. Thymidine diphosphate (dTDP)-D-fucose is the activated nucleotide sugar form of D-fucose, which has been identified as a constituent of structural polysaccharides in only a few bacteria. In this paper, we show that three dTDP-D-fucose synthetic enzymes are encoded by genes in the gene cluster responsible for the synthesis of serotype b-specific polysaccharide in A. actinomycetemcomitans. The first and second steps of the dTDP-D-fucose synthetic pathway are catalyzed by D-glucose-1-phosphate thymidylyltransferase and dTDP-D-glucose 4,6-dehydratase, which are encoded by rmlA and rmlB in the gene cluster, respectively. These two reactions are common to the well studied dTDP-L-rhamnose synthetic pathway. However, the enzyme catalyzing the last step of the dTDP-D-fucose synthetic pathway has never been reported. We identified the fcd gene encoding a dTDP-4-keto-6-deoxy-D-glucose reductase. After purifying the three enzymes, their enzymatic activities were analyzed by reversed-phase high performance liquid chromatography. In addition, nuclear magnetic resonance analysis and gas-liquid chromatography analysis proved that the fcd gene product converts dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose. Moreover, kinetic analysis of the enzyme indicated that the Km values for dTDP-4-keto-6-deoxy-D-glucose and NADPH are 97.3 and 28.7 microM, respectively, and that the enzyme follows the sequential mechanism. This paper is the first report on the dTDP-D-fucose synthetic pathway and dTDP-4-keto-6-deoxy-D-glucose reductase.  (+info)

Purification and characterization of D-glucosaminitol dehydrogenase from Agrobacterium radiobacter. (5/380)

D-Glucosaminitol dehydrogenase, which catalyzes the conversion of D-glucosaminitol to 3-keto-D-glucosaminitol, was purified to apparent homogeneity from extracts of Agrobacterium radiobacter. This organism has constitutively depressed levels of the enzyme but expression of the enzyme is induced by addition of D-glucosamine to the medium. Purification included ammonium sulfate fractionation and chromatography on columns of DEAE-Sephacel, Octyl-Sepharose CL-4B, and Cellulofine. The purified enzyme migrated as a single band, coinciding with dehydrogenase activities specific for D-glucosaminitol and ethanol, when electrophoresed on a 7.5% polyacrylamide gel at pH 8.0. Electrophoresis on a 12.5% PAGE in the presence of 1% SDS also yielded a single band. The enzyme had an apparent molecular mass of 79 kDa, as measured by the pattern of elution from a column of Cellulofine. The results indicated that the enzyme was a dimer of identical (or nearly identical) subunits of 39.5 kDa. D-Glucosaminitol dehydrogenase required NAD+ as a cofactor and used ethanol as the preferred substrate, as well as aliphatic alcohols with 2 to 4 carbon atoms, D-glucosaminitol, D-glucosaminate, DL-allothreonine, glycerol, and erythritol as additional substrates. In 50 mM Tris-HCl buffer (pH 9.0) at 25 degrees C, the K(m) for D-glucosaminitol, ethanol, and NAD+ were 2.2, 2.0, and 0.08 mM, respectively. The enzyme had a pH optimum of 10 for D-glucosaminitol and 8.5 for ethanol. The enzyme lost substantial activity when treated with pyrazole, with certain reagents that react with sulfhydryl groups and with Zn2+ ion. The various results together suggest that the enzyme exploits different amino acid residues for the dehydrogenation of ethanol and of D-glucosaminitol.  (+info)

Characterization of dTDP-4-dehydrorhamnose 3,5-epimerase and dTDP-4-dehydrorhamnose reductase, required for dTDP-L-rhamnose biosynthesis in Salmonella enterica serovar Typhimurium LT2. (6/380)

The thymidine diphosphate-L-rhamnose biosynthesis pathway is required for assembly of surface glycoconjugates in a growing list of bacterial pathogens, making this pathway a potential therapeutic target. However, the terminal reactions have not been characterized. To complete assignment of the reactions, the four enzymes (RmlABCD) that constitute the pathway in Salmonella enterica serovar Typhimurium LT2 were overexpressed. The purified RmlC and D enzymes together catalyze the terminal two steps involving NAD(P)H-dependent formation of dTDP-L-rhamnose from dTDP-6-deoxy-D-xylo-4-hexulose. RmlC was assigned as the thymidine diphosphate-4-dehydrorhamnose 3,5-epimerase by showing its activity to be NAD(P)H-independent. Spectrofluorometric and radiolabeling experiments were used to demonstrate the ability of RmlC to catalyze the formation of dTDP-6-deoxy-L-lyxo-4-hexulose from dTDP-6-deoxy-D-xylo-4-hexulose. Under reaction conditions, RmlC converted approximately 3% of its substrate to product. RmlD was unequivocally identified as the thymidine diphosphate-4-dehydrorhamnose reductase. The reductase property of RmlD was shown by equilibrium analysis and its ability to enable efficient biosynthesis of dTDP-L-rhamnose, even in the presence of low amounts of dTDP-6-deoxy-L-lyxo-4-hexulose. Comparison of 23 known and predicted RmlD sequences identified several conserved amino acid residues, especially the serine-tyrosine-lysine catalytic triad, characteristic for members of the reductase/epimerase/dehydrogenase protein superfamily. In conclusion, RmlD is a novel member of this protein superfamily.  (+info)

Interstrain variation of the polysaccharide B biosynthesis locus of Bacteroides fragilis: characterization of the region from strain 638R. (7/380)

The sequence and analysis of the capsular polysaccharide biosynthesis locus, PS B2, of Bacteroides fragilis 638R are described, and the sequence is compared with that of the PS B1 biosynthesis locus of B. fragilis NCTC 9343. Two genes of the region, wcgD and wcgC, are shown by complementation to encode a UDP-N-acetylglucosamine 2-epimerase and a UDP-N-acetylmannosamine dehydrogenase, respectively.  (+info)

PCR identification of Pseudomonas aeruginosa and direct detection in clinical samples from cystic fibrosis patients. (8/380)

This report describes a PCR primer pair that targets the algD GDP mannose gene of Pseudomonas aeruginosa and produces a specific 520-bp PCR product useful for P. aeruginosa identification. This PCR assay was tested with 182 isolates of P. aeruginosa and 20 isolates of other bacterial species, and demonstrated 100% specificity and sensitivity. The test was also able to detect P. aeruginosa directly in clinical samples such as sputum or throat swabs obtained from cystic fibrosis patients. The combination of this primer with a universal bacterial primer, acting as a control to assess DNA quality in the sample, resulted in a robust PCR method that can be used for rapid P. aeruginosa detection.  (+info)

AA3 enzymes belong to the glucose-methanol-choline (GMC) oxidoreductases family. AA3 enzymes are flavoproteins containing a flavin-adenine dinucleotide (FAD)-binding domain. Family AA3 can be divided into 4 subfamilies: AA3_1 (mostly cellobiose dehydrogenases), AA3_2 (including both aryl alcohol oxidase and glucose 1-oxidase), AA3_3 (alcohol oxidase) and AA3_4 (pyranose 2-oxidase ...
SWISS-MODEL Template Library (SMTL) entry for 1mfz. Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa
Boc Sciences offers cas 18422-53-2 1,2:4,5-Di-O-isopropylidene-b-D-erythro-2,3-hexodiulo-2,6-pyranose in bulk,please inquire us to get a quote for 18422-53-2 1,2:4,5-Di-O-isopropylidene-b-D-erythro-2,3-hexodiulo-2,6-pyranose.
Proliferating cells, including cancer cells, obtain serine both exogenously and via the metabolism of glucose. By catalyzing the first, rate-limiting step in the synthesis of serine from glucose, phosphoglycerate dehydrogenase (PHGDH) controls flux through the biosynthetic pathway for this important amino acid and represents a putative target in oncology. To discover inhibitors of PHGDH, a coupled biochemical assay was developed and optimized to enable high-throughput screening for inhibitors of human PHGDH. Feedback inhibition was minimized by coupling PHGDH activity to two downstream enzymes (PSAT1 and PSPH), providing a marked improvement in enzymatic turnover. Further coupling of NADH to a diaphorase/resazurin system enabled a red-shifted detection readout, minimizing interference due to compound autofluorescence. With this protocol, over 400,000 small molecules were screened for PHGDH inhibition, and following hit validation and triage work, a piperazine-1-thiourea was identified. Following ...
TY - JOUR. T1 - Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis. AU - Locasale, Jason W.. AU - Grassian, Alexandra R.. AU - Melman, Tamar. AU - Lyssiotis, Costas A.. AU - Mattaini, Katherine R.. AU - Bass, Adam J.. AU - Heffron, Gregory. AU - Metallo, Christian M.. AU - Muranen, Taru. AU - Sharfi, Hadar. AU - Sasaki, Atsuo T.. AU - Anastasiou, Dimitrios. AU - Mullarky, Edouard. AU - Vokes, Natalie I.. AU - Sasaki, Mika. AU - Beroukhim, Rameen. AU - Stephanopoulos, Gregory. AU - Ligon, Azra H.. AU - Meyerson, Matthew. AU - Richardson, Andrea L.. AU - Chin, Lynda. AU - Wagner, Gerhard. AU - Asara, John M.. AU - Brugge, Joan S.. AU - Cantley, Lewis C.. AU - Vander Heiden, Matthew G.. PY - 2011/9/1. Y1 - 2011/9/1. N2 - Most tumors exhibit increased glucose metabolism to lactate, however, the extent to which glucose-derived metabolic fluxes are used for alternative processes is poorly understood. Using a metabolomics approach with isotope labeling, we found that ...
BioAssay record AID 400045 submitted by ChEMBL: Antimicrobial activity against Sporotrichum pulverulentum after 60 mins by agar diffusion method.
It is reasonable that efficient conversion of L-serine to pyruvate requires sufficient availability of L-serine. To enhance the biosynthesis of L-serine, we overexpressed the genes of de novo L-serine biosynthetic pathway. L-serine is synthesized from D-3-phosphoglycerate by three reactions catalyzed by D-3-phosphoglycerate dehydrogenase, D-3-phosphoserine aminotransferase and phosphoserine phosphatase, which are encoded by serA, serC and serB, respectively (Figure 1). D-3-phosphoglycerate dehydrogenase is regulated by allosteric end-product inhibition. Moreover, a published report has showed that a truncated D-3-phosphoglycerate dehydrogenase (PGDH) serA Δ197 was no longer inhibited by L-serine in C. glutamicum [18]. As such, we combined serA Δ197 together with serB and serC into an artificial operon driven by the constitutive promoter trc, creating plasmid pTSer. Strain SD01 was transformed with plasmid pTSer for activating the Serine-Deamination (SD) pathway. After 48h cultivation, 3.96 g/L ...
Carbohydrate dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde, lactone, or ketose.. Carbohydrate dehydrogenases are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of molecules.. An example includes L-gulonolactone oxidase.. They are categorized under EC number 1.1. More specifically, they are in three subcodes: 1, 2, and 99, categorized as follows:. ...
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TY - JOUR. T1 - Kinetic modeling of a bi-enzymatic system for efficient conversion of lactose to lactobionic acid. AU - Van, Wouter. AU - Bhagwat, Aditya. AU - Ludwig, Roland. AU - Dewulf, Jo. AU - Haltrich, Dietmar. AU - Van Langenhove, Herman. PY - 2009/4/1. Y1 - 2009/4/1. N2 - A model has been developed to describe the interaction between two enzymes and an intermediary redox mediator. In this bi-enzymatic process, the enzyme cellobiose dehydrogenase oxidizes lactose at the C-1 position of the reducing sugar moiety to lactobionolactone, which spontaneously hydrolyzes to lactobionic acid. 2,20 Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt is used as electron acceptor and is continuously regenerated by laccase. Oxygen is the terminal electron acceptor and is fully reduced to water by laccase, a coppercontaining oxidase. Oxygen is added to the system by means of bubble-free oxygenation. Using the model, the productivity of the process is investigated by simultaneous solution ...
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PHGDH antibody [N3C2], Internal (phosphoglycerate dehydrogenase) for IHC-Fr, IHC-P, WB. Anti-PHGDH pAb (GTX101949) is tested in Human, Rat samples. 100% Ab-Assurance.
D-serine is an endogenous ligand for NMDARs generated from L-serine by the enzyme serine racemase (Srr). Both neuronal and glial localizations have been reported for D-serine and Srr. 3-phosphoglycerate dehydrogenase ...
Recognized as one of the 100 most technologically significant products introduced to the marketplace in the past year. The Remote Methane Leak Detector can quickly and efficiently detect leaks up to one hundred feet away. Using laser technology, remote detection allows the user to safely survey areas that may be difficult to reach, such as busy roadways, yards with large dogs, locked gates, pipe suspended under a bridge and other hard to access places. In the independent validation tests, the RMLD has proven to be a highly effective leak survey instrument, compared to flame ionization and similar equipment, but with the added advantage of remote detection. By design the RMLD is capable of achieving significant productivity gains and drastically reduce operations and maintenance costs ...
Hi Vivek, There are a number of hidden parameters changed in 9i that affected CBO (as compared to 8i CBO). I suggest contacting Oracle Support before changing any hidden parameters. I think this is know problem. If possible, test your application with 9.2.0.6. That seems to a stable version of 9i, so far. Regards, - Kirti --- VIVEK_SHARMA ,[email protected], wrote: , , ISSUE - Getting HIGH Latch Free Wait on the following Latches after moving , from RBO to , CBO. ( ALL Objects been analyzed at 100 %). CPU Usage on DB Server has gone , up by about , 30 %. NOTE - Application has also been migrated to a Higher release along , with the CBO , movement. , , Qs Any init.ora parameters to Tune ? , , Would increasing _shared_pool_reserved_min_alloc to 6140 from the Default of , 4400 Help? , , Setting cursorsharing = FORCE/SIMILAR caused %sys component of CPU Usage to , shoot to , 99 % within minutes of Database startup. Seemed to be hitting some Bug in , 9.2.0.5 (64 , Bit) on Solaris 9. Has ...
When determining the effects on the deficit of a certain legislative action, both revenues and spending have to be accounted for. Indeed, you cant determine
Neu-Laxova syndrome (NLS) is an autosomal recessive disorder characterized by severe congenital malformations leading to prenatal or early postnatal lethality. Main findings include intrauterine growth retardation, microcephaly, ichthyosis, flexion deformities, edema of the hands and feet, and abnormal facial features including abnormal or absent eyelids, flat or abnormal nose, and a round gaping mouth. NLS1 (MIM 256520) and NLS2 (MIM 616038) are caused by mutations in the PHGDH and PSAT1 genes. They code for D-3-phosphoglycerate dehydrogenase and phosphoserine aminotransferase enzymes, respectively. These enzymes are involved in L-serine biosynthesis. Phosphoglycerate dehydrogenase deficiency (PHGDHD; MIM 601815) and phosphoserine aminotransferase deficiency (PSATD; MIM 610992) are autosomal recessive disorders allelic to more severe disorders, NLS1 and NLS2. PHGDHD and PSATD are characterized by congenital microcephaly, hypertonia, psychomotor retardation and seizures.. Read less ...
The PHGDH gene provides instructions for making the parts (subunits) that make up the phosphoglycerate dehydrogenase enzyme. Four PHGDH subunits combine to form the enzyme. This enzyme is involved in the production (synthesis) of the protein building block (amino acid) serine. Specifically, the enzyme converts a substance called 3-phosphoglycerate to 3-phosphohydroxypyruvate in the first step in serine production. Serine is necessary for the development and function of the brain and spinal cord (central nervous system). Serine is a part of chemical messengers called neurotransmitters that transmit signals in the nervous system. Proteins that form cell membranes and the fatty layer of insulation (myelin) that surrounds many nerves also contain serine.. Serine can be obtained from the diet, but brain cells must produce their own serine because dietary serine cannot cross the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). ...
The sugar oxidising enzymes glucose oxidase, glucose dehydrogenases (GDH) and cellobiose dehydrogenases (CDH) were co-immobilised, in the presence of multiwalled carbon nanotubes, with osmium redox polymers. Under pseudo-physiological conditions of 5 mM glucose, 150 mM NaCl, 37?degrees C, glucose oxidation current densities above 800 mu A?cm-2 are obtained from films containing an [Os(4,4xxx-dimethyl-2,2xxx-bipyridine)2(poly-vinylimidazole)10Cl]+ redox polymer, redox potential 0.1 V vs. Ag/AgCl, and either glucose oxidase or FAD-dependant GDH. Current produced by, and stability of, glucose-oxidising half-cells is compared in 100 mM glucose, with films containing CDHs proving most stable. Such results show promise for development of glucose-oxidising enzymatic fuel cells ...
Pyranose Oxidase antibody LS-C744693 is an unconjugated goat polyclonal antibody to Pyranose Oxidase from e. coli. It is reactive with bacteria and e. coli. Validated for ELISA, IP and WB.
This Research Topic addresses the metabolism and function of the amino acid Serine in plants. We emphasize the interaction and coordination between the Serine biosynthetic pathways and other metabolic pathways.Serine is a polar amino acid that plays a fundamental role in plant metabolism, plant development, and cell signalling. In addition to being a building block for proteins, Serine participates in the biosynthesis of biomolecules such as amino acids, nucleotides, phospholipids, and sphingolipids. Plants possess at least two serine biosynthetic pathways: i) the glycolate pathway associated with photorespiration and ii) the so-called Phosphorylated Pathway of Serine Biosynthesis. The biological significance of the coexistence of several pathways for the biosynthesis of Serine is not known. In particular, we poorly understand the contribution that each pathway makes to plant serine homeostasis, how pathways are integrated and coordinated, and how they interact at the transcriptional/translational
Blog on Phgdh elisa kit product: The Mouse Phgdh phgdh (Catalog #MBS2602994) is an ELISA Kit and is intended for research purposes only. T...
ID E7A1S5_SPORE Unreviewed; 226 AA. AC E7A1S5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313,EMBL:CBQ73432.1}; GN ORFNames=sr14090 {ECO:0000313,EMBL:CBQ73432.1}; OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium. OX NCBI_TaxID=999809 {ECO:0000313,EMBL:CBQ73432.1, ECO:0000313,Proteomes:UP000008867}; RN [1] {ECO:0000313,EMBL:CBQ73432.1, ECO:0000313,Proteomes:UP000008867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRZ2 {ECO:0000313,Proteomes:UP000008867}; RX PubMed=21148393; DOI=10.1126/science.1195330; RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K., RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., RA Pester D., Mueller O., Winterberg B., Meyer E., Ghareeb H., RA Wollenberg T., ...
The following are the more stable anomers of the pyranose forms of d-glucose, d-mannose, and d-galactose: O HO HO OH OH O HO HO HO OH OH OH O HO HO OH OH -D-Glucopyranose (64% at equilibrium) -D-Mannopyranose (68% at equilibrium) -D-Galactopyranose (64% at equilibrium) OH On the basis of these empirical observations
An improved method is presented for the purification of 8 α-(N1-histidyl)riboflavin, 8 α-(N3-histidyl)riboflavin and their 2′,5′-anhydro forms, which permits the isolation of sizeable quantities of each of these compounds from a synthetic mixture in pure form. Flavin peptides were isolated from the D-gluconate dehydrogenases of Pseudomonas aeruginosa and Pseudomonas fluorescens and from the 2-keto-D-gluconate dehydrogenase of Gluconobacter melanogenus. After conversion into the aminoacyl-riboflavin, the flavin in all three enzymes was identified as 8 α-(N3-histidyl)riboflavin. By sequential treatment with nucleotide pyrophosphatase and alkaline phosphatase, the flavin in each enzyme was shown to be in the dinucleotide form. ...
Biomass is constructed of dense recalcitrant polymeric materials: proteins, lignin, and holocellulose, a fraction constituting fibrous cellulose wrapped in hemicellulose-pectin. Bacteria and fungi are abundant in soil and forest floors, actively recycling biomass mainly by extracting sugars from holocellulose degradation. Here we review the genome-wide contents of seven Aspergillus species and unravel hundreds of gene models encoding holocellulose-degrading enzymes. Numerous apparent gene duplications followed functional evolution, grouping similar genes into smaller coherent functional families according to specialized structural features, domain organization, biochemical activity, and genus genome distribution. Aspergilli contain about 37 cellulase gene models, clustered in two mechanistic categories: 27 hydrolyze and 10 oxidize glycosidic bonds. Within the oxidative enzymes, we found two cellobiose dehydrogenases that produce oxygen radicals utilized by eight lytic polysaccharide ...
Pyranose is a collective term for saccharides that have a chemical structure that includes a six-membered ring consisting of five carbon atoms and one oxygen atom. There may be other carbons external to the ring. The name derives from its similarity to the oxygen heterocycle pyran, but the pyranose ring does not have double bonds. A pyranose in which the anomeric OH at C(l) has been converted into an OR group is called a pyranoside. The pyranose ring is formed by the reaction of the hydroxyl group on carbon 5 (C-5) of a sugar with the aldehyde at carbon 1. This forms an intramolecular hemiacetal. If reaction is between the C-4 hydroxyl and the aldehyde, a furanose is formed instead. The pyranose form is thermodynamically more stable than the furanose form, which can be seen by the distribution of these two cyclic forms in solution. Hermann Emil Fischer won the Nobel Prize in Chemistry (1902) for his work in determining the structure of the D-aldohexoses. However, the linear, free-aldehyde ...
1H6B: Crystal Structures of the Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas Mobilis and its Complexes with Bound Ligands
1RWB: Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state.
Holzer, H. & Holldorf, A. (1957). „Isolation of a D-glycerate dehydrogenase, its properties, and its use for the optical determination of hydroxypyruvate in the presence of pyruvate". Biochem. Z. 329: 292-312. PMID 13522707 ...
Treatment for Cortisone Reductase Deficiency in Sewri West, Mumbai. Find Doctors Near You, Book Appointment, Consult Online, View Doctor Fees, Address, Phone Numbers and Reviews. Doctors for Cortisone Reductase Deficiency in Sewri West, Mumbai | Lybrate
Treatment for Cortisone Reductase Deficiency. Find Doctors Near You, Book Appointment, Consult Online, View Doctor Fees, Address, Phone Numbers and Reviews. Doctors for Cortisone Reductase Deficiency | Lybrate
Influence of Carbon Source on the Production of Extracellular Ligninolytic Enzymes by Phanerochaete chrysosporium. Fangfang Wang,a Mingqiang Ai,a Guihua Yang,b Jiachuan Chen,b Xiulan Chen,a and Feng Huang a,*. The effect of altering the carbon source in the growing environment was investigated relative to the production of ligninolytic enzymes by Phanerochaete chrysosporium. Glucose, cellobiose, and cellulose (or mixtures thereof) were used as the carbon sources. Glucose oxidase and glyoxal oxidase activities in all carbon sources were produced during cultivation. High peak levels (0.17 to 0.24 IU/mL) of manganese peroxidase activity were observed only in mediums containing oligosaccharides. Lignin peroxidase activity was high in glucose medium (0.21 IU/mL of peak value); however, minimal amounts were formed in the cellulose medium (0.01 IU/mL of peak value). High amounts of cellobiose:quinone oxidoreductase (3.33-3.99 IU/mL of peak value) and cellobiose dehydrogenase (0.04-0.2 IU/mL of peak ...
Effects of kraft pulp and lignin on Trametes versicolor carbon metabolism. Purification and characterization of cellobiose dehydrogenases from the white rot fungus Trametes versicolor
Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
Isolation and purification of Pyranose 2-oxidase from Phanerochaete chrysosporium and characterization of gene structure and regulation
Published in the January 2001 Issue of Anvil Magazine Note: Images with captions are included at the end of this article. "Scratches" is a term that refers to a skin problem on the lower legs of horses, caused by a fungus (and sometimes complicated by bacteria). The affected area becomes crusted, scabby and thickened, creating bumps and sometimes open sores. In severe cases the affected skin may ooze or the whole lower leg may swell, and the horse may become lame. This skin condition generally affects unpigmented skin (the areas of white leg markings) more readily than dark skin, since the unpigmented skin is not as tough-and more apt to chaff and scrape, opening the way for infection. Scratches is a dermatitis, or inflammation of the skin, and the most common cause seems to be the fungus Sporotrichum schenki. Some horses seem to be more susceptible than others, just as some seem more vulnerable to other fungal infections such as ringworm and girth itch. The fungus lives in organic matter and ...
A glucuronoyl esterase (GE) from the thermophilic fungus Sporotrichum thermophile, belonging to the carbohydrate esterase family 15 (CE-15), was functionally expressed in the methylotrophic yeast Pich
A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, quinoprotein glucose dehydrogenase ...
Wolbachia sp. subsp. Drosophila simulans UDP-N-acetylenolpyruvoylglucosamine reductase (murB) datasheet and description hight quality product and Backed by our Guarantee
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 201.9) ...
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 180.6) ...
Quinoprotein glucose dehydrogenase (EC 1.1.99.17) from Acinetobacter calcoaceticus L.M.D. 79.41 was purified to homogeneity. It is a basic protein with an isoelectric point of 9.5 and an Mr of 94,000. Denaturation yields two molecules of PQQ/molecule and a protein with an Mr of 48000, indicating that the enzyme consists of two subunits, which are probably identical because even numbers of aromatic amino acids were found. The oxidized enzyme form has an absorption maximum at 350 nm, and the reduced form, obtained after the addition of glucose, at 338 nm. Since double-reciprocal plots of initial reaction rates with various concentrations of glucose or electron acceptor show parallel lines, and substrate inhibition is observed for glucose as well as for electron acceptor at high concentrations, a ping-pong kinetic behaviour with the two reactants exists. From the plots, Km values for glucose and Wursters Blue of 22 mM and 0.78 mM respectively, and a Vmax. of 7.730 mumol of glucose oxidized/min per ...
The practice of exposing liquid cultures of the white-rot fungus Phanerochaete chrysosporium to a pure oxygen atmosphere under conditions of nutrient starvation has been widely adopted to induce lignin peroxidase (LiP) synthesis. Transmission electron microscopy was used to examine hyphal cells of carbon-limited cultures that had been exposed to an atmosphere of pure oxygen, and revealed evidence of a major loss in organization of cellular ultrastructure, which may be attributed to oxygen toxicity. Under some conditions (continuous agitation in air with cellulose as the carbon source) cultures will produce LiP without needing to be exposed to a pure oxygen atmosphere. A similar major loss of cellular ultrastructure was found in hyphal cells from such cultures upon examination. Investigation of the levels of H2O2, catalase and carbonyl content of intracellular proteins suggests that the latter cultures developed a hyperoxidant state because the rate of supply of carbon from cellulose hydrolysis was
This paper reports the isolation of phenoloxidase-negative mutants of the white-rot fungus Phanerochaete chrysosporium and the results of a survey of idiophasic functions among these mutants. The mutant strains were isolated from a medium containing o-anisidine after gamma irradiation of wild-type spores and fell into four classes, divided by the manner in which they mineralized 14C-lignin wheat lignocellulose. Examples are strain LMT7, which degraded lignin at a rate similar to that of the wild type; strain LMT26, in which degradation was enhanced; strain LMT16, whose degradation rate was apparently unaffected, although the onset of lignin attack was delayed compared with that in the wild type; and strain LMT24, which was unable to evolve significant amounts of 14CO2 from the radiolabeled substrate. The mutants were not necessarily defective in other functions associated with idiophasic activities (intracellular cyclic AMP levels, sporulation, extracellular glucan production, veratryl alcohol ...
Myc transcriptionally regulates genes involved in processes such as cell proliferation, metabolism, differentiation, and angiogenesis. MYC expression is deregulated in many types of human cancer; therefore discovering the mechanisms behind MYCs role in tumorigenesis is essential. In this dissertation, I have focused on several Myc target genes, Spermidine synthase (Srm); Lactate dehydrogenase (Ldh); 3-phosphoglycerate dehydrogenase (Phgdh); Serine hydroxymethyltransferase (SHMT) 1 and 2; and Pim-3 (a member of the Pim family of serine/threonine kinases). These enzymes play a role in various functions: Spermidine synthase (polyamine synthesis); Lactate dehydrogenase (glycolysis); Phgdh and Shmt (serine metabolism); and Pim-3 (cell signaling). In order to elucidate the impact Myc over-expression has on metabolism in tumorigenesis, we use human cell lines, and transgenic mice as well as cell lines and tissues derived from these mice. The impact of inhibition of these target genes on Myc-driven ...
1. Two enzymes that catalyse the reduction of glyoxylate to glycollate have been separated and purified from a species of Pseudomonas. Their molecular weights were estimated as 180000. 2. Reduced nicotinamide nucleotides act as the hydrogen donators for the enzymes. The NADH-linked enzyme is entirely specific for its coenzyme but the NADPH-linked reductase shows some affinity towards NADH. 3. Both enzymes convert hydroxypyruvate into glycerate. 4. The glyoxylate reductases show maximal activity at pH6.0-6.8, are inhibited by keto acids and are strongly dependent on free thiol groups for activity. 5. The Michaelis constants for glyoxylate and hydroxypyruvate were found to be of a high order. 6. The reversibility of the reaction has been demonstrated for both glyoxylate reductases and the equilibrium constants were determined. 7. The reduction of glyoxylate and hydroxypyruvate is not stimulated by anions.. ...
article{31e17f38-485f-4324-be67-f72cc473b767, abstract = {Both the antibody affinity and the detectability of the label are essential in deciding the final characteristics of a heterogeneous immunoassay. This paper describes an approach to obtain a supplementary enhancement of the signal generated by using an enzyme label, e.g., by including the product of the enzymatic reaction in an additional amplification cycle during the detection step performed with an amperometric biosensor based on glucose dehydrogenase (GDH). An immunoassay format with a labelled analyte derivative that competes with the analyte present in the sample for a limited amount of antibody binding sites was employed. The beta-galactosidase label hydrolyses the substrate aminophenyl-beta-galactopyranoside, and the generated aminophenol enters then into a bioelectrocatalytic amplification cycle at the GDH biosensor. The principle was applied for determination of 4-nitrophenol, with the best minimal concentration of 1.5 microM ...
Strain YM16-304T lacks the dapE gene for succinyl-diaminopimelate desuccinylase (EC:3.5.1.18) in the biosynthesis pathway of lysine and diaminopimelic acids (DAPs). Instead, two candidate genes (YM304_26990 and YM304_19190) for LL-DAP aminotransferase (EC:2.6.1.83, dapL), that constitutes an alternative DAP-lysine biosynthesis pathway (DAP aminotransferase pathway [24,25]), were identified. The dapL gene is found in discrete lineages of Bacteria and Archaea, and is known to complement Escherichia coli dapD and dapE mutants, although purified proteins favor the reverse reaction rather than the synthesis of LL-DAP [25].. Among the genes of serine biosynthesis pathway, the serB gene for phosphoserine phosphatase (EC:3.1.3.3) was not identified by similarity searches. On the other hand, the thrH gene for phosphoserine / homoserine phosphotransferase [26] (EC:3.1.3.3, 2.7.1.39) was identified (YM304_28950). The possibility of using thrH gene product for serine biosynthesis instead of serB gene ...
Acer campestre is a slow-growing deciduous tree with dark, oval leaves that turn yellow in the autumn. The 5 lobed leaves are composed of 3 to 5 entire lobes. Blooms in corymbs of 5 green flowers followed by winged fruit. The cultivar, Pulverulentum is a small tree to 12 feet tall with a large crown, wider than
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CTBP2 Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB ...
Fructose-Glucose Syrup as sugar replacement and sweetener: Information, tolerance and effect of Fructose-Glucose Syrup within the human body - Frusano
This reaction has also been observed in Pseudomonas A2697 , Sporotrichum B124 , Trichosporon B368, D232 , Arthrobacter H270 , Aspergillus H236 , Bradyrhizobium
Growth in real (inflation-adjusted) GDP in calendar year 2013 will be just 0.5 percent, CBO expects-with the economy projected to contract at an annual rate of 1.3 percent in the first half of the year and expand at an annual rate of 2.3 percent in the second half. Given the pattern of past recessions as identified by the National Bureau of Economic Research, such a contraction in output in the first half of 2013 would probably be judged to be a recession. ...
Domain combinations containing the Serine metabolism enzymes domain superfamily . Domain architectures illustrate each occurrence of the Serine metabolism enzymes domain superfamily.
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The report generally describes copper d-gluconate, examines its uses, production methods, patents. Copper D-gluconate market situation is overviewed;
The primary structure of bovine liver UDP-glucose dehydrogenase (UDPGDH), a hexameric, NAD(+)-linked enzyme, has been determined at the protein level. The 52-kDa subunits are composed of 468 amino acid residues, with a free N-terminus and a Ser/Asn microhetergeneity at one position. The sequence sha …
Older research outputs will score higher simply because theyve had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 271,050 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 61% of its contemporaries ...
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Yesterday afternoon, House Speaker John Boehner got word from the Congressional Budget Office that his debt plan didnt reduce the
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Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
RESULTS:. We observed that increased production of hepatic H6PDH in db/db mice was paralleled by upregulation of hepatic G6PT production and responded to elevated circulating levels of corticosterone. Treatment of db/db mice with the glucocorticoid antagonist RU486 markedly reduced production of both H6PDH and 11β-HSD1 and improved hyperglycaemia and insulin resistance. The reduction of H6PDH and 11β-HSD1 production by RU486 was accompanied by RU486-induced suppression of hepatic G6pt (also known as Slc37a4) mRNA. Incubation of mouse primary hepatocytes with corticosterone enhanced G6PT and H6PDH production with corresponding activation of 11β-HSD1 and PEPCK: effects that were blocked by RU486. Knockdown of H6pd by small interfering RNA showed effects comparable with those of RU486 for attenuating the corticosterone-induced H6PDH production and 11ß-HSD1 reductase activity in these intact cells. Addition of the G6PT inhibitor chlorogenic acid to primary hepatocytes suppressed H6PDH production ...
Oxygen-dependent alginate synthesis and enzymes in Pseudomonas aeruginosa.: Alginate production by the highly alginate-producing Pseudomonas aeruginosa 8821M wa
L-serine is a promising building block biochemical with a high theoretical production yield from glucose. Toxicity of L-serine is however prohibitive for high-titer production in E. coli. Here, E. coli lacking L-serine degradation pathways was evolved for improved tolerance by gradually increasing L-serine concentration from 3 to 100 g/L using adaptive laboratory evolution (ALE). Genome sequencing of isolated clones revealed multiplication of genetic regions, as well as mutations in thrA, thereby showing a potential mechanism of serine inhibition. Other mutations were evaluated by MAGE combined with amplicon sequencing, revealing role of rho, lrp, pykF, eno, and rpoB on tolerance and fitness in minimal medium. Production using the tolerant strains resulted in 37 g/L of L-serine with a 24% mass yield. The resulting titer is similar to the highest production reported for any organism thereby highlighting the potential of ALE for industrial biotechnology ...
Glucose-fructose syrup is commonly added to foods as a sweetener, in order not only to give a sweet taste, but also to increase the attractiveness of the product by improving consistency, aroma and color, but excessive consumption of products containing glucose-fructose syrup is a health risk. Why is glucose-fructose syrup harmful? Glucose-fructose syrup is a sweetener obtained in a technological process mainly from corn starch,… ...
Resources on the mental health parity bills from the Congressional Budget Office: CBO score on H.R. 1424 (Commerce), 11-21-07: http://www.cbo.gov/ftpdocs/88xx/doc8837/hr1424e&c.pdf CBO score on H.R. 1424 (Ways & Means), 10-4-07: http://www.cbo.gov/ftpdocs/86xx/doc8679/hr1424w&m.pdf CBO score on H.R. 1424 (Ed & Labor) 9-7-07: http://www.cbo.gov/ftpdocs/86xx/doc8608/hr1424.pdf CBO score on S. 558, 3-20-07 ...
A CBO aide said the agency will not release its analysis of the revised healthcare bill drafted by Senate Republicans on Monday, following a vote delay.
The Congressional Budget Office (CBO), a non-partisan congressional budget review agency, recently came up with their latest multi-year actual versus forecast for some key economic indicators. While a number of… Read more ». ...
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We talk to Lan T. Pham, the famous CBO whistleblower who was fired from her job for telling the truth about systemic fraud and corruption in Americas mortgage market and financial system. Dr. Lan T. Pham, former Principal Analyst and Financial Economist at the Congressional Budget Office (CBO) was beginning to explore the fallout from MERS (Mortgage Electronic Registration Systems) in her work there in 2010, before she was quickly fired. She joins us in a TV exclusive interview to tell her story, and to tell you why Americans should be asking some tough questions about who the CBO and Congress are REALLY serving… ...
glucose-fructose-syrup definition: Noun (plural glucose-fructose syrups) 1. (UK) high fructose corn syrupI dont drink anything let alone eat anything with glucose-fructose syrup in it, its not natural.Origin glucose-fructose + syrup...
Atheliachaete sanguinea Phanerochaete sanguinea helo-orvakka r dvedskinn r dvedbarksopp v r s ter lőgomba k rnatec krvav kornatec krvav R tender ...
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Those who say they know the least about the Health Bill are the most against it. Its feels vs thinking. Even those for it know little about it. The CBO is not believed by some, but they say it will reduce the deficit.. Continue reading ...
The performance of a fluidized bed reactor using immobilized Phanerochaete chrysosporium to remove 2,4-dichlorophenol (2,4-DCP) from aqueous solution was investigated. The contribution of lignin peroxidase (LiP) and manganese peroxidase (MnP) secreted by Phanerochaete chrysosporium to the 2,4-DCP degradation was examined. Results showed that Lip and Mnp were not essential to 2,4-DCP degradation while their presence enhanced the degradation process and reaction rate. In sequential batch experiment, the bioactivity of immobilized cells was recovered and improved during the culture and the maximum degradation rate constant of 13.95 mg (Ld)−1 could be reached. In continuous bioreactor test, the kinetic behavior of the Phanerochaete chrysosporium immobilized on loofa sponge was found to follow the Monod equation. The maximum reaction rate was 7.002 mg (Lh)−1, and the saturation constant was 26.045 mg L−1. ...
The first steps of wood degradation by fungi lead to the release of toxic compounds known as extractives. To better understand how lignolytic fungi cope with the toxicity of these molecules, a transcriptomic analysis of Phanerochaete chrysosporium genes was performed in presence of oak acetonic extracts. It reveals that in complement to the extracellular machinery of degradation, intracellular antioxidant and detoxification systems contribute to the lignolytic capabilities of fungi presumably by preventing cellular damages and maintaining fungal health. Focusing on these systems, a glutathione transferase (PcGTT2.1) has been selected for functional characterization. This enzyme, not characterized so far in basidiomycetes, has been first classified as a GTT2 in comparison to the Saccharomyces cerevisiae isoform. However, a deeper analysis shows that GTT2.1 isoform has functionally evolved to reduce lipid peroxidation by recognizing high-molecular weight peroxides as substrates. Moreover, the ...
The temporal and spatial effects of selenite (SeO32−) on the physical properties and respiratory activity of Phanerochaete chrysosporium biofilms, grown in flow-cell reactors, were investigated using oxygen microsensors and confocal laser scanning microscopy (CLSM) imaging. Exposure of the biofilm to a SeO32− load of 1.67 mg Se L−1 h−1 (10 mg Se L−1 influent concentration), for 24 h, resulted in a 20% reduction of the O2 flux, followed by a ∼10% decrease in the glucose consumption rate. Long-term exposure (4 days) to SeO32− influenced the architecture of the biofilm by creating a more compact and dense hyphal arrangement resulting in a decrease of biofilm thickness compared to fungal biofilms grown without SeO32−. To the best of our knowledge, this is the first time that the effect of SeO32− on the aerobic respiratory activity on fungal biofilms is described.
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Furylglycolic acid (FA), a pseudoaromatic hydroxy-acid suitable for copolymerization with lactic acid, can be produced from glucose via enzymatically derived cortalcerone using a combination of Brønsted and Lewis acid catalysts. Cortalcerone is first converted to furylglyoxal hydrate (FH) over a Brønsted acid site (HCl or Al-containing betazeolite), and FH is subsequently converted to FA over a Lewis acid site (Sn-beta zeolite). Selectivity for conversion of FH to FA is as high as 80% at 12% conversion using tetrahydrofuran (THF) as a solvent at 358 K. Higher conversion of FH leads to FA-catalyzed degradation of FH and subsequent deactivation of the catalyst by the deposition of carbonaceous residues. The deactivated catalyst can be regenerated by calcination. Cortalcerone can be produced from 10% glucose solution using recombinant Escherichia coli strains expressing pyranose 2-oxidase and aldos-2-ulose dehydratase from the wood-decay fungus Phanerochaete chrysosporium BKM-F-1767. This ...
I am having a hard time in identifying a Candida with microscopic morpholoy somewhat resembles C. pseudotropicalis. The biochemical profile is, however, not entirely consistent with that of C. pseudotropicalis. The biggest trouble is that it neither ferments nor assimilates sucrose. Is this possible for this species. Where can I find additional database for its ID? Both the ViTech and the API systems failed to give an ID. For those with database-in-brains, heres its biochemical profile: Fermentation: Assimilation: Dextrose + Glucose + Maltose +/- Glycerol - Lactose + 2-keto-D-gluconate - Sucrose - L-arabinose + Trehalose +/- xylose + Raffinose - Adonitol(Ribitol) + xylitol + galactose + inositol - sorbitol + Methyl-D-glucoside - N-acetyl-D-glucosamine - cellobiose + lactose + maltose - sucrose - trehalose - melezitose - raffinose + Thank you all for your help. Kai Leung, M.D. Dept. of Laboratory Medicine and Pathology University of Minnesota ...
You Are Here: Alginate synthesis in Azotobacter vinelandii is increased by reducing the intracellular production of ubiquinone. ...
TY - JOUR. T1 - Discovery of function in the enolase superfamily. T2 - D-mannonate and d-gluconate dehydratases in the d-mannonate dehydratase subgroup. AU - Wichelecki, Daniel J.. AU - Balthazor, Bryan M.. AU - Chau, Anthony C.. AU - Vetting, Matthew W.. AU - Fedorov, Alexander A.. AU - Fedorov, Elena V.. AU - Lukk, Tiit. AU - Patskovsky, Yury V.. AU - Stead, Mark B.. AU - Hillerich, Brandan S.. AU - Seidel, Ronald D.. AU - Almo, Steven C.. AU - Gerlt, John A.. PY - 2014/4/29. Y1 - 2014/4/29. N2 - The continued increase in the size of the protein sequence databases as a result of advances in genome sequencing technology is overwhelming the ability to perform experimental characterization of function. Consequently, functions are assigned to the vast majority of proteins via automated, homology-based methods, with the result that as many as 50% are incorrectly annotated or unannotated (Schnoes et al. PLoS Comput. Biol. 2009, 5 (12), e1000605). This manuscript describes a study of the d-mannonate ...
Also see the JGI Mycocosm for information on the Genomic Encyclopedia of Fungi: a range of interests into the fungal genomes that impact on mycorrhyzal symbiosis, plant pathogenicity, biocontrol as well as industrial applications such as lignocellulose degradation, sugar fermentation and other industrial applications. ...
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The glucose content of blood can be determined by contacting a blood sample with a test strip containing a glucose dehydrogenase dependent on PQQ (or derivatives or isomers) thereof as a co-factor, a tetrazolium salt indicator, but in the absence of a mediator.
Lactobacillus rhamnosus strain ATCC 9595 Wzd (wzd), Wze (wze), Wzx (wzx),WelF (welF), WelG (welG), WelH (welH), WelI (welI), Wzy (wzy), WelJ (welJ),Wzm (wzm), RmlA (rmlA), RmlC (rmlC), RmlB (rmlB), RmlD (rmlD), WelE (welE),Wzr (wzr), Wzb (wzb), ClpL (clpL), and Nrp (nrp) genes, complete ...
APHOTOFUNGI - Photographic Stock Image Library Page for Trametes versicolor - Turkeytail (Polyporale images). A-P-H-O-T-O - Furthering environmental awareness and education through the medium of photography.
The Golm Metabolome Database (GMD) facilitates the search for and dissemination of mass spectra from biologically active metabolites quantified using GC-MS.
The Golm Metabolome Database (GMD) facilitates the search for and dissemination of mass spectra from biologically active metabolites quantified using GC-MS.
3262-72-4|Boc-Ser-OH|Boc-L-serine|N-Boc-L-serine|N-Boc-L-Serine|N-α-t-BOC-L-SERINE|N-(tert-Butoxycarbonyl)-L-serine|(2S)...
n என்னும் வேதி வாய்பாடு கொண்ட கரிமச் சேர்மம் ஆகும். ஒவ்வொரு குழுவான ஆறு கரிம அணுக்களுக்கும், 10 ஐதரச அணுக்களும் 5 ஆக்சிச அணுக்களும் இணைப்பு கொண்ட நெடுந்தொடர் கரிமச்சேர்பம். அது பல நூற்றில் இருந்து ஒன்பதாயிரத்திற்கும் மேற்பட்ட எளிய இனியமாகிய D-குளுக்கோசு அலகுகளை நீண்ட சங்கிலியாக இணைத்த பல்லினியம் அல்லது பாலிசாக்கரைடு என்னும் வகையைச் சேர்ந்த ஒரு சேர்மம். [1][2] மாவியம், பசும் ...
2-oxoglutarate dehydrogenase, and transketolase which are all involved in carbohydrate metabolism. Vitamin B2 (riboflavin) is a ... Primary metabolites include carbohydrates, lipids, amino acids, and nucleic acids which are the basic building blocks of life. ... Hermann Emil Fischer in 1884, turned his attention to the study of carbohydrates and purines, work for which he was awarded the ... Vitamin B5 (pantothenic acid) is a constituent of coenzyme A, a basic component of carbohydrate and amino acid metabolism as ...
... alcohol dehydrogenase MeSH D08.811.682.047.150 --- carbohydrate dehydrogenases MeSH D08.811.682.047.150.225 --- fructuronate ... 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 ...
... carbohydrate metabolism, and renal hypertension has garnered international attention and fame and has led to significant ... more specifically the effects of cyanide and pyrophosphate on succinic dehydrogenase; from this moment Leloir began to ... made discoveries regarding carbohydrate storage and its subsequent transformation into a reserve energy form in organisms. ... Leloir and his team identified the sugar nucleotides that were fundamental to the metabolism of carbohydrates, turning the ...
... glutamate dehydrogenase gain-of-function mutations) Short chain acyl coenzyme A dehydrogenase deficiency Carbohydrate-deficient ...
showed that there is a therapeutic effect of maintaining a ketogenic diet - a diet consisting of high fat/low carbohydrate ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Pearl, P. L.; Novotny, E. J.; Acosta, M. T.; Jakobs, C.; Gibson, K. M. (2003). "Succinic semialdehyde dehydrogenase deficiency ...
... is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into ... Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+ --> fructose + NADH + H+. A zinc ion is also ... Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. ... Sorbitol dehydrogenase belongs to the oxidoreductase family, which means that it helps catalyze oxidation reduction reactions. ...
This pathway is regulated through changes in the activity of glucose-6-phosphate dehydrogenase. Fructose must undergo certain ... Some simple carbohydrates have their own enzymatic oxidation pathways, as do only a few of the more complex carbohydrates. The ... Carbohydrates are central to many essential metabolic pathways. Plants synthesize carbohydrates from carbon dioxide and water ... Although humans consume a variety of carbohydrates, digestion breaks down complex carbohydrates into a few simple monomers for ...
Carbohydrate dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion ... Carbohydrate dehydrogenases are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ... Carbohydrate Dehydrogenases at the US National Library of Medicine Medical Subject Headings (MeSH) ... Kulys, J., Tetianec, L. and Bratkovskaja, I. (2010), Pyrroloquinoline quinone-dependent carbohydrate dehydrogenase: Activity ...
Avoiding factors that might precipitate condition Glucose Low fat/high carbohydrate nutrition Long-chain acyl-CoA dehydrogenase ... "HADHA hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit [Homo ... "OMIM Entry - * 600890 - HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT; HADHA". omim. ... "Long-Chain Acyl CoA Dehydrogenase Deficiency: Background, Pathophysiology, Epidemiology". eMedicine. 24 March 2016. Retrieved ...
"Decreased PDH activation and glycogenolysis during exercise following fat adaptation with carbohydrate restoration". American ... Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. ... PDPC 1 is an enzyme which serves to reverse the effects of pyruvate dehydrogenase kinase upon pyruvate dehydrogenase. ... Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial ...
Phosphorylated carbohydrate substrate and transition state analogues, non-carbohydrate substrate analogues and triphenylmethane ... 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase". Biochem. J. 55: 23- ... 6-phosphogluconate dehydrogenase (decarboxylating), and 6-phospho-D-gluconate dehydrogenase. This enzyme participates in ... "Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities in normal canine mammary gland and in mammary ...
Frampton EW, Wood WA (1961). "Carbohydrate oxidation by Pseudomonas fluorescens VI. Conversion of 2-keto-6-phosphogluconate to ... phosphogluconate dehydrogenase, gluconate 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase (NAD+), and 2-keto-6- ... In enzymology, a phosphogluconate 2-dehydrogenase (EC 1.1.1.43) is an enzyme that catalyzes the chemical reaction 6-phospho-D- ... Other names in common use include 6-phosphogluconic dehydrogenase, ...
Kohn LD; Jakoby WB (1966). "L- and mesotartaric acid dehydrogenase (crystalline)". Carbohydrate Metabolism. Methods in ... In enzymology, a meso-tartrate dehydrogenase (EC 1.3.1.7) is an enzyme that catalyzes the chemical reaction meso-tartrate + ...
As is mentioned above, galactitol is not a suitable substrate for the enzyme, polyol dehydrogenase, which catalyzes the next ... Infant formula based on casein hydrolysates and dextrin maltose as a carbohydrate source can also be used for initial ... step in the carbohydrate metabolic cycle. Thus, the sugar alcohol idly begins to accumulate in the lens. As galactitol ...
... protein belonging to the glyceraldehyde-3-phosphate dehydrogenase family of enzymes that play an important role in carbohydrate ... Glyceraldehyde-3-phosphate dehydrogenase, spermatogenic or glyceraldehyde-3-phosphate dehydrogenase, testis-specific is an ... Benham FJ, Povey S (Aug 1989). "Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to ... Westhoff D, Kamp G (Aug 1997). "Glyceraldehyde 3-phosphate dehydrogenase is bound to the fibrous sheath of mammalian ...
"Pentose phosphate pathway of carbohydrate metabolism and NADP-dependent glycerol 3-phosphate dehydrogenase activity in some ... glycerin-3-phosphate dehydrogenase, NADPH-dependent glycerin-3-phosphate dehydrogenase, and glycerol-3-phosphate 1- ... In enzymology, a glycerol-3-phosphate 1-dehydrogenase (NADP+) (EC 1.1.1.177) is an enzyme that catalyzes the chemical reaction ... Other names in common use include glycerol phosphate (nicotinamide adenine dinucleotide phosphate), dehydrogenase, L-glycerol 3 ...
"MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies". Journal of Molecular ... Pyruvate dehydrogenase (lipoamide) beta, also known as pyruvate dehydrogenase E1 component subunit beta, mitochondrial or PDHE1 ... Mutations in the PDHB gene have been known to cause one form of pyruvate dehydrogenase deficiency. Pyruvate dehydrogenase ... Korotchkina LG, Patel MS (Feb 2008). "Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex ...
... serves as a major link between carbohydrate metabolism and lipid metabolism. It is also a ... Older terms for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase (alphaGPDH) and ... glycerol-3-phosphate dehydrogenase is not the same as glyceraldehyde 3-phosphate dehydrogenase (GAPDH), whose substrate is an ... "Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces ...
... dehydrogenase. Palleroni NJ; Doudoroff M (1957). "Metabolism of carbohydrates by Pseudomonas saccharophilla. III Oxidation of D ... Sugar dehydrogenases in mammalian liver. I. Differentiation of various sugar dehydrogenases from pig liver by disc ... In enzymology, a D-arabinose 1-dehydrogenase (EC 1.1.1.116) is an enzyme that catalyzes the chemical reaction D-arabinose + ... Other names in common use include NAD+-pentose-dehydrogenase, and arabinose(fucose) ...
"Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress". Journal of Biology. 6 (4): 10. doi: ... Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) (EC 1.2.1.12) is an enzyme of ~37kDa ... Wang D, Moothart DR, Lowy DR, Qian X (2013). "The expression of glyceraldehyde-3-phosphate dehydrogenase associated cell cycle ... Piszczatowski RT, Rafferty BJ, Rozado A, Tobak S, Lents NH (August 2014). "The glyceraldehyde 3-phosphate dehydrogenase gene ( ...
Carbohydrate dehydrogenases. *Carnitine dehydrogenase. *D-malate dehydrogenase (decarboxylating). *DXP reductoisomerase. * ... Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, ... In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction ... Rowley B, Tucci AF (1970). "Homoisocitric dehydrogenase from yeast". Arch. Biochem. Biophys. 141 (2): 499-, 510. doi:10.1016/ ...
Metabolism: carbohydrate metabolism: glycolysis/gluconeogenesis enzymes. Glycolysis. *Hexokinase (HK1, HK2, HK3, Glucokinase)→/ ... lactate dehydrogenase A. (subunit M). Human lactate dehydrogenase M4 (the isoenzyme found in skeletal muscle). From PDB: 1I10​. ... D-lactate dehydrogenase, membrane binding. crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ...
Carbohydrate dehydrogenases. *Carnitine dehydrogenase. *D-malate dehydrogenase (decarboxylating). *DXP reductoisomerase. * ... In enzymology, a cholest-5-ene-3β,7α-diol 3β-dehydrogenase (EC 1.1.1.181) is an enzyme that catalyzes the chemical reaction[1] ... The human version of this enzyme is known as hydroxy-Δ-5-steroid dehydrogenase, 3 β- and steroid delta-isomerase 7 or HSD3B7 ... Cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase. From Wikipedia, the free encyclopedia ...
Supplementation of simple carbohydrates or glucose during illness is key to prevent catabolism. The duration of fasting for ... Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ... Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Wilcken, B.; Hammond, J.; Silink, M. (1994-05-01). "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase ...
The citric acid cycle is a cyclic metabolic pathway involved in cellular respiration, which eventually converts carbohydrates, ... a b c d e f g h i Mastrogiacoma, F., Bergeron, C. and Kish, S.J., (1993) Brain α-ketoglutarate dehydrogenase complex activity ... It has been found to be a component of other systems like pyruvate dehydrogenase and branched-chain dehydrogenase [25]. This ... The α-ketoglutarate dehydrogenase complex[edit]. The α-KGDHC is found in the tricarboxylic acid cycle (TCA), which situated ...
Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ...
showed that there is a therapeutic effect of maintaining a ketogenic diet - a diet consisting of high fat/low carbohydrate ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Pearl, P. L.; Novotny, E. J.; Acosta, M. T.; Jakobs, C.; Gibson, K. M. (2003). "Succinic semialdehyde dehydrogenase deficiency ...
Carbohydrate dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion ... Carbohydrate dehydrogenases are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ... Carbohydrate Dehydrogenases at the US National Library of Medicine Medical Subject Headings (MeSH) ... Kulys, J., Tetianec, L. and Bratkovskaja, I. (2010), Pyrroloquinoline quinone-dependent carbohydrate dehydrogenase: Activity ...
Phosphorylation of PDH by one of the pyruvate dehydrogenase kinases 1-4 (PDK1-4) decreases the flux of carbohydrates into the ... Inhibition of PDKs increases oxidative metabolism of carbohydrates, so targeting PDKs has emerged as an important therapeutic ... The pyruvate dehydrogenase complex (PDH) critically regulates carbohydrate metabolism. ... The pyruvate dehydrogenase complex (PDH) critically regulates carbohydrate metabolism. Phosphorylation of PDH by one of the ...
The primary structure of bovine liver UDP-glucose dehydrogenase (UDPGDH), a hexameric, NAD(+)-linked enzyme, has been ... Carbohydrate Dehydrogenases * UDP-N-acetylmannosamine dehydrogenase * GDPmannose dehydrogenase * Uridine Diphosphate Glucose ... UDP-glucose Dehydrogenase From Bovine Liver: Primary Structure and Relationship to Other Dehydrogenases Protein Sci. 1994 Jul;3 ... The primary structure of bovine liver UDP-glucose dehydrogenase (UDPGDH), a hexameric, NAD(+)-linked enzyme, has been ...
Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the ... Carbohydrate Dehydrogenases*Uridine Diphosphate Glucose Dehydrogenase: 10*Arabidopsis UGD1 protein. *C elegans SQV-4 protein ... Dehydrogenase, UDP Glucose; Dehydrogenase, UDPG; Glucose Dehydrogenase, UDP; UDP Glucose Dehydrogenase; UDPG Dehydrogenase; ... Uridine Diphosphate Glucose Dehydrogenase. Subscribe to New Research on Uridine Diphosphate Glucose Dehydrogenase ...
Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome containing flavin and b-type heme, and plays a key role in ... Carbohydrate Dehydrogenases / chemistry* * Carbohydrate Dehydrogenases / genetics * Carbohydrate Dehydrogenases / metabolism * ... Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome containing flavin and b-type heme, and plays a key role in ... Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete ...
Carbohydrate Dehydrogenases. *Fructuronate Reductase. *Galactose Dehydrogenases. *Glucose Dehydrogenases. *Glucosephosphate ... "Sugar Alcohol Dehydrogenases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Sugar Alcohol Dehydrogenases" by people in Harvard Catalyst ... Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden ...
The three-dimensional structure of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 has been obtained in ... A versatile dehydrogenase oxidizing alcohols and carbohydrates.. *Henriëtte J. Rozeboom, Shukun Yu, Rene Mikkelsen, I. N. ... Formaldehyde dehydrogenase preparations from Methylococcus capsulatus (Bath) comprise methanol dehydrogenase and methylene ... PQQ-dependent methanol dehydrogenases: rare-earth elements make a difference. *J. T. M. Keltjens, A. N. van den Pol, Joachim ...
Carbohydrate refeeding rapidly reverses the adaptive upregulation of human skeletal muscle pyruvate dehydrogenase kinase ... Following carbohydrate re-feeding, (88% carbohydrate; 5% fat; 7% protein), PDK activity had returned to baseline (0.111 ± 0.014 ... The time course for the reversal of the adaptive increase in pyruvate dehydrogenase kinase (PDK) activity following a 6d high ... This adaptive increase in PDK4 protein content was reversed with carbohydrate re-feeding. It was concluded that the adaptive up ...
0 (Fungal Proteins); 0 (Metals); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.99.18 (cellobiose-quinone oxidoreductase); EC ... and carbohydrate esterases (CE) in addition to cellobiose dehydrogenase (CDH) indicating the presence of functional classical ...
Carbohydrate Dehydrogenases / genetics * Corneal Ulcer / microbiology * Cross Infection / microbiology * Cystic Fibrosis / ...
Carbohydrate Dehydrogenases); EC 1.1.1.- (L-galactonate oxidoreductase); EC 1.1.1.45 (gulonate dehydrogenase); EC 1.1.1.57 ( ... EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.57 (Fructuronate Reductase); EC 3.2.1.- (Galactosidases); EC 3.2.1.23 (beta- ... 0 (Hexuronic Acids); 0 (Uronic Acids); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.57 (Fructuronate Reductase); EC 4.2.1 ... 0 (Bacterial Proteins); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.57 (Fructuronate Reductase); EC 1.1.1.58 (tagaturonate ...
Glycerol dehydrogenase. L-sorbose-1-phosphate reductase. Pentosuria. (. More. ). Broader. (. 1. ). Carbohydrate Dehydrogenases ... Sugar Alcohol Dehydrogenases. Known as: Sugar Alcohol Dehydrogenases [Chemical/Ingredient], Oxidoreductases, Sugar Alcohol, ...
Transcriptional regulation of pyruvate dehydrogenase kinase 4 in skeletal muscle during and after exercise - Volume 63 Issue 2 ... Mourtzakis, M, Saltin, B, Graham, T & Pilegaard, H (2002) Pyruvate dehydrogenase active form (PDHa) and carbohydrate (CHO) ... Thus, increased PDK4 expression when carbohydrate availability is low seems to contribute to the sparing of carbohydrates by ... Effect of training in the fasted state on metabolic responses during exercise with carbohydrate intake. Journal of Applied ...
Mouse monoclonal Pyruvate Dehydrogenase Immunocapture antibody [15D3G9C11] validated for IP, Flow Cyt, ICC/IF and tested in ... The pyruvate dehydrogenase complex (PDH) is at the center of aerobic carbohydrate metabolism. It is localized in the matrix ... These are pyruvate dehydrogenase (E1), dihydrolipoamide transacetylase (E2) and dihydrolipoamide dehydrogenase (E3). PDH ... 100 µg ab109866 can capture at least 5 µg Pyruvate Dehydrogenase complex from 1 mg solubilized Bovine heart mitochondria. ...
... glyceraldehyde-3-phosphate dehydrogenase; LDH, lactate dehydrogenase; ChoRE, carbohydrate response element; HIF, hypoxia- ... Yamada K., Tanaka T., Noguchi T. Characterization and purification of carbohydrate response element-binding protein of the rat ... Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter. ...
Glycerol-3-phosphate dehydrogenase serves as a major link between carbohydrate metabolism and lipid metabolism. It is also a ... Older terms for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase (alphaGPDH) and ... glycerol-3-phosphate dehydrogenase is not the same as glyceraldehyde 3-phosphate dehydrogenase (GAPDH), whose substrate is an ... "Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces ...
Carbohydrate Dehydrogenases * D-fructose 5-dehydrogenase * Glucose Grant support * R01 CA123273/CA/NCI NIH HHS/United States ... The fructose dehydrogenase-based enzymatic assay correlated highly with gas chromatography-mass spectroscopic analysis of serum ... Methods: Using fructose dehydrogenase-catalyzed conversion of d-fructose to 5-ketofructose, followed by quantitation of MTT [3 ...
A novel inhibitor of pyruvate dehydrogenase kinase stimulates myocardial carbohydrate oxidation in diet-induced obesity. ... Short-term weight loss and hepatic triglyceride reduction: evidence of a metabolic advantage with dietary carbohydrate ... FGF21 induces PGC-1alpha and regulates carbohydrate and fatty acid metabolism during the adaptive starvation response. ... Alterations in hepatic glucose and energy metabolism as a result of calorie and carbohydrate restriction. ...
6-Phosphogluconate Dehydrogenase Links Cytosolic Carbohydrate Metabolism to Protein Secretion via Modulation of Glutathione ... Inhibition of Dihydroorotate Dehydrogenase Overcomes Differentiation Blockade in Acute Myeloid Leukemia.. Sykes DB, Kfoury YS, ... Discovery of Antimalarial Azetidine-2-carbonitriles That Inhibit P. falciparum Dihydroorotate Dehydrogenase. ... Discovery of 8-Membered Ring Sulfonamides as Inhibitors of Oncogenic Mutant Isocitrate Dehydrogenase 1. ...
Genetics Home Reference: pyruvate dehydrogenase deficiency (National Library of Medicine) * Genetics Home Reference: Schindler ... Carbohydrate metabolism disorders are a group of metabolic disorders. Normally your enzymes break carbohydrates down into ... ClinicalTrials.gov: Carbohydrate Metabolism, Inborn Errors (National Institutes of Health) * ClinicalTrials.gov: ... Genetics Home Reference: lactate dehydrogenase deficiency (National Library of Medicine) * Genetics Home Reference: ...
Kohn LD; Jakoby WB (1966). "L- and mesotartaric acid dehydrogenase (crystalline)". Carbohydrate Metabolism. Methods in ... In enzymology, a meso-tartrate dehydrogenase (EC 1.3.1.7) is an enzyme that catalyzes the chemical reaction meso-tartrate + ...
Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into ... Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+ fructose + NADH + H+. A zinc ion is also ... Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. ... Sorbitol dehydrogenase belongs to the oxidoreductase family, which means that it helps catalyze oxidation reduction reactions. ...
A novel inhibitor of pyruvate dehydrogenase kinase stimulates myocardial carbohydrate oxidation in diet-induced obesity. J. ... The dysregulation of carbohydrate and lipid metabolism due to unbalanced diets (i.e., fast food) in western societies has led ... either actively through activation of pyruvate dehydrogenase [58,59,60] or passively by inhibiting fatty acid oxidation [61,62 ... Canagliflozin mediated dual inhibition of mitochondrial glutamate dehydrogenase and complex I: an off-target adverse effect. ...
6-Phosphogluconate Dehydrogenase Links Cytosolic Carbohydrate Metabolism to Protein Secretion via Modulation of Glutathione ...
  • Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric aciduria, is a rare autosomal recessive disorder of the degradation pathway of the inhibitory neurotransmitter γ-aminobutyric acid, or GABA. (wikipedia.org)
  • However, because of the deficiency, the final intermediate of the GABA degradation pathway, succinic semialdehyde, accumulates and cannot be oxidized to succinic acid and is therefore reduced to gamma-hydroxybutyric acid (GHB) by gamma-hydroxybutyric dehydrogenase. (wikipedia.org)