Glutamine
Glutamate-Ammonia Ligase
Glutaminase
Ammonia
Methionine Sulfoximine
Diazooxonorleucine
Glutamates
Glutamic Acid
Amino Acids
Nitrogen
Glutamate Synthase
Nitrogen Isotopes
Ketoglutaric Acids
Glutamate Dehydrogenase
Amidophosphoribosyltransferase
Alanine
Nitrogenous Group Transferases
Aspartic Acid
Molecular Sequence Data
Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
Amino Acid Sequence
Transaminases
Asparagine
Amino Acid Transport Systems, Neutral
Quaternary Ammonium Compounds
RNA, Transfer, Gln
Glucose
Escherichia coli
Azaserine
Citric Acid Cycle
Anthranilate Synthase
Hyperammonemia
Amino Acid Transport System ASC
Urea
Mutation
Ammonium Chloride
Carbon-Nitrogen Ligases
Parenteral Nutrition, Total
Enteral Nutrition
Magnetic Resonance Spectroscopy
Carbon Isotopes
Liver
Base Sequence
Biological Transport
Histidine Ammonia-Lyase
Citrulline
beta-Alanine
Amino Acid Transport System A
Transglutaminases
Mutagenesis, Site-Directed
Parenteral Nutrition
Aminooxyacetic Acid
PII Nitrogen Regulatory Proteins
Role of glutamine in human carbohydrate metabolism in kidney and other tissues. (1/3706)
Glutamine is the most abundant amino acid in the human body and is involved in more metabolic processes than any other amino acid. Until recently, the understanding of many aspects of glutamine metabolism was based on animal and in vitro data. However, recent studies using isotopic and balance techniques have greatly advanced the understanding of glutamine metabolism in humans and its role in glucose metabolism in the kidney and other tissues. There is now evidence that in postabsorptive humans, glutamine is an important glucose precursor and makes a significant contribution to the addition of new carbon to the glucose carbon pool. The importance of alanine for gluconeogenesis, viewed in terms of the addition of new carbons, is less than previously assumed. It appears that glutamine is predominantly a renal gluconeogenic substrate, whereas alanine gluconeogenesis is essentially confined to the liver. As shown recently, renal gluconeogenesis contributes 20 to 25% to whole-body glucose production. Moreover, glutamine has been shown not only to stimulate net muscle glycogen storage but also to stimulate gluconeogenesis in normal humans. Finally, in humans with type II diabetes, conversion of glutamine to glucose is increased (more so than that of alanine). The available evidence on the hormonal regulation of glutamine gluconeogenesis in kidney and liver and its alterations under pathological conditions are discussed. (+info)The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. (2/3706)
The substitution of arginine for glutamine at amino acid 188 (Q188R) ablates the function of human galactose-1-phosphate uridyltransferase (GALT) and is the most common mutation causing galactosemia in the white population. GALT catalyzes two consecutive reactions. The first reaction binds UDP-glucose (UDP-Glu), displaces glucose-1-phosphate (glu-1-P), and forms the UMP-GALT intermediate. In the second reaction, galactose-1-phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme is recycled. In this study, we modeled glutamine, asparagine, and a common mutation arginine at amino acid 188 on the three-dimensional model of the Escherichia coli GALT-UMP protein crystal. We found that the amide group of the glutamine side chain could provide two hydrogen bonds to the phosphoryl oxygens of UMP with lengths of 2.52 and 2.82 A. Arginine and asparagine could provide only one hydrogen bond of 2. 52 and 3.02 A, respectively. To test this model, we purified recombinant human Gln188-, Arg188-, and Asn188-GALT and analyzed the first reaction in the absence of gal-1-P by quantitating glu-1-P released using enzyme-linked methods. Gln188-GALT displaced 80 +/- 7. 0 nmol glu-1-P/mg GALT/min in the first reaction. By contrast, both Arg188- and Asn188-GALT released more glu-1-P (170 +/- 8.0 and 129 +/- 28.4 nmol/mg GALT/min, respectively). The overall, double displacement reaction was quantitated in the presence of gal-1-P. Gln188-GALT produced 80,030 +/- 5,910 nmol glu-1-P/mg GALT/min, whereas the mutant Arg188- and Asn188-GALT released only 600 +/- 71. 2 and 2960 +/- 283.6 nmole glu-1-P/mg GALT/min, respectively. We conclude from these data that glutamine at position 188 stabilizes the UMP-GALT intermediate through hydrogen bonding and enables the double displacement of both glu-1-P and UDP-Gal. The substitution of arginine or asparagine at position 188 reduces hydrogen bonding and destabilizes UMP-GALT. The unstable UMP-GALT allows single displacement of glu-1-P with release of free GALT but impairs the subsequent binding of gal-1-P and displacement of UDP-Gal. (+info)Kinetic impairment of nitrogen and muscle glutamine metabolisms in old glucocorticoid-treated rats. (3/3706)
Aged rats are more sensitive to injury, possibly through an impairment of nitrogen and glutamine (Gln) metabolisms mediated by glucocorticoids. We studied the metabolic kinetic response of adult and old rats during glucocorticoid treatment. The male Sprague-Dawley rats were 24 or 3 mo old. Both adult and old rats were divided into 7 groups. Groups labeled G3, G5, and G7 received, by intraperitoneal injection, 1.50 mg/kg of dexamethasone (Dex) for 3, 5, and 7 days, respectively. Groups labeled G3PF, G5PF, and G7PF were pair fed to the G3, G5, or G7 groups and were injected with an isovolumic solution of NaCl. One control group comprised healthy rats fed ad libitum. The response to aggression induced specifically by Dex (i.e., allowing for variations in pair-fed controls) appeared later in the aged rats (decrease in nitrogen balance from day 1 in adults but only from day 4 in old rats). The adult rats rapidly adapted to Dex treatment, whereas the catabolic state worsened until the end of treatment in the old rats. Gln homeostasis was not maintained in the aged rats; despite an early increase in muscular Gln synthetase activity, the Gln pool was depleted. These results suggest a kinetic impairment of both nitrogen and muscle Gln metabolisms in response to Dex with aging. (+info)Paraoxonase 192 Gln/Arg gene polymorphism, coronary artery disease, and myocardial infarction in type 2 diabetes. (4/3706)
Paraoxonase is an HDL-associated enzyme implicated in the pathogenesis of atherosclerosis by protecting lipoproteins against peroxidation. Its biallelic gene polymorphism at codon 192 (glutamine/arginine) has been associated with coronary artery disease (CAD). To further evaluate the role of this paraoxonase gene polymorphism for CAD in type 2 diabetes, we determined the paraoxonase genotype in 288 type 2 diabetic patients (170 with and 118 without angiographically documented CAD). The paraoxonase 192 Gln/Arg genotype was assessed using polymerase chain reaction followed by AlwI digestion. The frequency of the Gln allele was 0.656 in the CAD patients and 0.746 in the controls (chi2 = 5.36, P = 0.02). Compared with the Gln/Gln genotypes, the age-adjusted odds ratio for CAD was 1.78 (95% CI 1.08-2.96, P = 0.02) in subjects carrying at least one Arg allele. In the multivariate analysis, this association was even stronger after correction for the possible confounders age, sex, smoking history, and hypertension. Among current and former smokers, the odds ratio (OR) for having CAD among patients with at least one Arg allele was 3.58 (1.45-9.53, P < 0.01). The paraoxonase Arg allele was not associated with the history of myocardial infarction (OR 1.20 [0.73-1.99, NS]), but was with the extent of CAD (OR for three-vessel disease 1.92 [1.15-3.27, P = 0.01]). Our data indicate that the 192 Arg allele of the human paraoxonase gene is a risk factor for CAD but not myocardial infarction in type 2 diabetic patients, a risk factor further modified by cigarette smoking. This risk could possibly be explained by a reduced ability of the paraoxonase Arg isoform to protect lipoproteins against peroxidation. (+info)Analysis of zinc binding sites in protein crystal structures. (5/3706)
The geometrical properties of zinc binding sites in a dataset of high quality protein crystal structures deposited in the Protein Data Bank have been examined to identify important differences between zinc sites that are directly involved in catalysis and those that play a structural role. Coordination angles in the zinc primary coordination sphere are compared with ideal values for each coordination geometry, and zinc coordination distances are compared with those in small zinc complexes from the Cambridge Structural Database as a guide of expected trends. We find that distances and angles in the primary coordination sphere are in general close to the expected (or ideal) values. Deviations occur primarily for oxygen coordinating atoms and are found to be mainly due to H-bonding of the oxygen coordinating ligand to protein residues, bidentate binding arrangements, and multi-zinc sites. We find that H-bonding of oxygen containing residues (or water) to zinc bound histidines is almost universal in our dataset and defines the elec-His-Zn motif. Analysis of the stereochemistry shows that carboxyl elec-His-Zn motifs are geometrically rigid, while water elec-His-Zn motifs show the most geometrical variation. As catalytic motifs have a higher proportion of carboxyl elec atoms than structural motifs, they provide a more rigid framework for zinc binding. This is understood biologically, as a small distortion in the zinc position in an enzyme can have serious consequences on the enzymatic reaction. We also analyze the sequence pattern of the zinc ligands and residues that provide elecs, and identify conserved hydrophobic residues in the endopeptidases that also appear to contribute to stabilizing the catalytic zinc site. A zinc binding template in protein crystal structures is derived from these observations. (+info)Deamidation of alpha-A crystallin from nuclei of cataractous and normal human lenses. (6/3706)
PURPOSE: To quantitate the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 of alpha-A crystallin in the nucleus from human cataractous and normal lenses. METHODS: Reverse phase chromatography was used to prepare alpha-A crystallin from total proteins of the nucleus from cataractous and age-matched normal human lenses. Synthetic peptides were made corresponding to the expected amidated and deamidated tryptic fragments containing asparagine-101, glutamine-50, and glutamine-6. The peptides were used to identify and quantitate amidated and deamidated forms of tryptic fragments from alpha-A crystallin eluting from a reverse phase column. RESULTS: Significant amounts of deamidation of asparagine-101 and glutamine-50, but not glutamine-6, were present in alpha-A crystallin from nuclear sections of both cataractous and age-matched normal lenses. Quantitative analysis of tryptic peptides containing these residues indicated no statistical difference in deamidation in cataractous versus normal lenses. CONCLUSIONS: There was no significant difference in the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 for alpha-A crystallin, purified from the nucleus of cataractous versus age-matched normal lenses. These results strongly suggest that deamidation of these residues does not play a role in the biogenesis of human nuclear cataract. (+info)Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. (7/3706)
Peptide toxins selective for particular subunit interfaces of the nicotinic acetylcholine receptor have proven invaluable in assigning candidate residues located in the two binding sites and for determining probable orientations of the bound peptide. We report here on a short alpha-neurotoxin from Naja mossambica mossambica (NmmI) that, similar to other alpha-neurotoxins, binds with high affinity to alphagamma and alphadelta subunit interfaces (KD approximately 100 pM) but binds with markedly reduced affinity to the alphaepsilon interface (KD approximately 100 nM). By constructing chimeras composed of portions of the gamma and epsilon subunits and coexpressing them with wild type alpha, beta, and delta subunits in HEK 293 cells, we identify a region of the subunit sequence responsible for the difference in affinity. Within this region, gammaPro-175 and gammaGlu-176 confer high affinity, whereas Thr and Ala, found at homologous positions in epsilon, confer low affinity. To identify an interaction between gammaGlu-176 and residues in NmmI, we have examined cationic residues in the central loop of the toxin and measured binding of mutant toxin-receptor combinations. The data show strong pairwise interactions or coupling between gammaGlu-176 and Lys-27 of NmmI and progressively weaker interactions with Arg-33 and Arg-36 in loop II of this three-loop toxin. Thus, loop II of NmmI, and in particular the face of this loop closest to loop III, appears to come into close apposition with Glu-176 of the gamma subunit surface of the binding site interface. (+info)Solution structure of the alpha-subunit of human chorionic gonadotropin. (8/3706)
The three-dimensional solution structure of the alpha-subunit in the alpha, beta heterodimeric human chorionic gonadotropin (hCG), deglycosylated with endo-beta-N-acetylglucosaminidase-B (dg-alpha hCG), was determined using 2D homonuclear and 2D heteronuclear 1H, 13C NMR spectroscopy at natural abundance in conjunction with the program package XPLOR. The distance geometry/simulated annealing protocol was modified to allow for the efficient modelling of the cystine knot motif present in alpha hCG. The protein structure was modelled with 620 interproton distance restraints and the GlcNAc residue linked to Asn78 was modelled with 30 protein-carbohydrate and 3 intraresidual NOEs. The solution structure of dg-alpha hCG is represented by an ensemble of 27 structures. In comparison to the crystal structure of the dimer, the solution structure of free dg-alpha hCG exhibits: (a) an increased structural disorder (residues 33-57); (b) a different backbone conformation near Val76 and Glu77; and (c) a larger flexibility. These differences are caused by the absence of the interactions with the beta-subunit. Consequently, in free dg-alpha hCG, compared to the intact dimer, the two hairpin loops 20-23 and 70-74 are arranged differently with respect to each other. The beta-GlcNAc(78) is tightly associated with the hydrophobic protein-core in between the beta-hairpins. This conclusion is based on the NOEs from the axial H1, H3, H5 atoms and the N-acetyl protons of beta-GlcNAc(78) to the protein-core. The hydrophobic protein-core between the beta-hairpins is thereby shielded from the solvent. (+info)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.
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.
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.
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.
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.
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.
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.
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.
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).
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.
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.
Nitrogen isotopes are different forms of the nitrogen element (N), which have varying numbers of neutrons in their atomic nuclei. The most common nitrogen isotope is N-14, which contains 7 protons and 7 neutrons in its nucleus. However, there are also heavier stable isotopes such as N-15, which contains one extra neutron.
In medical terms, nitrogen isotopes can be used in research and diagnostic procedures to study various biological processes. For example, N-15 can be used in a technique called "nitrogen-15 nuclear magnetic resonance (NMR) spectroscopy" to investigate the metabolism of nitrogen-containing compounds in the body. Additionally, stable isotope labeling with nitrogen-15 has been used in clinical trials and research studies to track the fate of drugs and nutrients in the body.
In some cases, radioactive nitrogen isotopes such as N-13 or N-16 may also be used in medical imaging techniques like positron emission tomography (PET) scans to visualize and diagnose various diseases and conditions. However, these applications are less common than the use of stable nitrogen isotopes.
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.
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.
Amidophosphoribosyltransferase is an enzyme involved in the metabolic pathway of purine synthesis. Its systematic name is phosphoribosylamine-phosphate transaminase, and it catalyzes the reaction between phosphoribosyl pyrophosphate (PRPP) and glutamine to produce 5-phosphoribosyl-α-[glutamate-1-formimino]-triose phosphate (GAR) and ammonia.
This enzyme plays a crucial role in the biosynthesis of purine nucleotides, which are essential components of DNA, RNA, and many other important molecules in the body. Deficiencies in this enzyme can lead to serious medical conditions, such as Lesch-Nyhan syndrome, a rare genetic disorder characterized by mental retardation, self-mutilation, spasticity, and an excess of uric acid in the blood (hyperuricemia).
Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.
Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.
In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.
Nitrogenous group transferases are a class of enzymes that catalyze the transfer of nitrogen-containing groups from one molecule to another. These enzymes play a crucial role in various metabolic pathways, including the biosynthesis and degradation of amino acids, nucleotides, and other nitrogen-containing compounds.
The term "nitrogenous group" refers to any chemical group that contains nitrogen atoms. Examples of nitrogenous groups include amino groups (-NH2), amide groups (-CONH2), and cyano groups (-CN). Transferases that move these groups from one molecule to another are classified as nitrogenous group transferases.
These enzymes typically require cofactors such as ATP, NAD+, or other small molecules to facilitate the transfer of the nitrogenous group. They follow the general reaction mechanism of a transferase enzyme, where the substrate (donor) binds to the active site of the enzyme and transfers its nitrogenous group to an acceptor molecule, resulting in the formation of a new product.
Examples of nitrogenous group transferases include:
* Glutamine synthetase, which catalyzes the conversion of glutamate to glutamine by adding an ammonia group (-NH3) from ATP.
* Aspartate transcarbamylase, which catalyzes the transfer of a carbamoyl group (-CO-NH2) from carbamoyl phosphate to aspartate during pyrimidine biosynthesis.
* Argininosuccinate synthetase, which catalyzes the formation of argininosuccinate by transferring an aspartate group from aspartate to citrulline during the urea cycle.
Understanding nitrogenous group transferases is essential for understanding various metabolic pathways and their regulation in living organisms.
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.
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.
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.
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.
Asparagine is an organic compound that is classified as a naturally occurring amino acid. It contains an amino group, a carboxylic acid group, and a side chain consisting of a single carbon atom bonded to a nitrogen atom, making it a neutral amino acid. Asparagine is encoded by the genetic codon AAU or AAC in the DNA sequence.
In the human body, asparagine plays important roles in various biological processes, including serving as a building block for proteins and participating in the synthesis of other amino acids. It can also act as a neurotransmitter and is involved in the regulation of cellular metabolism. Asparagine can be found in many foods, particularly in high-protein sources such as meat, fish, eggs, and dairy products.
Neutral amino acid transport systems refer to a group of membrane transporters that facilitate the movement of neutral amino acids across cell membranes. Neutral amino acids are those that have a neutral charge at physiological pH and include amino acids such as alanine, serine, threonine, valine, leucine, isoleucine, methionine, cysteine, tyrosine, phenylalanine, and tryptophan.
There are several different transport systems that have been identified for neutral amino acids, each with its own specificity and affinity for different amino acids. Some of the major neutral amino acid transport systems include:
1. System A: This transporter preferentially transports small, neutral amino acids such as alanine, serine, and threonine. It is found in many tissues, including the intestines, kidneys, and brain.
2. System B0+: This transporter preferentially transports large, neutral amino acids such as leucine, isoleucine, valine, methionine, and phenylalanine. It is found in many tissues, including the intestines, kidneys, and brain.
3. System L: This transporter preferentially transports large, neutral amino acids such as leucine, isoleucine, valine, methionine, and phenylalanine. It is found in many tissues, including the intestines, kidneys, and brain.
4. System y+: This transporter preferentially transports cationic amino acids such as lysine and arginine, but it can also transport some neutral amino acids. It is found in many tissues, including the intestines, kidneys, and brain.
5. System b0,+: This transporter preferentially transports cationic amino acids such as lysine and arginine, but it can also transport some neutral amino acids. It is found in many tissues, including the intestines, kidneys, and brain.
These transport systems play important roles in maintaining amino acid homeostasis in the body, as well as in various physiological processes such as protein synthesis, neurotransmitter synthesis, and cell signaling. Dysregulation of these transport systems has been implicated in several diseases, including cancer, neurological disorders, and metabolic disorders.
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.
Transfer RNA (tRNA) that carries glutamine (Gln) is a type of RNA molecule involved in protein synthesis. Glutamine is one of the twenty standard amino acids used by cells to construct proteins. During protein synthesis, tRNAs serve as adaptors between the mRNA code and the corresponding amino acids. Specifically, the tRNA with the anticodon complementary to the mRNA codon for glutamine (CAA or CAG) binds to glutamine and delivers it to the growing polypeptide chain during translation. This particular tRNA is referred to as 'tRNA Gln' or 'tRNA for Gln'.
Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.
In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.
Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.
'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.
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.
The Citric Acid Cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, is a crucial metabolic pathway in the cell's powerhouse, the mitochondria. It plays a central role in the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins, into carbon dioxide and high-energy electrons. This process generates energy in the form of ATP (adenosine triphosphate), reducing equivalents (NADH and FADH2), and water.
The cycle begins with the condensation of acetyl-CoA with oxaloacetate, forming citrate. Through a series of enzyme-catalyzed reactions, citrate is converted back to oxaloacetate, releasing two molecules of carbon dioxide, one GTP (guanosine triphosphate), three NADH, one FADH2, and regenerating oxaloacetate to continue the cycle. The reduced coenzymes (NADH and FADH2) then donate their electrons to the electron transport chain, driving ATP synthesis through chemiosmosis. Overall, the Citric Acid Cycle is a vital part of cellular respiration, connecting various catabolic pathways and generating energy for the cell's metabolic needs.
Anthranilate synthase is a key enzyme in the synthesis of aromatic amino acids, specifically tryptophan. It catalyzes the reaction of chorismate and glutamine to form anthranilate, which is the first committed step in the biosynthetic pathway leading to tryptophan. Anthranilate synthase is a heterotetrameric enzyme composed of two different subunits, ASα and ASβ, in eukaryotes and some bacteria. In other bacteria, anthranilate synthase is a single polypeptide chain with both active sites. The activity of anthranilate synthase is tightly regulated at the transcriptional and allosteric levels to control the flow of carbon into the tryptophan biosynthetic pathway.
Hyperammonemia is a medical condition characterized by an excessively high level of ammonia (a toxic byproduct of protein metabolism) in the blood. This can lead to serious neurological symptoms and complications, as ammonia is highly toxic to the brain. Hyperammonemia can be caused by various underlying conditions, including liver disease, genetic disorders that affect ammonia metabolism, certain medications, and infections. It is important to diagnose and treat hyperammonemia promptly to prevent long-term neurological damage or even death. Treatment typically involves addressing the underlying cause of the condition, as well as providing supportive care such as administering medications that help remove ammonia from the blood.
The amino acid transport system ASC, also known as system asc or L system, is a type of amino acid transporter found in the membranes of cells. It is responsible for the uptake of small neutral amino acids, such as alanine, serine, and cysteine, into the cell. This transport system is important for maintaining proper levels of these amino acids within the cell, which are necessary for various cellular processes including protein synthesis and metabolism. It is also known to be upregulated in certain cancer cells, allowing them to take up more amino acids from their environment and support their rapid growth. The system asc transporter is a part of the solute carrier 7 (SLC7) family, which are membrane-bound proteins that facilitate the transport of various molecules across cell membranes.
Urea is not a medical condition but it is a medically relevant substance. Here's the definition:
Urea is a colorless, odorless solid that is the primary nitrogen-containing compound in the urine of mammals. It is a normal metabolic end product that is excreted by the kidneys and is also used as a fertilizer and in various industrial applications. Chemically, urea is a carbamide, consisting of two amino groups (NH2) joined by a carbon atom and having a hydrogen atom and a hydroxyl group (OH) attached to the carbon atom. Urea is produced in the liver as an end product of protein metabolism and is then eliminated from the body by the kidneys through urination. Abnormal levels of urea in the blood, known as uremia, can indicate impaired kidney function or other medical conditions.
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.
Ammonium chloride is an inorganic compound with the formula NH4Cl. It is a white crystalline salt that is highly soluble in water and can be produced by combining ammonia (NH3) with hydrochloric acid (HCl). Ammonium chloride is commonly used as a source of hydrogen ions in chemical reactions, and it has a variety of industrial and medical applications.
In the medical field, ammonium chloride is sometimes used as a expectorant to help thin and loosen mucus in the respiratory tract, making it easier to cough up and clear from the lungs. It may also be used to treat conditions such as metabolic alkalosis, a condition characterized by an excess of base in the body that can lead to symptoms such as confusion, muscle twitching, and irregular heartbeat.
However, it is important to note that ammonium chloride can have side effects, including stomach upset, nausea, vomiting, and diarrhea. It should be used under the guidance of a healthcare professional and should not be taken in large amounts or for extended periods of time without medical supervision.
Ornithine is not a medical condition but a naturally occurring alpha-amino acid, which is involved in the urea cycle, a process that eliminates ammonia from the body. Here's a brief medical/biochemical definition of Ornithine:
Ornithine (NH₂-CH₂-CH₂-CH(NH₃)-COOH) is an α-amino acid without a carbon atom attached to the amino group, classified as a non-proteinogenic amino acid because it is not encoded by the standard genetic code and not commonly found in proteins. It plays a crucial role in the urea cycle, where it helps convert harmful ammonia into urea, which can then be excreted by the body through urine. Ornithine is produced from the breakdown of arginine, another amino acid, via the enzyme arginase. In some medical and nutritional contexts, ornithine supplementation may be recommended to support liver function, wound healing, or muscle growth, but its effectiveness for these uses remains a subject of ongoing research and debate.
Arginine is an α-amino acid that is classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. The adult human body can normally synthesize sufficient amounts of arginine to meet its needs, but there are certain circumstances, such as periods of rapid growth or injury, where the dietary intake of arginine may become necessary.
The chemical formula for arginine is C6H14N4O2. It has a molecular weight of 174.20 g/mol and a pKa value of 12.48. Arginine is a basic amino acid, which means that it contains a side chain with a positive charge at physiological pH levels. The side chain of arginine is composed of a guanidino group, which is a functional group consisting of a nitrogen atom bonded to three methyl groups.
In the body, arginine plays several important roles. It is a precursor for the synthesis of nitric oxide, a molecule that helps regulate blood flow and immune function. Arginine is also involved in the detoxification of ammonia, a waste product produced by the breakdown of proteins. Additionally, arginine can be converted into other amino acids, such as ornithine and citrulline, which are involved in various metabolic processes.
Foods that are good sources of arginine include meat, poultry, fish, dairy products, nuts, seeds, and legumes. Arginine supplements are available and may be used for a variety of purposes, such as improving exercise performance, enhancing wound healing, and boosting immune function. However, it is important to consult with a healthcare provider before taking arginine supplements, as they can interact with certain medications and have potential side effects.
Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.
Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.
Carbon-Nitrogen (C-N) ligases are a class of enzymes that catalyze the joining of a carbon atom from a donor molecule to a nitrogen atom in an acceptor molecule through a process called ligase reaction. This type of enzyme plays a crucial role in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules that contain both carbon and nitrogen atoms.
C-N ligases typically require ATP or another energy source to drive the reaction forward, as well as cofactors such as metal ions or vitamins to facilitate the chemical bond formation between the carbon and nitrogen atoms. The specificity of C-N ligases varies depending on the enzyme, with some acting only on specific donor and acceptor molecules while others have broader substrate ranges.
Examples of C-N ligases include glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia, and asparagine synthetase, which catalyzes the formation of asparagine from aspartate and ammonia. Understanding the function and regulation of C-N ligases is important for understanding various biological processes and developing strategies to modulate them in disease states.
Total Parenteral Nutrition (TPN) is a medical term used to describe a specialized nutritional support system that is delivered through a vein (intravenously). It provides all the necessary nutrients that a patient needs, such as carbohydrates, proteins, fats, vitamins, and minerals. TPN is typically used when a patient cannot eat or digest food through their gastrointestinal tract for various reasons, such as severe malabsorption, intestinal obstruction, or inflammatory bowel disease. The term "total" indicates that the nutritional support is complete and meets all of the patient's nutritional needs.
Enteral nutrition refers to the delivery of nutrients to a person through a tube that is placed into the gastrointestinal tract, specifically into the stomach or small intestine. This type of nutrition is used when a person is unable to consume food or liquids by mouth due to various medical conditions such as swallowing difficulties, malabsorption, or gastrointestinal disorders.
Enteral nutrition can be provided through different types of feeding tubes, including nasogastric tubes, which are inserted through the nose and down into the stomach, and gastrostomy or jejunostomy tubes, which are placed directly into the stomach or small intestine through a surgical incision.
The nutrients provided through enteral nutrition may include commercially prepared formulas that contain a balance of carbohydrates, proteins, fats, vitamins, and minerals, or blenderized whole foods that are pureed and delivered through the feeding tube. The choice of formula or type of feed depends on the individual's nutritional needs, gastrointestinal function, and medical condition.
Enteral nutrition is a safe and effective way to provide nutrition support to people who are unable to meet their nutritional needs through oral intake alone. It can help prevent malnutrition, promote wound healing, improve immune function, and enhance overall health and quality of life.
Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.
During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.
There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.
Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.
Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.
Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.
Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.
The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:
1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.
Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.
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.
Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.
Passive transport does not require the input of energy and includes:
1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.
Active transport requires the input of energy (in the form of ATP) and includes:
1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.
Histidine Ammonia-Lyase (HAL) is an enzyme that catalyzes the conversion of the amino acid L-histidine into trans-urocanic acid, ammonia, and water. This reaction is a part of the histidine catabolism pathway in many organisms, including humans. The enzyme accomplishes this transformation by removing an ammonia group from the imidazole ring of L-histidine, resulting in the formation of trans-urocanic acid. Histidine Ammonia-Lyase plays a crucial role in histidine metabolism and has been studied for its potential implications in various physiological processes and diseases.
L-Citrulline is a non-essential amino acid that plays a role in the urea cycle, which is the process by which the body eliminates toxic ammonia from the bloodstream. It is called "non-essential" because it can be synthesized by the body from other compounds, such as L-Ornithine and carbamoyl phosphate.
Citrulline is found in some foods, including watermelon, bitter melon, and certain types of sausage. It is also available as a dietary supplement. In the body, citrulline is converted to another amino acid called L-Arginine, which is involved in the production of nitric oxide, a molecule that helps dilate blood vessels and improve blood flow.
Citrulline has been studied for its potential benefits on various aspects of health, including exercise performance, cardiovascular function, and immune system function. However, more research is needed to confirm these potential benefits and establish safe and effective dosages.
Beta-alanine is a non-essential amino acid, which means that it is not required in the diet because the body can produce it from other amino acids. It is produced in the liver and is also found in some foods such as meat, poultry, and fish.
Beta-alanine plays a role in the production of carnosine, a dipeptide molecule that helps to regulate muscle pH and improve muscle function during high-intensity exercise. When muscles contract during intense exercise, they produce hydrogen ions, which can cause the muscle pH to decrease (become more acidic), leading to fatigue and reduced muscle function. Carnosine acts as a buffer against this acidity, helping to maintain optimal muscle pH levels and improve performance during high-intensity exercise.
Beta-alanine supplements have been shown to increase carnosine levels in muscles, which may lead to improved athletic performance, particularly in activities that require short bursts of intense effort, such as weightlifting or sprinting. However, more research is needed to fully understand the effects and potential benefits of beta-alanine supplementation.
It's important to note that while beta-alanine supplements are generally considered safe for most people, they can cause a tingling sensation in the skin (paresthesia) when taken in high doses. This is a harmless side effect and typically subsides within an hour or so of taking the supplement.
Amino acid transport system A, also known as system ASC or alanine-serine-cysteine transporter, is a type of amino acid transporter found in the membranes of cells. It is responsible for the uptake of small neutral amino acids, such as alanine, serine, and cysteine, into the cell. This transport system plays an important role in maintaining amino acid homeostasis within the body and is particularly important in tissues with high rates of protein turnover, such as the intestines and kidneys. It is also expressed in the brain, where it is involved in the regulation of neurotransmitter synthesis. Defects in this transport system have been implicated in various diseases, including neurological disorders and cancer.
Transglutaminases are a family of enzymes that catalyze the post-translational modification of proteins by forming isopeptide bonds between the carboxamide group of peptide-bound glutamine residues and the ε-amino group of lysine residues. This process is known as transamidation or cross-linking. Transglutaminases play important roles in various biological processes, including cell signaling, differentiation, apoptosis, and tissue repair. There are several types of transglutaminases, such as tissue transglutaminase (TG2), factor XIII, and blood coagulation factor XIIIA. Abnormal activity or expression of these enzymes has been implicated in various diseases, such as celiac disease, neurodegenerative disorders, and cancer.
Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.
The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.
Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.
Parenteral nutrition (PN) is a medical term used to describe the delivery of nutrients directly into a patient's bloodstream through a vein, bypassing the gastrointestinal tract. It is a specialized medical treatment that is typically used when a patient cannot receive adequate nutrition through enteral feeding, which involves the ingestion and digestion of food through the mouth or a feeding tube.
PN can be used to provide essential nutrients such as carbohydrates, proteins, fats, vitamins, minerals, and electrolytes to patients who have conditions that prevent them from absorbing nutrients through their gut, such as severe gastrointestinal tract disorders, malabsorption syndromes, or short bowel syndrome.
PN is administered through a catheter that is inserted into a vein, typically in the chest or arm. The nutrient solution is prepared under sterile conditions and delivered through an infusion pump to ensure accurate and controlled delivery of the solution.
While PN can be a life-saving intervention for some patients, it also carries risks such as infection, inflammation, and organ damage. Therefore, it should only be prescribed and administered by healthcare professionals with specialized training in this area.
Aminooxyacetic acid (AOAA) is a chemical compound that is an irreversible inhibitor of pyridoxal phosphate-dependent enzymes. Pyridoxal phosphate is a cofactor involved in several important biochemical reactions, including the transamination of amino acids. By inhibiting these enzymes, AOAA can alter the normal metabolism of amino acids and other related compounds in the body.
AOAA has been studied for its potential therapeutic uses, such as in the treatment of neurodegenerative disorders like Huntington's disease and epilepsy. However, more research is needed to fully understand its mechanisms of action and potential side effects before it can be used as a routine therapy.
It is important to note that AOAA is not a naturally occurring substance in the human body and should only be used under medical supervision.
PII nitrogen regulatory proteins are a type of signal transduction protein involved in the regulation of nitrogen metabolism in bacteria and archaea. They are named "PII" because they contain two identical subunits, each with a molecular weight of approximately 12 kilodaltons. These proteins play a crucial role in sensing and responding to changes in the energy status and nitrogen availability within the cell.
The PII protein is composed of three domains: the T-domain, which binds ATP and ADP; the N-domain, which binds 2-oxoglutarate (an indicator of carbon and nitrogen status); and the B-domain, which is involved in signal transduction. The PII protein can exist in different conformational states depending on whether it is bound to ATP or ADP, and this affects its ability to interact with downstream effectors.
One of the primary functions of PII proteins is to regulate the activity of glutamine synthetase (GS), an enzyme that catalyzes the conversion of glutamate to glutamine. When nitrogen is abundant, PII proteins bind to GS and stimulate its activity, promoting the assimilation of ammonia into organic compounds. Conversely, when nitrogen is scarce, PII proteins dissociate from GS, allowing it to be inhibited by other regulatory proteins.
PII proteins can also interact with other enzymes and regulators involved in nitrogen metabolism, such as nitrogenase, uridylyltransferase/uridylyl-removing enzyme (UT/UR), and transcriptional regulators. Through these interactions, PII proteins help to coordinate the cell's response to changes in nitrogen availability and energy status, ensuring that resources are allocated efficiently and effectively.
Glutamine
Alanyl-glutamine
Glutamine synthetase
Glutamine riboswitch
Glutamine amidotransferase
Glutamate-glutamine cycle
Protein-glutamine glutaminase
Glutamine (data page)
Glutamine N-acyltransferase
Glutamine-phenylpyruvate transaminase
Glutamine-tRNA ligase
Glutamine-pyruvate transaminase
Glutamine N-phenylacetyltransferase
Glutamine-scyllo-inositol transaminase
NAD+ synthase (glutamine-hydrolysing)
Asparagine synthase (glutamine-hydrolysing)
Asparaginyl-tRNA synthase (glutamine-hydrolysing)
Adenosylcobyric acid synthase (glutamine-hydrolysing)
Glutaminyl-tRNA synthase (glutamine-hydrolysing)
Glutamine-fructose-6-phosphate transaminase (isomerizing)
Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)
Glutaminyl-trna synthase (glutamine-hydrolyzing)-like 1
Hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing)
Cachexia
6-Diazo-5-oxo-L-norleucine
List of OMIM disorder codes
GATA1
Earl Reece Stadtman
Sirtuin 4
Glutaminolysis
Glutamine - Wikipedia
glutamine (CHEBI:28300)
Glutamine gluttony of efferocytes | Nature Metabolism
L-glutamine: MedlinePlus Drug Information
Is glutamine a conditionally essential amino acid?
L-Arginine & L-Glutamine | livestrong
L-(+)-glutamine | C5H10N2O3 | ChemSpider
Glutamine (Oral Route) Description and Brand Names - Mayo Clinic
RPMI-1640 Medium liquid with L-glutamine Sigma
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- In 2017, the U.S. Food and Drug Administration (FDA) approved L-glutamine oral powder, marketed as Endari, to reduce severe complications of sickle cell disease in people aged five years and older with the disorder. (wikipedia.org)
- The safety and efficacy of L-glutamine oral powder were studied in a randomized trial of subjects ages five to 58 years old with sickle cell disease who had two or more painful crises within the 12 months prior to enrollment in the trial. (wikipedia.org)
- Subjects were assigned randomly to treatment with L-glutamine oral powder or placebo, and the effect of treatment was evaluated over 48 weeks. (wikipedia.org)
- Subjects who were treated with L-glutamine oral powder experienced fewer hospital visits for pain treated with a parenterally administered narcotic or ketorolac (sickle cell crises), on average, compared to subjects who received a placebo (median 3 vs. median 4), fewer hospitalizations for sickle cell pain (median 2 vs. median 3), and fewer days in the hospital (median 6.5 days vs. median 11 days). (wikipedia.org)
- Subjects who received L-glutamine oral powder also had fewer occurrences of acute chest syndrome (a life-threatening complication of sickle cell disease) compared with patients who received a placebo (8.6 percent vs. 23.1 percent). (wikipedia.org)
- L-glutamine oral powder received orphan drug designation. (wikipedia.org)
- L-glutamine comes as a powder to be mixed with a liquid or soft wet food and taken by mouth twice a day. (medlineplus.gov)
- On July 7, 2017, the U.S. Food and Drug Administration approved L-glutamine oral powder (Endari, Emmaus Medical, Inc.) for oral administration to reduce the acute complications of sickle cell disease in adult and pediatric patients 5 years and older. (fda.gov)
- supplements L- Glutamine Powder For Maintain Strength of the Immune System Product name L- Glutamine CAS No. 56-85-9 MF C5H10N2O3 MW 146.14 Melting point 185 °C (dec.)(lit. (opencroquet.org)
- 98% L- Glutamine Powder is the most abundant amino acid found in human muscle and plasma. (opencroquet.org)
- No problems with this glutamine powder. (mrsupplement.com.au)
- L-Glutamine Powder by Nutri-Dyn provides an accessible source of L-glutamine. (blueskyvitamin.com)
- Due to its form, L-Glutamine Powder by Nutri-Dyn can be dissolved easily in water or other items. (blueskyvitamin.com)
Glutamate7
- Glutamine synthesis from glutamate and ammonia is catalyzed by the enzyme glutamine synthetase. (wikipedia.org)
- Glutaminolysis consists of glutamine hydrolyzation into glutamate by GLS1, and this metabolic process is known to be upregulated in IL4-induced reparative macrophages. (nature.com)
- Also be aware that people who are sensitive to monosodium glutamate (MSG -- a food flavoring agent) should use glutamine with caution, as the body metabolizes glutamine to glutamate. (consumerlab.com)
- Those metabolic reactions involving D-glutamine and D-glutamate as depicted in the KEGG diagram. (mcw.edu)
- Elevated level expression of glutamine Synthetase in glial cells has shown to protect neurons from degeneration due to excess glutamate. (biogenex.com)
- We employed, at 7 T, a previously validated 1 H-MRS protocol to measure glutamate, GABA, and glutathione, as well as glutamine, N-acetyl aspartate, choline, and myoinositol, in the frontal cortex of individuals with relapsing-remitting (N = 26) or progressive (N = 21) multiple sclerosis or healthy control adults (N = 25) in a cross-sectional analysis. (lu.se)
- As a group, multiple sclerosis patients demonstrated significant negative correlations between disease duration and glutamate or GABA (ρ = -0.4, p = 0.02) but not glutamine or glutathione. (lu.se)
Glutamic acid3
- 8615202961574 The Introductction of Glutamine Glutamine is the amide of glutamic acid. (opencroquet.org)
- Glutamine Synthetase (Gl Syn) forms a homo octamer that is a catalyst for the amination of glutamic acid to glutamine. (biogenex.com)
- It is a marker for astrocytes that serve as the primary site of conversion of glutamic acid to glutamine in the brain. (biogenex.com)
Glucose6
- Glutamine is produced industrially using mutants of Brevibacterium flavum, which gives ca. 40 g/L in 2 days using glucose as a carbon source. (wikipedia.org)
- In addition, glutamine can be transformed and then it can get rid of one or two amidogens before transforming into some intermediate metabolites and then compose some other substances in response to the demand of the body For instance, when our body needs more glucose, it can be transformed into dextrose water through gluconeogenesis. (futurelearn.com)
- However, for fast-growing cells or cell in the division, these cells utilize energy from glutamine more than glucose. (futurelearn.com)
- Both glucose and glutamine are important fuels for neutrophils, yet little has been done to investigate the comparative effects of glucose and glutamine on neutrophil apoptosis. (portlandpress.com)
- We hypothesized that glucose and/or glutamine significantly alter rates of spontaneous and anti-Fas antibody-induced apoptosis of human neutrophils cultured ex vivo . (portlandpress.com)
- Neutrophil apoptosis was reduced by increasing the extracellular concentration of glucose, but was unaffected by glutamine concentration. (portlandpress.com)
Supplementation3
- This study elucidated effects of glutamine (Gln) supplementation on the cellular muscle development of LBW and normal birth weight (NBW) piglets. (nature.com)
- In this project, we aimed to ameliorate the retarded growth of LBW piglets by oral glutamine (Gln) supplementation. (nature.com)
- I've read some recent articles arguing against L Glutamine supplementation saying it doesn't work as it should etc... but take my word for it - Glutamine works. (bodybuildingforyou.com)
Conditionally essential amin2
- L-Glutamine is a conditionally essential amino acid (which is elevated to an essential amino acid during sickness and illness) which promotes optimal immune function (hence why it is essential during sickness) as well as inhibiting muscle wasting and breakdown. (predatornutrition.com)
- Under these circumstances Glutamine may be considered a "conditionally essential" amino acid. (buywell.com)
Immune15
- The most eager consumers of glutamine are the cells of intestines, the kidney cells for the acid-base balance, activated immune cells, and many cancer cells. (wikipedia.org)
- L-glutamine can help athletes avoid illnesses, particularly after exercise when the immune system may be compromised. (livestrong.com)
- Because l-glutamine is important for immune function and gut health, low levels may have negative health consequences. (livestrong.com)
- Strengthen your immune system with the power of Glutamine, enabling you to maintain optimal health and performance. (musclepharm.com)
- It is also recommend to supplement on glutamine during illness to strengthen the immune system and speed up the recovery rate. (predatornutrition.com)
- Beyond its benefits for athletic performance, glutamine is known to support a robust immune system. (veganessentials.com)
- Glutamine is an amino acid which can help to support the immune system and bolster muscle recovery processes. (mrsupplement.com.au)
- Unlock the potential of L-Glutamine supplements for improved muscle recovery, immune system support, gut health, exercise performance, & weight management. (mrsupplement.com.au)
- The glutamine amino acid plays an integral role in muscle growth and repair, as well as playing an important role in the immune system's stress response mechanism. (discount-supplements.co.uk)
- In numerous animal studies, in which hyper-permeability of the intestine is experimentally induced, the addition of glutamine improved permeability function as well as the gut's immune function. (alchemyelixir.com)
- Two other nutrients complement the muscle-building effects of whey: creatine supports muscle strength and prevents muscle wasting with aging, while the amino acid glutamine helps preserve lean tissue mass and supports immune system health. (lifeextension.com)
- Glutamine is involved in maintaining a positive nitrogen balance (an anabolic state) and also aids rapidly growing cells (immune system lymphocytes and intestinal cell enterocytes). (buywell.com)
- Glutamine is involved in maintaining a positive nitrogen balance (an anabolic state) and acts as the primary fuel for rapidly growing cells (immune system and intestinal cells). (buywell.com)
- L-glutamine is an amino acid that supports a healthy intestinal lining and immune function, and assists in healing after injury or surgery and in muscle cell repair. (vitaminlife.com)
- We also list the roles of glutamine in resisting oxidative stress and promoting immune escape. (bvsalud.org)
Metabolism6
- Glutamine metabolism is a carbon and nitrogen source. (wikipedia.org)
- Although the liver is capable of relevant glutamine synthesis, its role in glutamine metabolism is more regulatory than producing, since the liver takes up large amounts of glutamine derived from the gut. (wikipedia.org)
- Fig. 1: Reparative macrophages bypass the canonical glutamine metabolism pathway to potentiate efferocytosis. (nature.com)
- Glutamine metabolism in tumor metastasis: Genes, mechanisms and the therapeutic targets. (bvsalud.org)
- This review summarises the key enzymes and transporters involved in glutamine metabolism that are related to the pathogenesis of malignant tumour metastasis . (bvsalud.org)
- Finally, the significance of targeting glutamine metabolism in inhibiting tumour metastasis was proposed, research in this field improving our understanding of amino acid metabolism rewiring and simultaneously bringing about new and exciting therapeutic prospects. (bvsalud.org)
Glutathione1
- Glutamine maintains redox balance by participating in glutathione synthesis and contributing to anabolic processes such as lipid synthesis by reductive carboxylation. (wikipedia.org)
Labs Glutamine3
- https://www.mrsupplement.com.au/ehplabs-glutamine?variation=10689 EHP Labs Glutamine (500g Natural) EHP Labs Glutamine offers 100% pharmaceutical grade, pure, micronized glutamine to help support faster recovery from intense exercise. (mrsupplement.com.au)
- EHP Labs Glutamine offers 100% pharmaceutical grade, pure, micronized glutamine to help support faster recovery from intense exercise. (mrsupplement.com.au)
- EHP Labs Glutamine is flavourless and doesn't contain any additives or fillers making it a clean addition to any serious trainers stack. (mrsupplement.com.au)
Ingredients1
- Other Ingredients: L-Glutamine. (blueskyvitamin.com)
Supplements7
- I'll Pump You Up carries a wide variety of Glutamine Supplements. (illpumpyouup.com)
- Glutamine Supplements can help treat leaky gut, ulcers, and it may improve IBS symptoms, promotes muscle growth and decrease muscle wasting, may improve athletic performance and recovery from endurance exercise, and supports metabolic and heart health. (illpumpyouup.com)
- For more information about side effects from glutamine, see the Concerns and Cautions section of our Muscle & Workout Supplements Review, which also discusses what glutamine can and cannot do based on clinical studies. (consumerlab.com)
- Glutamine supplements are therefore a perfect way to inject more of this essential amino acid into your healthy diet and exercise routine. (discount-supplements.co.uk)
- Glutamine is one of the most beneficial supplements that athletes and bodybuilders can take. (sportsfuel.co.nz)
- Over the many years I've worked out, I've continually used glutamine as one of my basic supplements, and when not using it, it just doesn't feel the same. (bodybuildingforyou.com)
- Fortunately, whey protein, creatine, and glutamine are available as meal replacements or supplements to provide the amino acids needed to help offset the age-related decline in muscle mass (sarcopenia) while supporting the muscle-building effects of resistance training. (lifeextension.com)
Metabolic3
- The FDA granted the approval of Endari to Emmaus Medical Inc. Glutamine is marketed as medical food and is prescribed when a medical professional believes a person in their care needs supplementary glutamine due to metabolic demands beyond what can be met by endogenous synthesis or diet. (wikipedia.org)
- In times of metabolic stress, glutamine is released from the muscles into the bloodstream, where it is transported to the tissues in need but concentration in the skeletal muscles can be affected by various insults, including injury, infection, prolonged stress, malnutrition, and the use of glucocorticoids. (alchemyelixir.com)
- We applied stable isotope assisted metabolic profiling to investigate the effect of a functional loss of DJ-1 and show that DJ-1 deficient neuronal cells exhibit decreased glutamine influx and reduced serine biosynthesis. (uni-muenchen.de)
Nitrogen6
- Glutamine Synthetase is present in the Testis and is involved in nitrogen homeostasis. (biogenex.com)
- This is the structure of glutamine, the structure of amino acid is composed by 4 elements- carbon, hydrogen, oxygen and nitrogen. (futurelearn.com)
- The first is that glutamine transports substance containing nitrogen. (futurelearn.com)
- Glutamine contains two amidogens and it can transport the substances containing nitrogen from organs in the body to discharge. (futurelearn.com)
- In addition, Glutamine is a regulator of acid-base balance and a nitrogen transporter. (buywell.com)
- In addition, Glutamine is also a major nitrogen transporter and helps to regulate the body's acid-base balance. (buywell.com)
Orphan drug designation1
- FDA previously granted Orphan Drug Designation to L-glutamine for this indication. (fda.gov)
Sickle cell di2
- Glutamine is also used to reduce the acute complications of sickle cell disease (blood disorder) in adults and children. (mayoclinic.org)
- Appropriate studies performed to date have not demonstrated pediatric-specific problems that would limit the usefulness of glutamine to reduce acute complications of sickle cell disease in children 5 years of age and older. (mayoclinic.org)
Grams2
- The recommended dose of L-glutamine is 10 grams to 30 grams per day (based on body weight) taken orally, twice daily. (fda.gov)
- Taking 2 grams of L-glutamine in water on an empty stomach (as directed) caused me to be nauseous, dizzy and anxious. (consumerlab.com)
Alanyl1
- Alanyl-glutamine intermediate CAS 7474 - 05 - 7 of Alanyl-glutamine intermediate series Product Description: Appearance: Colorless to yellowish transparent liquid Purification: ≥99% We are a professional company which integrates R & D, production and trade. (opencroquet.org)
C5H10N2O31
- C5H10N2O3 MW: 146.14 EINECS: 200-292-1 Mol File: 56-85-9.mol L- Glutamine . (opencroquet.org)
Synthetase1
- Over expression of glutamine Synthetase was seen in Testis cancers. (biogenex.com)
Catabolism3
- Humans obtain glutamine through catabolism of proteins in foods they eat. (wikipedia.org)
- A new study shows that glutamine catabolism supports efficient apoptotic cell efferocytosis via non-canonical glutamine transamination but not canonical GLUD1-dependent α-ketoglutarate production, in a process that may operate in human atherosclerosis. (nature.com)
- However, whether glutamine catabolism can bridge the anti-inflammatory response through the machinery of efferocytosis had remained unknown up until now. (nature.com)
Naturally5
- Glutamine is the most abundant naturally occurring, nonessential amino acid in the human body, and one of the few amino acids that can directly cross the blood-brain barrier. (wikipedia.org)
- Glutamine is a substance naturally produced in the body to help regulate cell growth and function. (mayoclinic.org)
- Boiling point 265.74°C (rough estimate) L- Glutamine is an amino acid (a structural unit of protein) that is naturally found in the body. (opencroquet.org)
- Glutamine is a naturally occurring amino acid and is generally safe at the dose you used and even several times higher. (consumerlab.com)
- This naturally fermented source of L-glutamine is vegan-friendly. (lifestylemarkets.com)
Creatine4
- If you're just starting out, or even have been working out and supplementing for some time, all you really need is just the basics: proteins, creatine, glutamine, and maybe some weight gainers. (bodybuildingforyou.com)
- Glutamine is something that doesn't need to be cycled, unlike creatine. (bodybuildingforyou.com)
- How long after the glutamine should creatine be taken? (steroid.com)
- I only ask because someone said that if creatine and glutamine are taken together, one won't be absorbed. (steroid.com)
BCAA1
- By partnering glutamine with BCAA in quantities clinically-proven to be effective in bodybuilding athletes, its tremendous anabolic energy can finally be uncapped, enabling users to achieve levels of muscle protein, glycogen, mass, strength and hardness not possible by relying on the diet alone. (netrition.com)
Essential amino1
- L-glutamine and l-arginine are both conditionally essential amino acids. (livestrong.com)
Muscle glutamine1
- Start using Dynamik Muscle Glutamine today! (sportsfuel.co.nz)
Purity3
- MusclePharm Glutamine is rigorously tested for purity and banned substances, ensuring it meets the highest standards for safety and effectiveness. (musclepharm.com)
- BioSteel Fermented Glutamine is derived through a natural fermentation process, ensuring the highest purity and bioavailability. (veganessentials.com)
- Elevate your fitness experience with BioSteel Fermented Glutamine from Vegan Essentials - the epitome of purity, performance, and plant-based excellence. (veganessentials.com)
Absorption1
- Our formula contains the finest quality L-Glutamine, ensuring maximum absorption and effectiveness. (musclepharm.com)
Arginine3
- Glutamine and arginine may both provide benefits related to exercise. (livestrong.com)
- Both l-glutamine and l-arginine may be helpful in improving a variety of medical conditions and can be useful for more common purposes, such as improved response to exercise. (livestrong.com)
- Although there is a lack of research on the combined effects of l-arginine and l-glutamine, the preliminary data shows that combining the two may benefit those with intestinal inflammation. (livestrong.com)
Enterocytes1
- L-glutamine supports the development of enterocytes, a type of cell that is plentiful in the epithelial lining of the gastrointestinal tract. (allergyresearchgroup.com)
Amino acid in the huma1
- L-glutamine, which is necessary for digestion and normal brain function, is the most plentiful amino acid in the human body. (livestrong.com)
Abundant amino acid2
- Glutamine is regarded as the most abundant amino acid in the body, is mainly synthesized in skeletal muscle 10 , and muscle tissue is the most important site for Gln storage 11 . (nature.com)
- Glutamine is the most abundant amino acid in the body and plays an important role in muscle protein development. (a1supplements.com)
Brain2
- Glutamine is also released, in small amounts, by the lungs and brain. (wikipedia.org)
- L-glutamine also supports muscle glycogen stores, growth hormone production, and can cross the blood-brain barrier where the brain uses it for fuel. (allergyresearchgroup.com)
Intense3
- It hasn't been shown to promote muscle growth but athletes primarily supplement on glutamine due to its ability to inhibit muscle breakdown from increase mental and physical stress during intense workouts or competitions. (predatornutrition.com)
- During prolonged periods of intense exercise, glutamine levels may be depleted faster than the body can replenish them, which limits protein synthesis and can even encourage muscle breakdown. (a1supplements.com)
- BioSteel Fermented Glutamine empowers you to bounce back from intense workouts, allowing you to stay consistent in your fitness routine. (veganessentials.com)
Body's4
- It is non-essential and conditionally essential in humans, meaning the body can usually synthesize sufficient amounts of it, but in some instances of stress, the body's demand for glutamine increases, and glutamine must be obtained from the diet. (wikipedia.org)
- University of Maryland Medical Center notes that l-glutamine is used for improving wound healing and inflammatory bowel disease, treating symptoms of AIDS and cancer and for improving the body's response to athletic training. (livestrong.com)
- By incorporating BioSteel Fermented Glutamine into your daily regimen, you're not only investing in your fitness goals but also fortifying your body's defense mechanisms. (veganessentials.com)
- While glutamine is considered a non-essential amino acid, regular training and life stressors can deplete the body's stores. (sportsfuel.co.nz)
Powders3
- Worked fine just like most other glutamine powders I've used. (mrsupplement.com.au)
- We provide a wide selection of both glutamine tablets and glutamine powders, across a broad range of well-known and popular brands . (discount-supplements.co.uk)
- All of our glutamine powders are unflavoured, meaning you can conveniently add them to any of your favourite sports drinks and take them on the go to fit into your busy lifestyle workout routine. (discount-supplements.co.uk)
Aminotransferase1
- 4S1W: Structure of a putative Glutamine--Fructose-6-Phosphate Aminotransferase from Staphylococcus aureus subsp. (rcsb.org)
Gastrointestinal tract1
- However, the gastrointestinal tract is the greatest user of glutamine in the body because glutamine provides the primary fuel for the nutrient-absorbing cells that line the walls of the small intestine. (alchemyelixir.com)
Body12
- L-glutamine is used to is used to reduce the frequency of painful episodes (crises) in adults and children 5 years of age and older with sickle cell anemia (an inherited blood disorder in which the red blood cells are abnormally shaped [shaped like a sickle] and cannot bring enough oxygen to all parts of the body). (medlineplus.gov)
- Glutamine is one of the most abundant amino acids in the body. (vitanetonline.com)
- The body is capable of making enough of glutamine for its own regular needs although at times of extreme stress and age, the body may need more. (vitanetonline.com)
- This means your body can efficiently absorb and utilize the glutamine for enhanced results. (veganessentials.com)
- As one of the most abundant amino acids in the human body, glutamine has many functions. (discount-supplements.co.uk)
- Skeletal muscle contains the greatest intracellular concentration of glutamine, comprising up to 60 percent of total body glutamine stores, and muscle is the primary storage depot and exporter of glutamine to other tissues. (alchemyelixir.com)
- When the body is low in glutamine it starts breaking down muscle tissue to use the glutamine stored in muscle cells. (sportsfuel.co.nz)
- Glutamine is used by the body for both muscle growth and recovery. (sportsfuel.co.nz)
- Thus, through glutamine, the amidogen is transported away to other places in the body that can metabolize or discharge it. (futurelearn.com)
- When there is more glutamine existing in the body, it can compose more antioxidant substance to maintain the antioxidant capacity in the cell. (futurelearn.com)
- Glutamine can also maintain antioxidant capacity for the body to function normally. (futurelearn.com)
- A growing body of evidence suggests that during certain stressful times, the body may require more Glutamine than it can produce. (buywell.com)
Reactions2
- The most common adverse reactions occurring in greater than 10% of patients treated with L-glutamine were constipation, nausea, headache, abdominal pain, cough, pain in extremity, back pain, and chest pain. (fda.gov)
- Treatment discontinuation due to adverse reactions was reported in 2.7% (n=5) of patients receiving L-glutamine. (fda.gov)
Deficient1
- Many people with cancer are deficient in l-glutamine. (livestrong.com)
Complications of sickle1
- Safety and efficacy of glutamine to reduce acute complications of sickle cell anemia in children younger than 5 years of age has not been established. (mayoclinic.org)
Efficacy2
- Safety and efficacy of glutamine to treat short bowel syndrome in children has not been established. (mayoclinic.org)
- Efficacy was demonstrated by a reduction in the number of sickle cell crises through Week 48 among patients who received L-glutamine compared to those receiving placebo. (fda.gov)
Skeletal1
- Over 60% of the free-floating amino acid pool in skeletal muscle cells is made up of L glutamine . (opencroquet.org)