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 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)
A dye used as a reagent in the determination of vitamin C.
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 flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
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)
The rate dynamics in chemical or physical systems.
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 group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
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.
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.
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.
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.
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.
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 coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
A type I G protein-coupled receptor mostly expressed post-synaptic pyramidal cells of the cortex and CENTRAL NERVOUS SYSTEM.
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.
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 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.
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.
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 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 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 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.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A family of vesicular neurotransmitter transporter proteins that were originally characterized as sodium dependent inorganic phosphate cotransporters. Vesicular glutamate transport proteins sequester the excitatory neurotransmitter GLUTAMATE from the CYTOPLASM into SECRETORY VESICLES in exchange for lumenal PROTONS.
The process in certain BACTERIA; FUNGI; and CYANOBACTERIA converting free atmospheric NITROGEN to biologically usable forms of nitrogen, such as AMMONIA; NITRATES; and amino compounds.
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.
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.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
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.
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 sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.
A vesicular glutamate transporter protein that is predominately expressed in the DIENCEPHALON and lower brainstem regions of the CENTRAL NERVOUS SYSTEM.
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.
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.
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).
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.
Inorganic or organic salts and esters of nitric acid. These compounds contain the NO3- radical.
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 species of bacteria whose spores vary from round to elongate. It is a common soil saprophyte.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
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.
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.
Proteins found in any species of bacterium.
A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.
A species of gram-positive bacteria that is a common soil and water saprophyte.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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 glial type glutamate plasma membrane transporter protein found predominately in ASTROCYTES. It is also expressed in HEART and SKELETAL MUSCLE and in the PLACENTA.
The functional hereditary units of BACTERIA.
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.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
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.
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.

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.

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.

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.

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.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

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.

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.

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.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

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.

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.

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.

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).

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.

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.

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.

'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.

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.

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.

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.

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.

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.

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.

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.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

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.

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.

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.

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.

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.

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.

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.

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.

"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."

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.

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.

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.

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.

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.

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.

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.

'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.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

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.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

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.

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.

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.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

"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.

'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).

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

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.

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).

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.

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.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

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.

Cyanobacteria, also known as blue-green algae, are a type of bacteria that obtain their energy through photosynthesis, similar to plants. They can produce oxygen and contain chlorophyll a, which gives them a greenish color. Some species of cyanobacteria can produce toxins that can be harmful to humans and animals if ingested or inhaled. They are found in various aquatic environments such as freshwater lakes, ponds, and oceans, as well as in damp soil and on rocks. Cyanobacteria are important contributors to the Earth's oxygen-rich atmosphere and play a significant role in the global carbon cycle.

... glutamate synthase (NADH), L-glutamate synthetase(NADH), NADH-dependent glutamate synthase, NADH-glutamate synthase, and NADH- ... 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+ ... Purification and properties of NADH-dependent glutamate synthase from lupin nodules". Eur. J. Biochem. 79 (2): 355-62. doi: ...
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- ...
Glutamate synthase (NADH) Glutamate synthase (NADPH) Jang JE, Shaw K, Yu XJ, Petersen D, Pepper K, Lutzko C, Kohn DB (2006). " ... ferredoxin-dependent glutamate synthase, ferredoxin-glutamate synthase, glutamate synthase (ferredoxin-dependent), and ... 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 ...
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, ...
... glutamate synthase (NADPH) EC 1.4.1.14: glutamate synthase (NADH) EC 1.4.1.15: lysine dehydrogenase EC 1.4.1.16: ... NADH) EC 1.3.1.96: Botryococcus squalene synthase EC 1.3.1.97: botryococcene synthase EC 1.3.1.98: Now known to be catalyzed by ... pyruvate synthase EC 1.2.7.2: Now included with EC 1.2.7.1, pyruvate synthase. EC 1.2.7.3: 2-oxoglutarate synthase EC 1.2.7.4: ... berbamunine synthase EC 1.1.3.35: Now EC 1.14.21.4, salutaridine synthase EC 1.1.3.36: Now EC 1.14.21.5, (S)-canadine synthase ...
... alpha-ketoglutarate is a product of deamination of glutamate by glutamate dehydrogenase. Furthermore, genes encoding NADH ... dehydrogenase, succinate dehydrogenase, cytochrome c reductase, ATP synthase, and a terminal oxidase are found in Taylorella ... Studies show that the organic acids, malate, glutamate, and alpha-ketoglutarate serve as the main carbon sources for Taylorella ... While both malate and glutamate are TCA cycle intermediates, ...
Glutamate racemase, hydroxymethylglutaryl-CoA synthase, diphosphomevalonate decarboxylase, topoisomerase DNA gyrase B, D- ... alanine-D-serine ligase, alanine racemase, phosphate acetyltransferase, NADH peroxidase,Phosphopantetheine adenylyltransferase ...
It binds to the D subunit of ATP synthase and NADH dehydrogenase. General anaesthesia with isoflurane reduces plasma ... Isoflurane likely binds to GABA, glutamate and glycine receptors, but has different effects on each receptor. Isoflurane acts ... It inhibits receptor activity in the NMDA glutamate receptor subtypes. Isoflurane inhibits conduction in activated potassium ...
... (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 ... NADH-GOGAT is found in the nucleus of vascular plants, fungi, and diatoms, while NADPH-GOGAT is found in non-photosynthetic ...
... glutamate forming), aminoadipic semialdehyde synthase, saccharopine dehydrogenase (NAD+, L-glutamate-forming), 6-N-(L-1,3- ... L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine ... NAD+, and H2O, whereas its 4 products are L-glutamate, 2-aminoadipate 6-semialdehyde, NADH, and H+. This enzyme belongs to the ... Portal: Biology v t e (EC 1.5.1, NADH-dependent enzymes, Enzymes of unknown structure, All stub articles, Oxidoreductase stubs) ...
Homospermidine synthase proteins (EC). Homospermidine synthase (HSS) catalyses the synthesis of the polyamine homospermidine ... One domain is a Rossmann fold that binds NAD+/NADH, and the other is relatively similar. Both domains contain a six-stranded ... Kumar VP, West AH, Cook PF (June 2012). "Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of ... This protein family also includes saccharopine dehydrogenase and homospermidine synthase. It is found in prokaryotes, ...
NADH can act as an inhibitor for α-ketoglutarate, isocitrate dehydrogenase, citrate synthase, and pyruvate dehydrogenase. The ... Transamination of α-ketoglutarate produces glutamate, proline, and arginine. These amino acids are then used either within the ... The oxidation of NADH and FADH2 produces GTP from succinyl-CoA synthetase. NADH and FADH2 are produced in the matrix or ... NADH and FADH2 undergo oxidation in the electron transport chain by transferring an electrons to regenerate NAD+ and FAD. ...
... glutamate synthase (NADPH) MeSH D08.811.682.664.500.484 - glutamate synthase (NADH) MeSH D08.811.682.664.500.498 - glycine ... peptide synthases MeSH D08.811.464.259.850.400 - glutamate-cysteine ligase MeSH D08.811.464.259.850.500 - glutathione synthase ... riboflavin synthase MeSH D08.811.913.225.825 - spermidine synthase MeSH D08.811.913.225.912 - spermine synthase MeSH D08.811. ... amide synthases MeSH D08.811.464.259.200.200 - aspartate-ammonia ligase MeSH D08.811.464.259.200.600 - glutamate-ammonia ligase ...
... of the inner membrane Glutamate aspartate transporter Pyrimidine metabolism Dihydroorotate dehydrogenase Thymidylate synthase ( ... Electron transport chain NADH dehydrogenase (ubiquinone) Electron-transferring-flavoprotein dehydrogenase Electron-transferring ...
L-glutamate + (S)-2-amino-6-oxohexanoate + NADH. The native human enzyme is bifunctional, much like the LKR/SHD found in plants ... Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine ... Glutamate is an important compound within the body which acts as a neurotransmitter tied to learning and Huntington's disease. ... Alpha-aminoadipic semialdehyde synthase is encoded for by the AASS gene, and mutations in this gene lead to hyperlysinemia. ...
Due to low glutamate dehydrogenase and glutamate pyruvate transaminase activities, in tumor cells the conversion of glutamate ... Glutamine can be converted to citrate without NADH production, uncoupling NADH production from biosynthesis. Citric acid cycle ... citrate synthase, EC 2.3.3.1 The conversion of malate to pyruvate and lactate is catalyzed by NAD(P) dependent malate ... For the conversion of glutamate to α-ketoglutarate three different reactions are possible: Catalyzing enzymes: glutamate ...
Nicotinamide adenine dinucleotide exists in two related forms in the cell, NADH and NADPH. The NAD+/NADH form is more important ... Fatty acids are made by fatty acid synthases that polymerize and then reduce acetyl-CoA units. The acyl chains in the fatty ... Nitrogen is provided by glutamate and glutamine. Nonessensial amino acid synthesis depends on the formation of the appropriate ... Although some more ATP is generated in the citric acid cycle, the most important product is NADH, which is made from NAD+ as ...
... and glutamate-5-semialdehyde dehydrogenase (which requires NADH or NADPH). This can then either spontaneously cyclize to form 1 ... Ring A is synthesized from L-proline through the nonribosomal peptide synthase (NRPS) pathway (figure 2), wherein the ... Proline is biosynthetically derived from the amino acid L-glutamate. Glutamate-5-semialdehyde is first formed by glutamate 5- ... Ring A is then expanded via the polyketide synthase pathway to incorporate L-serine into ring B (figure 3). Ring A fragment is ...
The reactions related to the urea cycle produce NADH, and NADH can be produced in two different ways. One of these uses ... It is an anabolic pathway occurring in plants and bacteria utilizing the enzymes isocitrate lyase and malate synthase. Some ... Aspartate and alanine are formed from oxaloacetate and pyruvate, respectively, by transamination from glutamate. Asparagine is ... NADH reduces oxaloacetate to malate. This transformation is needed to transport the molecule out of the mitochondria. Once in ...
... glutamate; 2-OG = oxoglutarate; fdx = ferredoxin. It is probable that Natronomonas uses ferredoxin and not NADH as the electron ... which use sodium Na+ instead of protons H+ as coupling ion between respiratory chain and ATP synthase, Natronomonas uses ... which is then assimilated into glutamate: direct uptake of ammonia, uptake of nitrate and subsequent reduction to ammonia, and ...
2-oxobutyrate synthase - (2,3-dihydroxybenzoyl)adenylate synthase - 2,4-Dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase - ... NADH) - (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase - 3(or 17)a-hydroxysteroid dehydrogenase - 3110001I22Rik - 3alpha- ... glutamate-ammonia ligase) hydrolase - agarose gel electrophoresis - agarose gel - akaryocyte - Alagille syndrome - alkaline ... licodione synthase - ligase - linear epitope - linkage - linker protein - linoleate diol synthase - lipofectin - ...
The reducing agents NADH, NADPH, and FADH2, as well as metal ions, act as cofactors at various steps in anabolic pathways. NADH ... Glycogen synthase adds this UDP-glucose to a glycogen chain. Glucagon is traditionally a catabolic hormone, but also stimulates ... From the citric acid cycle, α-ketoglutarate is converted into glutamate and subsequently glutamine, proline, and arginine; and ...
In its oxidative phosphorylation pathway, the organism uses a multi-subunit NADH-quinone oxidoreductase, genes encoding ... L-glutamate, L-asparagine, L-glycine, and L-glutamine. Deinococcus marmoris is a Gram-positive, non-motile bacterium that is UV ... and citrate synthase. The D. marmoris genome also contains genes necessary for the glycolysis and gluconeogenesis pathways, ... radiodurans is fructose which undergoes several catabolic reactions to eventually the TCA cycle and produces the molecules NADH ...
... is a required co-agonist along with glutamate for NMDA receptors. In contrast to the inhibitory role of glycine in the ... The predominant pathway in animals and plants is the reverse of the glycine synthase pathway mentioned above. In this context, ... NADH + H+ In the second pathway, glycine is degraded in two steps. The first step is the reverse of glycine biosynthesis from ... In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme). This ...
... encoding enzyme subunit ATP synthase-coupling factor 6, mitochondrial ATP5PO: encoding enzyme subunit ATP synthase subunit O, ... encoding glutamate receptor ionotropic, kainate 1 H2BC12L: encoding histone H2B type F-S HLCS: encoding enzyme holocarboxylase ... encoding NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial NRIP1: nuclear receptor-interacting protein 1 OLIG1: ... encoding enzyme lanosterol synthase LTN1: encoding enzyme E3 ubiquitin-protein ligase listerin MAP3K7CL: encoding MAP3K7 C- ...
... and glutamate This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism. This enzyme belongs ... Portal: Biology v t e (EC 6.3.5, NADH-dependent enzymes, Enzymes of known structure, All stub articles, Ligase stubs). ... In enzymology, a NAD+ synthase (glutamine-hydrolysing) (EC 6.3.5.1) is an enzyme that catalyzes the chemical reaction ATP + ... deamido-NAD+ + L-glutamine + H2O ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + NAD+ + L-glutamate. In eukaryotes, ...
The NADH is produced in two ways: One NADH molecule is produced by the enzyme glutamate dehydrogenase in the conversion of ... Synthesis of NAcGlu by N-acetylglutamate synthase (NAGS) is stimulated by both Arg, allosteric stimulator of NAGS, and Glu, a ... 2 NADH The two NADH produced can provide energy for the formation of 5 ATP (cytosolic NADH provides 2.5 ATP with the malate- ... Glutamate is the non-toxic carrier of amine groups. This provides the ammonium ion used in the initial synthesis of carbamoyl ...
... like the reaction carried out by pyruvate synthase. Ferredoxin can also be reduced by using NADH (-320 mV) or H 2 (-414 mV), ... such as glutamate synthase, nitrite reductase, sulfite reductase, and the cyclase of chlorophyll biosynthesis. Since the ... Fd0 ox + NADH + Na+ outside ↽ − − ⇀ {\displaystyle {\ce {<=>}}} Fd2− red + NAD+ + Na+ inside Fd0 ox + H 2 + H+ outside ... The chemiosmotic potential of the membrane is consumed to power the unfavorable reduction of Fd ox by NADH. This reaction is an ...
D-serine is a potent agonist at the glycine site (NR1) of the NMDA-type glutamate receptor (NMDAR). For the receptor to open, ... Glycine can also be formed from CO2, NH+ 4, and mTHF in a reaction catalyzed by glycine synthase. Industrially, L-serine is ... to 3-phosphohydroxypyruvate and NADH by phosphoglycerate dehydrogenase (EC 1.1.1.95). Reductive amination (transamination) of ... glutamate and either glycine or D-serine must bind to it; in addition a pore blocker must not be bound (e.g. Mg2+ or Zn2+). In ...
Glutamate synthase catalyzes the conversion of 2-oxoglutarate into L-glutamate with L-glutamine serving as the nitrogen source ... For instance, native fluorescence of a FAD and NADH is varied in normal tissue and oral submucous fibrosis, which is an early ... All glutamate syntheses are iron-sulfur flavoproteins containing an iron-sulfur cluster and FMN. The three classes of glutamate ... The enzyme produces two glutamate molecules: one by the hydrolysis of glutamine (forming glutamate and ammonia), and the second ...
... glutamate synthase (NADH), L-glutamate synthetase(NADH), NADH-dependent glutamate synthase, NADH-glutamate synthase, and NADH- ... 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+ ... Purification and properties of NADH-dependent glutamate synthase from lupin nodules". Eur. J. Biochem. 79 (2): 355-62. doi: ...
NADH], putative (Plasmodium falciparum 3D7). Find diseases associated with this biological target and compounds tested against ...
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] ...
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 ... The NADH-GOGAT enzyme has a 101-amino acid presequence but it is unclear as to the subcellular localization of the enzyme. ... Of all the enzymes we have evaluated, to date, only NADH-GOGAT expression appears to have an absolute requirement for some ...
Studies on the in Vitro Oxygen-Dependnet Inactivation of Nadh-Glutamate Synthase from Chlamydomonas Reinhardtii Stimulated by ... Analytical and Physico-Chemical Studies of the Nadh-Glutamate Synthase from Chlamydomonas Reinhardtii. Comunicaci n en congreso ... Purification and characterization of the NADH-Glutamate Synthase from CHLAMYDOMONAS REINHARDII. En: Plant Science Letters. 1984 ... In Vitro Inactivation of the Chlamydomonas Reinhardtii Nadh-Glutamate Synthase by Reduced Pyridine Nucleotide Plus Flavin. ...
glutamate synthase [NADH], putative. 1.4.1.14. 40690. PF3D7_0720400. ferrodoxin reductase-like protein. 1.7.1.1. ... 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin), putative. 1.17.7.1. ... S-adenosyl-l-methionine-dependent trna 4-demethylwyosine synthase, putative. 4.1.3.44. ...
glutamate synthase (NADH) activity GO:0016040 * lignostilbene alpha beta-dioxygenase activity GO:0050054 ...
mitochondrial glutamate synthase complex (NADH) GO:0043294 * mitochondrial isocitrate dehydrogenase complex (NAD+) ...
NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase. ... synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; ... glutamate synthase (NADH). Reaction: 2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+. (1a) L-glutamate + NH3 = ... Other name(s): ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent ...
NADH-dependent glutamate synthase small subunit. 8.37. 0.8212. 11. sll1294 Methyl-accepting chemotaxis protein. 9.00. 0.8341. ... Carbamoyl-phosphate synthase, pyrimidine-specific, large chain. 70.01. 0.6832. 81. slr1275 Hypothetical protein. 70.82. 0.6785 ... NADH dehydrogenase subunit 4 (involved in photosystem-1 cyclic electron flow). 169.83. 0.5792. ...
GO:0043294 mitochondrial glutamate synthase complex (NADH) * GO:0042719 mitochondrial intermembrane space protein transporter ... mitochondrial glutamate synthase complex (NADH) (GO:0043294) is_a mitochondrial protein complex ...
AutoFact: glutamate synthase 1 [NADH] [Arabidopsis thaliana] ref,NP_001190529.1, glutamate synthase 1 [NADH] [Arabidopsis ... AutoFact: glutamate synthase 1 [NADH] [Arabidopsis thaliana] ref,NP_001190529.1, glutamate synthase 1 [NADH] [Arabidopsis ... Ferredoxin-dependent glutamate synthase; Glutamate synthase, large subunit region 1 and 3, putative; Glutamate synthase, ... Glutamate synthase 1 [NA 0.0 • FL-Next: sp=Glutamate synthase 1 [NADH], chloroplastic; Arabidopsis thaliana (Mouse-ear cress). ...
glutamate synthase, NADH/NADPH, small subunit (TIGR01317; EC 1.4.1.-; HMM-score: 31.6) ... Metabolism Amino acid biosynthesis Glutamate family glutamate synthase (NADPH), homotetrameric (TIGR01316; EC 1.4.1.13; HMM- ... glutamate synthase, small subunit (TIGR01318; HMM-score: 21.8) Metabolism Energy metabolism Amino acids and amines sarcosine ... Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin precorrin 3B synthase CobZ ...
glutamate synthase, NADH/NADPH, small subunit (TIGR01317; EC 1.4.1.-; HMM-score: 28) ... Metabolism Amino acid biosynthesis Glutamate family glutamate synthase (NADPH), homotetrameric (TIGR01316; EC 1.4.1.13; HMM- ... glutamate synthase, small subunit (TIGR01318; HMM-score: 32.4) mycofactocin system FadH/OYE family oxidoreductase 2 (TIGR03997 ...
Partial purification and characterization of NADH-glutamate synthase from faba bean (Vicia faba) root nodules Plant Science, ...
... expression of HpXBCP3 might improve chlorophyll content by up-regulating the expression of NADH-dependent glutamate synthases ... Nitric oxide synthase (NOS) catalyzes NO formation from the substrate l-arginine (Arg). Previously, NOS with distinct ... Nitric oxide synthases from photosynthetic organisms improve growth and confer nitrosative stress tolerance in E. coli. ...
Glutamate. 66,004. 48,568. 62,474. Glutamate synthase (ferredoxin); glutamate synthase (NADPH/NADH); glutamate N- ... acetyltransferase; glutamate decarboxylase; glutamate dehydrogenase; glutamate racemase; glutamate 5-kinase; glutamate ... Asparagine synthase; L-asparagine permease. Tyrosine. 3,592. 2,646. 3,616. Tyrosine decarboxylase; protein-tyrosine phosphatase ... Cysteine synthase; cysteine desulfurase. Alanine. 10,654. 7,352. 9,622. Alanine-synthesizing transaminase; alanine racemase; ...
"Glutamate synthase 1 [NADH], chloroplastic OS=Oryza sativa subsp. japonica (sp,q0jkd0,glt1_orysj : 111.0)" "Zm00001e006313_P001 ... ","Nitrate reductase [NADH] (Fragment) OS=Zea mays (sp,p17571,nia1_maize : 95.1)" "Zm00001e034333_P001","Zm00001e034333_P001"," ... ","Nitrate reductase [NADH] 1 OS=Oryza sativa subsp. japonica (sp,p16081,nia1_orysj : 103.0)" "Zm00001e037086_P001"," ... ","subunit alpha of tryptophan synthase complex" "Zm00001e006259_P002","Zm00001e006259_P002","No alias"," ...
"NADH-dependent glutamate synthase 1","protein_coding" "AT5G53490","No alias","Arabidopsis thaliana","Tetratricopeptide repeat ( ... ","glutamate-1-semialdehyde-2,1-aminomutase","protein_coding" "AT5G63590","FLS3","Arabidopsis thaliana","flavonol synthase 3"," ... ","ATP synthase alpha/beta family protein","protein_coding" "AT5G08680","No alias","Arabidopsis thaliana","ATP synthase alpha/ ... ","NADH-ubiquinone oxidoreductase-related","protein_coding" "AT3G03100","No alias","Arabidopsis thaliana","NADH:ubiquinone ...
L-Glutamate Synthetase use Glutamate Synthase (NADH) L-Glutamate, Aluminum use Glutamic Acid ... L Glutamate use Glutamic Acid L Glutamate Synthetase use Glutamate Synthase (NADH) ...
NADH), L-glutamate synthetase, NADH-glutamate synthase, NADH-dependent glutamate synthase, glutamate synthase (NADH). click to ... 1.4.1.14Name: glutamate synthase (NADH). Other names: glutamate (reduced nicotinamide adenine dinucleotide) synthase, NADH: ... click to see details on this item + glu-LName: L-Glutamate. Formula: C5H8NO4. Charge: -1. click to see details on this item + h ... click to see details on this item + glu-LName: L-Glutamate. Formula: C5H8NO4. Charge: -1. click to see details on this item + h ...
Glutamate Synthase (NADH) [D12.776.331.737] * Methylenetetrahydrofolate Reductase (NADPH2) [D12.776.331.775] * NADH ... NADH Diaphorase Term UI T024013. Date10/18/1974. LexicalTag ABX. ThesaurusID UNK (19XX). ... NADH Diaphorase Valine Lipoamide Dehydrogenase Registry Number. EC 1.8.1.4. Related Numbers. EC 1.8.1.4. CAS Type 1 Name. ... A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. ...
1.4.1.13 glutamate synthase (NADPH) 1.4.1.14 glutamate synthase (NADH) 1.4.1.15 lysine dehydrogenase ... 1.6 Acting on NADH or NADPH EC subclass 1.7", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px", BORDER, 1 ...
L-Glutamate Synthetase use Glutamate Synthase (NADH) L-Glutamate, Aluminum use Glutamic Acid ... L Glutamate use Glutamic Acid L Glutamate Synthetase use Glutamate Synthase (NADH) ...
L-Glutamate Synthetase use Glutamate Synthase (NADH) L-Glutamate, Aluminum use Glutamic Acid ... L Glutamate use Glutamic Acid L Glutamate Synthetase use Glutamate Synthase (NADH) ...
L-Glutamate Synthetase use Glutamate Synthase (NADH) L-Glutamate, Aluminum use Glutamic Acid ... L Glutamate use Glutamic Acid L Glutamate Synthetase use Glutamate Synthase (NADH) ...
L-Glutamate Synthetase use Glutamate Synthase (NADH) L-Glutamate, Aluminum use Glutamic Acid ... L Glutamate use Glutamic Acid L Glutamate Synthetase use Glutamate Synthase (NADH) ...
Glutamate Dehydrogenase. *Glutamate Dehydrogenase (NADP+). *Glutamate Synthase. *Glutamate Synthase (NADH). *Glycine ...
What enzyme catalyzes α-ketoglutarate → glutamate by reductive amination. Definition. Glutamate dehydrogenase (with use of NADH ... What enzyme catalyzes glutamate → glutamine? What enzyme does the reverse reaction?. Definition. Glutamine synthase (requires ... How is alanine formed from pyruvate and glutamate?. Definition. By transamination. Catalyzed by an aminotransferase, also ... Methionine synthase forms methionine from homocysteine (and FH4). Methionine adenosyl transferase converts methionine and ATP ...
Glutamate Synthase [D08.811.682.664.500.470] * Glutamate Synthase (NADH) [D08.811.682.664.500.484] * Glycine Decarboxylase ...
  • Steffen W, Gemperli AC, Cvetesic N & Steuber J. Organelle-specific expression of subunit ND5 of human complex I (NADH dehydrogenase) alters cation homeostasis in Saccharomyces cerevisiae. (uzh.ch)
  • Tao, M., Fritz, G. & Steuber, J. The Na+ -translocating NADH:quinone oxidoreductase (Na+ -NQR) from Vibrio cholerae enhances insertion of FeS in overproduced NqrF subunit. (uzh.ch)
  • protein_coding" "CCP46688","gltB","Mycobacterium tuberculosis","Probable ferredoxin-dependent glutamate synthase [NADPH] (large subunit) GltB (L-glutamate synthase) (L-glutamate synthetase) (NADH-glutamate synthase) (glutamate synthase (NADH))(NADPH-GOGAT) [Ensembl]. (ntu.edu.sg)
  • It binds to the D subunit of ATP synthase and NADH dehydrogenase . (mdwiki.org)
  • 1. Frieden, C. L -Glutamate dehydrogenase. (qmul.ac.uk)
  • 3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. (qmul.ac.uk)
  • Cytosolic malate dehydrogenase converts oxaloacetate+NADH to malate. (bioblast.at)
  • Glutamate dehydrogenase (GDH) activity (EC 1.4.1.2) GDH activity was evaluated from the decrease in OD450 as a result of NADH oxidation. (thetechnoant.info)
  • Glutamate synthase (ferredoxin) Glutamate synthase (NADPH) Konishi, Noriyuki (27 February 2014). (wikipedia.org)
  • The systematic name of this enzyme class is L-glutamate:NAD+ oxidoreductase (transaminating). (wikipedia.org)
  • Casutt MS, Huber T, Brunisholz R, Tao M, Fritz G & Steuber J. Localization and function of the membrane-bound riboflavin in the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae. (uzh.ch)
  • Tao, M., Casutt, M. & Steuber, J. Oxidant-induced formation of a neutral flavosemiquinone in the Na(+)-translocating NADH:Quinone oxidoreductase (Na(+)-NQR) from Vibrio cholerae. (uzh.ch)
  • Vgenopoulou, I., Gemperli, A. C. & Steuber, J. Specific modification of a Na+ binding site in the NADH:quinone oxidoreductase (NDH-1) from Klebsiella pneumoniae with dicyclohexylcarbodiimide. (uzh.ch)
  • Steuber, J. The Na+ -translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: implications for the mechanism of redox-driven cation translocation by complex I. (uzh.ch)
  • In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction 2 L-glutamate + NAD+ ⇌ {\displaystyle \rightleftharpoons } L-glutamine + 2-oxoglutarate + NADH + H+ Glutamate synthase facilitates the ammonium assimilation pathway, which follows the enzymes, nitrite reductase and glutamine synthase. (wikipedia.org)
  • The enzymes phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) and NADH- glutamate synthase (NADH-GOGAT, EC 1.4.1.14) are pivotal in N and C metabolism. (usda.gov)
  • Thus, the two substrates of this enzyme are L-glutamate and NAD+, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADH, and H+. (wikipedia.org)
  • This enzyme participates in glutamate metabolism and nitrogen assimilation. (wikipedia.org)
  • The NADH-GOGAT enzyme has a 101-amino acid presequence but it is unclear as to the subcellular localization of the enzyme. (usda.gov)
  • What enzyme regenerates BH4 from BH2 by use of NADH? (flashcardmachine.com)
  • What enzyme catalyzes glutamate → glutamine? (flashcardmachine.com)
  • The form is more widely occurring in nature, but the form occurs in some special contexts, such as the bacterial capsule and cell wall s of the bacteria (which produce it from the form with the enzyme glutamate racemase ) and the liver of mammals. (explained.today)
  • An enzyme encoding valencene synthase gene ( Cstps1 ) was more abundant in Temple than in Murcott. (biomedcentral.com)
  • Methionine synthase that requires cofactor methyl-Clb is important for one carbon transfer and is a key enzyme in the methionine cycle. (medscape.com)
  • Other names in common use include: glutamate (reduced nicotinamide adenine dinucleotide) synthase, glutamate synthase (NADH), L-glutamate synthetase(NADH), NADH-dependent glutamate synthase, NADH-glutamate synthase, and NADH-Glutamine oxoglutarate aminotransferase (NADH-GOGAT). (wikipedia.org)
  • An ammonium produced by the nitrite reductase reaction will be incorporated into carbon skeleton backbone by glutamine synthase. (wikipedia.org)
  • Glutamine will be produced because of the introduction of ammonium in the carbon backbone, which can be converted into glutamate by glutamate synthase of another pathway. (wikipedia.org)
  • GXGXG motif, Glutamate synthase central domain, Glutamine amidotransferases class-II, Conserved region in glutamate synthase [Interproscan]. (ntu.edu.sg)
  • Glutamate synthase central domain, Glutamine amidotransferase type 2 domain [InterProScan]. (ntu.edu.sg)
  • Decreased NADH glutamate synthase activity in nodules and flowers of alfalfa ( Medicago sativa L.) transformed with an antisense glutamate synthase transgene. (usda.gov)
  • NADH-glutamate synthase in alfalfa root nodules. (usda.gov)
  • By comparison, NADH-GOGAT transcripts are detectable in ineffective nodules at only root background levels. (usda.gov)
  • Of all the enzymes we have evaluated, to date, only NADH-GOGAT expression appears to have an absolute requirement for some factor(s) associated with effective nodules. (usda.gov)
  • We postulate that NADH-GOGAT is the limiting step in nodule N metabolism. (usda.gov)
  • Clb is a cofactor for only 2 enzymes in mammals, methionine synthase and L-methylmalonyl-CoA mutase. (medscape.com)
  • [1] the ionic form is known as glutamate ) is an α- amino acid that is used by almost all living beings in the biosynthesis of protein s. (explained.today)
  • Isoflurane likely binds to GABA , glutamate and glycine receptors, but has different effects on each receptor. (mdwiki.org)
  • hrd1_orysj : 197.0)" "Zm00001e036670_P001","Zm00001e036670_P001","No alias","Nitrate reductase [NADH] 1 OS=Oryza sativa subsp. (ntu.edu.sg)
  • Alfalfa NADH-dependent glutamate synthase: structure of the gene and importance in symbiotic N 2 fixation. (usda.gov)
  • We have isolated the alfalfa genes encoding the nodule enhanced PEPC and NADH-GOGAT. (usda.gov)
  • He then patented a method of mass-producing a crystalline salt of glutamic acid, monosodium glutamate . (explained.today)
  • Diminished methionine synthase leads to the "folate trap" in which 5-methyl-THF accumulates and cannot serve as a methyl donor and cannot be converted to the THF needed for methionine synthesis (ie, biological dead end). (medscape.com)
  • Puhar, A. & Steuber, J. NADH oxidation drives respiratory Na(+) transport in mitochondria from Yarrowia lipolytica. (uzh.ch)
  • Nitric oxide synthase (NOS) catalyzes NO formation from the substrate l-arginine (Arg). (bvsalud.org)
  • The reaction mixture contained 1?M -ketoglutarate, 7.5?mM NADH, and GDH Developer LSN 3213128 (#K729-100-3, Biovision). (thetechnoant.info)
  • B/(TV)/g wet wt, where B is amount of NADH in nmol calculated from the standard curve, T is the reaction time (in min), and V is sample volume in mL added to the reaction well. (thetechnoant.info)
  • Methyl-Clb is the cofactor for methionine synthase, and 5'-deoxyladenosyl-Clb is the cofactor for L-methylmalonyl-CoA mutase. (medscape.com)
  • In this review, we briefly describe the underlying mechanisms of oxidative stress-mediated glutamate secretion and endocannabinoid production in alcoholic steatosis and suggest a novel metabolic synapse between hepatic stellate cells (HSCs) and hepatocytes. (e-cmh.org)
  • Aspartate aminotransferase (AST) activity (EC 2.6.1.1) AST activity was used to calculate glutamate deamination at OD450. (thetechnoant.info)
  • In the cytosol, oxoglutarate+aspartate are transaminated to form oxaloacetate+glutamate. (bioblast.at)
  • Nitrate Reductase (NADH)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This graph shows the total number of publications written about "Nitrate Reductase (NADH)" by people in this website by year, and whether "Nitrate Reductase (NADH)" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Nitrate Reductase (NADH)" by people in Profiles. (uchicago.edu)
  • In response to the elevated glutamate in the liver, the expression of metabotropic glutamate receptor 5 (mGluR5) is up-regulated in hepatic stellate cells (HSCs) along with enhanced production of 2-arachidonoylglycerol, which in turn stimulates cannabinoid receptor 1 (CB 1 R) on neighboring hepatocytes to increase de novo lipogenesis. (e-cmh.org)
  • [17] It inhibits receptor activity in the NMDA glutamate receptor subtypes. (mdwiki.org)
  • Diminished activity of methionine synthase or decreased tetrahydrofolate can cause defective DNA maturation and megaloblastic changes. (medscape.com)
  • Lotus Japonicus como Modelo para la Identificaci n de Nuevos Genes Implicados en la Respuesta a Estr s Abi tico y Productividad en Leguminosas. (us.es)
  • The glutamate neurotransmitter plays the principal role in neural activation . (explained.today)
  • During effective nodule development PEPC and NADH-GOGAT transcripts increase some 10- to 20-fold. (usda.gov)
  • The xCT transporter mediates the uptake of cystine coupled to the efflux of glutamate, leading to an increase in blood glutamate. (e-cmh.org)
  • Gemperli, A. C., Dimroth, P. & Steuber, J. Sodium ion cycling mediates energy coupling between complex I and ATP synthase. (uzh.ch)