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.
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
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)
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
A 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.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
Cell-surface proteins that bind glutamate and trigger changes which influence the behavior of cells. Glutamate receptors include ionotropic receptors (AMPA, kainate, and N-methyl-D-aspartate receptors), which directly control ion channels, and metabotropic receptors which act through second messenger systems. Glutamate receptors are the most common mediators of fast excitatory synaptic transmission in the central nervous system. They have also been implicated in the mechanisms of memory and of many diseases.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
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.
An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.
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.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
The rate dynamics in chemical or physical systems.
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.
A genus of ascomycetous fungi, family Sordariaceae, order SORDARIALES, comprising bread molds. They are capable of converting tryptophan to nicotinic acid and are used extensively in genetic and enzyme research. (Dorland, 27th ed)
Cell surface proteins that bind glutamate and act through G-proteins to influence second messenger systems. Several types of metabotropic glutamate receptors have been cloned. They differ in pharmacology, distribution, and mechanisms of action.
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.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
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).
Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.
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.
A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.
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.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
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.
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.
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.
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 1.1.1.14
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.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The removal of an amino group (NH2) from a chemical compound.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
One of the FLAVORING AGENTS used to impart a meat-like flavor.
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)
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.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
A family of POTASSIUM and SODIUM-dependent acidic amino acid transporters that demonstrate a high affinity for GLUTAMIC ACID and ASPARTIC ACID. Several variants of this system are found in neuronal tissue.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Oxidoreductases that are specific for ALDEHYDES.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
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.
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).
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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)
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.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
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.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
The creation of an amine. It can be produced by the addition of an amino group to an organic compound or reduction of a nitro group.
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.
A family of plasma membrane neurotransmitter transporter proteins that couple the uptake of GLUTAMATE with the import of SODIUM ions and PROTONS and the export of POTASSIUM ions. In the CENTRAL NERVOUS SYSTEM they regulate neurotransmission through synaptic reuptake of the excitatory neurotransmitter glutamate. Outside the central nervous system they function as signal mediators and regulators of glutamate metabolism.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
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.
Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.
A genus of gram-positive, anaerobic, coccoid bacteria that is part of the normal flora of humans. Its organisms are opportunistic pathogens causing bacteremias and soft tissue infections.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
A type I G protein-coupled receptor mostly expressed post-synaptic pyramidal cells of the cortex and CENTRAL NERVOUS SYSTEM.
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
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.
An acidifying agent that has expectorant and diuretic effects. Also used in etching and batteries and as a flux in electroplating.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
An organic mercurial used as a sulfhydryl reagent.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
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.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A group of inherited and sporadic disorders which share progressive ataxia in combination with atrophy of the CEREBELLUM; PONS; and inferior olivary nuclei. Additional clinical features may include MUSCLE RIGIDITY; NYSTAGMUS, PATHOLOGIC; RETINAL DEGENERATION; MUSCLE SPASTICITY; DEMENTIA; URINARY INCONTINENCE; and OPHTHALMOPLEGIA. The familial form has an earlier onset (second decade) and may feature spinal cord atrophy. The sporadic form tends to present in the fifth or sixth decade, and is considered a clinical subtype of MULTIPLE SYSTEM ATROPHY. (From Adams et al., Principles of Neurology, 6th ed, p1085)
A class of amino acids characterized by a closed ring structure.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Sulfuric acid diammonium salt. It is used in CHEMICAL FRACTIONATION of proteins.
A family of THERMOPROTEALES consisting of variable length rigid rods without septa. They grow either chemolithoautotrophically or by sulfur respiration. The four genera are: PYROBACULUM; THERMOPROTEUS; Caldivirga; and Thermocladium. (From Bergey's Manual of Systematic Bacteriology, 2d ed)
A compound that inhibits aminobutyrate aminotransferase activity in vivo, thereby raising the level of gamma-aminobutyric acid in tissues.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
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.
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).
A family of vesicular neurotransmitter transporter proteins that were originally characterized as sodium dependent inorganic phosphate cotransporters. Vesicular glutamate transport proteins sequester the excitatory neurotransmitter GLUTAMATE from the CYTOPLASM into SECRETORY VESICLES in exchange for lumenal PROTONS.
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.
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
Oxidoreductases that are specific for KETONES.
An essential branched-chain amino acid important for hemoglobin formation.
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.
Drugs that bind to but do not activate excitatory amino acid receptors, thereby blocking the actions of agonists.
The sum of the weight of all the atoms in a molecule.
Nonmotile unicellular green algae potentially valuable as a source of high-grade protein and B-complex vitamins.
Measurement of this acid in the urine after oral administration of histidine provides the basis for the diagnostic test of folic acid deficiency and of megaloblastic anemia of pregnancy.
A glutamate plasma membrane transporter protein found in ASTROCYTES and in the LIVER.
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.
A vesicular glutamate transporter protein that is predominately expressed in the DIENCEPHALON and lower brainstem regions of the CENTRAL NERVOUS SYSTEM.
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
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.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
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.
A vesicular glutamate transporter protein that is predominately expressed in TELENCEPHALON of the BRAIN.
A class of ionotropic glutamate receptors characterized by their affinity for the agonist AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid).
Drugs that bind to and activate excitatory amino acid receptors.
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.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
Proteins found in any species of bacterium.
An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine and is called histidinemia (AMINO ACID METABOLISM, INBORN ERRORS).
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.
A class of ionotropic glutamate receptors characterized by affinity for N-methyl-D-aspartate. NMDA receptors have an allosteric binding site for glycine which must be occupied for the channel to open efficiently and a site within the channel itself to which magnesium ions bind in a voltage-dependent manner. The positive voltage dependence of channel conductance and the high permeability of the conducting channel to calcium ions (as well as to monovalent cations) are important in excitotoxicity and neuronal plasticity.
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.
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.
The functional hereditary units of BACTERIA.
A site on an enzyme which upon binding of a modulator, causes the enzyme to undergo a conformational change that may alter its catalytic or binding properties.
A glial type glutamate plasma membrane transporter protein found predominately in ASTROCYTES. It is also expressed in HEART and SKELETAL MUSCLE and in the PLACENTA.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
A pyridoxal-phosphate protein that catalyzes the alpha-decarboxylation of L-glutamic acid to form gamma-aminobutyric acid and carbon dioxide. The enzyme is found in bacteria and in invertebrate and vertebrate nervous systems. It is the rate-limiting enzyme in determining GAMMA-AMINOBUTYRIC ACID levels in normal nervous tissues. The brain enzyme also acts on L-cysteate, L-cysteine sulfinate, and L-aspartate. EC 4.1.1.15.
A class of enzymes that catalyze oxidation-reduction reactions of amino acids.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
A common inhabitant of the colon flora in human infants and sometimes in adults. It produces a toxin that causes pseudomembranous enterocolitis (ENTEROCOLITIS, PSEUDOMEMBRANOUS) in patients receiving antibiotic therapy.
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).
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
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.
A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A species of parasitic EUKARYOTES that attaches itself to the intestinal mucosa and feeds on mucous secretions. The organism is roughly pear-shaped and motility is somewhat erratic, with a slow oscillation about the long axis.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
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.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
Proteins prepared by recombinant DNA technology.
A heterogenous group of degenerative syndromes marked by progressive cerebellar dysfunction either in isolation or combined with other neurologic manifestations. Sporadic and inherited subtypes occur. Inheritance patterns include autosomal dominant, autosomal recessive, and X-linked.
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
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.
Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
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).
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.
(2S-(2 alpha,3 beta,4 beta))-2-Carboxy-4-(1-methylethenyl)-3-pyrrolidineacetic acid. Ascaricide obtained from the red alga Digenea simplex. It is a potent excitatory amino acid agonist at some types of excitatory amino acid receptors and has been used to discriminate among receptor types. Like many excitatory amino acid agonists it can cause neurotoxicity and has been used experimentally for that purpose.
A class of ligand-gated ion channel receptors that have specificity for GLUTAMATE. They are distinct from METABOTROPIC GLUTAMATE RECEPTORS which act through a G-protein-coupled mechanism.
A neuronal and epithelial type glutamate plasma membrane transporter protein.
A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides. (1/966)

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.  (+info)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptides from digestion with a staphylococcal proteinase. (2/966)

The extracellular proteinase of Staphylococcus aureus strain V8 was used to digest the NADP-specific glutamate dehydrogenase of Neurospora crassa. Of 35 non-overlapping peptides expected from the glutamate content of the polypeptide chain, 29 were isolated and substantially sequenced. The sequences obtained were valuable in providing overlaps for the alignment of about two-thirds of the sequences found in tryptic peptides [Wootton, J. C., Taylor, J, G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 739-748]. The blocked N-terminal peptide of the protein was isolated. This peptide was sequenced by mass spectrometry, and found to have N-terminal N-acetylserine by Howard R. Morris and Anne Dell, whose results are presented as an Appendix to the main paper. The staphylococcal proteinase showed very high specificity for glutamyl bonds in the NH4HCO3 buffer used. Partial splits of two aspartyl bonds, both Asp-Ile, were probably attributable to the proteinase. No cleavage of glutaminyl or S-carboxymethylcysteinyl bonds was found. Additional experimental detail has been deposited as Supplementary Publication SUP 50053 (5 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K, from whom copies may be obtained under the terms given in Biochem. J. (1975) 1458 5.  (+info)

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence. (3/966)

Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J. 149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem. 250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5.  (+info)

Activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenases, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissues from vertebrates and invertebrates. (4/966)

1. The activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenases were measured in nervous tissue from different animals in an attempt to provide more information about the citric acid cycle in this tissue. In higher animals the activities of citrate synthase are greater than the sum of activities of the isocitrate dehydrogenases, whereas they are similar in nervous tissues from the lower animals. This suggests that in higher animals the isocitrate dehydrogenase reaction is far-removed from equilibrium. If it is assumed that isocitrate dehydrogenase activities provide an indication of the maximum flux through the citric acid cycle, the maximum glycolytic capacity in nervous tissue is considerably greater than that of the cycle. This suggest that glycolysis can provide energy in excess of the aerobic capacity of the tissue. 2. The activities of glutamate dehydrogenase are high in most nervous tissues and the activities of aspartate aminotransferase are high in all nervous tissue investigated. However, the activities of alanine aminotransferase are low in all tissues except the ganglia of the waterbug and cockroach. In these insect tissues, anaerobic glycolysis may result in the formation of alanine rather than lactate.  (+info)

The effect of bile salts and calcium on isolated rat liver mitochondria. (5/966)

Intact mitochondria were incubated with and without calcium in solutions of chenodeoxycholate, ursodeoxycholate, or their conjugates. Glutamate dehydrogenase, protein and phospholipid release were measured. Alterations in membrane and organelle structure were investigated by electron paramagnetic resonance spectroscopy. Chenodeoxycholate enhanced enzyme liberation, solubilized protein and phospholipid, and increased protein spin label mobility and the polarity of the hydrophobic membrane interior, whereas ursodeoxycholate and its conjugates did not damage mitochondria. Preincubation with ursodeoxycholate or its conjugate tauroursodeoxycholate for 20 min partially prevented damage by chenodeoxycholate. Extended preincubation even with 1 mM ursodeoxycholate could no longer prevent structural damage. Calcium (from 0.01 mM upward) augmented the damaging effect of chenodeoxycholate (0.15-0.5 mM). The combined action of 0.01 mM calcium and 0.15 mM chenodeoxycholate was reversed by ursodeoxycholate only, not by its conjugates tauroursodeoxycholate and glycoursodeoxycholate. In conclusion, ursodeoxycholate partially prevents chenodeoxycholate-induced glutamate dehydrogenase release from liver cell mitochondria by membrane stabilization. This holds for shorter times and at concentrations below 0.5 mM only, indicating that the different constitution of protein-rich mitochondrial membranes does not allow optimal stabilization such as has been seen in phospholipid- and cholesterol-rich hepatocyte cell membranes, investigated previously.  (+info)

Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. (6/966)

L-Glutamate dehydrogenase (GLDH) independent of NAD(P) and oxygen was first obtained from the psychrotrophic bacterium Aeromonas sp. L101, originally isolated from the organs of salmon (Oncorhynchus keta). GLDH was purified by a series of chromatography steps on DEAE-Sepharose, Superdex 200pg, Q-Sepharose, CM-Sepharose, and Phenyl-Sepharose. The purified protein was determined to have a molecular mass of 110 kDa and a pI of 5.7. Maximum activity was obtained at 55 degrees C and pH 8.5. The activity of GLDH at 4 and 20 degrees C was 38 and 50%, respectively, of that at 50 degrees C. GLDH was coupled to cytochrome c and several redox dyes including 1-methoxy-5-methylphenazinium methylsulfate (1-Methoxy PMS), 2, 6-dichlorophenylindophenol (DCIP), 9-dimethylaminobenzo[alpha]phenoxazin-7-ium chloride (meldola's blue), 3,3'-[3,3'-dimethoxy-(1,1'-biphenyl)-4, 4'-diyl]-bis[2-(4-nitrophenyl)-5-phenyl-2H tetrazolium chloride] (nitroblue tetrazolium; NBT), and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2H tetrazolium (INT). The presence of NAD(P) and oxygen gave no oxidation activity to GLDH. Spectroscopic profile and ICP data indicated a b-type cytochrome containing iron.  (+info)

Reactive cysteine residue of bovine brain glutamate dehydrogenase isoproteins. (7/966)

Protein chemical studies of glutamate dehydrogenase isoproteins (GDH I and GDH II) from bovine brain reveal that one cystein residue is accessible for reaction with thiol-modifying reagent. Reaction of the two types of GDH isoproteins with p-chloromercuribenzoic acid resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo first-order kinetics with the second-order rate constant of 83 M(-1) s(-1) and 75 M(-1) s(-1) for GDH I and GDH II, respectively. The inactivation was partially prevented by preincubation of the glutamate dehydrogenase isoproteins with NADH. A combination of 10 mM 2-oxoglutarate with 2 mM NADH gave complete protection against the inactivation. There were no significant differences between the two glutamate dehydrogenase isoproteins in their sensitivities to inactivation by p-chloromercuribenzoic indicating that the microenvironmental structures of the GDH isoproteins are very similar to each other. Allosteric effectors such as ADP and GTP had no effects on the inactivation of glutamate dehydrogenase isoproteins by thiol-modifying reagents. By a combination of peptide mapping analysis and labeling with [14C] p-chloromercuribenzoic acid, a reactive cystein residue was identified as Cys323 in the overall sequence. The cysteine residue was clearly identical to sequences of other GDH species known.  (+info)

Cyclic AMP can decrease expression of genes subject to catabolite repression in Saccharomyces cerevisiae. (8/966)

External cyclic AMP (cAMP) hindered the derepression of gluconeogenic enzymes in a pde2 mutant of Saccharomyces cerevisiae, but it did not prevent invertase derepression. cAMP reduced nearly 20-fold the transcription driven by upstream activation sequence (UAS1FBP1) from FBP1, encoding fructose-1,6-bisphosphatase; it decreased 2-fold the activation of transcription by UAS2FBP1. Nuclear extracts from cells derepressed in the presence of cAMP were impaired in the formation of specific UASFBP1-protein complexes in band shift experiments. cAMP does not appear to act through the repressing protein Mig1. Control of FBP1 transcription through cAMP is redundant with other regulatory mechanisms.  (+info)

TY - JOUR. T1 - Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. AU - Smith, Thomas. AU - Peterson, Peter E.. AU - Schmidt, Timothy. AU - Fang, Jie. AU - Stanley, Charles A.. PY - 2001/3/23. Y1 - 2001/3/23. N2 - Glutamate dehydrogenase is found in all organisms and catalyses the oxidative deamination of L-glutamate to 2-oxoglutarate. However, only animal GDH utilizes both NAD(H) or NADP(H) with comparable efficacy and exhibits a complex pattern of allosteric inhibition by a wide variety of small molecules. The major allosteric inhibitors are GTP and NADH and the two main allosteric activators are ADP and NAD+. The structures presented here have refined and modified the previous structural model of allosteric regulation inferred from the original boGDH·NADH·GLU·GTP complex. The boGDH·NAD+·α-KG complex structure clearly demonstrates that the second coenzyme-binding site lies directly under the pivot helix of the NAD+ binding domain. In ...
TY - JOUR. T1 - Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. AU - Fang, Jie. AU - Hsu, Betty Y L. AU - MacMullen, Courtney M.. AU - Poncz, Mortimer. AU - Smith, Thomas. AU - Stanley, Charles A.. PY - 2002/4/1. Y1 - 2002/4/1. N2 - Glutamate dehydrogenase (GDH) catalyses the reversible oxidative deamination of L-glutamate to 2-oxoglutarate in the mitochondrial matrix. In mammals, this enzyme is highly regulated by allosteric effectors. The major allosteric activator and inhibitor are ADP and GTP, respectively; allosteric activation by leucine may play an important role in amino acid-stimulated insulin secretion. The physiological significance of this regulation has been highlighted by the identification of children with an unusual hyperinsulinism/hyperammonaemia syndrome associated with dominant mutations in GDH that cause a loss in GTP inhibition. In order to determine the effects of these mutations on the function of the ...
TY - JOUR. T1 - Inactivation of human glutamate dehydrogenase by aluminum. AU - Yang, S. J.. AU - Huh, J. W.. AU - Lee, J. E.. AU - Choi, S. Y.. AU - Kim, T. U.. AU - Cho, S. W.. PY - 2003/11. Y1 - 2003/11. N2 - Aluminum inactivated glutamate dehydrogenase (GDH) by a pseudo-first-order reaction at micromolar concentrations. A double-reciprocal plot gave a straight line with a kinact, of 2.7 min-1 and indicated the presence of a binding step prior to inactivation. The inactivation was strictly pH dependent and a marked increase in sensitivity to aluminum was observed as the pH decreased. At a pH higher than 8.5, no inactivation was observed. The completely inactivated GDH contained 2 mol of aluminum per mole of enzyme subunit monomer. When preincubated with enzyme, several chelators such as citrate, NaF, N-(2-hydroxyethyl) ethylenediaminetriacetic acid or ethylenediaminetriacetic acid efficiently protected the enzyme against the aluminum inactivation. In a related experiment, only citrate and NaF ...
Variations in ambient temperature are a common phenomenon in nature that influences the microbial growth and metabolism. Temperature drops modifies the molecular topology, the enzyme kinetics, and increases the molecular order of membrane lipids [1, 2], affecting key cellular processes as transcription, translation and membrane-associated activities [3]. Cold is also relevant for the industrial exploitation of microorganisms. Processes involving yeasts, like brewing and some wine fermentations, take place at temperatures around 10-12°C, which is far below the optimal temperature of this organism (~28°C). Therefore, understanding the mechanisms of cold survival and adaptation is of great interest for both basic and applied aspects.. The essential coenzymes nicotinamide adenine dinucleotides, NAD and NADP, participate in key redox reactions and contribute to maintaining cell fitness and genome stability [4]. Factors regulating their metabolism and homeostasis become thus crucial in providing ...
Protein target information for NAD-specific glutamate dehydrogenase (Mycobacterium tuberculosis H37Rv). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
ab Glutamate Dehydrogenase Detection Kit Instructions for Use For the rapid, sensitive and accurate measurement of Glutamate Dehydrogenase activity in various samples This product is for research
Glutamate dehydrogenase (GDH; EC 1.4.1.2-1.4.1.4) catalyses in vitro the reversible amination of 2-oxoglutarate to glutamate. In vascular plants the in vivo direction(s) of the GDH reaction and hence the physiological role(s) of this enzyme remain obscure. A phylogenetic analysis identified two clea …
Glutamate dehydrogenase (GLDH, GDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant K m {\displaystyle K_{m}} of about 1 mM), and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed (that is, α-ketoglutarate and ammonia to glutamate and NAD(P)+). However, in brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination (i.e. α-ketoglutarate to glutamate). In bacteria, the ammonia is assimilated to amino acids via glutamate and ...
Creative Proteomics offer Glutamate Dehydrogenase Activity Colorimetric Assay Kit. We are specialized in manufacturing Assay Kits.
Regulation and differential expression of gdhA encoding NADP-specific glutamate dehydrogenase in Neisseria meningitidis clinical isolates. In this article, a direct association was found between the virulence of meningococcal on infant rats with the degree of glutamate dehydrogenase expression. Glutamate dehydrogenase converts glutamate to alpha-ketoglutarate, an intermediate in the TCA cycle. The degree of expression is dictated by the number of active copies of the gdhA gene. On a wildtype strain, there are two copies, gdhA P1 and gdhA P2. P2s activity is regulated by a positive regulatory ligand (activator) gdhR as demonstrated through complementation experiments where gdhR knockouts failed to grow on glucose media. In the presence of glucose, NADP linked GDH levels increase and enhances growth by facilitating nitrogen metabolism. In the mice infected with different mutants, it was found that the most virulent strains were those with both copies active followed by one copy followed by no ...
[114 Pages Report] Check for Discount on China Glutamate Dehydrogenase Market Research Report 2017 report by QYResearch Group. The global Glutamate Dehydrogenase market is valued at XX million...
Glutamate has been shown to lead to neurotoxicity and subsequent neurodegeneration through changes in synaptic function, loss of glutamatergic neurons, synapses, and dendrites. All of these characteristics are also observed during aging or in age-associated neurodegenerative diseases. To probe the effects of excess glutamate and determine if these effects might contribute to the morphological and functional changes associated with aging, our laboratory generated a transgenic mouse model that over-expresses the mitochondrial glutamate dehydrogenase 1 (GLUD1) gene. This transgene was only expressed in neurons through the use of the neuron-specific enolase promoter. The Glud1 Tg mouse model generated in our laboratory demonstrated significantly increased GLUD1 levels, GLUD activity, extracellular glutamate levels, and increased glutamate release after stimulation as compared to wild type (wt). There were also many significant morphological changes observed in the Tg mice including cell layer ...
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Aravind, L., R. L. Tatusov, Y. I. Wolf, D. R. Walker, and E. V. Koonin. 1998. Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles. Trends in Genetics 14:442-444.. Baldauf, S. L., J. D. Palmer, and W. F. Doolittle. 1996. The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny. Proceedings of the National Academy of Sciences of the United States of America 93:7749-7754.. Becerra, A., L. Delaye, S. Islas, and A. Lazcano. 2007. The very early stages of biological evolution and the nature of the last common ancestor of the three major cell domains. Annual Review of Ecology, Evolution, and Systematics 38:361-379.. Benachenhou, L. N., P. Forterre and B. Labedan. 1993. Evolution of glutamate dehydrogenase genes: Evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. Journal Of Molecular Evolution 36:335-346.. Brinkmann, H. and H. Phillippe. 1999. Archaea ...
The purification of glutamate dehydrogenase from sheep rumen mucosa on DEAE-cellulose afforded two enzyme fractions with glutamate dehydrogenase activity. The enzyme fraction II (tissue glutamate dehydrogenase) was freed of contaminating proteins in the subsequent purification step on Sephadex G-200. The approximate relative molecular weight (260 000) of tissue glutamate dehydrogenase (fraction II) was determined by gel filtration on Sephadex G-200 and the approximate relative molecular weight of its polypeptide chain (48 000) was established by polyacrylamide gel electrophoresis in SDS. The pH-optimum of fraction II was 7.9. The effect of substrate concentration on the rate of the enzymatic reaction was examined and the following apparent Michaelis constants were found for the individual substrates: NADH 6.25 . 10-5 mol/l, 2-oxoglutarate 4.5 . 10-3 mol/l, and NH4+ 77 . 10-3 mol/l.. ...
Two pathways serve for assimilation of ammonia inParacoccus denitrificans. Glutamate dehydrogenase (NADP+) catalyzes the assimilation at a high NH4+ concentration. If nitrate serves as the nitrogen source, glutamate is synthesized by glutamate-ammonia ligase and glutamate synthase (NADPH). At a very low NH4+ concentration, all three enzymes are synthesized simultaneously. No direct relationship exists between glutamate dehydrogenase (NADP+) and glutamate-ammonia ligase inP. denitrificans, while the glutamate synthase (NADPH) activity changes in parallel with that of the latter enzyme. Ammonia does not influence the induction or repression of glutamate dehydrogenase (NADP+). The inner concentration of metabolites indicates a possible repression of glutamate dehydrogenase (NADP+) by the high concentration of glutamine or its metabolic products as in the case when NH4+ is formed by assimilative nitrate reduction. No direct effect of the intermediates of nitrate assimilation on the synthesis of glutamate
GLUD1 (Glutamate dehydrogenase 1) is a mitochondrial matrix enzyme, with a key role in the nitrogen and glutamate (Glu) metabolism and the energy homeostasis. GLUD1 is expressed at high levels in liver, brain, pancreas and kidney, but not in…
A simple and rapid method is described for the determination of ammonia in plasma without deproteinization, using the enzyme glutamate dehydrogenase and NADPH as coenzyme. ADP is used to stabilize glutamate dehydrogenase. The measuring principle is a kinetic one, determining the reaction rate on the Enzyrator. The whole determination takes only ... read more 7 min, including the preincubation time. The plasma sample is only 100 μl, which makes it possible to determine the ammonia values in capillary blood. Comparing the values of venous and capillary blood, we found that capillary values are 2-3 times higher than those in venous blood. The normal range for venous plasma NHs was 6.5-35.0 μmol/l. The mean value of non-fasting persons was 22.0 μmol/l. show less ...
1. Abounit S, Bousset L, Loria F, Zhu S, de Chaumont F, Pieri L. Tunneling nanotubes spread fibrillary α-synuclein by intercellular trafficking lysosomes. EMBO J. 2016. 35: 2120-38. 2. Alam Q, Alam MZ, Mushtaq G, Damenhouri GA, Rasool M, Kamai MA, Haque A. Inflammatory process in Alzheimers and Parkinsons diseases: Central role of cytokines. Curr Pharm Des. 2016. 22: 541-8. 3. Allan SM, Rothwell NJ. Cytokines and acute neurodegeneration. Nat Rev Neurosci. 2001. 2: 734-44. 4. Alvarez-Erviti L, Couch Y, Richardson J, Cooper JM, Wood MJ. Alpha-synuclein released by neurons activate the inflammatory response in microglial cell line. Neurosci Res. 2011. 69: 337-42. 5. Ambrosi G, Cerri S, Blandini F. A further update of excitotoxicity in the pathogenesis of Parkinsons disease. J Neural Transm. 2014. 121: 849-59. 6. Aquirre J, Rodriguez R, Hansberg W. Oxidation of Neurospora crassa NADP-specific glutamate dehydrogenase by activated oxygen species. J Bacteriol. 1989. 17: 6243-50. 7. Assous M, ...
Glutamate released from brain slices under study was detected with a fluorescence assay in a Hitachi (Tokyo, Japan) F-2000 fluorometer. Each slice was gently fixed to a mesh holder and placed in a fluorometer cuvette containing 1.6 ml of 37 degrees Celsius ABECF, 1 mM nicotinamide adenine dinucleotide phosphate, and 5 IU/ml glutamate dehydrogenase (Figure 1). The formation of the reduced form of nicotinamide adenine dinucleotide phosphate from nicotinamide adenine dinucleotide phosphate by glutamate dehydrogenase was measured fluorometrically (excitation light 340 nm, emission intensity 460 nm) in the solution above the slice. A stir bar ensured rapid detection of released neurotransmitter. The temperature of the cuvette fluid was maintained at 37 degrees Celsius throughout the study. The assay was calibrated by injecting known quantities of L-glutamate into the cuvette. The assay permitted detection of about 1 nmol (approximately 0.01 nmol/sec) of glutamate. Studies were performed to ensure ...
EC 1.4.1.4; systematic name: l‐glutamate:NADP+ oxidoreductase (deaminating). An enzyme that catalyses the oxidation by NADP+ of l‐glutamate to form 2‐oxoglutarate, NH3, and NADPH. Two forms exist. One is a homotetramer. ... ...
A negative result for GDH has been associated with a high value for prediction of a true negative result; however, a positive result is not necessarily associated with a toxin producing strain. A second assay on positive samples for detection of toxin production is required in these algorithms ...
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As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
What does SLC25A22 do? Mitochondria are the cellular energy plant of the cell, and molecular transport is tightly regulated at both the outer and inner mitochondrial membrane. SCL25A22, also known as GC1, is the main glutamate transporter across the inner mitochondrial membrane. Why do the mitochondria need glutamate? Glutamate plays an important role in fuelling both the Krebs cycle and urea cycle, and impairment of glutamate import may have a devastating effect on the energy homeostasis of the cell. As demonstrated by the catastrophic epilepsy arising from SLC25A22 deficiency, the effect is particularly damaging in the developing nervous system where SLC25A22 is highly expressed. However, it remains to be shown whether the effect of recessive SLC25A22 mutations actually result in mitochondrial glutamate starvation.. The SLC25A22 phenotype. Recessive mutations in SCL25A22 were previously described in a family with neonatal epileptic encephalopathy with suppression bursts (NEESB), cerebellar ...
Hi, I have a mouse anti-bovine glutamate dehydrogenase mAb and Im curious whether anyone would know whether it will crossreact with Human GDH. I think the two proteins are fairly similiar but how similiar are humans with cows??? Please send a reply to my E-mail dsho at med.unc.edu Thanx for any thoughts. Moo Moo, Dave Shock ...
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Hayakawa Toshihiko , Sakai Takahiro , Ishiyama Keiki , HIROSE Naoya , NAKAJIMA Hiroyuki , TAKEZAWA Masae , NAITO Kazutaka , HINO-NAKAYAMA Mutsumi , AKAGAWA Takumi , GOTO Satoshi , YAMAYA Tomoyuki Plant biotechnology 20(1), 43-55, 2003-03-03 J-STAGE 参考文献37件 被引用文献2件 ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Background as confirmed by Southern blot traditional western blot and enzymatic activity dimension. at these proteins concentrations. The NADH-dependent reduced amount of α-ketoglutarate also appeared affected in D10Δgdh-1 and D10Δgdh-2 (10.6 ± 4.1 nmol/min/mg proteins and 10.7 ± 4.1 TSPAN32 nmol/min/mg proteins respectively) in comparison to D10 parasites (20.1 ± 0.5 nmol/min/mg protein) recommending the fact that NADH-dependent GDH activity continues to be within the mutant parasite lines albeit at lower levels. Development of P. falciparum D10Δgdha and susceptibility to raised oxidative stress The result of low (1%) and high air tension (20%) in the development price of D10Δgdh-1 and D10Δgdh-2 was evaluated and in comparison to that of D10 parasites. The lack of GDHa got no influence on the development of D10Δgdh-1 and D10Δgdh-2 under low air or elevated air tension (Body ?(Figure3).3). That is surprising since it was previously recommended that GDHa is certainly very important to ...
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A 76-year-old woman was admitted to our hospital via the emergency room in June 2008 for persistent fever (temperature on admission, 102 °F; maximum temperature, 102.8 °F). She was ill-appearing without concerns of clinical instability. Her physical examination was normal except for abdominal tenderness with no rebound or guarding, and infection work-up was unrevealing. Her erythrocyte sedimentation rate was 110 mm/h and her c-reactive protein level was 302 mg/L. A chest radiograph was negative, but computed tomography of the abdomen and pelvis showed a 3.8 cm collection of complex fluid within the uterine endometrium (Image A). She remained febrile despite treatment with vancomycin, imipenem, and fluconazole. Examination under anesthesia with dilation and curettage yielded negative pathology and cultures including bacterial, fungal, and acid-fast bacilli. Given the patients lack of improvement with medical therapy and a presumed uterine source of infection, the decision was made in ...
O:13:\PanistOpenUrl\:36:{s:10:\\u0000*\u0000openUrl\;N;s:6:\\u0000*\u0000idc\;N;s:6:\\u0000*\u0000fmt\;s:7:\journal\;s:6:\\u0000*\u0000doi\;s:0:\\;s:6:\\u0000*\u0000pii\;s:0:\\;s:7:\\u0000*\u0000pmid\;s:0:\\;s:9:\\u0000*\u0000atitle\;s:144:\EFFECT OF 2,4-DICHLOROPHENOXYACETIC ACID AND AMMONIUM ON GLUTAMATE DEHYDROGENASE ACTIVITY AND ISOENZYME PATTERN IN CALLUS OF PAULS SCARLET ROSE\;s:9:\\u0000*\u0000jtitle\;s:0:\\;s:9:\\u0000*\u0000stitle\;s:0:\\;s:7:\\u0000*\u0000date\;s:4:\1981\;s:9:\\u0000*\u0000volume\;s:0:\\;s:8:\\u0000*\u0000issue\;s:0:\\;s:8:\\u0000*\u0000spage\;s:0:\\;s:8:\\u0000*\u0000epage\;s:0:\\;s:8:\\u0000*\u0000pages\;s:0:\\;s:7:\\u0000*\u0000issn\;s:0:\\;s:8:\\u0000*\u0000eissn\;s:0:\\;s:9:\\u0000*\u0000aulast\;s:7:\GABARDO\;s:10:\\u0000*\u0000aufirst\;s:3:\MLL\;s:9:\\u0000*\u0000auinit\;N;s:10:\\u0000*\u0000auinitm\;N;s:5:\\u0000*\u0000au\;a:4:{i:0;s:11:\GABARDO MLL\;i:1;s:9:\ARAUJO ...
Nitrogen assimilation during growth of Candida boidinii on methylated amines as sole nitrogen source involves NADP-dependent glutamate dehydrogenase. Changes in enzyme activities during the adaptation of the yeast from growth on ammonium to growth on trimethylamine were examined. No ammonia, dimethylamine or monomethylamine could be detected in the medium during growth on trimethylamine. When two methylated amines were supplied together, they were used simultaneously, although monomethylamine was metabolized more quickly than the others. When cells were grown on a low concentration of ammonium plus higher concentrations of di- or trimethylamine, the ammonium was used first. NADP-dependent glutamate dehydrogenase was the first enzyme to be derepressed, followed by methylamine oxidase and formaldehyde dehydrogenase. Di- and trimethylamine mono-oxygenase activities only appeared when the ammonium concentration fell below 0.5 mM. At this point amine utilization could be detected and no diauxic lag was
Two glutamate dehydrogenases, NADH-linked (EC 1.2.1.2) and NADPH-linked (EC 1.2.1.4) were isolated from the epimastigote forms of Trypanosoma cruzi and purified. Both enzymes exist as hexamers. The molecular weights of the native NADH-and NADPH-linked glutamate dehydrogenases were estimated to be 360,000 and 265,000, respectively, and those of the subunits to be 58,000 and 43,000, respectively. The isoelectric point of the NADH-linked dehydrogenase is at pH 5.25 and that of the NADPH-linked enzyme at pH 5.1. The activities of both enzymes are regulated by product inhibition. In addition, purine nucleotides were shown to be potent inhibitors of the NADH-linked glutamate dehydrogenase. ...
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Low concentrations of hexachlorophene (HCP) inhibit a number of pyridine nucleotide-linked dehydrogenase enzymes. The I₅₀ HCP concentrations were 105 μM for pig heart isocitrate dehydrogenase (ICD), 65 μM for horse liver alcohol dehydrogenase, 39 μM for torula yeast glucose-6-phosphate dehydrogenase (G6PD), 6.0 μM for beef heart malate dehydrogenase, and 1.6 μM for bovine liver glutamate dehydrogenase (GDH) at the enzyme concentrations tested. HCP exhibited cooperative inhibition of these enzymes since the observed maximum interaction coefficient, n, between HCP binding sites ranged between 1.62 and 3.33 but it was not an allosteric effector as evidenced by Hill coefficients for the substrates of approximately 1.0 both in the absence and the presence of HCP. More detailed kinetic analysis showed that HCP in most cases exhibited mixed kinetics, giving average K[subscript i] values with G6PD of 16.6 μM for NADP⁺ and 18.2 μM for glucose -6- phosphate; with ICD of 171 µM for NADP⁺ ...
Mammals have three enzymes that can overcome the thermodynamic hurdles of ammonia assimilation: (i) carbamoyl phosphate synthetase I (CPS1), the adenosine triphosphate (ATP)-dependent, rate-limiting step of the urea cycle; (ii) glutamate dehydrogenase (GDH), a NADPH (reduced nicotinamide adenine dinucleotide phosphate)-dependent enzyme that catalyzes the reductive amination of α-ketoglutarate; and (iii) glutamine synthetase (GS), which catalyzes the ATP-dependent amination of glutamate to generate glutamine (12, 13) (fig. S1A). Analysis of transcriptomic data from The Cancer Genome Atlas for the ammonia-assimilating enzymes in healthy and cancerous tissues revealed that expression of GS and GDH mRNA is significantly increased across many cancer subtypes, whereas CPS1 mRNA is increased only in the colon (Fig. 1B). Among healthy tissues, GS and GDH are ubiquitously expressed and CPS1 is expressed only in the liver (fig. S1B). Breast cancers display increased expression of both GS and GDH. ...
NADP-linked glutamate dehydrogenase (NADP+-GluDH, EC 1.4.1.4) has been purified to homogeneity from epimastigotes of Trypanosoma cruzi by an improved procedure, and the amino acid sequences of 11 internal peptides obtained by digestion with trypsin, endopeptidase Lys-C, endopeptidase Arg-C or CNBr have been obtained. Using oligonucleotide primers synthesized according to the amino acid sequence of the N-terminus of the mature enzyme and to the nucleotide sequence of a clone corresponding to the C-terminus, obtained by immunological screening of an expression library, two complete open reading frames (TcGluDH1 and TcGluDH2) were isolated and sequenced. The sequences obtained are most similar to that of the NADP+-GluDH of Escherichia coli (70-72% identity), and less similar (50-56%) to those of lower eukaryotes. Using TcGluDH1 as a probe, evidence for the presence of several genes and developmental regulation of the expression of NADP+-GluDH in different parasite stages was obtained. TcGluDH1 ...
Two ammonium-inducible, chloroplast-localized NADP-specific glutamate dehydrogenase isoenzymes were purified to homogeneity from Chlorella sorokiniana. These isoenzymes were homopolymers of either α- or β-subunits with molecular weights of 55,500 or 53,000, respectively. The α-isoenzyme was preferentially induced at low ammonium concentrations (2 millimolar or lower), whereas only the β-isoenzyme accumulated after cells were fully induced (120 minutes) at high ammonium concentrations (29 millimolar). Purification of isoenzymes was achieved by (NH4)2SO4 fractionation, gel-filtration, anion-exchange fast protein liquid chromatography, and affinity chromatography. The α- and β-isoenzymes were separated by their differential binding to Type 4 nicotinamide adenine dinucleotide phosphate-Sepharose. Both isoenzymes bound to an antibody affinity column to which purified antibody (prepared against β-isoenzyme) was covalently attached. Peptide mapping of the subunits showed them to have a high ...
The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases. ...
1. Gonz lez, A., Rodr guez, L., Olivera, H. and Sober n M. (1985). NADP Glutamate dehydrogenase activity is impaired in aconitase-less mutants of Saccharomyces cerevisiae. Journal of General Microbiology. 131: 2565-2571. 2. Sober n, M., Gama, M.J., Richelle, J. and Martuscelli, J. (1986). Behaviour of temperate phage Mu in Salmonella typhi. Journal of General Microbiology. 132: 83-89. 3. Sober n, M., Gonz lez, A. (1987). Physiological role of glutaminase activity in Saccharomyces cerevisiae.Journal of General Microbiology. 133: 01-08. 4. Sober n, M., Gonz lez, A. (1987).Glutamine degradation through the omega-amidase pathway in Saccharomyces cerevisiae. Journal of General Microbiology. 133: 09-14. 5. Gonz lez, A., Rodr guez, L., Folch, J.L., Sober n, M., Olivera, H. (1987). Coordinated regulation of ammonium assimilation and carbon catabolism by glyoxylate in Saccharomyces cerevisiae. Journal of General Microbiology.133: 2497-2501. 6. Sober n, M., Williams, H.D., Poole, R.K., Escamilla, E. ...
Moreover, while most of the organs in the human body have the ability to store glucose by increasing their mass, the brain, prisoner of the cranial bones, cannot count on these variations in volume.. Unable to store its food, it depends on sugar supplied in real-time by the rest of the body. This distribution of energy is controlled by the liver.. Pierre Maechler, professor at the Faculty of Medicine at UNIGE, and his team therefore decided to verify if glutamate was indeed an energy source for the brain.. To do so, the researchers analyzed the role of the glutamate dehydrogenase enzyme in the brain. In mutant form, this enzyme, encoded by the Glud1 gene, is responsible for a congenital hyperinsulinism syndrome, a severe disease affecting at the same time the endocrine pancreas, the liver and the brain.. Individuals affected by this syndrome suffer from intellectual disability and have a high risk of epilepsy. ...
Summary Proliferating mammalian cells use glutamine as a source of nitrogen and as a key anaplerotic source to provide metabolites to the tricarboxylic acid cycle (TCA) for biosynthesis. Recently, mammalian target of rapamycin complex 1 (mTORC1) activation has been correlated with increased nutrient uptake and metabolism, but no molecular connection to glutaminolysis has been reported. Here, we show that mTORC1 promotes glutamine anaplerosis by activating glutamate dehydrogenase (GDH). This regulation requires transcriptional repression of SIRT4, the mitochondrial-localized sirtuin that inhibits GDH. Mechanistically, mTORC1 represses SIRT4 by promoting the proteasome-mediated destabilization of cAMP-responsive element binding 2 (CREB2). Thus, a relationship between mTORC1, SIRT4, and cancer is suggested by our findings. Indeed, SIRT4 expression is reduced in human cancer, and its overexpression reduces cell proliferation, transformation, and tumor development. Finally, our data indicate that ...
Recombinant protein of human glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa) (GAD2), transcript variant 2, 20 ug available for purchase from OriGene - Your Gene Company.
Lenti ORF particles, GRIK2 (Myc-DDK tagged) - Human glutamate receptor, ionotropic, kainate 2 (GRIK2), transcript variant 2 , 200ul, >10^7 TU/mL ...
DAM)-25 tests, (DAM)-50 tests, (GLDH) -2 X 150 ml, (GLDH) -2 X 75 ml, (GLDH)-75ml, B -2 X 150 Assays, B -3 X 75 Assays, B -75 Assays. ...
00:01, 24 October 2009 (diff , hist) . . (+138)‎ . . N Talk:Does learning from examples improved tutored problem solving? ‎ (New page: Authors listed are Renkl, Aleven, Salden, but clearly this is a Hausman study. The title may actually be from the Renkl et al. project.) ...
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Question: Does Cialis lower blood pressure? Answer: Cialis can lead to drop in blood pressure and at times to unsafe levels. It works by
Glutamate dehydrogenase. Other. *cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. * ...
Glutamate dehydrogenase. Other. *cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. * ...
This dehydrogenase is one of the family of glutamate dehydrogenases that are ubiquitous in life. Glutamate dehydrogenase 2 is ... Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene. ... "Entrez Gene: glutamate dehydrogenase 2". Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A ... Spanaki C, Zaganas I, Kleopa KA, Plaitakis A (2010). "Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular ...
Glutamate dehydrogenase pseudogene 5, also known as GLUDP5, is a human gene. "Human PubMed Reference:". National Center for ... Julliard JH, Smith EL (1979). "Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the ... "Entrez Gene: GLUDP5 glutamate dehydrogenase pseudogene 5". Meissner T, Beinbrech B, Mayatepek E (1999). "Congenital ... 1993). "Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to ...
Glutamate dehydrogenase provides an oxidizable carbon source used for the production of energy as well as a reduced electron ... Werner C, Stubbs MT, Krauth-Siegel RL, Klebe G (2005). "The crystal structure of Plasmodium falciparum glutamate dehydrogenase ... 1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum" (PDF). Parasitology. 92 (2): 313-324. doi:10.1017/ ... The first malaria antigen suitable as target for such a test was a soluble glycolytic enzyme Glutamate dehydrogenase. None of ...
regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase). to α-ketoglutaric acid. *Glutamate ...
regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase). to α-ketoglutaric acid. *Glutamate ...
Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
glycine dehydrogenase (decarboxylating) or just glycine dehydrogenase. L-protein (GCSL or DLD) EC 1.8.1.4 known by many names, ... G→glutamate→. α-ketoglutarate. HISTIDINE→. *Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase ... but most commonly dihydrolipoyl dehydrogenase H-protein (GCSH) is modified with lipoic acid and interacts with all other ...
Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
Robinson, Sharon A.; Stewart, George R.; Phillips, Richard (1992). "Regulation of glutamate dehydrogenase activity in relation ... "The Role of Glutamate Dehydrogenase in Plant Nitrogen Metabolism". Plant Physiology. 95 (2): 509-516. doi:10.1104/pp.95.2.509. ... An early career highlights was demonstrating a role for the enzyme glutamate dehydrogenase in nitrogen mobilisation. Some of ... "The role of glutamate dehydrogenase in plant nitrogen metabolism". Plant Physiology. 95 (2): 509-516. doi:10.1104/pp.95.2.509. ...
Ling IT, Cooksley S, Bates PA, Hempelmann E, Wilson RJ (1986). "Antibodies to the glutamate dehydrogenase of Plasmodium ... Consequences included natural selection for sickle-cell disease, thalassaemias, glucose-6-phosphate dehydrogenase deficiency, ... and glucose-6-phosphate dehydrogenase deficiency) were present in the Mediterranean world by the time of the Roman Empire, ...
HI/HA is caused by increased Glutamate dehydrogenase 1 (GDH) activity due to the presence of overactivating point mutations in ... Smith, Hong Q.; Smith, Thomas J. (2016). "Identification of a Novel Activator of Mammalian Glutamate Dehydrogenase". ...
Ling I.T.; Cooksley S.; Bates P.A.; Hempelmann E.; Wilson R.J.M. (1986). "Antibodies to the glutamate dehydrogenase of ... The first rapid diagnostic tests were using Plasmodium glutamate dehydrogenase as antigen. PGluDH was soon replaced by ... "Evaluation of a new Plasmodium lactate dehydrogenase assay (OptiMAL-IT) for the detection of malaria". Transact Royal Soc Trop ... Plasmodium lactate dehydrogenase (pLDH). Depending on which monoclonal antibodies are used, this type of assay can distinguish ...
1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum" (PDF). Parasitology. 92 (2): 313-324. doi:10.1017/ ...
These liver enzymes included lactate dehydrogenase and glutamate pyruvate transaminase. Although they were described as having ... These transformations are catalyzed by 5α- and 5β-reductase and 3α- and 3β-hydroxysteroid dehydrogenase both in the liver and ... The enzymes involved in these metabolic processes are 5α- and 5β-reductase as well as 3α- and 3β-hydroxysteroid dehydrogenase ( ...
Huang, CY; Frieden, C (1972). "The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the ... Fisher, Harvey F. (2006). "Glutamate Dehydrogenase-ligand Complexes and Their Relationship to the Mechanism of the Reaction". ... Ashiuchi, M.; Kuwana, E; Yamamoto, T; Komatsu, K; Soda, K; Misono, H (2002). "Glutamate Racemase is an Endogenous DNA Gyrase ... Snook, Christopher F.; Tipton, Peter A.; Beamer, Lesa J. (2003). "Crystal Structure of GDP-Mannose Dehydrogenase: A Key Enzyme ...
For instance, Bacillus subtilis encodes two paralogues of glutamate dehydrogenase: GudB is constitutively transcribed whereas ... "Bacilli glutamate dehydrogenases diverged via coevolution of transcription and enzyme regulation". EMBO Reports. 18 (7): 1139- ... Characterization of the proteins shows that, compared to RocG, GudB's enzymatic activity is highly dependent on glutamate and ...
Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate. A transamination reaction takes ... α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate Glutamate itself is formed by amination of α-ketoglutarate: α- ... In E. coli, proline allosterically inhibits Glutamate 5-kinase which catalyzes the reaction from L-glutamate to an unstable ... PheA uses a simple dehydrogenase to convert prephenate to phenylpyruvate, while TyrA uses a NAD-dependent dehydrogenase to make ...
"Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase". FEBS Letters ... He worked primarily on liver alcohol dehydrogenases, and is well known in enzymology for his idiosyncratic way of representing ...
gdhA codes for the glutamate dehydrogenase and links citrate cycle and nitrogen metabolism. A study combining a transcriptome ... Pirin has key roles in the central metabolism by regulating the activity of pyruvate dehydrogenase E1 and therefore select if ...
Fahien LA, Kmiotek EH, MacDonald MJ, Fibich B, Mandic M (Aug 1988). "Regulation of malate dehydrogenase activity by glutamate, ... "Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus ... which is then converted back to oxaloacetate and glutamate, respectively. Another function of GOT2 is that it is believed to ... "Assignment to chromosome 16 of a gene necessary for the expression of human mitochondrial glutamate oxaloacetate transaminase ( ...
This is confirmed by the presence of glutamine synthetase, glutamate synthase, and alanine dehydrogenase. Since M. scandinavica ... The TCA cycle is incomplete due to the inactivity of the α-ketoglutarate dehydrogenase enzyme. M. scandinavica also uses ... These precursor metabolites are incorporated via the glutamate cycle and reductive amination of pyruvate. ...
Kinnaird, J.; Keighren, M.; Kinsey, J.; Eaton, M.; Fincham, J. (1982). "Cloning of the am (glutamate dehydrogenase) gene of ... NADP-specific glutamate dehydrogenase) gene". Gene. 26 (2-3): 253-260. doi:10.1016/0378-1119(83)90195-6. PMID 6231215. ... using mutants of Neurospora crassa deficient in a specific enzyme called glutamate dehydrogenase. Fincham was appointed first ...
Glutamate can then be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate. The histidine amino acid ... The formimino group is transferred to tetrahydrofolate, and the remaining five carbons form glutamate. Overall, these reactions ... result in the formation of glutamate and ammonia. ...
Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. (1975). "Glutamate dehydrogenases". u: Boyer, P.D.. The Enzymes. 11 ( ... Frieden, C. (1963). "L-Glutamate dehydrogenase". u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York ... Pahlich, E. and Joy, K.W. (1971). "Glutamate dehydrogenase from pea roots: purification and properties of the enzyme". Can. J. ...
SIRT4 is a mitochondrial ADP-ribosyltransferase that inhibits mitochondrial glutamate dehydrogenase 1 activity, thereby ... "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells". Cell. 126 (5 ...
Glutamate can then be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate.[19] ... and the remaining five carbons form glutamate.[19] Overall, these reactions result in the formation of glutamate and ammonia.[ ... The histidine-bound heme group of succinate dehydrogenase, an electron carrier in the mitochondrial electron transfer chain. ...
Glutamate in the liver enters mitochondria and is broken down by glutamate dehydrogenase into α-ketoglutarate and ammonium, ... In the first step, α-ketoglutarate, ammonia and NADH are converted by glutamate dehydrogenase to glutamate, NAD+ and water. In ... Glutamate can then transfer its amino group to pyruvate, a product of muscle glycolysis, through the action of alanine ... In muscle and other tissues that degrade amino acids for fuel, amino groups are collected in the form of glutamate by ...
Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
Pyruvate is oxidized to acetyl-CoA and CO2 by the pyruvate dehydrogenase complex (PDC). The PDC contains multiple copies of ... Lactate formation is catalyzed by lactate dehydrogenase in a reversible reaction. Lactate can also be used as an indirect ... low Km transporter to bring it into the mitochondrial matrix for oxidation by the pyruvate dehydrogenase complex. ... Glutamate. group. & proline Arginine Creatine. & polyamines Ketogenic &. glucogenic. amino acids Amino acids ...
"aldehyde dehydrogenase - Homo sapiens". BRENDA. Technische Universität Braunschweig. January 2015. Retrieved 13 April 2015.. ... Phenethylamine also appears to induce acetylcholine release via a glutamate-mediated mechanism.[35] ... and then aldehyde dehydrogenase (ALDH), which convert it to phenylacetic acid.[5] This means that for significant ... product which is produced by monoamine oxidase and then further metabolized into β-phenylacetic acid by aldehyde dehydrogenase. ...
GABA is synthesized in a single step from its precursor glutamate by glutamic acid decarboxylase. GABA is metabolized by ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency. From Wikipedia, the free encyclopedia. (Redirected from Gamma-hydroxybutyric ...
... is enzymatically oxidized to yield taurine by hypotaurine dehydrogenase.[2] Hypotaurine (3) is an intermediate in ... Ionotropic glutamate receptor modulators. This drug article relating to the nervous system is a stub. You can help Wikipedia by ...
Succinic semialdehyde dehydrogenase deficiency[edit]. Succinic semialdehyde dehydrogenase deficiency is an autosomal-recessive ... Antibodies against the enzyme glutamic acid decarboxylase (GAD: enzyme changing glutamate into GABA) cause cerebellar deficits. ... "Disease-specific monoclonal antibodies targeting glutamate decarboxylase impair GABAergic neurotransmission and affect motor ...
glutamate-5-semialdehyde dehydrogenase Ja 1.2.1.47 4-trimethylammoniobutyraldehyde dehydrogenase Ja 1.2.1.50 long-chain-fatty- ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ... D-arabitol 4-dehydrogenase 1.1.1.12 L-arabitol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. L-xylulose + NADH + H+ L-arabitol ...
It is formed by the oxidation of succinate by the enzyme succinate dehydrogenase. Fumarate is then converted by the enzyme ... G→glutamate→. α-ketoglutarate. histidine→. *Urocanic acid. *Imidazol-4-one-5-propionic acid ... in eukaryotic organisms from succinate in complex 2 of the electron transport chain via the enzyme succinate dehydrogenase. It ...
... residue in the tripeptide glutamate-cysteine-glycine to carbon 6 of LTA4 thereby forming LTC4 (i.e. 5S-hydroxy,6R-(S- ... 5-HETE may be further metabolized by 5-Hydroxyeicosanoid dehydrogenase (5-HEDH) to 5-oxo-eicosatetraenoic acid (5-oxo-ETE). ...
In bacteria, carbon monoxide is produced via the reduction of carbon dioxide by the enzyme carbon monoxide dehydrogenase, an Fe ... Major excitatory/inhibitory systems: Glutamate system: Agmatine. *Aspartic acid (aspartate). *Cycloserine. *Glutamic acid ( ...
Zinc required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ...
Examples include zinc in zinc fingers and alcohol dehydrogenase, copper in the blue copper proteins, iron in cytochrome P450, ... While glutamic acid is usually sufficient because amino acid nitrogen is recycled through glutamate as an intermediary, dietary ...
1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum". Parasitology. 92, : 313-24. doi:10.1017/ ... "Evaluation of a new Plasmodium lactate dehydrogenase assay (OptiMAL-IT) for the detection of malaria". Transact Royal Soc Trop ...
L-glutamate N-methyltransferase would be the standard naming convention for the transferase methylamine-glutamate N- ... Herbst EA, MacPherson RE, LeBlanc PJ, Roy BD, Jeoung NH, Harris RA, Peters SJ (Jan 2014). "Pyruvate dehydrogenase kinase-4 ... This same action by the transferase can be illustrated as follows: methylamine + L-glutamate ⇌ {\displaystyle \ ... L-glutamate. While EC 2.7 includes enzymes that transfer phosphorus-containing groups, it also includes nuclotidyl transferases ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... G→glutamate→. α-ketoglutarate. histidine→. *Urocanic acid. *Imidazol-4-one-5-propionic acid ... The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by ... Acetyl-CoA serves as an allosteric regulator of pyruvate dehydrogenase kinase (PDK). It regulates through the ratio of acetyl- ...
Isovaleryl coenzyme A dehydrogenase. References[edit]. *^ a b c Wilson JM, Fitschen PJ, Campbell B, Wilson GJ, Zanchi N, Taylor ... G→glutamate→. α-ketoglutarate. histidine→. *Urocanic acid. *Imidazol-4-one-5-propionic acid ... whereas the dehydrogenase enzyme is found exclusively in the mitochondrion (Sabourin and Bieber 1981, 1983). Importantly, this ...
... similar to glutamate-1-semialdehyde 2,1- aminomutase) gene (btrB, neo18); a putative alcohol dehydrogenase gene (btrE, neo5); ... another putative dehydrogenase (similar to chorine dehydrogenase and related flavoproteins) gene (btrQ, neo11).[14] A ...
regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase). to α-ketoglutaric acid. *Glutamate ...
... is also a metabolic product of amino acid deamination catalyzed by enzymes such as glutamate dehydrogenase 1. Ammonia ...
Examples include zinc in zinc fingers and alcohol dehydrogenase, copper in the blue copper proteins, iron in cytochrome P450 ... G→glutamate→. α-ketoglutarate. histidine→. *Urocanic acid. *Imidazol-4-one-5-propionic acid ...
The critical enzyme step is two-fold using a 3β-hydroxysteroid dehydrogenase and a Δ5-4 isomerase. The latter transfers the ... Glutamic acid (glutamate). *Ivermectin. *Ketamine. *Neuroactive steroids (e.g., alfaxolone, pregnenolone (eltanolone), ...
GABA is synthesized in a single step from its precursor glutamate by glutamic acid decarboxylase. GABA is metabolized by ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... This disruption has the potential to impair glutamate homeostasis and may lead to uncoupling of the normal balance between ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ...
Other allosteric activators include glutamate and other dicarboxylic acids.[16] Long and short chain fatty acyl CoAs are ... "Bimodal activation of acetyl-CoA carboxylase by glutamate". The Journal of Biological Chemistry. 275 (15): 10819-25. doi ...
Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase,[15] as follows: glutamate + H2O + ... glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the presynaptic cell. Glutamate acts on ... Extracellular glutamate in Drosophila brains has been found to regulate postsynaptic glutamate receptor clustering, via a ... Main article: Glutamate (neurotransmitter). Glutamate is the most abundant excitatory neurotransmitter in the vertebrate ...
... inhibits alcohol dehydrogenase, and thus slows the metabolism of ethanol.[29] It also inhibits metabolism of ... Ionotropic glutamate receptor modulators. AMPAR. *Agonists: Main site agonists: 5-Fluorowillardiine. *Acromelic acid ( ... "Diethyl Ether Inhibits Ethanol Metabolism in Vivo by Interaction with Alcohol Dehydrogenase". Alcoholism: Clinical and ...
It is also known to maintain high internal glutamate concentrations under stress conditions. The expression of genes in the ... Succinate semialdehyde is then oxidized into succinate by succinate semialdehyde dehydrogenase which is encoded by the gabP ... gabD : encodes an NADP-dependent succinic semialdehyde dehydrogenase, which oxidizes succinic semialdehyde to succinate. gabP ... that encode for a succinate semialdehyde dehydrogenase, GABA transaminase and a GABA permease respectively. There is a ...
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In humans the relevant genes are called GLUD1 (glutamate dehydrogenase 1) and GLUD2 (glutamate dehydrogenase 2), and there are ... L-Glutamate Dehydrogenase, in The Enzymes, Vol VII. Academic Press. pp. 3-24. Frieden C (May 1965). "Glutamate Dehydrogenase. ... as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has ... glutamate dehydrogenase enzymes are divided into the following three classes: EC 1.4.1.2: L-glutamate + H2O + NAD+ ⇌ {\ ...
... glutamate dehydrogenase 3 is mitochondrial.. Leucine dehydrogenase (EC:1.4.1.9) (LeuDH) is a NAD-dependent enzyme that ... Glutamate dehydrogenases (EC:1.4.1.2, EC:1.4.1.3, and EC:1.4.1.4) (GluDH) are enzymes that catalyse the NAD- and/or NADP- ... Glutamate/phenylalanine/leucine/valine dehydrogenase, dimerisation domain (IPR006097). Short name: Glu/Leu/Phe/Val_DH_dimer_dom ... Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the ...
... glutamic acid dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, NAD(P)+-glutamate dehydrogenase, NAD(P)H ... Glutamate dehydrogenase (NADP+) (EC 1.4.1.4, glutamic dehydrogenase, dehydrogenase, glutamate (nicotinamide adenine ... glutamate dehydrogenase, glutamate dehydrogenase (NADP+)) is an enzyme with systematic name L-glutamate:NADP+ oxidoreductase ( ... "Glutamate dehydrogenases". In Boyer, P.D. (ed.). The Enzymes. 11 (3rd ed.). New York: Academic Press. pp. 293-367. Glutamate+ ...
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH. UniProt ...
Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ... Glutamate receptor blockers. Class Summary. Mechanism of action is unknown, but it enhances GABA transmission and inhibits ... It stimulates GABA transmission, inhibits glutamate, and decreases alcohol consumption in alcohol-dependent rats. The main ... Hypothesized to interact with glutamate and GABA neurotransmitters centrally to restore neuronal excitation and inhibition ...
A new class of glutamate dehydrogenases (GDH). J Biol Chem. 2000;275:39529-42.CrossRefPubMedGoogle Scholar ... Glutamate dehydrogenase, is an enzyme that plays a key role in the metabolism of carbon and nitrogen catalyzing reversibly the ... One of the enzymes of high scientific and applied interest is glutamate dehydrogenase (GDH). GDH plays a major role in the ... Helianti I, Morita Y, Yamamura A, Murakami Y, Yokoyama K, Tamiya E. Characterization of native glutamate dehydrogenase from an ...
Browse our Glutamate Dehydrogenase RNAi catalog backed by our Guarantee+. ... glutamate dehydrogenase (NAD(P)+) RNAi, glutamate dehydrogenase 1 RNAi, glutamate dehydrogenase 1, mitochondrial RNAi, ... Glutamate Dehydrogenase RNAi. We offer Glutamate Dehydrogenase RNAi for use in common research applications. Each Glutamate ... Alternate Names for Glutamate Dehydrogenase RNAi. Glutamate Dehydrogenase RNAi, GLUD1 RNAi, EC 1.4.1 RNAi, EC 1.4.1.3 RNAi, GDH ...
Regulation of glutamate dehydrogenase. In humans, the activity of glutamate dehydrogenase is controlled through ADP- ... In humans the relevant genes are called GLUD1 (glutamate dehydrogenase 1) and GLUD2 (glutamate dehydrogenase 2), and there are ... as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has ... Pyruvate dehydrogenase complex (E1, E2, E3). *(regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase ...
Δ1-pyrroline-5-carboxylate dehydrogenases; RocG, glutamate dehydrogenase. Proline is converted to glutamate via Δ1-pyrroline-5- ... for converting glutamate to 2-ketoglutarate (Fig. 1). An arginine-induced glutamate dehydrogenase also was described in ... Because rocG is not induced by glutamate, it is likely that RocG is a dedicated glutamate dehydrogenase responsible for the ... encoding a major catabolic glutamate dehydrogenase (GlutDH) (17), is a member of the RocR regulon. RocG activity (glutamate + ...
Glutaminase (GLS) and glutamate dehydrogenase (GDH) activities were followed by measuring transfer of 15N to 15NH4+. The time ... Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling.. Yang C1, ... Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling ... Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling ...
Role of Glutamate Dehydrogenase in Cancer Growth and Homeostasis, Dehydrogenases Rosa Angela Canuto, IntechOpen, DOI: 10.5772/ ... Role of Glutamate Dehydrogenase in Cancer Growth and Homeostasis, Dehydrogenases Rosa Angela Canuto, IntechOpen, DOI: 10.5772/ ... www.intechopen.com/embed/dehydrogenases/role-of-glutamate-dehydrogenase-in-cancer-growth-and-homeostasis /,. Embed this code ... www.intechopen.com/embed/dehydrogenases/role-of-glutamate-dehydrogenase-in-cancer-growth-and-homeostasis /, ...
... the gene that encodes mitochondrial enzyme glutamate dehydrogenase (GDH). Methods. The clinical data of glutamate dehydrogenase ... C. Fang, X. Ding, Y. Huang, J. Huang, P. Zhao, and J. Hu, "A novel mutation in the glutamate dehydrogenase (GLUD1) of a patient ... Y. Jin, D. Li, S. Lu et al., "Ebselen reversibly inhibits human glutamate dehydrogenase at the catalytic site," Assay and Drug ... R. Santer, M. Kinner, M. Passarge et al., "Novel missense mutations outside the allosteric domain of glutamate dehydrogenase ...
Glutamate dehydrogenase is derepressed in carbonlimited cells and in such cells the function of glutamate dehydrogenase appears ... The Role of Glutamate Dehydrogenase in Plant Nitrogen Metabolism. Sharon A. Robinson, Annette P. Slade, Gary G. Fox, Richard ... The Role of Glutamate Dehydrogenase in Plant Nitrogen Metabolism. Sharon A. Robinson, Annette P. Slade, Gary G. Fox, Richard ... 13C mass spectrometry have been used to demonstrate that glutamate dehydrogenase is active in the oxidation of glutamate, but ...
Role of NAD-linked glutamate dehydrogenase in nitrogen metabolism in Saccharomyces cerevisiae.. S M Miller, B Magasanik ... Our results indicate that the NAD-linked glutamate dehydrogenase catalyzes the major, but not sole, pathway for generation of ... We cloned GDH2, the gene that encodes the NAD-linked glutamate dehydrogenase in the yeast Saccharomyces cerevisiae, by ... Role of NAD-linked glutamate dehydrogenase in nitrogen metabolism in Saccharomyces cerevisiae. ...
The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over- ... The gene encoding the NAD(+)-dependent glutamate dehydrogenase (GDH) of Clostridium symbiosum was cloned using the polymerase ... The recombinant plasmid complemented the nutritional lesion of an E. coli glutamate auxotroph. There was a marked difference ...
... glutamate (glutamate M+1) (fig. S6D). We calculated the ratio of the total amount of glutamate (glutamate M+6 and glutamate M+1 ... The effect of pH and ADP on ammonia affinity for human glutamate dehydrogenases. Metab. Brain Dis. 28, 127-131 (2013). doi: ... to glutamate directly generated in glutaminolysis (glutamate M+6) (fig. S6E). In total, 1.57 molecules of glutamate were ... Glutamate dehydrogenase 1 signals through antioxidant glutathione peroxidase 1 to regulate redox homeostasis and tumor growth. ...
Protein target information for NAD-specific glutamate dehydrogenase (Mycobacterium tuberculosis H37Rv). Find diseases ...
Glutamine-Elicited Secretion of Glucagon-Like Peptide 1 (GLP-1) is Governed by an Activated Glutamate Dehydrogenase ... Glutamine-Elicited Secretion of Glucagon-Like Peptide 1 (GLP-1) is Governed by an Activated Glutamate Dehydrogenase ... Glutamine-Elicited Secretion of Glucagon-Like Peptide 1 (GLP-1) is Governed by an Activated Glutamate Dehydrogenase ... Glutamine-Elicited Secretion of Glucagon-Like Peptide 1 (GLP-1) is Governed by an Activated Glutamate Dehydrogenase ...
... especially the NADH-glutamate dehydrogenase (GDH) synthesis of nongenetic code-based RNA that optimizes crop nutritious yield ... Osuji, G.O. and Madu, W.C. (1995) Ammonium Ion-Dependent Isomerization of Glutamate Dehydrogenase in Relation to Glutamate ... Glutamate dehydrogenase (GDH; EC 1.4.1.2) has a complex chemical reaction mechanism [9]. In the narrow context, it is a redox ... Stoichiometric Mineral Salt Mixes, Glutamate Dehydrogenase Cycle, Photosynthesis, Nodulation, Vicilin, Double Grain Yields, ...
The global Glutamate Dehydrogenase market is valued at XX million... ... Check for Discount on China Glutamate Dehydrogenase Market Research Report 2017 report by QYResearch Group. ... 1 Glutamate Dehydrogenase Overview. 1.1 Product Overview and Scope of Glutamate Dehydrogenase. 1.2 Classification of Glutamate ... China Glutamate Dehydrogenase Market Research Report 2017 Table of Contents. China Glutamate Dehydrogenase Market Research ...
Putative NAD-dependent glutamate dehydrogenase GDH (NAD-GDH) (NAD-dependent GLUTAMIC dehydrogenase)Imported. ,p>Information ... Putative NAD-dependent glutamate dehydrogenase GDH (NAD-GDH) (NAD-dependent GLUTAMIC dehydrogenase). ... tr,G0TPV3,G0TPV3_MYCCP Putative NAD-dependent glutamate dehydrogenase GDH (NAD-GDH) (NAD-dependent GLUTAMIC dehydrogenase) OS= ...
An increase in mRNA expression of gdh1a could be essential for increased glutamate production in support of increases in ... An increase in mRNA expression of gdh1a could be essential for increased glutamate production in support of increases in ... Keywords: ammonia, glutamate, glutamate dehydrogenase, Monopterus albus, nitrogen metabolism, osmoregulation, mRNA expression, ... Plaitakis, A., and Zaganas, I. (2001). Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and ...
Bovine glutamate dehydrogenase (GDH) is allosterically regulated and requires substrate-induced subunit interactions for ... Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis ... glutamate and norvaline, on conformational stability. Glutamate has little effect on overall stability, whereas norvaline ... Deuterated glutamate shows a steady-state isotope effect but no effect on the presteady-state burst rate, demonstrating that ...
... glutamate dehydrogenase [GDH]) and toxin A. Evaluation of the test was carried out in 304 fecal samples from patients suspected ... Usefulness of Simultaneous Detection of Toxin A and Glutamate Dehydrogenase for the Diagnosis of Clostridium Difficile- ... glutamate dehydrogenase [GDH]) and toxin A. Evaluation of the test was carried out in 304 fecal samples from patients suspected ...
Glutamate Dehydrogenase (GDH) Antigen Assays. Some literature in recent years has suggested that assays for GDH, an enzyme ...
Localization of NAD-Isocitrate Dehydrogenase and Glutamate Dehydrogenase in Rice Roots : Candidates for Providing Carbon ... Are isocitrate dehydrogenases and 2-oxoglutarate involved in the regulation of glutamate synthesis? GALVEZ S. ... The essential active-site lysines of clostridial glutamate dehydrogenase : a study with pyridoxal-5-phosphate LILLY K. S. ... Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots YAMAYA T. ...
Site-directed mutagenesis studies of Escherichia coli glutamate dehydrogenase Biochem Soc Trans (October,1988) ... J. R. KINGHORN, J. A. PATEMAN; Nicotinamide-Adenine Dinucleotide Phosphate-Linked Glutamate Dehydrogenase Activity and Ammonium ... Nicotinamide-Adenine Dinucleotide Phosphate-Linked Glutamate Dehydrogenase Activity and Ammonium Regulation in Aspergillus ... dependent glutamate dehydrogenase of Clostridium symbiosum Biochem Soc Trans (October,1988) ...
... ... our laboratory generated a transgenic mouse model that over-expresses the mitochondrial glutamate dehydrogenase 1 (GLUD1) gene ... extracellular glutamate levels, and increased glutamate release after stimulation as compared to wild type (wt). There were ... Glutamate has been shown to lead to neurotoxicity and subsequent neurodegeneration through changes in synaptic function, loss ...
NADP-linked glutamate dehydrogenase (NADP+-GluDH, EC 1.4.1.4) has been purified to homogeneity from epimastigotes of ... The NADP+-linked glutamate dehydrogenase from Trypanosoma cruzi: sequence, genomic organization and expression. Patricia ... The NADP+-linked glutamate dehydrogenase from Trypanosoma cruzi: sequence, genomic organization and expression ... The NADP+-linked glutamate dehydrogenase from Trypanosoma cruzi: sequence, genomic organization and expression ...
  • Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. (ebi.ac.uk)
  • Glutamate α-Ketoglutarate GLDH can be measured in a medical laboratory to evaluate the liver function. (wikipedia.org)
  • Bovine liver glutamate dehydrogenase was found to be regulated by nucleotides in the late 1950s and early 1960s by Carl Frieden. (wikipedia.org)
  • We obtained a cDNA sequence of glutamate dehydrogenase ( gdh ), which consisted of a 133-bp 5′ UTR, a complete coding sequence region spanning 1629 bp and a 3′ UTR of approximately 717 bp, from the liver, intestine, and brain of M. albus . (frontiersin.org)
  • Full length Glutamate Dehydrogenase protein isolated from Bovine Liver. (lsbio.com)
  • Thusius' critique (1977) of the authors' work on the functional relationship between the equilibrium polymerization and catalytic activity of beef liver glutamate dehydrogenase is refuted on a point by point basis. (eurekamag.com)
  • The important functional relationship between the polymerization and allosteric control of beef liver glutamate dehydrogenase has been clearly demonstrated on a purely experimental basis. (eurekamag.com)
  • METHODS: Enzymes of the urea cycle as well as glutamine synthetase and glutamate dehydrogenase (GDH) were assayed in liver tissue and/or lymphocytes. (eur.nl)
  • 1. The interaction of beef liver glutamate dehydrogenase with cardiolipin from both beef liver mitochondria and beef heart mitochondria, with phosphatidylcholine from both beef liver mitochondria and egg-yolk, and with beef brain phosphatidylserine was investigated by steady-state kinetic methods. (semanticscholar.org)
  • Synthesis of 5-substituted isophthalic acids and competitive inhibition studies with bovine liver glutamate dehydrogenase. (microbiologyresearch.org)
  • The liver is rich in glutamate dehydrogenase (GDH) that catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate and ammonia, thus bridging amino acid to glucose pathways. (highwire.org)
  • Intro Bovine liver organ glutamate dehydrogenase [E.C. 1.4.1.3, GDH] catalyzes the oxidative 78712-43-3 manufacture deamination of L-glutamate and different monocarboxylic 78712-43-3 manufacture acidity substrates (1). (gasyblog.com)
  • To investigate how GDH is regulated under these conditions, kinetic properties of GDH were analyzed in liver from euthermic and torpid squirrels, revealing significant differences in Vmax, Km glutamate, Ka ADP and inhibition by urea between the two forms of GDH. (carleton.ca)
  • As a novel approach, we also offer combining serum isocitrate and glutamate dehydrogenase levels with ALT, AST tests to state liver functions more reliably in patients. (authorea.com)
  • Glutamate dehydrogenase, is an enzyme that plays a key role in the metabolism of carbon and nitrogen catalyzing reversibly the oxidative deamination of glutamate to alpha-ketoglutarate and ammonium. (springer.com)
  • Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling. (nih.gov)
  • The small amount of unlabeled ammonium (gray wedge) mostly resulted from metabolism of unlabeled glutamate by GDH. (nih.gov)
  • This catabolic role for glutamate dehydrogenase implies an important regulatory function in carbon and nitrogen metabolism. (plantphysiol.org)
  • Role of NAD-linked glutamate dehydrogenase in nitrogen metabolism in Saccharomyces cerevisiae. (asm.org)
  • By incubation of these cells in media containing different concentrations of glutamate (range 100-500 µM) in the presence or in the absence of glucose, the metabolism of these substrates was studied by using tritiated glutamate or 2-deoxyglucose as tracers. (eurekamag.com)
  • This study provides evidence of the importance of glutamate metabolism for C. difficile pathogenesis. (k-state.edu)
  • GLUD1 ( Glutamate dehydrogenase 1) is a mitochondrial matrix enzyme , with a key role in the nitrogen and glutamate (Glu) metabolism and the energy homeostasis. (en-academic.com)
  • Mammalian glutamate dehydrogenase is an allosterically regulated enzyme that is central to glutamate metabolism. (cdc.gov)
  • We hypothesized that the next step in the embryo's metabolism would be the utilization of the enzyme glutamate dehydrogenase to convert glutamate to aketoglutarate. (bsu.edu)
  • Glutamate dehydrogenase (GLUD) is an enzyme central to the glutamate and energy metabolism of the cell. (ox.ac.uk)
  • This MTS substitution arose in parallel with two crucial adaptive amino acid changes in the enzyme and likely contributed to the functional adaptation of GLUD2 to the glutamate metabolism of the hominoid brain and other tissues. (ox.ac.uk)
  • Glutamate dehydrogenase (GDH) is a key enzyme that links amino acid and carbohydrate metabolism in cells. (carleton.ca)
  • The pyruvate dehydrogenase complex (PDH) critically regulates carbohydrate metabolism. (nature.com)
  • Diab H, Limami AM. Reconfiguration of N Metabolism upon Hypoxia Stress and Recovery: Roles of Alanine Aminotransferase (AlaAT) and Glutamate Dehydrogenase (GDH). (mdpi.com)
  • In humans the relevant genes are called GLUD1 (glutamate dehydrogenase 1) and GLUD2 (glutamate dehydrogenase 2), and there are also at least 8 GLDH pseudogenes in the human genome as well, probably reflecting microbial influences on eukaryote evolution. (wikipedia.org)
  • To characterize the genotype and phenotype of Chinese patients with congenital hyperinsulinism (CHI) caused by activating mutations in GLUD1 , the gene that encodes mitochondrial enzyme glutamate dehydrogenase (GDH). (hindawi.com)
  • The mitochondrial matrix enzyme glutamate dehydrogenase (GDH, EC 1.4.1.3), encoded by GLUD1 , catalyzes the reversible reaction α -ketoglutarate + NH3 + NADH ↔ glutamate + NAD. (hindawi.com)
  • To probe the effects of excess glutamate and determine if these effects might contribute to the morphological and functional changes associated with aging, our laboratory generated a transgenic mouse model that over-expresses the mitochondrial glutamate dehydrogenase 1 (GLUD1) gene. (ku.edu)
  • The Glud1 Tg mouse model generated in our laboratory demonstrated significantly increased GLUD1 levels, GLUD activity, extracellular glutamate levels, and increased glutamate release after stimulation as compared to wild type (wt). (ku.edu)
  • Therefore, the Glud1 Tg mice may be used to probe the molecular and cellular pathways involved in selective neuronal vulnerability as it may relate to excess extracellular glutamate. (ku.edu)
  • Glutamate Dehydrogenase antibody LS-C59301 is an unconjugated rabbit polyclonal antibody to bovine Glutamate Dehydrogenase (GLUD1). (lsbio.com)
  • Glutamate Dehydrogenase antibody LS-B4661 is an unconjugated rabbit polyclonal antibody to Glutamate Dehydrogenase (GLUD1) from human, mouse, rat and other species. (lsbio.com)
  • abstract = "Aluminum inactivated glutamate dehydrogenase (GDH) by a pseudo-first-order reaction at micromolar concentrations. (elsevier.com)
  • Role of Glutamate Dehydrogenase in Cancer Growth and Homeostasis, Dehydrogenases Rosa Angela Canuto, IntechOpen, DOI: 10.5772/48606. (intechopen.com)
  • Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. (ebi.ac.uk)
  • Attempts to lower ammonia levels failed with different therapies such as protein restriction, benzoate, or N-carbamoyl glutamate. (hindawi.com)
  • Glutamate has little effect on overall stability, whereas norvaline markedly stabilizes the protein. (sigmaaldrich.com)
  • Among the various biomarkers, plasmodial lactate dehydrogenase and histidine-rich protein II (HRP II) have received increasing attention for developing rapid and reliable detection techniques for malaria. (hindawi.com)
  • The increases in mRNA expression of gdh1a and Gdh amination activity would probably lead to an increase in glutamate production in support of increased glutamine synthesis for the purpose of ammonia detoxification or cell volume regulation under these two different environmental conditions. (frontiersin.org)
  • Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation. (sigmaaldrich.com)
  • The substrate glutamate exhibits negative cooperativity and complex allosteric regulation but has only minor effects on global GDH stability, while promoting certain local conformational fluctuations. (sigmaaldrich.com)
  • Are isocitrate dehydrogenases and 2-oxoglutarate involved in the regulation of glutamate synthesis? (nii.ac.jp)
  • In order to improve our understanding of the regulation of nitrogen assimilation and recycling in wheat ( Triticum aestivum L.), we studied the localization of plastidic (GS2) and cytosolic (GS1) glutamine synthetase isoenzymes and of glutamate dehydrogenase (GDH) during natural senescence of the flag leaf and in the stem. (oup.com)
  • Clinical chemistry reagents intended to perform qualitative and/or quantitative chemical analyses of body fluids (typically serum) to determine the level of the enzyme glutamate dehydrogenase (GLD). (medicalproductguide.com)
  • GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. (ebi.ac.uk)
  • Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. (wikipedia.org)
  • In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases. (wikipedia.org)
  • of about 1 mM), and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed (that is, α-ketoglutarate and ammonia to glutamate and NAD(P)+). However, in brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination (i.e. glutamate to α-ketoglutarate and ammonia) [1] . (wikidoc.org)
  • Ammonia incorporation in animals and microbes occurs through the actions of glutamate dehydrogenase and glutamine synthetase . (wikidoc.org)
  • Our results indicate that the NAD-linked glutamate dehydrogenase catalyzes the major, but not sole, pathway for generation of ammonia from glutamate. (asm.org)
  • Accumulation of ammonia enabled glutamate dehydrogenase to function in reductive amination, which allowed incorporation of nitrogen from ammonia back into amino acids. (sciencemag.org)
  • Experiments in mice also showed incorporation of ammonia into glutamate, aspartate, and proline. (sciencemag.org)
  • Metabolomic tracking of 15 N-labeled ammonia showed rapid incorporation of 15 N into glutamate and glutamate-derived amino acids. (biologists.org)
  • Downregulating human GLUD2 [encoding mitochondrial glutamate dehydrogenase 2 (GDH2)], inhibiting GDH2 activity by SIRT4 overexpression, and supplementing cells with glutamate or glutamine alleviated ammonia-induced inhibition of mitochondrial respiration. (biologists.org)
  • CONCLUSION: A continuous conversion of glutamate to 2-oxoglutarate causes a depletion of glutamate needed for the synthesis of N-acetylglutamate, the catalyst of the urea synthesis starting with ammonia. (eur.nl)
  • Use Glutamate Dehydrogenase in diagnostic tests for the determination of ammonia, urea, L-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. (roche.com)
  • RocG activity (glutamate + NAD → 2-ketoglutarate + NH 3 + NADH) can be viewed as the final step in the use of arginine, ornithine, and proline as carbon or nitrogen sources (Fig. 1 ). (pnas.org)
  • Several potentially practical biochemical processes in plant systems still remain hidden, especially the NADH-glutamate dehydrogenase (GDH) synthesis of nongenetic code-based RNA that optimizes crop nutritious yield by degrading superfluous genetic code-based RNA. (scirp.org)
  • Lactate dehydrogenase allows for the occurrence of glycolysis by helping in the conversion of NADH to NAD+. (wikibooks.org)
  • The first step utilizes glutamate dehydrogenase (GDH)and utilizes the coenzyme NAD+, which is reduced to NADH [1] . (wikibooks.org)
  • The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis Bf1 is induced by peptides in the growth medium. (microbiologyresearch.org)
  • GDH in sample will consume glutamate as a specific substrate and generate NADH stoichiometrically, resulting in a proportional color development. (docplayer.net)
  • Apply OD = A 1 A 0 (or A n+1 A n ) to the Glutamate Standard Curve to get B nmol of NADH produced by GDH in the given time. (docplayer.net)
  • Two glutamate dehydrogenases, NADH-linked (EC 1.2.1.2) and NADPH-linked (EC 1.2.1.4) were isolated from the epimastigote forms of Trypanosoma cruzi and purified. (meta.org)
  • The molecular weights of the native NADH-and NADPH-linked glutamate dehydrogenases were estimated to be 360,000 and 265,000, respectively, and those of the subunits to be 58,000 and 43,000, respectively. (meta.org)
  • The isoelectric point of the NADH-linked dehydrogenase is at pH 5.25 and that of the NADPH-linked enzyme at pH 5.1. (meta.org)
  • In addition, purine nucleotides were shown to be potent inhibitors of the NADH-linked glutamate dehydrogenase. (meta.org)
  • Pyruvate produced by the reverse reaction of alanine aminotransferase is funneled to the TCA cycle, while deaminating glutamate dehydrogenase regenerates, reducing equivalent (NADH) and 2-oxoglutarate to maintain the cycle function. (mdpi.com)
  • NAD+(or NADP+) is a cofactor for the glutamate dehydrogenase reaction, producing α-ketoglutarate and ammonium as a byproduct. (wikipedia.org)
  • In cell suspension cultures of carrot ( Daucus carota L. cv Chantenay), primary assimilation of ammonium occurs via the glutamate synthase pathway. (plantphysiol.org)
  • Glutamate dehydrogenase (GDH) is a mitochondrial enzyme that catalyzes both the reversible conversion of ammonium nitrogen into organic nitrogen (glutamate production) and the oxidative deamination of glutamate resulting in 2-oxoglutarate. (eur.nl)
  • Schmidt, Robert 2004-10-06 00:00:00 Chlorella sorokiniana has seven ammonium-inducible, chloroplastic NADP-specific glutamate dehydrogenase (NADP-GDH) isozymes composed of varying ratios of α- and β-subunits. (deepdyve.com)
  • Glutamate dehydrogenase catalyzes the conversion of the nitrogen atom in glutamate into ammonium ions by oxidative deamination (See Reaction Scheme Below). (wikibooks.org)
  • The ammonium inducible nicotinamide phosphate-specific glutamate dehydrogenase from Chlorella sorokiniana has been purified 260-fold to homogeneity. (vt.edu)
  • Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells. (nii.ac.jp)
  • Peroxisomal NADP-dependent isocitrate dehydrogenase. (nii.ac.jp)
  • The incidence of isocitrate dehydrogenase (IDH) mutations is high in low-grade gliomas. (biomedcentral.com)
  • Glutamate dehydrogenases ( EC:1.4.1.2 , EC:1.4.1.3 , and EC:1.4.1.4 ) (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [ PMID: 1358610 , PMID: 8315654 ]. (ebi.ac.uk)
  • Glutamate dehydrogenase (GLDH, GDH) is an enzyme , present in most microbes and the mitochondria of eukaryotes , as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate , and vice versa. (wikidoc.org)
  • These results suggest a possibility that aluminum-induced alterations in enzymes of the glutamate system may be one of the causes of aluminum-induced neurotoxicity. (elsevier.com)
  • Glutamate dehydrogenase (GLDH, GDH) is an enzyme observed in both prokaryotes and eukaryotic mitochondria. (wikipedia.org)
  • The studies presented in this dissertation focused on investigating the role of mitochondria in inducing region specific neuronal degeneration under the conditions of the combined effects of aging and excess glutamate activity in the central nervous system. (ku.edu)
  • Glutamate dehydrogenase is located in the mitochondria of cells. (wikibooks.org)
  • We also isolated yeast mutants that lacked glutamate synthase activity and present evidence which shows that normally NAD-linked glutamate dehydrogenase is not involved in glutamate biosynthesis, but that if the enzyme is overexpressed, it may function reversibly in intact cells. (asm.org)
  • Tissue distribution of glutamate synthase and glutamine synthetase in rice leaves. (nii.ac.jp)
  • We propose a model showing (i) how pyruvate derived from active glycolysis upon hypoxia is competitively used by the alanine aminotransferase/glutamate synthase cycle, leading to alanine accumulation and NAD + regeneration. (mdpi.com)
  • Glutamate plays the central role in mammalian and microbe nitrogen flow, serving as both a nitrogen donor and a nitrogen acceptor. (wikipedia.org)
  • A yeast strain with a deletion-disruption allele of GDH2 which replaced the wild-type gene grew very poorly with glutamate as a nitrogen source, but growth improved significantly when the strain was also provided with adenine or other nitrogenous compounds whose biosynthesis requires glutamine. (asm.org)
  • GDH catalyzes the interconversion of glutamate into NH4+ and α-ketoglutarate, thereby linking nitrogen and Krebs cycles. (unamur.be)
  • On the other hand, molecular phylogenetic analysis showed that one tyrosinase gene is an ortholog of vertebrate tyrosinase genes and that the coral homologs, scyA and scyB , are similar to bacterial metabolic genes, phosphonopyruvate ( ppyr ) decarboxylase and glutamate dehydrogenase ( GDH ), respectively. (mdpi.com)
  • In SF188 glioblastoma cells, glucose deprivation did not affect net glutamine utilization but elicited a switch in the pathways used to deliver glutamine carbon to the tricarboxylic acid cycle, with a large increase in the activity of glutamate dehydrogenase (GDH). (nih.gov)
  • Both DMG and glutamine alone elicited GLP-1 secretion in GLUTag cells and in vivo , whereas activation of glutamate dehydrogenase (GDH) was required to stimulate insulin secretion from INS-1 832/13 cells. (diabetesjournals.org)
  • These data are consistent with the in vivo studies that have shown a redirection of glutamine carbon away from net hepatic glutamate release and into the citric acid cycle through the forward reaction catalyzed by GDH, i.e., glutamate to oxoglutarate. (eur.nl)
  • In addition, the shortage of glutamate may lead to an insufficient formation of glutamine by glutamine synthetase. (eur.nl)
  • U251 glioma cells were characterised by high levels of glutamine, glutamate and GABA oxidation. (biomedcentral.com)
  • This ability is unique because NADPH is used as the reductant in biosynthetic reactions, while NAD+ is usually used as the oxidant in most catabolic reaction, and glutamine dehydrogenase is not specific to either. (wikibooks.org)
  • Specifically, glutaminase (GLS) directs the conversion of glutamine to glutamate, which is then converted to α-ketoglutarate (αKG) by glutamate dehydrogenase that enters the TCA cycle. (jci.org)
  • In humans, the activity of glutamate dehydrogenase is controlled through ADP-ribosylation, a covalent modification carried out by the gene sirt4. (wikipedia.org)
  • The activities of brain glutamate dehydrogenase and malate dehydrogenase were not statistically different in samples from patients with autosomal dominant olivopontocerebellar atrophy or Joseph disease compared with control subject samples. (elsevier.com)
  • According to ROC analysis, malate dehydrogenase showed an outstanding diagnostic ability with the highest AUC value of 0.9 and the cut-off value of 51.2 IU/L. Discriminant analysis including malate, isocitrate and glutamate dehydrogenase had predicted preeclampsia with an overall %87.9 accuracy. (authorea.com)
  • The glutamate dehydrogenase gene of Clostridium symbiosum. (nih.gov)
  • The gene encoding the NAD(+)-dependent glutamate dehydrogenase (GDH) of Clostridium symbiosum was cloned using the polymerase chain reaction (PCR) because it could not be recovered by standard techniques. (nih.gov)
  • Biosite Diagnostics, BMD, France) for detecting both a specific antigen of Clostridium difficile (glutamate dehydrogenase [GDH]) and toxin A. Evaluation of the test was carried out in 304 fecal samples from patients suspected of having Clostridium difficile-associated diseases. (nih.gov)
  • In vivo nuclear magnetic resonance spectroscopy, in vitro gas chromatography-mass spectrometry, and automated 15 N/ 13 C mass spectrometry have been used to demonstrate that glutamate dehydrogenase is active in the oxidation of glutamate, but not in the reductive amination of 2-oxogiutarate. (plantphysiol.org)
  • Glutamate dehydrogenase is derepressed in carbonlimited cells and in such cells the function of glutamate dehydrogenase appears to be the oxidation of glutamate, thus ensuring sufficient carbon skeletons for effective functioning of the tricarboxylic acid cycle. (plantphysiol.org)
  • An enzyme that catalyses the oxidation by NADP + of l‐glutamate to form 2‐oxoglutarate, NH 3 , and NADPH. (oup.com)
  • Succinic semialdehyde dehydrogenase (SSADH) expression was correlated to GABA oxidation. (biomedcentral.com)
  • Dehydrogenases catalyze the oxidation of alcohols to carbonyl compounds by using either NAD+ or NADP+. (wikibooks.org)
  • In the oxidation of the alcohol, one in dehydrogenases transferred to the 4 position of the nicotinamide ring of the NAD+ by removing two hydrogens. (wikibooks.org)
  • The oxidation of L-glutamate is stimulated by ADP and inhibited by GTP. (roche.com)
  • Enhanced glutamate oxidation by Ala445-hGDH2 is thought to accelerate nigral cell degeneration in hemizygous males, and inhibition of the overactive variant by estrogens may protect heterozygous females. (cdc.gov)
  • When grown on isophthalate, all strains showed activity of NADP-dependent GDH (NADP-GDH), while cells grown on glucose, 2× yeast extract-tryptone broth (2YT) or glutamate showed activities of both NAD-dependent GDH (NAD-GDH) and NADP-GDH. (microbiologyresearch.org)
  • Leucine dehydrogenase ( EC:1.4.1.9 ) (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [ PMID: 3069133 ]. (ebi.ac.uk)
  • Quantification of free amino acids in the hamster gut during C. difficile infection showed that glutamate is among preferred amino acids utilized by C. difficile during its expansion. (k-state.edu)
  • The enzyme also displays the unique capability, among mammalian dehydrogenases, to be able to use either NAD+ or NADP+ as cofactor in the response with near similar affinity, although NAD(H) comes with an extra binding site per subunit (2). (gasyblog.com)
  • Glutamate dehydrogenase from mammalian resources is highly controlled by a varied array of little substances, with ADP, GTP, Leucine, as well as the mix of malate and palmitoyl CoA getting the very best regulators of the experience (20C22). (gasyblog.com)
  • Crystallization of the NADP(+)-dependent glutamate dehydrogenase from Escherichia coli. (ox.ac.uk)
  • The NADP(+)-dependent hexameric glutamate dehydrogenase from Escherichia coli has been crystallized as the apo-enzyme and also in the presence of its substrates 2-oxoglutarate, glutamate or NADP+, using either pulsed equilibrium microdialysis, or the hanging drop method of vapour diffusion. (ox.ac.uk)
  • When the gluD gene, which codes for glutamate dehydrogenase (GDH), was disrupted, the mutant C. difficile was unable to colonize and cause disease in a hamster model. (k-state.edu)
  • Guanidine hydrochloride unfolding, heat inactivation, and differential scanning calorimetry demonstrate the effects of alternative substrates, glutamate and norvaline, on conformational stability. (sigmaaldrich.com)
  • L-lactate dehydrogenase oxidizes the reversible reaction of L-lactate to pyruvate by using NAD+ as a coenzyme. (wikibooks.org)
  • Lactate dehydrogenase is especially important for the role that it plays in glycolysis. (wikibooks.org)
  • Lactate dehydrogenase does this by converting pyruvate to lactate. (wikibooks.org)
  • Finally, pyruvate is converted to lactate by the enzyme lactate dehydrogenase A (LDHA, Figure 1 ). (jci.org)
  • Phenylalanine dehydrogenase ( EC:1.4.1.20 ) (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [ PMID: 1880121 ]. (ebi.ac.uk)
  • Valine dehydrogenase ( EC:1.4.1.8 ) (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [ PMID: 8320231 ]. (ebi.ac.uk)
  • The rocG gene of Bacillus subtilis , encoding a catabolic glutamate dehydrogenase, is transcribed by SigL (σ 54 )-containing RNA polymerase and requires for its expression RocR, a member of the NtrC/NifA family of proteins that bind to enhancer-like elements, called upstream activating sequences (UAS). (pnas.org)
  • In the present work, we show that the B. subtilis rocG gene, encoding a major catabolic glutamate dehydrogenase (GlutDH) ( 17 ), is a member of the RocR regulon. (pnas.org)
  • The alcohol dehydrogenase catalyzes the reaction of alcohols to aldehydes and ketones by using NAD+ as a coenzyme. (wikibooks.org)
  • Dehydrogenase that catalyzes the conversion of glutamate to α-ketoglutarate. (roche.com)
  • Bovine glutamate dehydrogenase (GDH) is allosterically regulated and requires substrate-induced subunit interactions for maximum catalytic activity. (sigmaaldrich.com)
  • Expect a band approximately 56 kD in size corresponding to glutamate dehydrogenase monomer subunit by western blotting in the appropriate cell or tissue extract. (lsbio.com)
  • These outcomes claim that the V-type inhibition created with glutamate as the substrate outcomes from disruption of subunit relationships necessary for effective catalysis instead of by a direct impact on the energetic site conformation. (gasyblog.com)
  • Our latest work shows the need for conformational versatility (18) and the effectiveness of subunit relationships (19) in glutamate advertised cooperativity that's absent with norvaline. (gasyblog.com)
  • EC 1.4.1.2-1.4.1.4) catalyses in vitro the reversible amination of 2-oxoglutarate to glutamate. (nih.gov)
  • Polyclonal antisera raised against Plasmodium knowlesi reacted with NADP-specific glutamate dehydrogenase (GLDH) of P. knowlesi, GLDH of P. falciparum and GLDH of Proteus spp. (lancs.ac.uk)
  • We cloned GDH2, the gene that encodes the NAD-linked glutamate dehydrogenase in the yeast Saccharomyces cerevisiae, by purifying the enzyme, making polyclonal antibodies to it, and using the antibodies to screen a lambda gt11 yeast genomic library. (asm.org)
  • Under these circumstances, glutamate dehydrogenase activity is raised in order to increase the amount of α-ketoglutarate produced, which can be used to provide energy by being used in the citric acid cycle to ultimately produce ATP. (wikipedia.org)
  • The purpose of this study is to present the partial characterization of a thermophilic microorganism isolated from Deception Island, Antarctica, that displays glutamate dehydrogenase activity. (springer.com)
  • This microorganism contains a thermostable glutamate dehydrogenase with optimal activity at pH 8.0 and temperatures for its activity from 37 to 50 °C, range of temperature of interest for biotechnological applications. (springer.com)
  • This is the first report of a microorganism from Antarctica containing a thermostable glutamate dehydrogenase that maintains its activity in a broad range of temperatures making it of potential interest for biotechnological applications. (springer.com)
  • Detection of glutamate dehydrogenase enzyme activity in Plasmodium falciparum infection. (bvsalud.org)
  • 1 ab Glutamate Dehydrogenase Detection Kit Instructions for Use For the rapid, sensitive and accurate measurement of Glutamate Dehydrogenase activity in various samples This product is for research use only and is not intended for diagnostic use. (docplayer.net)
  • Because it has been proven that 78712-43-3 manufacture the complete hexamer must give ideal activity of the enzyme (17) with glutamate as substrate, chances are how the cooperative relationships between subunits in the hexamer are necessary for maximal activity. (gasyblog.com)
  • These data suggested an activation of the glutamate-oxidizing activity of GDH in the hypometabolic state. (carleton.ca)
  • We found that GdhZ (for glutamate dehydrogenase interacting with FtsZ) directly stimulates the GTPase activity of FtsZ in vitro, leading to protofilaments shrinkage, only when GdhZ was enzymatically active. (unamur.be)
  • Trypanosoma cruzi: inhibition of alpha-hydroxyacid dehydrogenase isozyme II by N-allyl and N-propyl oxamates and their effects on intact epimastigotes. (semanticscholar.org)
  • The physiological need for feasible zinc inhibition of glutamate dehydrogenase isn't very clear although zinc poisoning (26) stocks some comparable symptoms as Reyes symptoms which includes previously been proven to involve modifications in the rules of glutamate dehydrogenase (27) and 78712-43-3 manufacture raised zinc levels have already been connected with neurological disease (28). (gasyblog.com)
  • Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase. (ebi.ac.uk)
  • Glutamate dehydrogenase (NADP+) (EC 1.4.1.4, glutamic dehydrogenase, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), glutamic acid dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, NAD(P)+-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP+)) is an enzyme with systematic name L-glutamate:NADP+ oxidoreductase (deaminating). (wikipedia.org)
  • It is significant that GDH-deficient cells exhibited an increased utilization of glucose in the presence of 250 and 500 µM glutamate, monitored as an increase in the accumulation of tritiated 2-deoxyglucose-6-phosphate. (eurekamag.com)
  • l‐glutamate:NADP + oxidoreductase (deaminating). (oup.com)
  • NADP-linked glutamate dehydrogenase (NADP + -GluDH, EC 1.4.1.4) has been purified to homogeneity from epimastigotes of Trypanosoma cruzi by an improved procedure, and the amino acid sequences of 11 internal peptides obtained by digestion with trypsin, endopeptidase Lys-C, endopeptidase Arg-C or CNBr have been obtained. (biochemj.org)
  • Purification and some properties of the NADP-linked glutamate dehydrogenase from Trypanosoma cruzi. (semanticscholar.org)
  • Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases. (ebi.ac.uk)
  • Purification of nicotinamide adenine dinucleotide phosphate- specific glutamate dehydrogenase from Chlorella sorokiniana and partial characterization of its physical, kinetic, and immunological properties. (vt.edu)
  • This enzyme catalyses the following chemical reaction L-glutamate + H2O + NADP+ ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH3 + NADPH + H+ Coulton JW, Kapoor M (April 1973). (wikipedia.org)
  • Nucleotide sequence of the GDH gene coding for the NADP-specific glutamate dehydrogenase of Saccharomyces cerevisiae. (ymdb.ca)
  • In pancreatic β -cells, GDH participates in glucose-stimulated insulin secretion via glutamate formation, which is important for the amplifying pathway of insulin secretion. (hindawi.com)
  • We present data consistent with the idea that BCH induces insulin release through the allosteric activation of glutamate dehydrogenase. (meta.org)
  • Glutamate dehydrogenase (GDH) is a target for treating insulin-related disorders, such as hyperinsulinism hyperammonemia syndrome. (utmb.edu)