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 FLAVOPROTEIN enzyme for AMMONIA assimilation in BACTERIA, microorganisms and PLANTS. It catalyzes the oxidation of 2 molecules of L-GLUTAMATE to generate L-GLUTAMINE and 2-oxoglutarate in the presence of NAD+.
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.
A species of motile, free-living, gram-negative bacteria that occur in the soil. They are aerobic or microaerophilic and are sometimes capable of nitrogen fixation.
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.
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.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
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.
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.
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.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
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.
A class of enzymes that catalyze oxidation-reduction reactions of amino acids.
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 dye used as a reagent in the determination of vitamin C.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
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)
Antibiotic substance produced by various Streptomyces species. It is an inhibitor of enzymatic activities that involve glutamine and is used as an antineoplastic and immunosuppressive agent.
One of the FLAVORING AGENTS used to impart a meat-like flavor.
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.
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.
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.
An amino acid that inhibits phosphate-activated glutaminase and interferes with glutamine metabolism. It is an antineoplastic antibiotic produced by an unidentified species of Streptomyces from Peruvian soil. (From Merck Index, 11th ed)
Glutaminase is an enzyme that catalyzes the conversion of glutamine to glutamate and ammonia, playing a crucial role in nitrogen metabolism and amino acid homeostasis within various tissues and cells, including the brain, kidney, and immune cells.
The methyl imidoester of suberic acid used to produce cross links in proteins. Each end of the imidoester will react with an amino group in the protein molecule to form an amidine.
The rate dynamics in chemical or physical systems.
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.
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.
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.
A type I G protein-coupled receptor mostly expressed post-synaptic pyramidal cells of the cortex and CENTRAL NERVOUS SYSTEM.
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.
An enzyme that catalyzes the transfer of D-glucose from UDPglucose into 1,4-alpha-D-glucosyl chains. EC 2.4.1.11.
Pentanoic acid, also known as valeric acid, is a carboxylic acid with a 5-carbon chain (C5H10O2), having a distinctive pungent and rancid odor, found in some animals' sweat, certain foods, and produced through wood fermentation.
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.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
A 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)
A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.
An enzyme of the transferase class that catalyzes the reaction 5,10-methylenetetrahydrofolate and dUMP to dihydrofolate and dTMP in the synthesis of thymidine triphosphate. (From Dorland, 27th ed) EC 2.1.1.45.
Acetylene is not typically considered a medical term, but rather a chemical compound (C2H2) commonly used in industrial and laboratory settings for its high energy content and reactivity, which may have various applications in medicine such as wound healing and surgical procedures, but it is not a medical diagnosis or disease.
A CALCIUM-dependent, constitutively-expressed form of nitric oxide synthase found primarily in NERVE TISSUE.
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 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.
A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
Methionine Sulfoximine is a toxic compound that functions as an inhibitor of methionine metabolism, being formed through the oxidation of methionine by the enzyme methionine sulfoxide reductase.
The process in certain BACTERIA; FUNGI; and CYANOBACTERIA converting free atmospheric NITROGEN to biologically usable forms of nitrogen, such as AMMONIA; NITRATES; and amino compounds.
Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
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)
Drugs that bind to but do not activate excitatory amino acid receptors, thereby blocking the actions of agonists.
A glutamate plasma membrane transporter protein found in ASTROCYTES and in the LIVER.
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.
Derivatives of OXALOACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include a 2-keto-1,4-carboxy aliphatic structure.
A vesicular glutamate transporter protein that is predominately expressed in the DIENCEPHALON and lower brainstem regions of the CENTRAL NERVOUS SYSTEM.
A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Drugs that bind to and activate excitatory amino acid receptors.
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).
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
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.
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.
Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.
A genus of gram-negative, rod-shaped bacteria that derives energy from the oxidation of one or more reduced sulfur compounds. Many former species have been reclassified to other classes of PROTEOBACTERIA.
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.
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
A species of bacteria whose spores vary from round to elongate. It is a common soil saprophyte.
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.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.
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.
A species of gram-positive bacteria that is a common soil and water saprophyte.
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.
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
The functional hereditary units of BACTERIA.
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.

Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism. (1/194)

We have isolated mutant strains (nit) of Salmonella typhimurium that are defective in nitrogen metabolism. They have a reduced ability to use a variety of compounds including glutamate, proline, arginine, N-acetyl-glucosamine, alanine, and adenosine as sole nitrogen source. In addition, although they grow normally on high concentrations of ammonium chloride (greater than 1 mM) as nitrogen source, they grow substantially more slowly than wild type at low concentrations (less than 1 mM). We postulated that the inability of these strains to utilize low concentrations of ammonium chloride accounts for their poor growth on other nitrogen sources. The specific biochemical lesion in strains with a nit mutation is not known; however, mutant strains have no detectable alteration in the activities of glutamine synthetase, glutamate synthetase, or glutamate dehydrogenase, the enzymes known to be involved in assimilation of ammonia. A nit mutation is suppressed by second-site mutations in the structural gene for glutamine synthetase (glnA) that decrease glutamine synthetase activity.  (+info)

Carbon and ammonia metabolism of Spirillum lipoferum. (2/194)

Intact cells and extracts from Spirillum lipoferum rapidly oxidized malate, succinate, lactate, and pyruvate. Glucose, galactose, fructose, acetate, and citrate did not increase the rate of O2 uptake by cells above the endogenous rate. Cells grown on NH+/4 oxidized the various substrates at about the same rate as did cells grown on N2. Added oxidized nicotinamide adenine dinucleotide generally enhanced O2 uptake by extracts supplied organic acids, whereas oxidized nicotinamide adenine dinucleotide phosphate had little effect. Nitrogenase synthesis repressed by growth of cells in the presence of NH+/4 was derepressed by methionine sulfoximine or methionine sulfone. The total glutamine synthetase activity from N2-grown cells was about eight times that from NH+/4-grown S. lipoferum; the response of glutamate dehydrogenase was the opposite. The total glutamate synthetase activity from N2-grown S. lipoferum was 1.4 to 2.6 times that from NH+/4-grown cells. The levels of poly-beta-hydroxybutyrate and beta-hydroxybutyrate dehydrogenase were elevated in cells grown on N2 as compared with those grown on NH+/4. Cell-free extracts capable of reducing C2H2 have been prepared; both Mg2+ and Mn2+ are required for good activity.  (+info)

Inorganic nitrogen assimilation by the photosynthetic bacterium Rhodopseudomonas capsulata. (3/194)

The photosynthetic bacterium Rhodopseudomonas capsulata lacks glutamate dehydrogenase and normally uses the glutamine synthetase/glutamate synthase sequence of reactions for assimilation of N2 and ammonia. The glutamine synthetase in cell-free extracts of the organism is completely sedimented by centrifugation at 140,000 X g for 2 h, is inhibited by L-alanine but not by adenosine 5'-monophosphate, and exhibits two apparent Km values for ammonia (ca. 13 muM and 1 mM).  (+info)

Dynamics of correlated genetic systems. IV. Multilocus effects of ethanol stress environments. (4/194)

Four replicate populations of Drosophila melanogaster, two reared on medium supplemented with ethanol and two reared on standard medium, were electrophoretically monitored for 28 generations. During the first 12 generations, allelic, genotypic and gametic frequencies were determined for eight polymorphic enzymes: GOT, alpha-GPDH, MDH, ADH, TO, E6, Ec and ODH. Samples from generation 18 and 28 were electrophoretically typed for ADH and alpha-GPDH. In addition, samples from generation 27 were analyzed for the presence of inversion heterozygotes. The experimental results showed rapid gene-frequency divergence between control and treatment populations at the Adh locus in a direction consistent with the activity hierarchy of Adh genotypes. Gene-frequency divergence between control and treatment populations also occurred at the alpha-Gpdh locus, although the agreement among replicates appeared to have broken down by generation 28. No differential gene-frequency change occurred at any of the six remaining marker loci. Furthermore, values of linkage disequilibria among all linked pairs of genes were initially small and remained small throughout the course of the experiment. Taking these facts into account, it is argued that the gene-frequency response observed at ADH is most probably caused by selection at the Adh locus. The gene frequency response at alpha-Gpdh can also be be accounted for in terms of the effect of ethanol on energy metabolism, although other explanations cannot be excluded.  (+info)

Pathways for glutamate biosynthesis in the yeast Kluyveromyces lactis. (5/194)

Purified glutamate synthase (GOGAT) from Kluyveromyces lactis was characterized as a high-molecular-mass polypeptide, a distinction shared with previously described GOGATs from other eukaryotic micro-organisms. Using degenerate deoxyoligonucleotides, designed from conserved regions of the alfalfa, maize and Escherichia coli GOGAT genes, a 300 bp PCR fragment from the K. lactis GOGAT gene KIGLT1 was obtained. This fragment was used to construct null GOGAT mutants of K. lactis by gene replacement. These mutants showed no growth defect phenotype and were able to grow on ammonium as sole nitrogen source. Double mutants obtained from a cross between a previously described KIGDH1 mutant and the K. lactis null GOGAT strain were full glutamate auxotrophs. These results indicate that glutamate biosynthesis in K. lactis is afforded through the combined action of KIGDH1 and KIGLT1 products.  (+info)

Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein. (6/194)

Azospirillum brasilense glutamate synthase is a complex iron-sulfur flavoprotein that catalyses the NADPH-dependent reductive transfer of glutamine amide group to the C(2) carbon of 2-oxoglutarate to yield L-glutamate. Its catalytically active alphabeta protomer is composed of two dissimilar subunits (alpha subunit, 164.2 kDa; beta subunit, 52.3 kDa) and contains one FAD (at Site 1, the pyridine nucleotide site within the beta subunit), one FMN (at Site 2, the 2-oxoglutarate/L-glutamate site in the alpha subunit) and three different iron-sulfur clusters (one 3Fe-4S center on the alpha subunit and two 4Fe-4S clusters of unknown location). A plasmid harboring the gltD and gltB genes, the genes encoding the glutamate synthase beta and alpha subunits, respectively, each one under the control of the T7/lac promoter of pET11a was found to be suitable for the overproduction of glutamate synthase holoenzyme in Escherichia coli BL21(DE3) cells. Recombinant A. brasilense glutamate synthase could be purified to homogeneity from overproducing E. coli cells by ion exchange chromatography, gel filtration and affinity chromatography on a 2',5' ADP-Sepharose 4B column. The purified enzyme was indistinguishable from that prepared from Azospirillum cells with respect to cofactor content, N-terminal sequence of the subunits, aggregation state, kinetic and spectroscopic properties. The study of the recombinant holoenzyme allowed us to establish that the tendency of glutamate synthase to form a stable (alphabeta)4 tetramer at high protein concentrations is a property unique to the holoenzyme, as the isolated beta subunit does not oligomerize, while the isolated glutamate synthase alpha subunit only forms dimers at high protein concentrations. Furthermore, the steady-state kinetic analysis of the glutamate synthase reaction was extended to the study of the effect of adenosine-containing nucleotides. Compounds such as cAMP, AMP, ADP and ATP have no effect on the enzyme activity, while the 2'-phosphorylated analogs of AMP and NADP(H) analogs act as inhibitors of the reaction, competitive with NADPH. Thus, it can be ruled out that glutamate synthase reaction is subjected to allosteric modulation by adenosine containing (di)nucleotides, which may bind to the putative ADP-binding site at the C-terminus of the alpha subunit. At the same time, the strict requirement of a 2'-phosphate group in the pyridine nucleotide for binding to glutamate synthase (GltS) was established. Finally, by comparing the inhibition constants exhibited by a series of NADP+ analogs, the contribution to the binding energy of the various parts of the pyridine nucleotide has been determined along with the effect of substituents on the 3 position of the pyridine ring. With the exception of thio-NADP+, which binds the tightest to GltS, it appears that the size of the substituent is the factor that affects the most the interaction between the NADP(H) analog and the enzyme.  (+info)

Inactivation of gltB abolishes expression of the assimilatory nitrate reductase gene (nasB) in Pseudomonas putida KT2442. (7/194)

By using mini-Tn5 transposon mutagenesis, random transcriptional fusions of promoterless bacterial luciferase, luxAB, to genes of Pseudomonas putida KT2442 were generated. Insertion mutants that responded to ammonium deficiency by induction of bioluminescence were selected. The mutant that responded most strongly was genetically analyzed and is demonstrated to bear the transposon within the assimilatory nitrate reductase gene (nasB) of P. putida KT2442. Genetic evidence as well as sequence analyses of the DNA regions flanking nasB suggest that the genes required for nitrate assimilation are not clustered. We isolated three second-site mutants in which induction of nasB expression was completely abolished under nitrogen-limiting conditions. Nucleotide sequence analysis of the chromosomal junctions revealed that in all three mutants the secondary transposon had inserted at different sites in the gltB gene of P. putida KT2442 encoding the major subunit of the glutamate synthase. A detailed physiological characterization of the gltB mutants revealed that they are unable to utilize a number of potential nitrogen sources, are defective in the ability to express nitrogen starvation proteins, display an aberrant cell morphology under nitrogen-limiting conditions, and are impaired in the capacity to survive prolonged nitrogen starvation periods.  (+info)

Role of GOGAT in carbon and nitrogen partitioning in Rhizobium etli. (8/194)

The isolation and characterization of a Rhizobium etli glutamate auxotroph, TAD12, harbouring a single Tn5 insertion, is reported. This mutant produced no detectable glutamate synthase (GOGAT) activity. The cloning and physical characterization of a 7.2 kb fragment of R. etli DNA harbouring the structural genes gltB and gltD encoding the two GOGAT subunits GltB and GltD is also reported. In comparison with the wild-type strain (CFN42), the GOGAT mutant strain utilized less succinate and glutamate and grew less with this and other amino acids as nitrogen source. R. etli assimilates ammonium by the glutamine synthetase (GS)-GOGAT pathway and a GOGAT mutant prevents the cycling of glutamine by this pathway, something that impairs nitrogen and carbon metabolism and explains the decrease in the amino-nitrogen during exponential growth, with glutamate as nitrogen source. GOGAT activity also has a role in ammonium turnover and in the synthesis of amino acids and proteins, processes that are necessary to sustain cell viability in non-growing conditions. The assimilation of ammonium is important during symbiosis and glutamate constitutes 20-40% of the total amino-nitrogen. In symbiosis, the blockage of ammonium assimilation by a GOGAT mutation significantly decreases the amino-nitrogen pool of the bacteroids and may explain why more N(2) is fixed in ammonium, excreted to the plant cell, transported to the leaves and stored in the seeds.  (+info)

Glutamate synthase is an enzyme found in bacteria, plants, and some animals that plays a crucial role in the synthesis of the amino acid glutamate. There are two types of glutamate synthases: NADPH-dependent and NADH-dependent.

The NADPH-dependent glutamate synthase, also known as glutamine:2-oxoglutarate aminotransferase or GOGAT, catalyzes the following reversible reaction:

glutamine + 2-oxoglutarate -> 2 glutamate

This enzyme requires NADPH as a cofactor and is responsible for the conversion of glutamine and 2-oxoglutarate to two molecules of glutamate. This reaction is essential in the assimilation of ammonia into organic compounds, particularly in plants and some bacteria.

The NADH-dependent glutamate synthase, on the other hand, is found mainly in animals and catalyzes a different set of reactions that involve the conversion of L-glutamate to α-ketoglutarate and ammonia, with the concomitant reduction of NAD+ to NADH.

Both types of glutamate synthases are essential for maintaining the balance of nitrogen metabolism in living organisms.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Glutamates are the salt or ester forms of glutamic acid, which is a naturally occurring amino acid and the most abundant excitatory neurotransmitter in the central nervous system. Glutamate plays a crucial role in various brain functions, such as learning, memory, and cognition. However, excessive levels of glutamate can lead to neuronal damage or death, contributing to several neurological disorders, including stroke, epilepsy, and neurodegenerative diseases like Alzheimer's and Parkinson's.

Glutamates are also commonly found in food as a natural flavor enhancer, often listed under the name monosodium glutamate (MSG). While MSG has been extensively studied, its safety remains a topic of debate, with some individuals reporting adverse reactions after consuming foods containing this additive.

'Azospirillum brasilense' is a species of free-living, nitrogen-fixing bacteria that is commonly found in the soil and in the roots of various plants. It belongs to the genus Azospirillum and is known for its ability to promote plant growth through a process called bacterial colonization. The bacteria colonize the root system of the plant and enhance nutrient uptake, leading to improved growth and yield. Additionally, 'Azospirillum brasilense' can convert atmospheric nitrogen into ammonia, making it available to the plants as a natural fertilizer. It is widely used in agricultural practices as a bioinoculant to improve crop productivity and sustainability.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

Glutamate-ammonia ligase, also known as glutamine synthetase, is an enzyme that plays a crucial role in nitrogen metabolism. It catalyzes the formation of glutamine from glutamate and ammonia in the presence of ATP, resulting in the conversion of ammonia to a less toxic form. This reaction is essential for maintaining nitrogen balance in the body and for the synthesis of various amino acids, nucleotides, and other biomolecules. The enzyme is widely distributed in various tissues, including the brain, liver, and muscle, and its activity is tightly regulated through feedback inhibition by glutamine and other metabolites.

Glutamic acid is an alpha-amino acid, which is one of the 20 standard amino acids in the genetic code. The systematic name for this amino acid is (2S)-2-Aminopentanedioic acid. Its chemical formula is HO2CCH(NH2)CH2CH2CO2H.

Glutamic acid is a crucial excitatory neurotransmitter in the human brain, and it plays an essential role in learning and memory. It's also involved in the metabolism of sugars and amino acids, the synthesis of proteins, and the removal of waste nitrogen from the body.

Glutamic acid can be found in various foods such as meat, fish, beans, eggs, dairy products, and vegetables. In the human body, glutamic acid can be converted into gamma-aminobutyric acid (GABA), another important neurotransmitter that has a calming effect on the nervous system.

Glutamate receptors are a type of neuroreceptor in the central nervous system that bind to the neurotransmitter glutamate. They play a crucial role in excitatory synaptic transmission, plasticity, and neuronal development. There are several types of glutamate receptors, including ionotropic and metabotropic receptors, which can be further divided into subclasses based on their pharmacological properties and molecular structure.

Ionotropic glutamate receptors, also known as iGluRs, are ligand-gated ion channels that directly mediate fast synaptic transmission. They include N-methyl-D-aspartate (NMDA) receptors, α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, and kainite receptors.

Metabotropic glutamate receptors, also known as mGluRs, are G protein-coupled receptors that modulate synaptic transmission through second messenger systems. They include eight subtypes (mGluR1-8) that are classified into three groups based on their sequence homology, pharmacological properties, and signal transduction mechanisms.

Glutamate receptors have been implicated in various physiological processes, including learning and memory, motor control, sensory perception, and emotional regulation. Dysfunction of glutamate receptors has also been associated with several neurological disorders, such as epilepsy, Alzheimer's disease, Parkinson's disease, and psychiatric conditions like schizophrenia and depression.

Glutamine is defined as a conditionally essential amino acid in humans, which means that it can be produced by the body under normal circumstances, but may become essential during certain conditions such as stress, illness, or injury. It is the most abundant free amino acid found in the blood and in the muscles of the body.

Glutamine plays a crucial role in various biological processes, including protein synthesis, energy production, and acid-base balance. It serves as an important fuel source for cells in the intestines, immune system, and skeletal muscles. Glutamine has also been shown to have potential benefits in wound healing, gut function, and immunity, particularly during times of physiological stress or illness.

In summary, glutamine is a vital amino acid that plays a critical role in maintaining the health and function of various tissues and organs in the body.

Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.

In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.

Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.

Metabotropic glutamate receptors (mGluRs) are a type of G protein-coupled receptor (GPCR) that are activated by the neurotransmitter glutamate, which is the primary excitatory neurotransmitter in the central nervous system. There are eight different subtypes of mGluRs, labeled mGluR1 through mGluR8, which are classified into three groups (Group I, II, and III) based on their sequence homology, downstream signaling pathways, and pharmacological properties.

Group I mGluRs include mGluR1 and mGluR5, which are primarily located postsynaptically in the central nervous system. Activation of Group I mGluRs leads to increased intracellular calcium levels and activation of protein kinases, which can modulate synaptic transmission and plasticity.

Group II mGluRs include mGluR2 and mGluR3, which are primarily located presynaptically in the central nervous system. Activation of Group II mGluRs inhibits adenylyl cyclase activity and reduces neurotransmitter release.

Group III mGluRs include mGluR4, mGluR6, mGluR7, and mGluR8, which are also primarily located presynaptically in the central nervous system. Activation of Group III mGluRs inhibits adenylyl cyclase activity and voltage-gated calcium channels, reducing neurotransmitter release.

Overall, metabotropic glutamate receptors play important roles in modulating synaptic transmission and plasticity, and have been implicated in various neurological disorders, including epilepsy, pain, anxiety, depression, and neurodegenerative diseases.

Amino acid oxidoreductases are a class of enzymes that catalyze the reversible oxidation and reduction reactions involving amino acids. They play a crucial role in the metabolism of amino acids by catalyzing the interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing a cofactor such as NAD(P)+ or FAD.

The reaction catalyzed by these enzymes can be represented as follows:

L-amino acid + H2O + Coenzyme (Oxidized) → α-keto acid + NH3 + Coenzyme (Reduced)

Amino acid oxidoreductases are classified into two main types based on their cofactor requirements and reaction mechanisms. The first type uses FAD as a cofactor and is called amino acid flavoprotein oxidoreductases. These enzymes typically catalyze the oxidative deamination of L-amino acids to form α-keto acids, ammonia, and reduced FAD. The second type uses pyridine nucleotides (NAD(P)+) as cofactors and is called amino acid pyridine nucleotide-dependent oxidoreductases. These enzymes catalyze the reversible interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing or oxidizing NAD(P)H/NAD(P)+.

Amino acid oxidoreductases are widely distributed in nature and play important roles in various biological processes, including amino acid catabolism, nitrogen metabolism, and the biosynthesis of various secondary metabolites. Dysregulation of these enzymes has been implicated in several diseases, including neurodegenerative disorders and cancer. Therefore, understanding the structure, function, and regulation of amino acid oxidoreductases is crucial for developing novel therapeutic strategies to treat these diseases.

Nitrogen is not typically referred to as a medical term, but it is an element that is crucial to medicine and human life.

In a medical context, nitrogen is often mentioned in relation to gas analysis, respiratory therapy, or medical gases. Nitrogen (N) is a colorless, odorless, and nonreactive gas that makes up about 78% of the Earth's atmosphere. It is an essential element for various biological processes, such as the growth and maintenance of organisms, because it is a key component of amino acids, nucleic acids, and other organic compounds.

In some medical applications, nitrogen is used to displace oxygen in a mixture to create a controlled environment with reduced oxygen levels (hypoxic conditions) for therapeutic purposes, such as in certain types of hyperbaric chambers. Additionally, nitrogen gas is sometimes used in cryotherapy, where extremely low temperatures are applied to tissues to reduce pain, swelling, and inflammation.

However, it's important to note that breathing pure nitrogen can be dangerous, as it can lead to unconsciousness and even death due to lack of oxygen (asphyxiation) within minutes.

2,6-Dichloroindophenol is a chemical compound that is used as an indicator in various analytical procedures, particularly in the field of biochemistry and microbiology. It is a derivative of indophenol, which contains two chlorine atoms at the 2nd and 6th positions of the benzene ring.

The chemical formula for 2,6-Dichloroindophenol is C8H6Cl2O2. This compound is a deep blue color in its oxidized state and turns colorless when reduced. The reduction potential of this compound makes it useful as an indicator in various redox reactions, including the determination of the concentration of reducing agents such as ascorbic acid (vitamin C) and other antioxidants.

It is important to note that 2,6-Dichloroindophenol is a hazardous chemical and should be handled with care. It can cause skin and eye irritation, and prolonged exposure may lead to more serious health effects. Therefore, it is essential to follow proper safety precautions when working with this compound.

Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer reactions in various biological systems, particularly in photosynthesis and nitrogen fixation. They contain one or more clusters of iron and sulfur atoms (known as the iron-sulfur cluster) that facilitate the movement of electrons between different molecules during metabolic processes.

Ferredoxins have a relatively simple structure, consisting of a polypeptide chain that binds to the iron-sulfur cluster. This simple structure allows ferredoxins to participate in a wide range of redox reactions and makes them versatile electron carriers in biological systems. They can accept electrons from various donors and transfer them to different acceptors, depending on the needs of the cell.

In photosynthesis, ferredoxins play a critical role in the light-dependent reactions by accepting electrons from photosystem I and transferring them to NADP+, forming NADPH. This reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) is then used in the Calvin cycle for carbon fixation and the production of glucose.

In nitrogen fixation, ferredoxins help transfer electrons to the nitrogenase enzyme complex, which reduces atmospheric nitrogen gas (N2) into ammonia (NH3), making it available for assimilation by plants and other organisms.

Overall, ferredoxins are essential components of many metabolic pathways, facilitating electron transfer and energy conversion in various biological systems.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Azaserine is a antineoplastic and antibiotic agent. Its chemical name is O-diazoacetyl-L-serine. It is an analog of the amino acid serine, which inhibits the enzyme necessary for the synthesis of DNA and RNA, thus preventing the growth of cancer cells. Azaserine is used in research but not in clinical medicine due to its high toxicity.

Sodium glutamate, also known as monosodium glutamate (MSG), is the sodium salt of glutamic acid, which is a naturally occurring amino acid that is widely present in various foods. It is commonly used as a flavor enhancer in the food industry to intensify the savory or umami taste of certain dishes.

Medically speaking, sodium glutamate is generally considered safe for consumption in moderate amounts by the majority of the population. However, some individuals may experience adverse reactions after consuming foods containing MSG, a condition known as "MSG symptom complex." Symptoms can include headache, flushing, sweating, facial pressure or tightness, numbness, tingling or burning in the face, neck and other areas, rapid, fluttering heartbeats (heart palpitations), chest pain, nausea, and weakness.

It is important to note that these symptoms are usually mild and short-term, and not everyone who consumes MSG will experience them. If you suspect that you have an intolerance or sensitivity to MSG, it is best to consult with a healthcare professional for proper evaluation and guidance.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

I am not aware of a medical definition for an "amino acid transport system X-AG" as it is not a widely recognized or established term in the field of medicine or biology. It is possible that you may have misspelled or mistyped the name, as there are several known amino acid transporters labeled with different letters and numbers (e.g., Systems A, ASC, L, y+L).

If you meant to inquire about a specific amino acid transport system or a particular research study related to it, please provide more context or clarify the term so I can give you an accurate and helpful response.

Diazoxide is a medication that is used to treat hypoglycemia (low blood sugar) in certain circumstances, such as in patients with pancreatic tumors or other conditions that cause excessive insulin production. Diazooxonorleucine is not a recognized medical term or a known medication. It appears that there may be some confusion regarding the name of this compound.

Diazoxide itself is a vasodilator, which means it works by relaxing and widening blood vessels. This can help to lower blood pressure and improve blood flow to various parts of the body. Diazoxide is typically given intravenously (through an IV) in a hospital setting.

It's possible that "diazooxonorleucine" may be a typographical error or a misunderstanding of the name of a different compound. If you have more information about where you encountered this term, I may be able to provide further clarification.

Glutaminase is an enzyme that catalyzes the conversion of L-glutamine, which is a type of amino acid, into glutamate and ammonia. This reaction is an essential part of nitrogen metabolism in many organisms, including humans. There are several forms of glutaminase found in different parts of the body, with varying properties and functions.

In humans, there are two major types of glutaminase: mitochondrial and cytosolic. Mitochondrial glutaminase is primarily found in the kidneys and brain, where it plays a crucial role in energy metabolism by converting glutamine into glutamate, which can then be further metabolized to produce ATP (adenosine triphosphate), a major source of cellular energy.

Cytosolic glutaminase, on the other hand, is found in many tissues throughout the body and is involved in various metabolic processes, including nucleotide synthesis and protein degradation.

Glutaminase activity has been implicated in several disease states, including cancer, where some tumors have been shown to have elevated levels of glutaminase expression, allowing them to use glutamine as a major source of energy and growth. Inhibitors of glutaminase are currently being investigated as potential therapeutic agents for the treatment of cancer.

Dimethyl suberimidate is a homobifunctional cross-linking agent that is used in molecular biology for protein-protein or protein-nucleic acid cross-linking. It is an imidoester with the chemical formula (CH3)2N-CO-[CH2]8-CO-N(CH3)2.

This reagent works by reacting with primary amines (-NH2) on proteins or nucleic acids, forming stable amide bonds between them. The length of the spacer arm (comprising eight methylene groups) provides sufficient distance and flexibility for the cross-linked molecules to maintain their native structures and functions.

Dimethyl suberimidate is used in various applications, such as studying protein-protein interactions, mapping protein domains, and analyzing protein complexes' structures. It is crucial to perform cross-linking reactions under controlled conditions to ensure specificity and minimize non-specific binding.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Quaternary ammonium compounds (QACs) are a group of disinfectants and antiseptics that contain a nitrogen atom surrounded by four organic groups, resulting in a charged "quat" structure. They are widely used in healthcare settings due to their broad-spectrum activity against bacteria, viruses, fungi, and spores. QACs work by disrupting the cell membrane of microorganisms, leading to their death. Common examples include benzalkonium chloride and cetyltrimethylammonium bromide. It is important to note that some microorganisms have developed resistance to QACs, and they may not be effective against all types of pathogens.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Glutamate plasma membrane transport proteins, also known as excitatory amino acid transporters (EAATs), are a type of membrane protein responsible for the uptake of glutamate from the extracellular space into neurons and glial cells in the central nervous system. These transporters play a crucial role in maintaining appropriate levels of glutamate, an important neurotransmitter, in the synaptic cleft to prevent excitotoxicity and ensure normal neurotransmission. There are five subtypes of EAATs (EAAT1-EAAT5) identified in mammals, each with distinct expression patterns and functions.

A metabotropic glutamate receptor 5 (mGluR5) is a type of G protein-coupled receptor that binds to the neurotransmitter glutamate, which is the primary excitatory neurotransmitter in the brain. When activated, mGluR5 receptors trigger a variety of intracellular signaling pathways that modulate synaptic transmission, neuronal excitability, and neural plasticity.

mGluR5 receptors are widely expressed throughout the central nervous system, where they play important roles in various physiological processes, including learning and memory, anxiety, addiction, and pain perception. Dysregulation of mGluR5 signaling has been implicated in several neurological and psychiatric disorders, such as fragile X syndrome, Parkinson's disease, schizophrenia, and drug addiction.

Pharmacological targeting of mGluR5 receptors has emerged as a promising therapeutic strategy for the treatment of these disorders. Positive allosteric modulators (PAMs) of mGluR5 have shown potential in preclinical studies for improving cognitive function and reducing negative symptoms in schizophrenia, while negative allosteric modulators (NAMs) have shown promise in preclinical models of fragile X syndrome, Parkinson's disease, and addiction.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Glycogen synthase is an enzyme (EC 2.4.1.11) that plays a crucial role in the synthesis of glycogen, a polysaccharide that serves as the primary storage form of glucose in animals, fungi, and bacteria. This enzyme catalyzes the transfer of glucosyl residues from uridine diphosphate glucose (UDP-glucose) to the non-reducing end of an growing glycogen chain, thereby elongating it.

Glycogen synthase is regulated by several mechanisms, including allosteric regulation and covalent modification. The activity of this enzyme is inhibited by high levels of intracellular glucose-6-phosphate (G6P) and activated by the binding of glycogen or proteins that bind to glycogen, such as glycogenin. Phosphorylation of glycogen synthase by protein kinases, like glycogen synthase kinase-3 (GSK3), also reduces its activity, while dephosphorylation by protein phosphatases enhances it.

The regulation of glycogen synthase is critical for maintaining glucose homeostasis and energy balance in the body. Dysregulation of this enzyme has been implicated in several metabolic disorders, including type 2 diabetes and non-alcoholic fatty liver disease (NAFLD).

I am sorry for any confusion, but "Pentanoic Acids" is not a recognized medical term or concept. Pentanoic acid, also known as valeric acid, is an organic compound with the formula CH3CH2CH2CH2CO2H. It is a fatty acid with five carbon atoms, and it may have some uses in industry, but it does not have specific relevance to medical definition or healthcare.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Iron-sulfur proteins are a group of metalloproteins that contain iron and sulfur atoms in their active centers. These clusters of iron and sulfur atoms, also known as iron-sulfur clusters, can exist in various forms, including Fe-S, 2Fe-2S, 3Fe-4S, and 4Fe-4S structures. The iron atoms are coordinated to the protein through cysteine residues, while the sulfur atoms can be in the form of sulfide (S2-) or sulfane (-S-).

These proteins play crucial roles in many biological processes, such as electron transfer, redox reactions, and enzyme catalysis. They are found in various organisms, from bacteria to humans, and are involved in a wide range of cellular functions, including energy metabolism, photosynthesis, nitrogen fixation, and DNA repair.

Iron-sulfur proteins can be classified into several categories based on their structure and function, such as ferredoxins, Rieske proteins, high-potential iron-sulfur proteins (HiPIPs), and radical SAM enzymes. Dysregulation or mutations in iron-sulfur protein genes have been linked to various human diseases, including neurodegenerative disorders, cancer, and mitochondrial disorders.

Neurospora is not a medical term, but a genus of fungi commonly found in the environment. It is often used in scientific research, particularly in the fields of genetics and molecular biology. The most common species used in research is Neurospora crassa, which has been studied extensively due to its haploid nature, simple genetic structure, and rapid growth rate. Research using Neurospora has contributed significantly to our understanding of fundamental biological processes such as gene regulation, metabolism, and circadian rhythms.

Glycogen Synthase Kinase 3 (GSK-3) is a serine/threonine protein kinase that plays a crucial role in the regulation of several cellular processes, including glycogen metabolism, cell signaling, gene transcription, and apoptosis. It was initially discovered as a key enzyme involved in glycogen metabolism due to its ability to phosphorylate and inhibit glycogen synthase, an enzyme responsible for the synthesis of glycogen from glucose.

GSK-3 exists in two isoforms, GSK-3α and GSK-3β, which share a high degree of sequence similarity and are widely expressed in various tissues. Both isoforms are constitutively active under normal conditions and are regulated through inhibitory phosphorylation by several upstream signaling pathways, such as insulin, Wnt, and Hedgehog signaling.

Dysregulation of GSK-3 has been implicated in the pathogenesis of various diseases, including diabetes, neurodegenerative disorders, and cancer. In recent years, GSK-3 has emerged as an attractive therapeutic target for the development of novel drugs to treat these conditions.

Thymidylate synthase (TS) is an essential enzyme in the metabolic pathway for DNA synthesis and repair. It catalyzes the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), which is a crucial building block for DNA replication and repair. This reaction also involves the methylation of dUMP using a methyl group donated by N5,N10-methylenetetrahydrofolate, resulting in the formation of dihydrofolate as a byproduct. The regeneration of dihydrofolate to tetrahydrofolate is necessary for TS to continue functioning, making it dependent on the folate cycle. Thymidylate synthase inhibitors are used in cancer chemotherapy to interfere with DNA synthesis and replication, leading to cytotoxic effects in rapidly dividing cells.

Acetylene is defined as a colorless, highly flammable gas with a distinctive odor, having the chemical formula C2H2. It is the simplest and lightest hydrocarbon in which two carbon atoms are bonded together by a triple bond. Acetylene is used as a fuel in welding and cutting torches, and it can also be converted into other chemicals, such as vinyl acetate and acetic acid. In medical terms, acetylene is not a substance that is commonly used or discussed.

Nitric Oxide Synthase Type I, also known as NOS1 or neuronal nitric oxide synthase (nNOS), is an enzyme that catalyzes the production of nitric oxide (NO) from L-arginine. It is primarily expressed in the nervous system, particularly in neurons, and plays a crucial role in the regulation of neurotransmission, synaptic plasticity, and cerebral blood flow. NOS1 is calcium-dependent and requires several cofactors for its activity, including NADPH, FAD, FMN, and calmodulin. It is involved in various physiological and pathological processes, such as learning and memory, seizure susceptibility, and neurodegenerative disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Vesicular Glutamate Transport Proteins (VGLUTs) are a group of proteins that play a crucial role in the packaging and transport of the neurotransmitter glutamate into synaptic vesicles within neurons. Glutamate is the primary excitatory neurotransmitter in the central nervous system, and its release and uptake must be tightly regulated to maintain proper neural communication.

VGLUTs are integral membrane proteins located on the membranes of synaptic vesicles. They facilitate the accumulation of glutamate inside these vesicles through a process called antiport, where they exchange glutamate for protons from the cytoplasm. This results in a high concentration of glutamate within the vesicle, allowing for its regulated release upon neuronal stimulation.

There are three isoforms of VGLUTs (VGLUT1, VGLUT2, and VGLUT3) encoded by different genes (SLC17A7, SLC17A6, and SLC17A8, respectively). These isoforms exhibit distinct expression patterns in the central nervous system and are involved in various neurological functions. Dysregulation of VGLUTs has been implicated in several neurological disorders, including epilepsy, pain perception, and neurodegenerative diseases.

Flavin Mononucleotide (FMN) is a coenzyme that plays a crucial role in biological oxidation-reduction reactions. It is derived from the vitamin riboflavin (also known as vitamin B2) and is composed of a flavin molecule bonded to a nucleotide. FMN functions as an electron carrier, accepting and donating electrons in various metabolic pathways, including the citric acid cycle and the electron transport chain, which are essential for energy production in cells. It also participates in the detoxification of harmful substances and contributes to the maintenance of cellular redox homeostasis. FMN can exist in two forms: the oxidized form (FMN) and the reduced form (FMNH2), depending on its involvement in redox reactions.

Methionine Sulfoximine (MSO) is not a medical term itself, but it is a compound that has been used in research and scientific studies. It's a stable analogue of the essential amino acid methionine, which can be found in some foods like sesame seeds, Brazil nuts, and fish.

Methionine Sulfoximine has been used in research to study the metabolism and transport of methionine in cells and organisms. It is also known for its ability to inhibit the enzyme cystathionine β-synthase (CBS), which plays a role in the metabolism of homocysteine, an amino acid associated with cardiovascular disease when present at high levels.

However, Methionine Sulfoximine is not used as a therapeutic agent or medication in humans due to its potential toxicity and lack of established clinical benefits.

Nitrogen fixation is a process by which nitrogen gas (N2) in the air is converted into ammonia (NH3) or other chemically reactive forms, making it available to plants and other organisms for use as a nutrient. This process is essential for the nitrogen cycle and for the growth of many types of plants, as most plants cannot utilize nitrogen gas directly from the air.

In the medical field, nitrogen fixation is not a commonly used term. However, in the context of microbiology and infectious diseases, some bacteria are capable of fixing nitrogen and this ability can contribute to their pathogenicity. For example, certain species of bacteria that colonize the human body, such as those found in the gut or on the skin, may be able to fix nitrogen and use it for their own growth and survival. In some cases, these bacteria may also release fixed nitrogen into the environment, which can have implications for the ecology and health of the host and surrounding ecosystems.

Flavins are a group of naturally occurring organic compounds that contain a characteristic isoalloxazine ring, which is a tricyclic aromatic structure. The most common and well-known flavin is flavin adenine dinucleotide (FAD), which plays a crucial role as a coenzyme in various biological oxidation-reduction reactions. FAD accepts electrons and hydrogens to form the reduced form, flavin adenine dinucleotide hydride (FADH2). Another important flavin is flavin mononucleotide (FMN), which is derived from FAD and functions similarly as a coenzyme. Flavins are yellow in color and can be found in various biological systems, including animals, plants, and microorganisms. They are involved in several metabolic pathways, such as the electron transport chain, where they contribute to energy production.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Excitatory amino acid antagonists are a class of drugs that block the action of excitatory neurotransmitters, particularly glutamate and aspartate, in the brain. These drugs work by binding to and blocking the receptors for these neurotransmitters, thereby reducing their ability to stimulate neurons and produce an excitatory response.

Excitatory amino acid antagonists have been studied for their potential therapeutic benefits in a variety of neurological conditions, including stroke, epilepsy, traumatic brain injury, and neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. However, their use is limited by the fact that blocking excitatory neurotransmission can also have negative effects on cognitive function and memory.

There are several types of excitatory amino acid receptors, including N-methyl-D-aspartate (NMDA), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), and kainite receptors. Different excitatory amino acid antagonists may target one or more of these receptor subtypes, depending on their specific mechanism of action.

Examples of excitatory amino acid antagonists include ketamine, memantine, and dextromethorphan. These drugs have been used in clinical practice for various indications, such as anesthesia, sedation, and treatment of neurological disorders. However, their use must be carefully monitored due to potential side effects and risks associated with blocking excitatory neurotransmission.

Excitatory Amino Acid Transporter 2 (EAAT2) is a type of glutamate transporter protein found in the membranes of glial cells in the central nervous system. Glutamate is the primary excitatory neurotransmitter in the brain, and its levels must be carefully regulated to maintain normal neuronal function and survival. EAAT2 plays a critical role in this regulation by removing excess glutamate from the synaptic cleft and returning it to glial cells for storage or breakdown.

EAAT2 is responsible for the majority of glutamate reuptake in the brain, and its expression and function are crucial for maintaining proper neuronal excitability and preventing excitotoxicity, a form of neurodegeneration that can occur when glutamate levels become too high. Mutations or dysfunction in EAAT2 have been implicated in several neurological disorders, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and epilepsy.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Oxaloacetates are organic compounds that are integral to the Krebs cycle, also known as the citric acid cycle, in biological energy production. Specifically, oxaloacetate is an important intermediate compound within this metabolic pathway, found in the mitochondria of cells.

In the context of a medical definition, oxaloacetates are not typically referred to directly. Instead, the term "oxaloacetic acid" might be used, which is the conjugate acid of the oxaloacetate ion. Oxaloacetic acid has the chemical formula C4H4O5 and appears in various biochemical reactions as a crucial component of cellular respiration.

The Krebs cycle involves several stages where oxaloacetic acid plays a significant role:

1. In the first step, oxaloacetic acid combines with an acetyl group (derived from acetyl-CoA) to form citric acid, releasing coenzyme A in the process. This reaction is catalyzed by citrate synthase.
2. Throughout subsequent steps of the cycle, citric acid undergoes a series of reactions that generate energy in the form of NADH and FADH2 (reduced forms of nicotinamide adenine dinucleotide and flavin adenine dinucleotide, respectively), as well as GTP (guanosine triphosphate).
3. At the end of the cycle, oxaloacetic acid is regenerated to continue the process anew. This allows for continuous energy production within cells.

In summary, while "oxaloacetates" isn't a standard term in medical definitions, it does refer to an essential component (oxaloacetic acid) of the Krebs cycle that plays a critical role in cellular respiration and energy production.

Vesicular Glutamate Transport Protein 2 (VGLUT2) is a type of protein responsible for transporting the neurotransmitter glutamate from the cytoplasm into synaptic vesicles within neurons. This protein is specifically located in the presynaptic terminals and plays a crucial role in the packaging, storage, and release of glutamate, which is the primary excitatory neurotransmitter in the central nervous system.

Glutamate is involved in various physiological functions, such as learning, memory, and synaptic plasticity. Dysfunction of VGLUT2 has been implicated in several neurological disorders, including epilepsy, chronic pain, and neurodevelopmental conditions like autism and schizophrenia.

"Neurospora crassa" is not a medical term, but it is a scientific name used in the field of biology. It refers to a type of filamentous fungus that belongs to the phylum Ascomycota. This organism is commonly found in the environment and has been widely used as a model system for studying various biological processes, including genetics, cell biology, and molecular biology.

"Neurospora crassa" has a characteristic red pigment that makes it easy to identify, and it reproduces sexually through the formation of specialized structures called ascocarps or "fruiting bodies." The fungus undergoes meiosis inside these structures, resulting in the production of ascospores, which are haploid spores that can germinate and form new individuals.

The genome of "Neurospora crassa" was one of the first fungal genomes to be sequenced, and it has served as an important tool for understanding fundamental biological processes in eukaryotic cells. However, because it is not a medical term, there is no official medical definition for "Neurospora crassa."

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Excitatory amino acid agonists are substances that bind to and activate excitatory amino acid receptors, leading to an increase in the excitation or activation of neurons. The most common excitatory amino acids in the central nervous system are glutamate and aspartate.

Agonists of excitatory amino acid receptors can be divided into two main categories: ionotropic and metabotropic. Ionotropic receptors, such as N-methyl-D-aspartate (NMDA), α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), and kainite receptors, are ligand-gated ion channels that directly mediate fast excitatory synaptic transmission. Metabotropic receptors, on the other hand, are G protein-coupled receptors that modulate synaptic activity through second messenger systems.

Excitatory amino acid agonists have been implicated in various physiological and pathophysiological processes, including learning and memory, neurodevelopment, and neurodegenerative disorders such as stroke, epilepsy, and Alzheimer's disease. They are also used in research to study the functions of excitatory amino acid receptors and their roles in neuronal signaling. However, due to their potential neurotoxic effects, the therapeutic use of excitatory amino acid agonists is limited.

Vesicular Glutamate Transport Protein 1 (VGLUT1) is a type of protein responsible for transporting the neurotransmitter glutamate from the cytoplasm into synaptic vesicles within neurons. This protein plays a crucial role in the packaging and release of glutamate, which is the primary excitatory neurotransmitter in the central nervous system.

VGLUT1 is specifically expressed in the majority of glutamatergic neurons and helps regulate synaptic transmission and plasticity. Defects in VGLUT1 function have been implicated in several neurological disorders, including epilepsy, neurodevelopmental disorders, and chronic pain conditions.

AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptors are ligand-gated ion channels found in the postsynaptic membrane of excitatory synapses in the central nervous system. They play a crucial role in fast synaptic transmission and are responsible for the majority of the fast excitatory postsynaptic currents (EPSCs) in the brain.

AMPA receptors are tetramers composed of four subunits, which can be any combination of GluA1-4 (previously known as GluR1-4). When the neurotransmitter glutamate binds to the AMPA receptor, it causes a conformational change that opens the ion channel, allowing the flow of sodium and potassium ions. This leads to depolarization of the postsynaptic membrane and the generation of an action potential if the depolarization is sufficient.

In addition to their role in synaptic transmission, AMPA receptors are also involved in synaptic plasticity, which is the ability of synapses to strengthen or weaken over time in response to changes in activity. This process is thought to underlie learning and memory.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

A gene is a specific sequence of nucleotides in DNA that carries genetic information. Genes are the fundamental units of heredity and are responsible for the development and function of all living organisms. They code for proteins or RNA molecules, which carry out various functions within cells and are essential for the structure, function, and regulation of the body's tissues and organs.

Each gene has a specific location on a chromosome, and each person inherits two copies of every gene, one from each parent. Variations in the sequence of nucleotides in a gene can lead to differences in traits between individuals, including physical characteristics, susceptibility to disease, and responses to environmental factors.

Medical genetics is the study of genes and their role in health and disease. It involves understanding how genes contribute to the development and progression of various medical conditions, as well as identifying genetic risk factors and developing strategies for prevention, diagnosis, and treatment.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

N-Methyl-D-Aspartate (NMDA) receptors are a type of ionotropic glutamate receptor, which are found in the membranes of excitatory neurons in the central nervous system. They play a crucial role in synaptic plasticity, learning, and memory processes. NMDA receptors are ligand-gated channels that are permeable to calcium ions (Ca2+) and other cations.

NMDA receptors are composed of four subunits, which can be a combination of NR1, NR2A-D, and NR3A-B subunits. The binding of the neurotransmitter glutamate to the NR2 subunit and glycine to the NR1 subunit leads to the opening of the ion channel and the influx of Ca2+ ions.

NMDA receptors have a unique property in that they require both agonist binding and membrane depolarization for full activation, making them sensitive to changes in the electrical activity of the neuron. This property allows NMDA receptors to act as coincidence detectors, playing a critical role in synaptic plasticity and learning.

Abnormal functioning of NMDA receptors has been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, epilepsy, and chronic pain. Therefore, NMDA receptors are a common target for drug development in the treatment of these conditions.

Nitrates are chemical compounds that consist of a nitrogen atom bonded to three oxygen atoms (NO3-). In the context of medical science, nitrates are often discussed in relation to their use as medications or their presence in food and water.

As medications, nitrates are commonly used to treat angina (chest pain) caused by coronary artery disease. Nitrates work by relaxing and widening blood vessels, which improves blood flow and reduces the workload on the heart. Some examples of nitrate medications include nitroglycerin, isosorbide dinitrate, and isosorbide mononitrate.

In food and water, nitrates are naturally occurring compounds that can be found in a variety of vegetables, such as spinach, beets, and lettuce. They can also be present in fertilizers and industrial waste, which can contaminate groundwater and surface water sources. While nitrates themselves are not harmful, they can be converted into potentially harmful compounds called nitrites under certain conditions, particularly in the digestive system of young children or in the presence of bacteria such as those found in unpasteurized foods. Excessive levels of nitrites can react with hemoglobin in the blood to form methemoglobin, which cannot transport oxygen effectively and can lead to a condition called methemoglobinemia.

Thiobacillus is a genus of gram-negative, rod-shaped bacteria that are capable of oxidizing inorganic sulfur compounds and sulfides to produce sulfuric acid. These bacteria play a significant role in the biogeochemical cycles of sulfur and carbon, particularly in environments like soil, water, and sediments. They are widely distributed in nature and can be found in various habitats such as acid mine drainage, sewage treatment plants, and even in the human respiratory system. Some species of Thiobacillus have been used in industrial applications for the bioremediation of heavy metal-contaminated soils and wastewater treatment. However, they can also contribute to the corrosion of metals and concrete structures due to their acid production.

Enzyme repression is a type of gene regulation in which the production of an enzyme is inhibited or suppressed, thereby reducing the rate of catalysis of the chemical reaction that the enzyme facilitates. This process typically occurs when the end product of the reaction binds to the regulatory protein, called a repressor, which then binds to the operator region of the operon (a group of genes that are transcribed together) and prevents transcription of the structural genes encoding for the enzyme. Enzyme repression helps maintain homeostasis within the cell by preventing the unnecessary production of enzymes when they are not needed, thus conserving energy and resources.

Flavin-Adenine Dinucleotide (FAD) is a coenzyme that plays a crucial role in various metabolic processes, particularly in the electron transport chain where it functions as an electron carrier in oxidation-reduction reactions. FAD is composed of a flavin moiety, riboflavin or vitamin B2, and adenine dinucleotide. It can exist in two forms: an oxidized form (FAD) and a reduced form (FADH2). The reduction of FAD to FADH2 involves the gain of two electrons and two protons, which is accompanied by a significant conformational change that allows FADH2 to donate its electrons to subsequent components in the electron transport chain, ultimately leading to the production of ATP, the main energy currency of the cell.

'Bacillus megaterium' is a species of Gram-positive, rod-shaped bacteria that are widely distributed in the environment, including in soil, water, and air. They are known for their large size, with individual cells often measuring 1-2 micrometers in length and 0.5 micrometers in diameter.

'Bacillus megaterium' is a facultative anaerobe, which means that it can grow in the presence or absence of oxygen. It forms endospores, which are highly resistant to heat, radiation, and chemicals, allowing the bacteria to survive under harsh conditions for long periods of time.

These bacteria have been used in various industrial applications, such as the production of enzymes, vitamins, and other bioproducts. They are generally considered to be non-pathogenic, although there have been rare reports of infections associated with this species in immunocompromised individuals.

Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.

Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.

In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.

Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.

Nitric oxide (NO) is a molecule made up of one nitrogen atom and one oxygen atom. In the body, it is a crucial signaling molecule involved in various physiological processes such as vasodilation, immune response, neurotransmission, and inhibition of platelet aggregation. It is produced naturally by the enzyme nitric oxide synthase (NOS) from the amino acid L-arginine. Inhaled nitric oxide is used medically to treat pulmonary hypertension in newborns and adults, as it helps to relax and widen blood vessels, improving oxygenation and blood flow.

"Salmonella enterica" serovar "Typhimurium" is a subspecies of the bacterial species Salmonella enterica, which is a gram-negative, facultatively anaerobic, rod-shaped bacterium. It is a common cause of foodborne illness in humans and animals worldwide. The bacteria can be found in a variety of sources, including contaminated food and water, raw meat, poultry, eggs, and dairy products.

The infection caused by Salmonella Typhimurium is typically self-limiting and results in gastroenteritis, which is characterized by symptoms such as diarrhea, abdominal cramps, fever, and vomiting. However, in some cases, the infection can spread to other parts of the body and cause more severe illness, particularly in young children, older adults, and people with weakened immune systems.

Salmonella Typhimurium is a major public health concern due to its ability to cause outbreaks of foodborne illness, as well as its potential to develop antibiotic resistance. Proper food handling, preparation, and storage practices can help prevent the spread of Salmonella Typhimurium and other foodborne pathogens.

Excitatory Amino Acid Transporter 1 (EAAT1) is a type of glutamate transporter protein found in the membranes of glial cells in the central nervous system. Glutamate is the primary excitatory neurotransmitter in the brain, and its levels must be carefully regulated to maintain normal neuronal function and survival. EAAT1 plays a crucial role in this regulation by transporting glutamate from the synaptic cleft back into the glial cells, where it can be converted to glutamine or stored for later use. In this way, EAAT1 helps to terminate the excitatory signal and prevent excessive accumulation of glutamate in the extracellular space, which can lead to excitotoxicity and neurodegeneration. Mutations in the gene that encodes EAAT1 have been associated with certain neurological disorders, including episodic ataxia type 6 and amyotrophic lateral sclerosis (ALS).

'Bacillus subtilis' is a gram-positive, rod-shaped bacterium that is commonly found in soil and vegetation. It is a facultative anaerobe, meaning it can grow with or without oxygen. This bacterium is known for its ability to form durable endospores during unfavorable conditions, which allows it to survive in harsh environments for long periods of time.

'Bacillus subtilis' has been widely studied as a model organism in microbiology and molecular biology due to its genetic tractability and rapid growth. It is also used in various industrial applications, such as the production of enzymes, antibiotics, and other bioproducts.

Although 'Bacillus subtilis' is generally considered non-pathogenic, there have been rare cases of infection in immunocompromised individuals. It is important to note that this bacterium should not be confused with other pathogenic species within the genus Bacillus, such as B. anthracis (causative agent of anthrax) or B. cereus (a foodborne pathogen).

Glutamate decarboxylase (GAD) is an enzyme that plays a crucial role in the synthesis of the neurotransmitter gamma-aminobutyric acid (GABA) in the brain. GABA is an inhibitory neurotransmitter that helps to balance the excitatory effects of glutamate, another neurotransmitter.

Glutamate decarboxylase catalyzes the conversion of glutamate to GABA by removing a carboxyl group from the glutamate molecule. This reaction occurs in two steps, with the enzyme first converting glutamate to glutamic acid semialdehyde and then converting that intermediate product to GABA.

There are two major isoforms of glutamate decarboxylase, GAD65 and GAD67, which differ in their molecular weight, subcellular localization, and function. GAD65 is primarily responsible for the synthesis of GABA in neuronal synapses, while GAD67 is responsible for the synthesis of GABA in the cell body and dendrites of neurons.

Glutamate decarboxylase is an important target for research in neurology and psychiatry because dysregulation of GABAergic neurotransmission has been implicated in a variety of neurological and psychiatric disorders, including epilepsy, anxiety, depression, and schizophrenia.

An operon is a genetic unit in prokaryotic organisms (like bacteria) consisting of a cluster of genes that are transcribed together as a single mRNA molecule, which then undergoes translation to produce multiple proteins. This genetic organization allows for the coordinated regulation of genes that are involved in the same metabolic pathway or functional process. The unit typically includes promoter and operator regions that control the transcription of the operon, as well as structural genes encoding the proteins. Operons were first discovered in bacteria, but similar genetic organizations have been found in some eukaryotic organisms, such as yeast.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

... (NADPH) Glutamate synthase (NADH) Glutamate synthase (ferredoxin) "Phylogenetic Relationships Among ... Glutamate synthase (also known as Glutamine oxoglutarate aminotransferase) is an enzyme and frequently abbreviated as GOGAT. ... and glutamate synthase (glutamine:2-oxoglutarate aminotransferase; GOGAT). GOGAT isoenzymes catalyze the transfer of the amido ... Glutamate Synthase (GOGAT) Enzymes" Eva Zadykowicz and Deborah L. Robertson; Department of Biology, Clark University, Worcester ...
Glutamate synthase (NADH) Glutamate synthase (ferredoxin) Temple SJ, Vance CP, Gantt JS (1998). "Glutamate synthase and ... NADPH-dependent glutamate synthase, NADPH-glutamate synthase, and NADPH-linked glutamate synthase. As of late 2007, only one ... glutamate (reduced nicotinamide adenine dinucleotide phosphate), synthase, glutamate synthase (NADPH), glutamate synthetase ( ... L-glutamate synthase, L-glutamate synthetase, L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, ...
... ferredoxin-dependent glutamate synthase, ferredoxin-glutamate synthase, glutamate synthase (ferredoxin-dependent), and ... Glutamate synthase (NADH) Glutamate synthase (NADPH) Jang JE, Shaw K, Yu XJ, Petersen D, Pepper K, Lutzko C, Kohn DB (2006). " ... In enzymology, a glutamate synthase (ferredoxin) (EC 1.4.7.1) is an enzyme that catalyzes the chemical reaction 2 L-glutamate ... The systematic name of this enzyme class is L-glutamate:ferredoxin oxidoreductase (transaminating). Other names in common use ...
... synthase, glutamate synthase (NADH), L-glutamate synthetase(NADH), NADH-dependent glutamate synthase, NADH-glutamate synthase, ... Glutamate synthase (ferredoxin) Glutamate synthase (NADPH) Konishi, Noriyuki (27 February 2014). "NADH‐dependent glutamate ... In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction 2 L-glutamate + NAD+ ... which can be converted into glutamate by glutamate synthase of another pathway. These processes are common in plant roots due ...
Gottschalk G, Barker HA (1966). "Synthesis of glutamate and citrate by Clostridium kluyveri. A new type of citrate synthase". ... citrate synthase, Re-citrate-synthase, and citrate oxaloacetate-lyase [(pro-3R)-CH2COO-->acetyl-CoA]. Dittbrenner S, Chowdhury ... In enzymology, a citrate (Re)-synthase (EC 2.3.3.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O + ... Gottschalk G (1969). "Partial purification and some properties of the (R)-citrate synthase from Clostridium acidi-urici". Eur. ...
Otherwise histidine, glutamate, asparagine, cysteine are susceptible to methylation. Some of these products include S- ... Methionine synthase regenerates methionine (Met) from homocysteine (Hcy). The overall reaction transforms 5- ... "Cobalamin-Dependent and Cobalamin-Independent Methionine Synthases: Are There Two Solutions to the Same Chemical Problem?". ...
L-glutamate The 3 substrates of this enzyme are ATP, aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, ... In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical ... phosphate, asparaginyl-tRNA(Asn), and L-glutamate. This enzyme belongs to the family of ligases, specifically those forming ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Min B, Pelaschier JT, Graham DE, Tumbula ...
4 L-glutamate The four substrates of this enzyme are ATP, adenosylcobyrinic acid a,c-diamide, L-glutamine, and H2O; its four ... In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) (EC 6.3.5.10) is an enzyme that catalyzes the chemical ... products are ADP, phosphate, adenosylcobyric acid, and L-glutamate. This enzyme belongs to the family of ligases, specifically ...
L-glutamate The 3 substrates of this enzyme are ATP, glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, ... In enzymology, a glutaminyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.7) is an enzyme that catalyzes the chemical ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Horiuchi KY, Harpel MR, Shen L, Luo Y, ... phosphate, glutaminyl-tRNA(Gln), and L-glutamate. This enzyme belongs to the family of ligases, specifically those forming ...
This conversion requires the enzyme glutamate-cysteine ligase (GCL, glutamate cysteine synthase). This reaction is the rate- ... It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The ... Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS (June 1999). "Phytochelatin synthase ... Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS (June 1999). "Phytochelatin synthase ...
N-acetyl glutamate is required for the urea cycle to take place. Deficiency in N-acetylglutamate synthase or a genetic mutation ... Carbamoyl phosphate synthase 1, abbreviated as CPS1, is activated by its natural activator N-acetyl glutamate, which in turn is ... The chromosome found to be carrying the gene encoding for N-acetyl glutamate synthase is chromosome 17q (q stands for longer ... Carbamoyl phosphate synthase I is an enzyme found in mitochondrial matrix and it catalyzes the very first reaction of the urea ...
In enzymology, a γ-glutamylhistamine synthase (EC 6.3.2.18) is an enzyme that catalyzes the chemical reaction ATP + L-glutamate ... peptide synthases). The systematic name of this enzyme class is L-glutamate:histamine ligase. Other names in common use include ... L-glutamate, and histamine, whereas its two products are products of ATP breakdown and Nalpha-gamma-L-glutamylhistamine. This ...
Other names in common use include N-methylglutamate synthase, and methylamine-glutamate methyltransferase. This enzyme ... N-methyl-l-glutamate Thus, the two substrates of this enzyme are methylamine and l-glutamate, whereas its two products are NH3 ... In enzymology, a methylamine-glutamate N-methyltransferase (EC 2.1.1.21) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is methylamine:l-glutamate N-methyltransferase. ...
This is confirmed by the presence of glutamine synthetase, glutamate synthase, and alanine dehydrogenase. Since M. scandinavica ... These precursor metabolites are incorporated via the glutamate cycle and reductive amination of pyruvate. ...
... glutamine synthetase and glutamate synthase. The final product of the reactions is glutamate, which is thus normally the most ...
... coli K12 Glutamate synthase structural genes. Gene 60, 1-11. De Robertis, E.M., Oliver, G., & Wright, C.V.E. (1990). Homeobox ...
... is also involved in amino acid metabolism because it generates L-glutamate from L-glutamine. This enzyme is widely ... GMP synthase forms a tetramer in an open box shape, which is a dimer of dimers. The R interfaces are held together with a ... GMP synthase is the second step in the generation of GMP from IMP; the first step occurs when IMP dehydrogenase generates XMP, ... L-glutamate The 4 substrates of this enzyme are ATP, xanthosine 5'-phosphate, L-glutamine, and H2O, whereas its 4 products are ...
Neurosci Letters 274:167-170, 1999 Rodriguez de Turco EB, Jackson FR, DeCoster MA, Kolko M, Bazan NG: Glutamate signaling and ... Proc Natl Acad Sci 91:5252-5256, 1994 Marcheselli VL, Bazan NG: Sustained induction of prostaglandin endoperoxide synthase-2 by ... Moreover, his laboratory found that PAF modulates glutamate release and is a retrograde messenger of long-term potentiation and ... Moreover, they found that PAF activates transcription of the inducible prostaglandin synthase, cyclooxygenase-2 (COX-2). ...
... gamma-glutamate) synthetase-dihydrofolate synthase, FHFS, FHFS/FPGS, dihydropteroate:L-glutamate ligase (ADP-forming), and DHFS ... peptide synthases). The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other ... In enzymology, a dihydrofolate synthase (EC 6.3.2.12) is an enzyme that catalyzes the chemical reaction ATP + 7,8- ... Bognar AL, Osborne C, Shane B, Singer SC, Ferone R (1985). "Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase ...
... glutamate forming), aminoadipic semialdehyde synthase, saccharopine dehydrogenase (NAD+, L-glutamate-forming), 6-N-(L-1,3- ... In enzymology, a saccharopine dehydrogenase (NAD+, L-glutamate-forming) (EC 1.5.1.9) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming). ... Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and ...
... peptide synthases). The systematic name of this enzyme class is tetrahydropteroyl-gamma-polyglutamate:L-glutamate gamma-ligase ... Cichowicz DJ, Foo SK, Shane B (1981). "Folylpoly-gamma-glutamate synthesis by bacteria and mammalian cells". Mol. Cell. Biochem ... In enzymology, a tetrahydrofolate synthase (EC 6.3.2.17) is an enzyme that catalyzes the chemical reaction ATP + ... Bognar AL, Osborne C, Shane B, Singer SC, Ferone R (1985). "Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase ...
"Synthases and Ligases". IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN), and Nomenclature Commission of IUB (NC- ... Li H, Xu H, Graham DE, White RH (Aug 2003). "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic ... Glutathione synthase catalyzes the chemical reaction ATP + gamma-L-glutamyl-L-cysteine + glycine ⇌ {\displaystyle \ ... This enzyme participates in glutamate metabolism and glutathione metabolism. At least one compound, Phosphinate is known to ...
Glutamate synthase (Fd-GOGAT and NADH-GOGAT) transfer the amide group onto a 2-oxoglutarate molecule producing two glutamates. ... Lea, P. J.; Miflin, B. J. (2003). "Glutamate synthase and the synthesis of glutamate in plants". Plant Physiology and ... "Glutamine Synthetase-Glutamate Synthase Pathway and Glutamate Dehydrogenase Play Distinct Roles in the Sink-Source Nitrogen ... Ammonia (both absorbed and synthesized) is incorporated into amino acids via the glutamine synthetase-glutamate synthase (GS- ...
Delta-1-pyrroline-5-carboxylate synthase catalyzes the conversion of glutamate to delta-1-pyrroline-5-carboxylate synthase. ... Ornithine aminotransferase is an enzyme that converts arginine and ornithine into glutamate and GABA. Both of these proteins ... Mus musculus brain Some predicted proteins that interact with the human NOXRED1 are Delta-1-pyrroline-5-carboxylate synthase ...
... converts IMP into XMP GMP synthase converts XMP into GMP GMP reductase converts GMP back into IMP adenylosuccinate synthase ... PRPP + L-Glutamine + H2O → PRA + L-Glutamate + PPi In the second step react PRA, glycine and ATP to create GAR, ADP, and ... fGAR + L-Glutamine + ATP → fGAM + L-Glutamate + ADP + Pi The fifth is catalyzed by AIR synthetase (FGAM cyclase). fGAM + ATP → ... AICAR + fTHF → FAICAR + THF The last step is catalyzed by Inosine monophosphate synthase. FAICAR → IMP + H2O In eukaryotes the ...
... nitrogenase-generated ammonia is assimilated into glutamate through the glutamine synthetase/glutamate synthase pathway. The ...
"Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus ... Fahien LA, Kmiotek EH, MacDonald MJ, Fibich B, Mandic M (Aug 1988). "Regulation of malate dehydrogenase activity by glutamate, ... 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 ( ...
In the event of a mutation, the glutamate transporters are unable to pump the glutamate back into the cells; thus a higher ... via the activation of nitric oxide synthase, ultimately leading to cell death. Aβ was also found aiding this route to ... When disturbed, an accumulation of glutamate occurs as a result of a mutation in the glutamate transporters, which act like ... This causes glutamate concentration to be several times higher in the blood than in the brain; in turn, the body must act to ...
Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy Cell ... He first employed this assay to discover that endogenous NO mediates glutamate-linked increases of cyclic GMP in brain (PNAS, ... Localization of nitric oxide synthase indicating a neural role for nitric oxide Nature 347, 768 - 770 (25 October 1990). Nitric ... 8, 1995 Auxiliary subunits assist AMPA-type glutamate receptors Science March, 3, 2006 Nicotinic acetylcholine receptor redux: ...
α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate Glutamate itself is formed by amination of α-ketoglutarate: α- ... Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ... In E. coli, proline allosterically inhibits Glutamate 5-kinase which catalyzes the reaction from L-glutamate to an unstable ... ketoglutarate + NH+ 4 ⇄ glutamate The α-ketoglutarate family of amino acid synthesis (synthesis of glutamate, glutamine, ...
Glutamate synthase (NADPH) Glutamate synthase (NADH) Glutamate synthase (ferredoxin) "Phylogenetic Relationships Among ... Glutamate synthase (also known as Glutamine oxoglutarate aminotransferase) is an enzyme and frequently abbreviated as GOGAT. ... and glutamate synthase (glutamine:2-oxoglutarate aminotransferase; GOGAT). GOGAT isoenzymes catalyze the transfer of the amido ... Glutamate Synthase (GOGAT) Enzymes" Eva Zadykowicz and Deborah L. Robertson; Department of Biology, Clark University, Worcester ...
Protein target information for Glutamate synthase [NADH], putative (Plasmodium falciparum 3D7). Find diseases associated with ...
Lubeluzole, a novel long-term neuroprotectant, inhibits the glutamate-activated nitric oxide synthase pathway.. A S Lesage, L ... Lubeluzole, a novel long-term neuroprotectant, inhibits the glutamate-activated nitric oxide synthase pathway.. A S Lesage, L ... Lubeluzole, a novel long-term neuroprotectant, inhibits the glutamate-activated nitric oxide synthase pathway.. A S Lesage, L ... Lubeluzole, a novel long-term neuroprotectant, inhibits the glutamate-activated nitric oxide synthase pathway. ...
In this study, three enzymes consisting GABA pathway (isocitrate dehydrogenase, glutamate synthase and glutamate decarboxylase ... In this study, three enzymes consisting GABA pathway (isocitrate dehydrogenase, glutamate synthase and glutamate decarboxylase ... In this study, three enzymes consisting GABA pathway (isocitrate dehydrogenase, glutamate synthase and glutamate decarboxylase ... In this study, three enzymes consisting GABA pathway (isocitrate dehydrogenase, glutamate synthase and glutamate decarboxylase ...
Alfalfa NADH-dependent glutamate synthase: structure of the gene and importance in symbiotic N2 fixation. The Plant Journal. 8( ... Decreased NADH glutamate synthase activity in nodules and flowers of alfalfa (Medicago sativa L.) transformed with an antisense ... NADH-glutamate synthase in alfalfa root nodules. Genetic regulation and cellular expression. Plant Physiology. 119:817-828. [ ... glutamate synthase transgene. Journal of Experimental Botany. 51(342):29-39. [pdf 407 k] ...
... including effects on glutamate release, glutamate receptors and glutamate clearance and metabolism. This new understanding ... Recent studies have shed light on the mechanisms by which stress and glucocorticoids affect glutamate transmission, ... induces changes in glutamate neurotransmission in the prefrontal cortex and the hippocampus, thereby influencing some aspects ... Recent studies have shed light on the mechanisms by which stress and glucocorticoids affect glutamate transmission in the ...
Technical Abstract: The enzymes phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) and NADH- glutamate synthase (NADH-GOGAT, ... Title: ALFALFA ROOT NODULE PHOSPHOENOLPYRUVATE CARBOXYLASE AND NADH-GLUTAMATE SYNTHASE: CRITICAL AFFECTORS OF NITROGEN ...
Glutamine, Glutamate, Arginine. Term. How is Glutamine synthesized?. Definition. Glutamate+Ammonia, via Glutamine Synthase. ... How does heme inhibit ALA Synthase?. Definition. Blocks translation of mRNA, blocks import of ALAs into mito, destabilizes ... GABA (glutamate), Histamine (Histidine), Ethanolamine (Serine), Dopamine (DOPA), Serotonin (5HT), Putrescine (Ornithine); PLP/ ...
Regulation of the Expression of Ferredoxin Glutamate Synthase in Barley. En: Planta. 1997. Vol. 203. N m. 4. Pag. 517-525 ... Studies At the Protein and Mrna Level on the Ferredoxin-Glutamate Synthase from Leaves and Roots of Wild Type and Mutant Barley ... Association of Fd-Glutamate Synthase Activity With the Photosynthetic Electron Flow in the Green Alga Chlamydomonas Reinhardtii ... Ferredoxin Glutamate Synthase from Barley Leaves:Rapid Purification and Partial Characterization. En: Plant Physiology and ...
2000) Activation of glucose transport by AMP-activated protein kinase via stimulation of nitric oxide synthase. Diabetes 49: ... For glutamate-induced apoptosis, neurons were exposed to glutamate and glycine (100 and 10 μm) for 10 min, with (+)-5-methyl-10 ... CGNs were stimulated with glutamate (glutamate/glycine 100 μm/10 μm) for 10 min. A, Nuclei were stained with Hoechst at the ... A, Immunofluorescence of the cell surface expression of GLUT3 in sham- and glutamate- (glutamate and glycine 100 μm/10 μm, 10 ...
HMG-CoA synthase, hydroxymethyl glutaryl-CoA synthase; LC-FACS, long chain fatty acyl-CoA synthetase; LC-FFA, long chain free ... glutamate dehydrogenase; Gln, glutamine; GLS, glutaminase; Glu, glutamate; HADH, mitochondrial hydroxyacyl-coenzyme A ... HMG-CoA synthase, hydroxymethyl glutaryl-CoA synthase; LC-FACS, long chain fatty acyl-CoA synthetase; LC-FFA, long chain free ... glutamate dehydrogenase; Gln, glutamine; GLS, glutaminase; Glu, glutamate; HADH, mitochondrial hydroxyacyl-coenzyme A ...
Isolation and characterization of glutamate synthase mutants of Azospirillum brasilense. JOURNAL OF GENERAL MICROBIOLOGY, vol. ...
PDB Description: glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate ... Protein Glucosamine 6-phosphate synthase, N-terminal domain [56237] (1 species). *. Species Escherichia coli [TaxId:562] [56238 ... d1xffa_ d.153.1.1 (A:) Glucosamine 6-phosphate synthase, N-terminal domain {Escherichia coli [TaxId: 562]} ...
Kobylarz, M.J., Grigg, J.C., Liu, Y., Lee, M.S., Heinrichs, D.E., Murphy, M.E ...
Journal Article] NADH-dependent glutamate synthase plays a crucial role in assimilating ammonium in Arabidopsis root2014. *. ... Evidences supporting distinct functions of three cytosolic glutamine synthetases and two NADH-glutamate synthases in rice2014. ... Journal Article] Disruption of a novel NADH-glutamate synthase2 gene caused marked reduction in spike let number of rice2011. * ... NADH-glutamate synthase2 was tightly related to the determination of panicle number. These mutants showed metabolic disorder, ...
Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate.. Cell Mol Life Sci, 61, pp. 669-681. (2004) ... Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.. Structure ... The active conformation of glutamate synthase and its binding to ferredoxin.. J Mol Biol, 330, pp. 113-128. (2003) ... Structural studies on the synchronization of catalytic centers in glutamate synthase.. J Biol Chem, 277, pp. 24579-24583. (2002 ...
... and inducible nitric oxide synthase (iNOS), each one involved with specific events in the brain. In CNS, nNOS is involved with ... There are three isoforms of the NO synthesizing enzyme nitric oxide synthase (NOS): neuronal (nNOS), endothelial (eNOS), ... glutamate; Ins(1,4,5)P3: Inositol 1,4,5-triphosphate; CaMKII: calcium/calmodulin-dependent protein kinase II; PKA: protein ... Marletta, M. A., Hurshman, A. R., and Rusche, K. M. (1998). Catalysis by nitric oxide synthase. Curr. Opin. Chem .Biol. 2, 656- ...
Glutamate-Ammonia Ligase. *Glutamate Synthase. *Glutamate Dehydrogenase (NADP+). *Fungal Proteins. *Culture Media ... Alanine, glutamine, glutamate, arginine and ornithine.comprised over 80% of the total amino acid pool in the mycelium. Amino ... glutamate and glutamine were particularly accumulated. Of the amino acids that were initially accumulated in the mycelial mat, ...
Regulation of the Expression of Ferredoxin Glutamate Synthase in Barley. En: Planta. 1997. Vol. 203. N m. 4. Pag. 517-525 ... Studies At the Protein and Mrna Level on the Ferredoxin-Glutamate Synthase from Leaves and Roots of Wild Type and Mutant Barley ... Proteolysis of Barley (Hordeum Vulgare L.) Ferredoxin-Glutamate Synthase Affects Ferredoxin- and Methyl Viologen-Dependent ...
Part of glutamate synthase (GltAB, orange and magenta) blocks the active site of glutamate dehydrogenase (green). GltABs ... GltAB catalyzes glutamate formation, but when theres too much glutamate present, the cell shuts down GltAB but not GudB ... Bacterial enzyme pair regulates glutamate by inhibiting one of the enzymes by Celia Henry Arnaud January 5, 2022 ... Without GltAB to block it, GudB can degrade the excess glutamate (Nat. Chem. Biol. 2021, DOI: 10.1038/s41589-021-00919-y). ...
... the nitrogenase-generated ammonium is assimilated into glutamate through the glutamine synthetase/glutamate synthase pathway. ...
NMDAR1 glutamate receptor subunit isoforms in neostriatal, neocortical, and hippocampal nitric oxide synthase neurons. The ... Immunosuppressant FK506 enhances phosphorylation of nitric oxide synthase and protects against glutamate neurotoxicity. ... Immunologic NO synthase: elevation in severe AIDS dementia and induction by HIV-1 gp41. Science (New York, N.Y.). 274: 1917-21 ... Nitric oxide synthase in models of focal ischemia. Stroke; a Journal of Cerebral Circulation. 28: 1283-8. PMID 9183363 DOI: ...
... cluster in spinach glutamate synthase. Journal of Biological Chemistry 1991, 266, 15080 - 15084. ... Oxidation-reduction properties of the ferredoxin-linked glutamate synthase from spinach leaf. Biochimica et Biophysica Acta ... clusters in biotin synthase and pyruvate formate-lyase activating enzyme. Protein Science 2003, 12, 1573 - 1577. ... Recombinant Escherichia coli biotin synthase is a [2Fe-2S]2+ protein in whole cells. Febs Letters 2002, 529, 332 - 336. ...
6.3.2 Acid-D-amino-acid ligases (peptide synthases). 6.3.2.2 glutamate---cysteine ligase. 2729 (GCLC). ...
... Orphanet J Rare Dis. 2020 Oct ... Background: N-Acetylglutamate synthase (NAGS) deficiency is an extremely rare autosomal recessive metabolic disorder affecting ... Keywords: Carbaglu; Carbamylglutamate; Hyperammonemia; Inherited metabolic disorder; N-Acetylglutamate synthase; N- ... N-acetyl glutamate synthetase deficiency ...
They assimilated ammonium via the glutamate cycle enzymes glutamine synthetase and glutamate synthase. The DNA G+C contents of ... They lacked α-ketoglutarate dehydrogenase and glutamate dehydrogenase. ... They assimilated ammonium via the glutamate cycle enzymes glutamine synthetase and glutamate synthase. The DNA G+C contents of ... They lacked α-ketoglutarate dehydrogenase and glutamate dehydrogenase. ...
Tetrahydrofolate synthase.. based on mapping to UniProt P15925. ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + ... have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on ...

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