An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is a LIVER-specific enzyme that is the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.
An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and water and of indoleglycerol phosphate into indole and glyceraldehyde phosphate. (From Enzyme Nomenclature, 1992) EC 4.2.1.20.
An enzyme that catalyzes the hydroxylation of TRYPTOPHAN to 5-HYDROXYTRYPTOPHAN in the presence of NADPH and molecular oxygen. It is important in the biosynthesis of SEROTONIN.
Kynurenine is a metabolic product of the amino acid tryptophan, formed via the kynurenine pathway, and serves as an important intermediate in the biosynthesis of nicotinamide adenine dinucleotide (NAD+) and other neuroactive compounds, while also playing a role in immune response regulation and potential involvement in various neurological disorders.
A brominating agent that replaces hydrogen atoms in benzylic or allylic positions. It is used in the oxidation of secondary alcohols to ketones and in controlled low-energy brominations. (From Miall's Dictionary of Chemistry, 5th ed; Hawley's Condensed Chemical Dictionary, 12th ed,).
Measurement of the intensity and quality of fluorescence.
A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is an extrahepatic enzyme that plays a role in metabolism as the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.
An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precursor of tryptophan and numerous secondary metabolites, including inducible plant defense compounds. EC 4.1.3.27.
Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.
A colorless, odorless, highly water soluble vinyl monomer formed from the hydration of acrylonitrile. It is primarily used in research laboratories for electrophoresis, chromatography, and electron microscopy and in the sewage and wastewater treatment industries.
Xanthurenic acid and its salts, formed as byproducts during the metabolism of tryptophan, are collectively referred to as xanthurenates, which can accumulate in conditions like hyperphenylalaninemia and may contribute to oxidative stress and cellular damage.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A biochemical messenger and regulator, synthesized from the essential amino acid L-TRYPTOPHAN. In humans it is found primarily in the central nervous system, gastrointestinal tract, and blood platelets. Serotonin mediates several important physiological functions including neurotransmission, gastrointestinal motility, hemostasis, and cardiovascular integrity. Multiple receptor families (RECEPTORS, SEROTONIN) explain the broad physiological actions and distribution of this biochemical mediator.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Hydroxyindoleacetic acid (5HIAA) is a major metabolite of serotonin, a neurotransmitter, formed by the action of monoamine oxidase and aldehyde dehydrogenase, and its measurement in urine is often used as a biomarker for serotonin synthesis in clinical and research settings.
An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. (From Enzyme Nomenclature, 1992) EC 4.1.99.1.
An oxidation product of tryptophan metabolism. It may be a free radical scavenger and a carcinogen.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The rate dynamics in chemical or physical systems.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
An enzyme that catalyzes the formation of N-5'-phosphoribosylanthranilic acid from anthranilate and phosphoribosylpyrophosphate, the first step in tryptophan synthesis in E. coli. It exists in a complex with ANTHRANILATE SYNTHASE in bacteria. EC 2.4.2.18.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The property of emitting radiation while being irradiated. The radiation emitted is usually of longer wavelength than that incident or absorbed, e.g., a substance can be irradiated with invisible radiation and emit visible light. X-ray fluorescence is used in diagnosis.
An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.
Benzopyrroles with the nitrogen at the number one carbon adjacent to the benzyl portion, in contrast to ISOINDOLES which have the nitrogen away from the six-membered ring.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An NADPH-dependent flavin monooxygenase that plays a key role in the catabolism of TRYPTOPHAN by catalyzing the HYDROXYLATION of KYNURENINE to 3-hydroxykynurenine. It was formerly characterized as EC 1.14.1.2 and EC 1.99.1.5.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Measurement of the polarization of fluorescent light from solutions or microscopic specimens. It is used to provide information concerning molecular size, shape, and conformation, molecular anisotropy, electronic energy transfer, molecular interaction, including dye and coenzyme binding, and the antigen-antibody reaction.
A metabolite of tryptophan with a possible role in neurodegenerative disorders. Elevated CSF levels of quinolinic acid are correlated with the severity of neuropsychological deficits in patients who have AIDS.
An enzyme in the tryptophan biosynthetic pathway. EC 4.1.1.48.
A water-soluble vitamin of the B complex occurring in various animal and plant tissues. It is required by the body for the formation of coenzymes NAD and NADP. It has PELLAGRA-curative, vasodilating, and antilipemic properties.
The immediate precursor in the biosynthesis of SEROTONIN from tryptophan. It is used as an antiepileptic and antidepressant.
INDOLES which have two keto groups forming QUINONES like structures of the indole aromatic ring.
Colorless, odorless crystals that are used extensively in research laboratories for the preparation of polyacrylamide gels for electrophoresis and in organic synthesis, and polymerization. Some of its polymers are used in sewage and wastewater treatment, permanent press fabrics, and as soil conditioning agents.
Quinolinic acid is a physiologically occurring metabolite of the kynurenine pathway, involved in the metabolism of tryptophan, which functions as a neuroexcitatory agent and has been implicated in several neurological disorders, including Huntington's disease and HIV-associated dementia.
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.
The transfer of energy of a given form among different scales of motion. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed). It includes the transfer of kinetic energy and the transfer of chemical energy. The transfer of chemical energy from one molecule to another depends on proximity of molecules so it is often used as in techniques to measure distance such as the use of FORSTER RESONANCE ENERGY TRANSFER.
Skatole, also known as 3-methylindole, is a foul-smelling, crystalline compound that is a natural product of bacterial breakdown in the intestines and can be found in some plants, contributing to the characteristic odor of feces and certain flowers like jasmine.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
A disease due to deficiency of NIACIN, a B-complex vitamin, or its precursor TRYPTOPHAN. It is characterized by scaly DERMATITIS which is often associated with DIARRHEA and DEMENTIA (the three D's).
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins prepared by recombinant DNA technology.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Any salt or ester of glycerophosphoric acid.
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.
A broad-spectrum excitatory amino acid antagonist used as a research tool.
Proteins found in any species of bacterium.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
An essential amino acid that is required for the production of HISTAMINE.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
A class of organic compounds which contain an anilino (phenylamino) group linked to a salt or ester of naphthalenesulfonic acid. They are frequently used as fluorescent dyes and sulfhydryl reagents.

Enrichment of enzyme activity on deformylation of 1-NFK-lysozyme. (1/5574)

The formamide linkage of an inactive lysozyme derivative (1-NFK-lysozyme), formed by selective ozonization of tryptophan 62 in hen egg-white lysozyme [EC 3.2.1.17] was hydrolyzed with dilute acid faster in the frozen state at about --10 degrees than at 20 degrees. On hydrolysis of 1-NFK-lysozyme the low lytic activity increased to approximately 80% of that of native lysozyme. It is suggested that the binding ability associated with kynurenine 62 in the lysozyme derivative formed by this hydrolysis may be responsible for increase in enzymatic activity.  (+info)

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state. (2/5574)

Unfolded apocytochrome c acquires an alpha-helical conformation upon interaction with lipid. Folding kinetic results below and above the lipid's CMC, together with energy transfer measurements of lipid bound states, and salt-induced compact states in solution, show that the folding transition of apocytochrome c from the unfolded state in solution to a lipid-inserted helical conformation proceeds via a collapsed intermediate state (I(C)). This initial compact state is driven by a hydrophobic collapse of the polypeptide chain in the absence of the heme group and may represent a heme-free analogue of an early compact intermediate detected on the folding pathway of cytochrome c in solution. Insertion into the lipid phase occurs via an unfolding step of I(C) through a more extended state associated with the membrane surface (I(S)). While I(C) appears to be as compact as salt-induced compact states in solution with substantial alpha-helix content, the final lipid-inserted state (Hmic) is as compact as the unfolded state in solution at pH 5 and has an alpha-helix content which resembles that of native cytochrome c.  (+info)

Pathways of electron transfer in Escherichia coli DNA photolyase: Trp306 to FADH. (3/5574)

We describe the results of a series of theoretical calculations of electron transfer pathways between Trp306 and *FADH. in the Escherichia coli DNA photolyase molecule, using the method of interatomic tunneling currents. It is found that there are two conformationally orthogonal tryptophans, Trp359 and Trp382, between donor and acceptor that play a crucial role in the pathways of the electron transfer process. The pathways depend vitally on the aromaticity of tryptophans and the flavin molecule. The results of this calculation suggest that the major pathway of the electron transfer is due to a set of overlapping orthogonal pi-rings, which starts from the donor Trp306, runs through Trp359 and Trp382, and finally reaches the flavin group of the acceptor complex, FADH.  (+info)

Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus. (4/5574)

The location and environment of tryptophans in the soluble and membrane-bound forms of Staphylococcus aureus alpha-toxin were monitored using intrinsic tryptophan fluorescence. Fluorescence quenching of the toxin monomer in solution indicated varying degrees of tryptophan burial within the protein interior. N-Bromosuccinimide readily abolished 80% of the fluorescence in solution. The residual fluorescence of the modified toxin showed a blue-shifted emission maximum, a longer fluorescence lifetime as compared to the unmodified and membrane-bound alpha-toxin, and a 5- to 6-nm red edge excitation shift, all indicating a restricted tryptophan environment and deeply buried tryptophans. In the membrane-bound form, the fluorescence of alpha-toxin was quenched by iodide, indicating a conformational change leading to exposure of some tryptophans. A shorter average lifetime of tryptophans in the membrane-bound alpha-toxin as compared to the native toxin supported the conclusions based on iodide quenching of the membrane-bound toxin. Fluorescence quenching of membrane-bound alpha-toxin using brominated and spin-labeled fatty acids showed no quenching of fluorescence using brominated lipids. However, significant quenching was observed using 5- and 12-doxyl stearic acids. An average depth calculation using the parallax method indicated that the doxyl-quenchable tryptophans are located at an average depth of 10 A from the center of the bilayer close to the membrane interface. This was found to be in striking agreement with the recently described structure of the membrane-bound form of alpha-toxin.  (+info)

A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines. (5/5574)

Prion diseases are closely linked to the conversion of host-encoded cellular prion protein (PrPC) into its pathological isoform (PrPSc). PrP conversion experiments in scrapie infected tissue culture cells, transgenic mice, and cell-free systems usually require unique epitopes and corresponding monoclonal antibodies (MAbs) for the immunological discrimination of exogenously introduced and endogenous PrP compounds (e.g., MAb 3F4, which is directed to an epitope on hamster and human but not on murine PrP). In the current work, we characterize a novel MAb designated L42 that reacts to PrP of a variety of species, including cattle, sheep, goat, dog, human, cat, mink, rabbit, and guinea pig, but does not bind to mouse, hamster, and rat PrP. Therefore, MAb L42 may allow future in vitro conversion and transgenic studies on PrPs of the former species. The MAb L42 epitope on PrPC includes a tyrosine residue at position 144, whereas mouse, rat, and hamster PrPs incorporate tryptophane at this site. To verify this observation, we generated PrP expression vectors coding for authentic or mutated murine PrPCs (i.e., codon 144 encoding tyrosine instead of tryptophan). After transfection into neuroblastoma cells, MAb L42 did not react with immunoblotted wild-type murine PrPC, whereas L42 epitope-tagged murine PrPC was strongly recognized. Immunoblot and fluorescence-activated cell sorting data revealed that tagged PrPC was correctly posttranslationally processed and translocated to the cell surface.  (+info)

Helical structure and packing orientation of the S2 segment in the Shaker K+ channel. (6/5574)

Six transmembrane segments, S1-S6, cluster around the central pore-forming region in voltage-gated K+ channels. To investigate the structural characteristics of the S2 segment in the Shaker K+ channel, we replaced each residue in S2 singly with tryptophan (or with alanine for the native tryptophan). All but one of the 23 Trp mutants expressed voltage-dependent K+ currents in Xenopus oocytes. The effects of the mutations were classified as being of low or high impact on channel gating properties. The periodicity evident in the effects of these mutations supports an alpha-helical structure for the S2 segment. The high- and low-impact residues cluster onto opposite faces of a helical wheel projection of the S2 segment. The low-impact face is also tolerant of single mutations to asparagine. All results are consistent with the idea that the low-impact face projects toward membrane lipids and that changes in S2 packing occur upon channel opening. We conclude that the S2 segment is a transmembrane alpha helix and that the high-impact face packs against other transmembrane segments in the functional channel.  (+info)

A single hydrophobic residue confers barbiturate sensitivity to gamma-aminobutyric acid type C receptor. (7/5574)

Barbiturate sensitivity was imparted to the human rho1 homooligomeric gamma-aminobutyric acid (GABA) receptor channel by mutation of a tryptophan residue at position 328 (Trp328), which is located within the third transmembrane domain. Substitutions of Trp328 with a spectrum of amino acids revealed that nearly all hydrophobic residues produced receptor channels that were both directly activated and modulated by pentobarbital with similar sensitivities. Previous studies with ligand-gated ion channels (including GABA) have demonstrated that even conservative amino acid substitution within the agonist-dependent activation domain (N-terminal extracellular domain) can markedly impair agonist sensitivity. Thus, the lack of significant variation in pentobarbital sensitivity among the Trp328 mutants attests to an intrinsic difference between pentobarbital- and the GABA-dependent activation domain. Compared with the heterooligomeric alphabetagamma receptor channel, the mode of modulation for homooligomeric Trp328 mutants by pentobarbital was more dependent on the GABA concentration, yielding potentiation only at low concentrations of GABA (fractions of their respective EC50 values), yet causing inhibition at higher concentrations. Agonist-related studies have also demonstrated that residue 328 plays an important role in agonist-dependent activation, suggesting a functional interconnection between the GABA and pentobarbital activation domains.  (+info)

Inhibition of myosin ATPase by metal fluoride complexes. (8/5574)

Magnesium (Mg2+) is the physiological divalent cation stabilizing nucleotide or nucleotide analog in the active site of myosin subfragment 1 (S1). In the presence of fluoride, Mg2+ and MgADP form a complex that traps the active site of S1 and inhibits myosin ATPase. The ATPase inactivation rate of the magnesium trapped S1 is comparable but smaller than the other known gamma-phosphate analogs at 1.2 M-1 s-1 with 1 mM MgCl2. The observed molar ratio of Mg/S1 in this complex of 1.58 suggests that magnesium occupies the gamma-phosphate position in the ATP binding site of S1 (S1-MgADP-MgFx). The stability of S1-MgADP-MgFx at 4 degrees C was studied by EDTA chase experiments but decomposition was not observed. However, removal of excess fluoride causes full recovery of the K+-EDTA ATPase activity indicating that free fluoride is necessary for maintaining a stable trap and suggesting that the magnesium fluoride complex is bonded to the bridging oxygen of beta-phosphate more loosely than the other known phosphate analogs. The structure of S1 in S1-MgADP-MgFx was studied with near ultraviolet circular dichroism, total tryptophan fluorescence, and tryptophan residue 510 quenching measurements. These data suggest that S1-MgADP-MgFx resembles the M**.ADP.Pi steady-state intermediate of myosin ATPase. Gallium fluoride was found to compete with MgFx for the gamma-phosphate site in S1-MgADP-MgFx. The ionic radius and coordination geometry of magnesium, gallium and other known gamma-phosphate analogs were compared and identified as important in determining which myosin ATPase intermediate the analog mimics.  (+info)

Tryptophan is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C11H12N2O2. Tryptophan plays a crucial role in various biological processes as it serves as a precursor to several important molecules, including serotonin, melatonin, and niacin (vitamin B3). Serotonin is a neurotransmitter involved in mood regulation, appetite control, and sleep-wake cycles, while melatonin is a hormone that regulates sleep-wake patterns. Niacin is essential for energy production and DNA repair.

Foods rich in tryptophan include turkey, chicken, fish, eggs, cheese, milk, nuts, seeds, and whole grains. In some cases, tryptophan supplementation may be recommended to help manage conditions related to serotonin imbalances, such as depression or insomnia, but this should only be done under the guidance of a healthcare professional due to potential side effects and interactions with other medications.

Tryptophan oxygenase, also known as tryptophan 2,3-dioxygenase (TDO) or tryptophan pyrrolase, is an enzyme that catalyzes the breakdown of the essential amino acid tryptophan. This enzyme requires molecular oxygen and plays a crucial role in regulating tryptophan levels within the body.

The reaction catalyzed by tryptophan oxygenase involves the oxidation of the indole ring of tryptophan, leading to the formation of N-formylkynurenine. This metabolite is further broken down through several enzymatic steps to produce other biologically active compounds, such as kynurenine and niacin (vitamin B3).

Tryptophan oxygenase activity is primarily found in the liver and is induced by various factors, including corticosteroids, cytokines, and tryptophan itself. The regulation of this enzyme has implications for several physiological processes, such as immune response, neurotransmitter synthesis, and energy metabolism. Dysregulation of tryptophan oxygenase activity can contribute to the development of various pathological conditions, including neurological disorders and cancer.

Tryptophan synthase is a bacterial enzyme that catalyzes the final step in the biosynthesis of the essential amino acid tryptophan. It is a complex enzyme composed of two types of subunits, α and β, which form an αββα tetrameric structure.

Tryptophan synthase catalyzes the conversion of indole-3-glycerol phosphate (IGP) and L-serine into tryptophan through two separate reactions that occur in a coordinated manner within the active site of the enzyme. In the first reaction, the α subunit catalyzes the breakdown of IGP into indole and glyceraldehyde-3-phosphate (G3P). The indole molecule then moves through a tunnel to the active site of the β subunit, where it is combined with L-serine to form tryptophan in the second reaction.

The overall reaction catalyzed by tryptophan synthase is:

Indole-3-glycerol phosphate + L-serine → L-tryptophan + glyceraldehyde-3-phosphate

Tryptophan synthase plays a critical role in the biosynthesis of tryptophan, which is an essential amino acid that cannot be synthesized by humans and must be obtained through diet. Defects in tryptophan synthase can lead to various genetic disorders, such as hyperbeta-alaninemia and tryptophanuria.

Tryptophan hydroxylase is an enzyme that plays a crucial role in the synthesis of neurotransmitters and hormones, including serotonin and melatonin. It catalyzes the conversion of the essential amino acid tryptophan to 5-hydroxytryptophan (5-HTP), which is then further converted to serotonin. This enzyme exists in two isoforms, TPH1 and TPH2, with TPH1 primarily located in peripheral tissues and TPH2 mainly found in the brain. The regulation of tryptophan hydroxylase activity has significant implications for mood, appetite, sleep, and pain perception.

Kynurenine is an organic compound that is produced in the human body as part of the metabolism of the essential amino acid tryptophan. It is an intermediate in the kynurenine pathway, which leads to the production of several neuroactive compounds and NAD+, a coenzyme involved in redox reactions.

Kynurenine itself does not have any known physiological function, but some of its metabolites have been found to play important roles in various biological processes, including immune response, inflammation, and neurological function. For example, the kynurenine pathway produces several neuroactive metabolites that can act as agonists or antagonists at various receptors in the brain, affecting neuronal excitability, synaptic plasticity, and neurotransmission.

Abnormalities in the kynurenine pathway have been implicated in several neurological disorders, including depression, schizophrenia, Alzheimer's disease, and Huntington's disease. Therefore, understanding the regulation of this pathway and its metabolites has become an important area of research in neuroscience and neuropsychopharmacology.

Bromosuccinimide is a chemical compound with the formula C4H2BrNO2S. It is a white crystalline solid that is used as a brominating agent in organic synthesis. Bromosuccinimide is an important reagent for introducing bromine into organic molecules, and it is particularly useful for carrying out selective brominations of unsaturated compounds.

Bromosuccinimide is typically used in solution, and it can be prepared by reacting succinimide with bromine in the presence of a base. It is a relatively stable compound, but it can decompose if heated or if it is exposed to strong oxidizing agents. Bromosuccinimide is not commonly used in medical applications, but it may be encountered in laboratory settings where organic synthesis is performed.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catalyzes the oxidation of L-tryptophan to N-formylkynurenine, which is the first and rate-limiting step in the kynurenine pathway. This enzymatic reaction plays a crucial role in regulating tryptophan metabolism and immune responses. IDO is expressed in various tissues, including the brain, liver, and placenta, as well as in some immune cells such as dendritic cells and macrophages. It can be upregulated by inflammatory stimuli, and its expression has been associated with immune tolerance and suppression of T-cell responses. IDO is also being investigated as a potential therapeutic target for various diseases, including cancer, autoimmune disorders, and neuropsychiatric conditions.

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.

Ortho-Aminobenzoates are chemical compounds that contain a benzene ring substituted with an amino group in the ortho position and an ester group in the form of a benzoate. They are often used as pharmaceutical intermediates, plastic additives, and UV stabilizers. In medical contexts, one specific ortho-aminobenzoate, para-aminosalicylic acid (PABA), is an antibiotic used in the treatment of tuberculosis. However, it's important to note that "ortho-aminobenzoates" in general do not have a specific medical definition and can refer to any compound with this particular substitution pattern on a benzene ring.

Acrylamide is a chemical that is primarily used in the production of polyacrylamide, which is a widely used flocculent in the treatment of wastewater and drinking water. Acrylamide itself is not intentionally added to food or consumer products. However, it can form in certain foods during high-temperature cooking processes, such as frying, roasting, and baking, particularly in starchy foods like potatoes and bread. This occurs due to a reaction between amino acids (such as asparagine) and reducing sugars (like glucose or fructose) under high heat.

Acrylamide has been classified as a probable human carcinogen based on animal studies, but the risks associated with dietary exposure are still being researched. Public health organizations recommend minimizing acrylamide intake by varying cooking methods and avoiding overly browned or burnt foods.

I'm sorry for any confusion, but "xanthurenates" is not a recognized term in medicine or physiology. It seems that you might be referring to "xanthurenic acid," which is a metabolic byproduct produced during the breakdown of the amino acid tryptophan. An accumulation of xanthurenic acid can occur due to certain genetic disorders, such as Hartnup disease or defects in the coenzyme Q10 synthesis pathway. However, without more context, it's difficult for me to provide a precise definition related to your specific question. If you could provide additional information, I would be happy to help further!

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).

Serotonin, also known as 5-hydroxytryptamine (5-HT), is a monoamine neurotransmitter that is found primarily in the gastrointestinal (GI) tract, blood platelets, and the central nervous system (CNS) of humans and other animals. It is produced by the conversion of the amino acid tryptophan to 5-hydroxytryptophan (5-HTP), and then to serotonin.

In the CNS, serotonin plays a role in regulating mood, appetite, sleep, memory, learning, and behavior, among other functions. It also acts as a vasoconstrictor, helping to regulate blood flow and blood pressure. In the GI tract, it is involved in peristalsis, the contraction and relaxation of muscles that moves food through the digestive system.

Serotonin is synthesized and stored in serotonergic neurons, which are nerve cells that use serotonin as their primary neurotransmitter. These neurons are found throughout the brain and spinal cord, and they communicate with other neurons by releasing serotonin into the synapse, the small gap between two neurons.

Abnormal levels of serotonin have been linked to a variety of disorders, including depression, anxiety, schizophrenia, and migraines. Medications that affect serotonin levels, such as selective serotonin reuptake inhibitors (SSRIs), are commonly used to treat these conditions.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Hydroxyindoleacetic acid (5HIAA) is a major metabolite of the neurotransmitter serotonin, formed in the body through the enzymatic degradation of serotonin by monoamine oxidase and aldehyde dehydrogenase. 5HIAA is primarily excreted in the urine and its measurement can be used as a biomarker for serotonin synthesis and metabolism in the body.

Increased levels of 5HIAA in the cerebrospinal fluid or urine may indicate conditions associated with excessive serotonin production, such as carcinoid syndrome, while decreased levels may be seen in certain neurodegenerative disorders, such as Parkinson's disease. Therefore, measuring 5HIAA levels can have diagnostic and therapeutic implications for these conditions.

Tryptophanase is not a medical term per se, but rather a biochemical term used to describe an enzyme. However, I can provide a biochemical definition for you:

Tryptophanase (TPase or TnaA) is a pyridoxal-phosphate (PLP) dependent enzyme found in certain bacteria, such as Escherichia coli, that catalyzes the breakdown of the essential amino acid tryptophan into several compounds. The primary reaction catalyzed by tryptophanase is the conversion of L-tryptophan to indole, pyruvate, and ammonia. This reaction also produces ATP and ADP as co-products.

The production of indole from tryptophan by tryptophanase has diagnostic value in microbiology, as the presence of indole in a culture medium can indicate the growth of certain bacterial species that produce this enzyme.

3-Hydroxyanthranilic acid is an intermediate metabolite in the catabolism (breakdown) of tryptophan, an essential amino acid. It is formed from the oxidation of 3-hydroxykynurenine by the enzyme kynureninase. Further breakdown of 3-hydroxyanthranilic acid can lead to the formation of various other metabolites, including quinolinic acid and picolinic acid, which are involved in the synthesis of nicotinamide adenine dinucleotide (NAD+), a coenzyme that plays a crucial role in cellular metabolism.

Abnormal accumulation or dysregulation of 3-hydroxyanthranilic acid has been implicated in several pathological conditions, including neurodegenerative disorders and certain types of cancer. However, more research is needed to fully understand the role of this metabolite in human health and disease.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

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.

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.

Phenylalanine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet or supplementation. It's one of the building blocks of proteins and is necessary for the production of various molecules in the body, such as neurotransmitters (chemical messengers in the brain).

Phenylalanine has two forms: L-phenylalanine and D-phenylalanine. L-phenylalanine is the form found in proteins and is used by the body for protein synthesis, while D-phenylalanine has limited use in humans and is not involved in protein synthesis.

Individuals with a rare genetic disorder called phenylketonuria (PKU) must follow a low-phenylalanine diet or take special medical foods because they are unable to metabolize phenylalanine properly, leading to its buildup in the body and potential neurological damage.

'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.

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.

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

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

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

Anthranilate phosphoribosyltransferase is an enzyme involved in the metabolism of tryptophan, an essential amino acid. This enzyme catalyzes the conversion of anthranilic acid to 1-(o-amino phenyl)phosphoric acid, which is a critical step in the biosynthesis of the aromatic compound known as quinoline.

The reaction catalyzed by anthranilate phosphoribosyltransferase involves the transfer of a phosphoribosyl group from phosphoribosyl pyrophosphate (PRPP) to anthranilic acid, resulting in the formation of 1-(o-amino phenyl)phosphoric acid and pyrophosphate. This reaction is an important part of the tryptophan degradation pathway, which helps regulate the levels of this essential amino acid in the body.

Deficiencies or mutations in anthranilate phosphoribosyltransferase can lead to various metabolic disorders, including a rare genetic condition known as autosomal recessive alkaptonuria (ARA). ARA is characterized by the accumulation of homogentisic acid and its oxidation product, melanin, in various tissues, leading to joint stiffness, darkened skin, and other symptoms.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Fluorescence is not a medical term per se, but it is widely used in the medical field, particularly in diagnostic tests, medical devices, and research. Fluorescence is a physical phenomenon where a substance absorbs light at a specific wavelength and then emits light at a longer wavelength. This process, often referred to as fluorescing, results in the emission of visible light that can be detected and measured.

In medical terms, fluorescence is used in various applications such as:

1. In-vivo imaging: Fluorescent dyes or probes are introduced into the body to highlight specific structures, cells, or molecules during imaging procedures. This technique can help doctors detect and diagnose diseases such as cancer, inflammation, or infection.
2. Microscopy: Fluorescence microscopy is a powerful tool for visualizing biological samples at the cellular and molecular level. By labeling specific proteins, nucleic acids, or other molecules with fluorescent dyes, researchers can observe their distribution, interactions, and dynamics within cells and tissues.
3. Surgical guidance: Fluorescence-guided surgery is a technique where surgeons use fluorescent markers to identify critical structures such as blood vessels, nerves, or tumors during surgical procedures. This helps ensure precise and safe surgical interventions.
4. Diagnostic tests: Fluorescence-based assays are used in various diagnostic tests to detect and quantify specific biomarkers or analytes. These assays can be performed using techniques such as enzyme-linked immunosorbent assay (ELISA), polymerase chain reaction (PCR), or flow cytometry.

In summary, fluorescence is a physical process where a substance absorbs and emits light at different wavelengths. In the medical field, this phenomenon is harnessed for various applications such as in-vivo imaging, microscopy, surgical guidance, and diagnostic tests.

Tryptophan-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join tryptophan, one of the twenty standard amino acids, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between tryptophan and the tRNA during the translation process, where genetic information from messenger RNA (mRNA) is translated into a specific protein sequence. The correct pairing of amino acids with their respective tRNAs is essential for maintaining the fidelity of protein synthesis and ensuring the production of functional proteins.

Indole is not strictly a medical term, but it is a chemical compound that can be found in the human body and has relevance to medical and biological research. Indoles are organic compounds that contain a bicyclic structure consisting of a six-membered benzene ring fused to a five-membered pyrrole ring.

In the context of medicine, indoles are particularly relevant due to their presence in certain hormones and other biologically active molecules. For example, the neurotransmitter serotonin contains an indole ring, as does the hormone melatonin. Indoles can also be found in various plant-based foods, such as cruciferous vegetables (e.g., broccoli, kale), and have been studied for their potential health benefits.

Some indoles, like indole-3-carbinol and diindolylmethane, are found in these vegetables and can have anti-cancer properties by modulating estrogen metabolism, reducing inflammation, and promoting cell death (apoptosis) in cancer cells. However, it is essential to note that further research is needed to fully understand the potential health benefits and risks associated with indoles.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Kynurenine 3-Monooxygenase (KMO) is an enzyme that is involved in the metabolism of the amino acid tryptophan. Specifically, it is a key enzyme in the kynurenine pathway, which is the primary route of tryptophan breakdown in mammals.

KMO catalyzes the conversion of L-kynurenine to 3-hydroxykynurenine using molecular oxygen and nicotinamide adenine dinucleotide phosphate (NADPH) as cofactors. This reaction is an important step in the production of several neuroactive metabolites, including quinolinic acid and kynurenic acid, which have been implicated in various neurological disorders such as Alzheimer's disease, Parkinson's disease, and depression.

Inhibition of KMO has been suggested as a potential therapeutic strategy for the treatment of these disorders due to its role in regulating the balance between neuroprotective and neurotoxic kynurenine metabolites.

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.

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.

Fluorescence Polarization (FP) is not a medical term per se, but a technique used in medical research and diagnostics. Here's a general definition:

Fluorescence Polarization is a biophysical technique used to measure the rotational movement of molecules in solution after they have been excited by polarized light. When a fluorophore (a fluorescent molecule) absorbs light, its electrons become excited and then return to their ground state, releasing energy in the form of light. This emitted light often has different properties than the incident light, one of which can be its polarization. If the fluorophore is large or bound to a large structure, it may not rotate significantly during the time between absorption and emission, resulting in emitted light that maintains the same polarization as the excitation light. Conversely, if the fluorophore is small or unbound, it will rotate rapidly during this period, and the emitted light will be depolarized. By measuring the degree of polarization of the emitted light, researchers can gain information about the size, shape, and mobility of the fluorophore and the molecules to which it is attached. This technique is widely used in various fields including life sciences, biochemistry, and diagnostics.

Quinolinic acid is a metabolite found in the human body, produced during the metabolism of tryptophan, an essential amino acid. It is a component of the kynurenine pathway and acts as a neuroexcitatory chemical in the brain. In excessive amounts, quinolinic acid can lead to neurotoxicity, causing damage to neurons and contributing to several neurological disorders such as Huntington's disease, Alzheimer's disease, Parkinson's disease, AIDS-dementia complex, and multiple sclerosis. It also plays a role in the pathogenesis of psychiatric conditions like schizophrenia and major depressive disorder.

Indole-3-glycerol-phosphate synthase (IGPS) is an enzyme that catalyzes the conversion of tryptophan into indole-3-glycerol phosphate, which is a key intermediate in the biosynthesis of various physiologically important compounds such as auxins (a type of plant hormone). In humans, defects in the IGPS enzyme have been associated with the disorder phenylketonuria (PKU), which is characterized by an inability to metabolize the amino acid phenylalanine. However, it's worth noting that IGPS primarily functions in the context of plant and microbial metabolism.

Niacin, also known as vitamin B3 or nicotinic acid, is a water-soluble vitamin that is essential for human health. It is a crucial component of the coenzymes NAD (nicotinamide adenine dinucleotide) and NADP (nicotinamide adenine dinucleotide phosphate), which play key roles in energy production, DNA repair, and cellular signaling.

Niacin can be obtained from various dietary sources, including meat, poultry, fish, legumes, whole grains, and fortified foods. It is also available as a dietary supplement and prescription medication. Niacin deficiency can lead to a condition called pellagra, which is characterized by symptoms such as diarrhea, dermatitis, dementia, and, if left untreated, death.

In addition to its role in energy metabolism and DNA repair, niacin has been shown to have potential benefits for cardiovascular health, including lowering LDL (low-density lipoprotein) cholesterol and triglyceride levels while raising HDL (high-density lipoprotein) cholesterol levels. However, high-dose niacin therapy can also have adverse effects, such as flushing, itching, and liver toxicity, so it should be used under the guidance of a healthcare professional.

5-Hydroxytryptophan (5-HTP) is a chemical compound that is produced by the body as a precursor to serotonin, a neurotransmitter that helps regulate mood, appetite, sleep, and pain sensation. 5-HTP is not present in food but can be derived from the amino acid tryptophan, which is found in high-protein foods such as turkey, chicken, milk, and cheese.

5-HTP supplements are sometimes used to treat conditions related to low serotonin levels, including depression, anxiety, insomnia, migraines, and fibromyalgia. However, the effectiveness of 5-HTP for these conditions is not well established, and it can have side effects and interact with certain medications. Therefore, it's important to consult a healthcare provider before taking 5-HTP supplements.

Indolequinones are a type of chemical compound that consist of an indole ring, which is a heterocyclic aromatic organic compound, fused to a quinone ring. They can be found in some natural sources, including certain types of bacteria and fungi, as well as in synthetic forms.

Indolequinones have been studied for their potential use in medical treatments, particularly in the area of cancer research. Some indolequinones have been shown to have antitumor properties and are being investigated as possible chemotherapeutic agents. However, they can also be toxic and may have side effects, so further research is needed to determine their safety and effectiveness for medical use.

Acrylamides are a type of chemical that can form in some foods during high-temperature cooking processes, such as frying, roasting, and baking. They are created when certain amino acids (asparagine) and sugars in the food react together at temperatures above 120°C (248°F). This reaction is known as the Maillard reaction.

Acrylamides have been classified as a probable human carcinogen by the International Agency for Research on Cancer (IARC), based on studies in animals. However, more research is needed to fully understand the potential health risks associated with acrylamide exposure from food.

Public health organizations recommend limiting acrylamide intake by following some cooking practices such as:

* Avoiding overcooking or burning foods
* Soaking potatoes (which are high in asparagine) in water before frying to reduce the formation of acrylamides
* Choosing raw, unprocessed, or minimally processed foods when possible.

Quinolinic acid is a type of organic compound that belongs to the class of heterocyclic compounds known as quinolines, which contain a bicyclic system made up of a benzene ring fused to a piperidine ring. Quinolinic acid is specifically a derivative of quinoline with a carboxylic acid functional group.

In the context of medicine and biology, quinolinic acid is an endogenous excitatory neurotransmitter and a metabolite in the kynurenine pathway of tryptophan metabolism. It is mainly produced in the brain by activated microglia and to some extent by macrophages, neurons, and astrocytes.

Quinolinic acid has been implicated in several neurological disorders, including Huntington's disease, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis (ALS), HIV-associated dementia, and depression. High levels of quinolinic acid can cause excitotoxicity, which is a process of neurotoxicity induced by excessive stimulation of glutamate receptors leading to neuronal damage or death. It has also been suggested that quinolinic acid may play a role in the pathogenesis of some psychiatric disorders, such as schizophrenia and bipolar disorder.

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

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Transfer RNA (tRNA) for tryptophan (Trp) is a specific type of tRNA molecule that plays a crucial role in protein synthesis. In the process of translation, genetic information from messenger RNA (mRNA) is translated into a corresponding sequence of amino acids to form a protein.

Tryptophan is one of the twenty standard amino acids found in proteins. Each tRNA molecule carries a specific amino acid that corresponds to a particular codon (a sequence of three nucleotides) on the mRNA. The tRNA with tryptophan attached to it recognizes and binds to the mRNA codon UGG, which is the only codon that specifies tryptophan in the genetic code.

The tRNA molecule has a characteristic cloverleaf-like structure, composed of a stem region made up of base pairs and loop regions containing unpaired nucleotides. The anticodon loop contains the complementary sequence to the mRNA codon, allowing for specific recognition and binding. The other end of the tRNA molecule carries the amino acid, in this case tryptophan, which is attached via an ester linkage to a specific nucleotide called the 3'-end of the tRNA.

In summary, tRNA (Trp) is a key player in protein synthesis, responsible for delivering tryptophan to the ribosome during translation, where it can be incorporated into the growing polypeptide chain according to the genetic information encoded in mRNA.

"Energy transfer" is a general term used in the field of physics and physiology, including medical sciences, to describe the process by which energy is passed from one system, entity, or location to another. In the context of medicine, energy transfer often refers to the ways in which cells and organ systems exchange and utilize various forms of energy for proper functioning and maintenance of life.

In a more specific sense, "energy transfer" may refer to:

1. Bioenergetics: This is the study of energy flow through living organisms, including the conversion, storage, and utilization of energy in biological systems. Key processes include cellular respiration, photosynthesis, and metabolic pathways that transform energy into forms useful for growth, maintenance, and reproduction.
2. Electron transfer: In biochemistry, electrons are transferred between molecules during redox reactions, which play a crucial role in energy production and consumption within cells. Examples include the electron transport chain (ETC) in mitochondria, where high-energy electrons from NADH and FADH2 are passed along a series of protein complexes to generate an electrochemical gradient that drives ATP synthesis.
3. Heat transfer: This is the exchange of thermal energy between systems or objects due to temperature differences. In medicine, heat transfer can be relevant in understanding how body temperature is regulated and maintained, as well as in therapeutic interventions such as hyperthermia or cryotherapy.
4. Mechanical energy transfer: This refers to the transmission of mechanical force or motion from one part of the body to another. For instance, muscle contractions generate forces that are transmitted through tendons and bones to produce movement and maintain posture.
5. Radiation therapy: In oncology, ionizing radiation is used to treat cancer by transferring energy to malignant cells, causing damage to their DNA and leading to cell death or impaired function.
6. Magnetic resonance imaging (MRI): This non-invasive diagnostic technique uses magnetic fields and radio waves to excite hydrogen nuclei in the body, which then release energy as they return to their ground state. The resulting signals are used to generate detailed images of internal structures and tissues.

In summary, "energy transfer" is a broad term that encompasses various processes by which different forms of energy (thermal, mechanical, electromagnetic, etc.) are exchanged or transmitted between systems or objects in the context of medicine and healthcare.

Skatole is a medical term that refers to a chemical compound with the formula C9H9NO2. It is a crystalline substance with an extremely foul odor, resembling that of feces. Skatole is produced in the body as a byproduct of bacterial breakdown of tryptophan, an essential amino acid, in the intestines. Normally, skatole is excreted in the feces and does not cause any problems.

However, when there is an overgrowth of bacteria in the intestines or a problem with the normal flow of bile, which helps to eliminate skatole from the body, skatole can accumulate in the bloodstream and tissues. This can lead to a condition called "skatole poisoning," which can cause symptoms such as nausea, vomiting, abdominal pain, and neurological problems.

Skatole is also used in perfumes and other fragrances to create a fecal or animalistic odor, although it is typically used in very small amounts due to its strong smell.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Pellagra is a nutritional disorder caused by a deficiency of niacin (vitamin B3) or tryptophan, an amino acid that the body can convert into niacin. It's characterized by the four D's: diarrhea, dermatitis, dementia, and death. The skin lesions typically appear on sun-exposed areas and are often described as "photosensitive." Other symptoms can include inflammation of the mucous membranes, mouth sores, anemia, and depression. If left untreated, pellagra can be fatal. It was once common in regions where people subsisted on corn as a staple food, as corn is low in tryptophan and contains niacin in a form that is not easily absorbed by the body. Nowadays, it's most commonly seen in alcoholics, people with malabsorption disorders, and those with severely restricted diets.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

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.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

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.

Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.

Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).

In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.

Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.

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

Kynurenic acid is a metabolite of the amino acid tryptophan, which is formed through the kynurenine pathway. It functions as an antagonist at glutamate receptors and acts as a neuroprotective agent by blocking excessive stimulation of NMDA receptors in the brain. Additionally, kynurenic acid also has anti-inflammatory properties and is involved in the regulation of the immune response. Abnormal levels of kynurenic acid have been implicated in several neurological disorders such as schizophrenia, epilepsy, and Huntington's disease.

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

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

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

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

Amino acid transport systems refer to the various membrane transport proteins that are responsible for the active or passive translocation of amino acids across cell membranes in the body. These transport systems play a crucial role in maintaining amino acid homeostasis within cells and regulating their availability for protein synthesis, neurotransmission, and other physiological processes.

There are several distinct amino acid transport systems, each with its own specificity for particular types of amino acids or related molecules. These systems can be classified based on their energy requirements, substrate specificity, and membrane localization. Some of the major amino acid transport systems include:

1. System A - This is a sodium-dependent transport system that primarily transports small, neutral amino acids such as alanine, serine, and proline. It has several subtypes (ASC, A, and AN) with different substrate affinities and kinetic properties.
2. System L - This is a sodium-independent transport system that transports large, neutral amino acids such as leucine, isoleucine, valine, phenylalanine, and tryptophan. It has several subtypes (L1, L2, and y+L) with different substrate specificities and transport mechanisms.
3. System B0 - This is a sodium-dependent transport system that transports both neutral and basic amino acids such as arginine, lysine, and ornithine. It has several subtypes (B0,+, B0-, and b0,+) with different substrate affinities and kinetic properties.
4. System y+ - This is a sodium-independent transport system that transports primarily basic amino acids such as arginine, lysine, and ornithine. It has several subtypes (y+L, y+, b0,+) with different substrate specificities and transport mechanisms.
5. System X-AG - This is a sodium-independent antiporter system that exchanges glutamate and aspartate for neutral amino acids such as cystine, serine, and threonine. It plays an essential role in maintaining redox homeostasis by regulating the intracellular levels of cysteine, a precursor of glutathione.

These transport systems are critical for maintaining cellular homeostasis and regulating various physiological processes such as protein synthesis, neurotransmission, and immune function. Dysregulation of these transport systems has been implicated in several diseases, including cancer, neurological disorders, and cardiovascular disease. Therefore, understanding the molecular mechanisms underlying these transport systems is essential for developing novel therapeutic strategies to treat these conditions.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

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

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

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

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

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

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

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

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

Histidine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H9N3O2. Histidine plays a crucial role in several physiological processes, including:

1. Protein synthesis: As an essential amino acid, histidine is required for the production of proteins, which are vital components of various tissues and organs in the body.

2. Hemoglobin synthesis: Histidine is a key component of hemoglobin, the protein in red blood cells responsible for carrying oxygen throughout the body. The imidazole side chain of histidine acts as a proton acceptor/donor, facilitating the release and uptake of oxygen by hemoglobin.

3. Acid-base balance: Histidine is involved in maintaining acid-base homeostasis through its role in the biosynthesis of histamine, which is a critical mediator of inflammatory responses and allergies. The decarboxylation of histidine results in the formation of histamine, which can increase vascular permeability and modulate immune responses.

4. Metal ion binding: Histidine has a high affinity for metal ions such as zinc, copper, and iron. This property allows histidine to participate in various enzymatic reactions and maintain the structural integrity of proteins.

5. Antioxidant defense: Histidine-containing dipeptides, like carnosine and anserine, have been shown to exhibit antioxidant properties by scavenging reactive oxygen species (ROS) and chelating metal ions. These compounds may contribute to the protection of proteins and DNA from oxidative damage.

Dietary sources of histidine include meat, poultry, fish, dairy products, and wheat germ. Histidine deficiency is rare but can lead to growth retardation, anemia, and impaired immune function.

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.

Guanidine is not typically defined in the context of medical terminology, but rather, it is a chemical compound with the formula NH2(C=NH)NH2. However, guanidine and its derivatives do have medical relevance:

1. Guanidine is used as a medication in some neurological disorders, such as stiff-person syndrome, to reduce muscle spasms and rigidity. It acts on the central nervous system to decrease abnormal nerve impulses that cause muscle spasticity.

2. Guanidine derivatives are found in various medications used for treating diabetes, like metformin. These compounds help lower glucose production in the liver and improve insulin sensitivity in muscle cells.

3. In some cases, guanidine is used as a skin penetration enhancer in transdermal drug delivery systems to increase the absorption of certain medications through the skin.

It is essential to note that guanidine itself has limited medical use due to its potential toxicity and narrow therapeutic window. Its derivatives, like metformin, are more commonly used in medical practice.

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.

Apoproteins are the protein components of lipoprotein complexes, which are responsible for transporting fat molecules, such as cholesterol and triglycerides, throughout the body. Apoproteins play a crucial role in the metabolism of lipids by acting as recognition signals that allow lipoproteins to interact with specific receptors on cell surfaces.

There are several different types of apoproteins, each with distinct functions. For example, apolipoprotein A-1 (apoA-1) is the major protein component of high-density lipoproteins (HDL), which are responsible for transporting excess cholesterol from tissues to the liver for excretion. Apolipoprotein B (apoB) is a large apoprotein found in low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a). ApoB plays a critical role in the assembly and secretion of VLDL from the liver, and it also mediates the uptake of LDL by cells.

Abnormalities in apoprotein levels or function can contribute to the development of various diseases, including cardiovascular disease, diabetes, and Alzheimer's disease. Therefore, measuring apoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Anilino Naphthalenesulfonates are a group of compounds that contain both aniline and naphthalene sulfonate components. Aniline is a organic compound with the formula C6H5NH2, and naphthalene sulfonate is the sodium salt of naphthalene-1,5-disulfonic acid.

Anilino Naphthalenesulfonates are commonly used as fluorescent dyes in various applications such as histology, microscopy, and flow cytometry. These compounds exhibit strong fluorescence under ultraviolet light and can be used to label and visualize specific structures or molecules of interest. Examples of Anilino Naphthalenesulfonates include Propidium Iodide, Acridine Orange, and Hoechst 33258.

It is important to note that while these compounds are widely used in research and diagnostic settings, they may also have potential hazards and should be handled with appropriate safety precautions.

So high levels of tryptophan prevent tryptophan synthesis through a negative feedback loop, and when the cell's tryptophan ... Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino ... Hopkins recovered tryptophan from hydrolysed casein, recovering 4-8 g of tryptophan from 600 g of crude casein. As an essential ... By this reaction, tryptophan gives rise to tryptophol. Tryptophan affects brain serotonin synthesis when given orally in a ...
L-tryptophan Thus, the two substrates of this enzyme are dimethylallyl diphosphate and L-tryptophan, whereas its two products ... tryptophan dimethylallyl transferase, DMAT synthetase, and 4-(gamma,gamma-dimethylallyl)tryptophan synthase. Lee SL, Floss HG, ... In enzymology, a tryptophan dimethylallyltransferase (EC 2.5.1.34) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is dimethylallyl-diphosphate:L-tryptophan dimethylallyltransferase. Other names in ...
The activity of tryptophan hydroxylase (i.e. the rate at which it converts L-tryptophan into the serotonin precursor L-5- ... Tryptophan+Hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) See also tryptophan hydroxylase ... The pathway for the synthesis of serotonin from tryptophan Metabolic pathway from tryptophan to serotonin Biology portal ... Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin ...
... may refer to: Tryptophan 2,3-dioxygenase, an enzyme Indoleamine 2,3-dioxygenase, an enzyme This set index ...
... may refer to: Tryptophanyl aminopeptidase, an enzyme Tryptophanamidase, an enzyme This set index page ...
... (TTQ) is an enzyme cofactor, generated by posttranslational modification of amino acids within the ... Amicyanin Davidson, V. L.; Liu, A. (2012). "Tryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational ... Davidson VL, Liu A (2009). "Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor ...
L-tryptophan aminotransferase, and L-tryptophan transaminase. This enzyme participates in tryptophan metabolism. It employs one ... In enzymology, a tryptophan transaminase (EC 2.6.1.27) is an enzyme that catalyzes the chemical reaction L-tryptophan + 2- ... The systematic name of this enzyme class is L-tryptophan:2-oxoglutarate aminotransferase. Other names in common use include L- ... O'Neil SR, DeMoss RD (1968). "Tryptophan transaminase from Clostridium sporogenes". Arch. Biochem. Biophys. 127 (1): 361-9. doi ...
In enzymology, a tryptophan dehydrogenase (EC 1.4.1.19) is an enzyme that catalyzes the chemical reaction L-tryptophan + NAD(P ... Vackova K, Mehta A, Kutacek M (1985). "Tryptophan aminotransferase and tryptophan dehydrogenase - activities in some cell ... L-tryptophan dehydrogenase, L-tryptophan dehydrogenase, L-Trp-dehydrogenase, and TDH. This enzyme has at least one effector, ... The systematic name of this enzyme class is L-tryptophan:NAD(P)+ oxidoreductase (deaminating). Other names in common use ...
Tryptophan is one of the twenty standard amino acids and one of nine essential amino acids for humans. As such, tryptophan is a ... Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyses the final two steps in the biosynthesis ... The active sites of tryptophan synthase are allosterically coupled. Subunits: Tryptophan synthase typically exists as an α-ββ-α ... generating the corresponding tryptophan analogues. As humans do not have tryptophan synthase, this enzyme has been explored as ...
... proteins which make more tryptophan. When the cellular levels of tryptophan decline, the tryptophan molecules on the repressor ... The (tryptophan) repressor is a 25 kD protein homodimer which regulates transcription of the tryptophan biosynthetic pathway in ... When the amino acid tryptophan is in plentiful supply in the cell, trpR binds 2 molecules of tryptophan, which alters its ... The trp operon is active only when cellular tryptophan is scarce. If there isn't enough tryptophan, the repressor protein ...
C-glycosyltryptophan is a sugar-loaded amino acid that strongly correlates with age. Coghlan, Andy (July 10, 2013). "Blood test to estimate your age and predict health". New Scientist. Retrieved September 9, 2015. v t e (All stub articles, Amine stubs, Sugars, Chemistry ...
In enzymology, a tryptophan-phenylpyruvate transaminase (EC 2.6.1.28) is an enzyme that catalyzes the chemical reaction L- ... Transamination between tryptophan and phenylpyruvate". Biochem. J. 92 (3): 594-8. doi:10.1042/bj0920594. PMC 1206107. PMID ... The systematic name of this enzyme class is L-tryptophan:phenylpyruvate aminotransferase. This enzyme is also called L- ... tryptophan-alpha-ketoisocaproate aminotransferase. Koide Y, Honma M, Shimomura T (1980). "L-Tryptophan-alpha-ketoisocaproate ...
... (ATD) is a technique used extensively to study the effect of low serotonin in the brain. This ... van Donkelaar EL, Blokland A, Ferrington L, Kelly PA, Steinbusch HW, Prickaerts J (July 2011). "Mechanism of acute tryptophan ... Young SN (September 2013). "Acute tryptophan depletion in humans: a review of theoretical, practical and ethical aspects". ... experimental approach reduces the availability of tryptophan, an amino acid which serves as the precursor to serotonin. The ...
In enzymology, a tryptophan-tRNA ligase (EC 6.1.1.2) is an enzyme that catalyzes the chemical reaction ATP + L-tryptophan + ... tryptophan translase, and TrpRS. This enzyme participates in tryptophan metabolism and aminoacyl-trna biosynthesis. As of late ... The systematic name of this enzyme class is L-tryptophan:tRNATrp ligase (AMP-forming). Other names in common use include ... DAVIE EW, KONINGSBERGER VV, LIPMANN F (1956). "The isolation of a tryptophan-activating enzyme from pancreas". Arch. Biochem. ...
4-Hydroxy-L-tryptophan is accepted as a substrate by the enzyme in addition to L-tryptophan. This subsequent pathway is ... L-Tryptophan decarboxylase (EC 4.1.1.105) is an enzyme distinguished by the substrate L-tryptophan. This enzyme catalyzes the ... Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, which makes the molecule polar, ... The decarboxylase enzyme is able to transform L-tryptophan to tryptamine in the second step by cleaving off two oxygens and a ...
... tryptophan side chain oxidase type I, TSO I, TSO II, and tryptophan side chain oxidase. This enzyme participates in tryptophan ... tryptophan side-chain alpha,beta-oxidase, tryptophan side chain oxidase II, tryptophan side-chain oxidase, TSO, indolyl-3-alkan ... In enzymology, a tryptophan 2'-dioxygenase (EC 1.13.99.3) is an enzyme that catalyzes the chemical reaction L-tryptophan + O 2 ... A novel tryptophan-metabolizing enzyme". J. Biol. Chem. 252 (8): 2640-7. PMID 15994. Takai K, Ushiro H, Noda Y, Narumiya S, ...
a 73-22-3 EINECS for Tryptophan ^a CID 9060 from PubChem ^a CID 6305 from PubChem (Articles with short description, Short ...
... (EC 1.14.13.125, tryptophan N-hydroxylase, CYP79B1, CYP79B2, CYP79B3) is an enzyme with systematic ... N-hydroxy-L-tryptophan + NADP+ + H2O (1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } N,N- ... dihydroxy-L-tryptophan + NADP+ + H2O (1c) N,N-dihydroxy-L-tryptophan ⇌ {\displaystyle \rightleftharpoons } (E)-indol-3- ... Tryptophan+N-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles ...
... , or Custodiol HTK solution, is a high-flow, low-potassium preservation solution used for ... Finally, histidine is thought to aid buffering, mannitol and tryptophan to improve membrane stability, and ketoglutarate to ... 4. Pokorny H., et al.: Histidine-tryptophan-ketoglutarate solution for organ preservation in human liver transplantation - a ... 7. Hatano E., et al.: Hepatic preservation with histidine-tryptophan-ketoglutarate solution in living related and cadaveric ...
Other flavin-dependent tryptophan halogenases include tryptophan 5-halogenase and tryptophan 6-halogenase. Tryptophan 7- ... Media related to Tryptophan 7-halogenase at Wikimedia Commons Tryptophan+7-halogenase at the U.S. National Library of Medicine ... Tryptophan 7-halogenase (EC 1.14.19.9, PrnA, RebH) is an enzyme with systematic name L-tryptophan:FADH2 oxidoreductase (7- ... Tryptophan is bound by a number of interactions: other aromatic amino acid residues such as tryptophan, phenylalanine, and ...
In enzymology, a tryptophan 2-monooxygenase (EC 1.13.12.3) is an enzyme that catalyzes the chemical reaction L-tryptophan + O2 ... I. The conversion of L-tryptophan to indole-3-acetamide by an enzyme system from Pseudomonas savastanoi". J. Biol. Chem. 241 ( ... the two substrates of this enzyme are L-tryptophan and O2, and its 3 products are (indol-3-yl)acetamide, CO2, and H2O. This ... The systematic name of this enzyme class is L-tryptophan:oxygen 2-oxidoreductase (decarboxylating). This enzyme participates in ...
The Tryptophan operon leader is an RNA element found at the 5′ of some bacterial tryptophan operons. The leader sequence can ... Page for Tryptophan operon leader at Rfam v t e (Cis-regulatory RNA elements, All stub articles, Molecular and cellular biology ... Tryptophan RNA-binding attenuator protein inhibitory protein (Anti-TRAP protein or AT) is a short protein encoded by the rtpA ... TRAP protein forms an oligomer of 11 subunits, in the presence of tryptophan this binds to section of RNA containing 11 (G/U)AG ...
In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction L-tryptophan + ... Other names in common use include L-tryptophan 2',3'-oxidase, and L-tryptophan alpha,beta-dehydrogenase. It employs one ... Genet R, Benetti PH, Hammadi A, Menez A (1995). "L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate ... The systematic name of this enzyme class is L-tryptophan:oxygen alpha,beta-oxidoreductase. ...
... s (TspO) are a family of proteins that are involved in transmembrane signalling. In either ... Davey ME, de Bruijn FJ (December 2000). "A homologue of the tryptophan-rich sensory protein TspO and FixL regulate a novel ...
Other names in common use include D-tryptophan acetyltransferase, and acetyl-CoA-D-tryptophan-alpha-N-acetyltransferase. Zenk ... N-acetyl-D-tryptophan Thus, the two substrates of this enzyme are acetyl-CoA and D-tryptophan, whereas its two products are CoA ... In enzymology, a D-tryptophan N-acetyltransferase (EC 2.3.1.34) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:D-tryptophan N-acetyltransferase. ...
N2-malonyl-D-tryptophan Thus, the two substrates of this enzyme are malonyl-CoA and D-tryptophan, whereas its two products are ... The systematic name of this enzyme class is malonyl-CoA:D-tryptophan N-malonyltransferase. Matern U, Feser C, Heller W (1984 ... In enzymology, a D-tryptophan N-malonyltransferase (EC 2.3.1.112) is an enzyme that catalyzes the chemical reaction malonyl-CoA ... CoA and N2-malonyl-D-tryptophan. This enzyme belongs to the family of transferases, specifically those acyltransferases ...
This family includes tryptophan 2,3-dioxygenase (TDO, also sometimes referred to as tryptophan oxygenase and L-tryptophan ... In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L-tryptophan (L-Trp ... L-tryptophan + O2 ⇌ N-formyl-L-kynurenine Tryptophan 2,3-dioxygenase plays a central role in the physiological regulation of ... A tryptophan 2,3-dioxygenase inhibitor developed by the group restored the ability of these mice to reject tryptophan 2,3- ...
L-tryptophan + H2O This enzyme salvages the lost indole to L-tryptophan. Hettwer S, Sterner R (March 2002). "A novel tryptophan ... Tryptophan synthase (indole-salvaging) (EC 4.2.1.122, tryptophan synthase beta2) is an enzyme with systematic name L-serine ... Tryptophan+synthase+(indole-salvaging) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... hydro-lyase (adding indole, L-tryptophan-forming). This enzyme catalyses the following chemical reaction L-serine + indole ⇌ {\ ...
Other names in common use include tryptophan 2-methyltransferase, and S-adenosylmethionine:tryptophan 2-methyltransferase. ... In enzymology, a tryptophan 2-C-methyltransferase (EC 2.1.1.106) is an enzyme that catalyzes the chemical reaction S-adenosyl-L ... The systematic name of this enzyme class is S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase. ... L-tryptophan ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + L-2-methyltryptophan Thus, the two substrates of ...
... (EC 2.6.1.99, TAA1 (gene), vt2 (gene)) is an enzyme with systematic name L-tryptophan: ... L-tryptophan---pyruvate+aminotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Zhao Y (March 2012). "Auxin biosynthesis: a simple two-step pathway converts tryptophan to indole-3-acetic acid in plants". ... This enzyme catalyses the following chemical reaction L-tryptophan + pyruvate ⇌ {\displaystyle \rightleftharpoons } indole-3- ...
So high levels of tryptophan prevent tryptophan synthesis through a negative feedback loop, and when the cells tryptophan ... Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino ... Hopkins recovered tryptophan from hydrolysed casein, recovering 4-8 g of tryptophan from 600 g of crude casein. As an essential ... By this reaction, tryptophan gives rise to tryptophol. Tryptophan affects brain serotonin synthesis when given orally in a ...
Tryptophan is an amino acid needed for normal growth in infants and for the production and maintenance of the bodys proteins, ... Tryptophan is an amino acid needed for normal growth in infants and for the production and maintenance of the bodys proteins, ... Tryptophan is an amino acid needed for normal growth in infants and for the production and maintenance of the bodys proteins, ... The body uses tryptophan to help make melatonin and serotonin. Melatonin helps regulate the sleep-wake cycle, and serotonin is ...
Turkeys sleep-inducing amino acid tryptophan may affect your sense of trust. ... Tryptophan, Turkey and Trust. Turkeys sleep-inducing amino acid tryptophan may affect your sense of trust. ... Tryptophan is a chemical precursor to serotonin, one of the brains most important signaling molecules and the target of the ... While scientists say that the tryptophan in turkey is probably not the source of holiday fatigue, a possible new role for ...
Acetyl-DL-tryptophan; NSC 49124; Tryptophan, N-acetyl-; Nα-acetyl-DL-tryptophan ... Other names: Tryptophan, N-acetyl-, DL-; DL-α-Acetylamino-3-indolepropionic acid; DL-Acetyltryptophan; DL-N-Acetyltryptophan; N ... DL-Tryptophan, N-acetyl-. *Formula: C13H14N2O3 ... DL-tryptophan; N-Acetyl-DL-tryptophane; dl-α-Acetamidoindole-3- ...
L-tryptophan hydroxylase. indoleacetic acid-5-hydroxylase. tryptophan 5-monooxygenase 1. tryptophan hydroxylase (tryptophan 5- ... Tryptophan Hydroxylase 1 / TPH1 Antibody, Rabbit PAb, Antigen Affinity Purified * Tryptophan Hydroxylase 1 / TPH1 Antibody, ... TPH1 tryptophan hydroxylase 1 [Homo sapiens] TPH1 tryptophan hydroxylase 1 [Homo sapiens]. Gene ID:7166 ... tryptophan hydroxylase 1provided by HGNC. Primary source. HGNC:HGNC:12008 See related. Ensembl:ENSG00000129167 MIM:191060; ...
An Experience with Tryptophan - 5-HTP & Valerian. Dream Seizure by Empire ... "Dream Seizure: An Experience with Tryptophan - 5-HTP & Valerian (exp32948)". Erowid.org. Jun 28, 2006. erowid.org/exp/32948 ...
l-Tryptophan, 1 g, at bedtime reduces time to sleep onset in mild situational insomnia, and doses up to 15 g at bedtime may be ... l-Tryptophan is typically taken at bedtime because of its sedating properties and is dosed between 1.5 and 5.0 g, depending on ... L-Tryptophan and 5-Hydroxytryptophan in Mental Health Care Both amino acids have beneficial effects on many mental health ... Combining 2 g of l-tryptophan with 20 mg per day of fluoxetine resulted in more rapid response and improved sleep quality in ...
If needed, L-tryptophan converts to niacin in the body, which supports circulation, a healthy nervous system, the metabolism of ... L-Tryptophan also supports immune functions because it is the bodys precursor to the kynurenines that regulate immunity. ... Source Naturals L-Tryptophan is extremely pure and is regularly tested to ensure the highest standards of quality. ... The essential amino acid L-tryptophan helps support relaxation, restful sleep, and positive mood. It plays a part in the ...
... FASEB J. 1991 Aug;5(11):2516-22. ... In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), ... which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. The inhibitory effect of ... in vitro a primary mechanism of cytotoxicity is through the depletion of tryptophan. ...
Update: Eosinophilia-Myalgia Syndrome Associated with Ingestion of L-Tryptophan -- United States, through August 24, 1990 As of ... L-tryptophan and eosinophilia-myalgia syndrome in New Mexico. Lancet 1990;335:645-8. ... Update: eosinophilia-myalgia syndrome associated with ingestion of L-tryptophan--United States, as of January 9, 1990. MMWR ... Eosinophilia-myalgia syndrome and L-tryptophan-containing products--New Mexico, Minnesota, Oregon, and New York, 1989. MMWR ...
I guess no one informed you about tryptophan. Create and send your own custom Thanksgiving ecard. ...
Shop for Source Naturals L-Tryptophan (1000 mg - 60 Tablets) at Fred Meyer. Find quality health products to add to your ... This tryptophan tablet includes vitamin B6, which is required to convert tryptophan to serotonin. If needed, L-tryptophan is ... The essential amino acid L-tryptophan is he precursor for the synthesis of melatonin and serotonin, a hormone and a ... Source Naturals L-Tryptophan is extremely pure and is regularly tested to ensure the highest standards of quality. ...
Find out which L-Tryptophan and 5-Hydroxytryptophan (5-HTP) supplements passed our tests. ... evidence for using L-tryptophan or 5-HTP for sleep, depression, migraine, and more. Plus, dosage, safety, side effects and ... Learn how to find the best L-Tryptophan and 5-Hydroxytryptophan (5-HTP) supplements, ... L-tryptophan and 5-Hydroxy-L-tryptophan (5-HTP) Review! Become a Member to View the Latest Update: in our L-tryptophan and 5- ...
Body systems supported by tryptophan. Tryptophan is an amino acid crucial in mood regulation. Ergo, it is necessary for proper ... Patients who take tryptophan often report feeling less anxious and have fewer depressive symptoms. Tryptophan likewise reduces ... This process also implies that tryptophan can be used to control hyperactivity among children. Tryptophan can likewise be used ... heard of tryptophan. This essential amino acid, which is sometimes referred to as L-tryptophan, is used to regulate and mediate ...
tryptophan. Urban Myth Busted In Time For Thanksgiving: Turkey Does Not Make You Sleepy. ...
Complete information about our recommendation of Tryptophan / 5HTP, including why it is recommended. ... 5HTP (5-hydroxy tryptophan) is considered by many to be more effective than tryptophan for depression. L-Tryptophan (which is ... Tryptophan / 5HTP: Overview. Alternative names: 5-HTP, 5 HTP.. An essential amino acid, tryptophan is the least abundant amino ... Tryptophan / 5HTP can help with the following:. Habits. Night Eating Syndrome Taking Tryptophan or 5-HTP orally causes an ...
Tryptophan and Non-Tryptophan Fluorescence of the Eye Lens Proteins Provides Diagnostics of Cataract at the Molecular Level. ... The chemical nature of the non-tryptophan (non-Trp) fluorescence of porcine and human eye lens proteins was identified by Mass ... A novel route for early cataract diagnostics is investigated based on the excitation of tryptophan fluorescence (TF) at the red ... Such wavelength selection targets the population of tryptophan residues, side chains of which are exposed to the polar aqueous ...
Synechocystis PCC 6803 contains a single gene for the beta subunit of tryptophan synthase with strong homology to the trpB ...
... tryptophan in turkey meat causes drowsiness. Turkey does contain tryptophan, which does have a documented sleep-inducing effect ... You are at:Home»Forums»General Discussions»Blog Discussion»Tryptophan and Turkey Myth Exposed ...
diet pills that tryptophan supplements weight loss help you lose belly tryptophan supplements weight loss fat loss and lose ... This plant is a natural role of weight tryptophan supplements weight loss loss pills that help tryptophan supplements weight ... Tryptophan Supplements Weight Loss -- ATIME.org. The supplement is excellent for 14-day quick weight loss everyone that you ... It contains no tryptophan supplements weight loss high-quality ingredients that to help reduce your cravings and get you ...
Tryptophan metabolites suppress the Wnt pathway and promote adverse limb events in chronic kidney disease. Nkiruka V. Arinze,1 ... Int J Tryptophan Res. 2017;10:1178646917694600. View this article via: PubMed Google Scholar ... Tryptophan metabolism in patients with chronic kidney disease secondary to type 2 diabetes: relationship to inflammatory ... This work uncovers the tryptophan metabolite/AHR/β-catenin axis as a mediator of microvascular rarefaction in CKD patients and ...
These alterations can affect the metabolism of tryptophan (TRP), an essential amino acid and precursor of serotonin (5-HT), ... These alterations can affect the metabolism of tryptophan (TRP), an essential amino acid and precursor of serotonin (5-HT), ... Friedman M. Analysis, nutrition, and health benefits of tryptophan. Int J Tryptophan Res. (2018) 11:1178646918802282. doi: ... Tryptophan Metabolic Pathways Are Altered in Obesity and Are Associated With Systemic Inflammation. Sofia Cussotto1† Inês ...
The distribution of tryptophan content in human hair of various colours was evaluated, in order to study the accumulation of ... Tryptophan in human hair: correlation with pigmentation.. Bertazzo A, Biasiolo M, Costa CV, Cardin de Stefani E, Allegri G. ... not influence tryptophan contents, but at ages 13-19 and 20-40 years tryptophan content increased significantly from blond to ... Tryptophan also accumulates in hair during keratinization, as shown by the presence of high levels of this amino acid in grey ...
For years, tryptophan, an amino acid in turkey, garnered headlines in the media for making you sleepy. However, there is ... Most sources of tryptophan come from plants or animals. Whenever your body digests tryptophan, it travels through the blood to ... Foods highest in tryptophan. Chicken, pork and ham, not turkey, all have higher amounts of tryptophan per serving. Other foods ... L-Tryptophan, referred to more commonly as just tryptophan, is an essential amino acid, meaning your body doesnt produce it. ...
Tryptophan preparation information is provided by Wedgewood Pharmacy. ... Tryptophan Oral Oil Suspension may be prescribed for Dogs. ... Tryptophan: Oral Oil Suspension. Tryptophan may be prescribed ... 1 strength of Tryptophan Oral Oil Suspension is available in 200 mg/ml. What our customers are saying. Wedgewood Pharmacy ... Tryptophan Oral Oil Suspension. Prescribed For: Dogs. May be Prescribed For: Behavioral Disorders. If you have any questions ...
NATURAL L-Tryptophan 225 mg, 60 kapsúl. Aktuálna dostupnosť produktu nie je známa. Overiť dostupnosť v obchode. ...
... tryptophan is the least abundant amino acid found in foods. It is used by the brain to produce serotonin; it is a natural ... 5HTP (5-hydroxy tryptophan) is considered by many to be more effective than tryptophan for depression. L-Tryptophan (which is ... Tryptophan / 5 HTP. An essential amino acid, tryptophan is the least abundant amino acid found in foods. It is used by the ... Foods high in tryptophan and supplemental tryptophan should be removed from the diet as some children with asthma have a defect ...
Tryptophan hydroxylase-1 (TPH1) is expressed by non-neuronal cells including enterochromaffin cells of the gut, mast cells and ... Lack of tryptophan hydroxylase-1 in mice results in gait abnormalities. PLoS ONE 8(3): e59032. ... suggesting that tryptophan hydroxylase-1 expression has an impact on the nervous system. ...
Discover the impact of tryptophan metabolite plasma levels in monopolar and bipolar depression patients. Explore the findings ... Comparison of ratios of tryptophan metabolites per tryptophan. (a) Results of two way ANOVA tests for monopolar major ... 1) Tryptophan metabolites of patients with MDD.. Table 1 shows that by using one way ANOVA tests in patients of MDD only KYN ... Background: No research has been done for the determination of plasma levels of tryptophan metabolites in patients of monopolar ...
... both spontaneous and after ingestion of 1-tryptophan 5g per 1.73 sq, meters of body surface, was found to be greater than that ... both spontaneous and after ingestion of 1-tryptophan 5g per 1.73 sq, meters of body surface, was found to be greater than that ...
  • In addition, tryptophan functions as a biochemical precursor for the following compounds: Serotonin (a neurotransmitter), synthesized by tryptophan hydroxylase. (wikipedia.org)
  • Tryptophan hydroxylase 1 drives glioma progression by modulating the serotonin/L1CAM/NF-κB signaling pathway. (nih.gov)
  • TPH1 gene polymorphism rs211105 is associated with serotonin and tryptophan hydroxylase 1 concentrations in acute pancreatitis patients. (nih.gov)
  • Association study of single nucleotide polymorphism in tryptophan hydroxylase 1 gene with adolescent idiopathic scoliosis: A meta-analysis. (nih.gov)
  • Tryptophan hydroxylase-1 (TPH1) is expressed by non-neuronal cells including enterochromaffin cells of the gut, mast cells and the pineal gland and is the rate-limiting enzyme involved in the biosynthesis of peripheral serotonin. (harvard.edu)
  • However, here we report that Tph1 (−/−) mice display altered gait dynamics and deficits in rearing behavior compared to wild-type (WT) suggesting that tryptophan hydroxylase-1 expression has an impact on the nervous system. (harvard.edu)
  • "In vitro reactivation of rat cortical tryptophan hydroxylase following in vivo inactivation by methylenedioxymethamphetamine" J Neurochem . (erowid.org)
  • The activity of tryptophan hydroxylase (EC 1.14.16.4) from rat brain was significantly decreased 1 h following a single systemic injection of 3,4-methylenedioxymethamphetamine (MDMA) when assessed ex vivo by radioenzymatic assay or in vivo by the quantitation of 5-hydroxytryptophan accumulation following central L-aromatic amino acid decarboxylase inhibition. (erowid.org)
  • Cortical tryptophan hydroxylase acutely inactivated by methamphetamine or p-chloroamphetamine could be similarly reactivated. (erowid.org)
  • MDMA-inactivated cortical tryptophan hydroxylase derived from rats killed later than 3 days after drug treatment could not be significantly reactivated under the conditions described above, indicating the development of irreversible enzymatic damage. (erowid.org)
  • These studies suggest that MDMA and its congeners inactivate central tryptophan hydroxylase by inducing oxidation of key enzyme sulfhydryl groups. (erowid.org)
  • For instance, tryptophan and tyrosine residues play special roles in "anchoring" membrane proteins within the cell membrane. (wikipedia.org)
  • The chemical nature of the non-tryptophan (non-Trp) fluorescence of porcine and human eye lens proteins was identified by Mass Spectrometry (MS) and Fluorescence Steady-State and Lifetime spectroscopy as post-translational modifications (PTM) of Trp and Arg amino acid residues. (edinst.com)
  • Such wavelength selection targets the population of tryptophan residues, side chains of which are exposed to the polar aqueous environment. (edinst.com)
  • Here, we characterized oxidative modification of tryptophan (Trp) residues in the PSII core, and hypothesize that the oxidation of N-terminal Trp is one of the key oxidations in the PSII repair, likely enhancing D1's accessibility to FtsH. (elifesciences.org)
  • There is a well-documented study where the terms "hydrophobicity" and "hydrophobic collapse" were shown to be misleading for explanation of the absence of CIDNP signals of tryptophan residues in the unfolded HEWL protein under cw-illumination. (copernicus.org)
  • Since these frequencies are known to be strongly correlated with the visible absorption maximum of the chromophore, it is concluded that none of the tryptophan residues are essential for forming a normal bR 570 chromophore. (syr.edu)
  • In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. (nih.gov)
  • Chromium picolinate helps to promote conversion of tryptophan to serotonin. (diagnose-me.com)
  • De novo synthesis begins with the conversion of tryptophan to quinolate, which is converted to NaMN. (wikipathways.org)
  • The liver can also use tryptophan to produce niacin (vitamin B3), which is needed for energy metabolism and DNA production. (medlineplus.gov)
  • The best way to speed up tryptophan supplements weight loss your metabolism, reduce your appetite and improve the lean mood. (atime.org)
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  • These alterations can affect the metabolism of tryptophan (TRP), an essential amino acid and precursor of serotonin (5-HT), kynurenine (KYN), and indoles. (frontiersin.org)
  • A growing body of evidence indicates that inflammation is associated with alterations in the metabolism of tryptophan (TRP) ( 12 , 13 ), an essential amino acid and biochemical precursor of serotonin (5-HT), kynurenine (KYN) and indoles ( 14 ). (frontiersin.org)
  • Because of abnormal tryptophan metabolism and the possibility of promoting auto-antibody production SLE patients should avoid supplementation with tryptophan or 5HTP unless determined to be tolerated by any particular patient. (digitalnaturopath.com)
  • If needed, L-Tryptophan converts to niacin in the body, which supports circulation, a healthy nervous system, the metabolism of food, and the production of hydrochloric acid for the digestive system. (food4less.com)
  • Scholars@Duke publication: A mathematical model of tryptophan metabolism via the kynurenine pathway provides insights into the effects of vitamin B-6 deficiency, tryptophan loading, and induction of tryptophan 2,3-dioxygenase on tryptophan metabolites. (duke.edu)
  • Vitamin B-6 deficiency is associated with impaired tryptophan metabolism because of the coenzyme role of pyridoxal 5'-phosphate (PLP) for kynureninase and kynurenine aminotransferase. (duke.edu)
  • To investigate the underlying mechanism, we developed a mathematical model of tryptophan metabolism via the kynurenine pathway. (duke.edu)
  • These results show that the model successfully simulated tryptophan metabolism via the kynurenine pathway and can be used to complement experimental investigations. (duke.edu)
  • Monitoring tryptophan metabolism in chronic immune activation. (bvsalud.org)
  • Niacin, also known as vitamin B3, is synthesized from tryptophan via kynurenine and quinolinic acids. (wikipedia.org)
  • If needed, L-tryptophan is converted to niacin in the body, an important B vitamin. (fredmeyer.com)
  • Tryptophan is metabolized into niacin , melatonin and serotonin and has relaxing and calming effects. (diagnose-me.com)
  • Since it is the precursor of niacin , tryptophan supplementation may help to lower cholesterol and blood fat levels. (diagnose-me.com)
  • The distribution of tryptophan content in human hair of various colours was evaluated, in order to study the accumulation of this amino acid, precursor of serotonin, melatonin and niacin, in hair and the influence on hair pigmentation. (anagen.net)
  • The digestion process also converts tryptophan to niacin, a B vitamin that plays an important role in converting food into energy. (integrisok.com)
  • Primary niacin deficiency results from extremely inadequate intake of both niacin and tryptophan , which usually occurs in areas where maize (Indian corn) constitutes a substantial part of the diet. (msdmanuals.com)
  • We simulated the effects of graded reduction in cellular PLP concentration, tryptophan loads and induction of tryptophan 2,3-dioxygenase (TDO) on metabolite profiles and urinary excretion. (duke.edu)
  • The kynurenine pathway of tryptophan catabolism is altered in several diseases, including psychiatric disorders such as schizophrenia, major depressive disorder, and bipolar disorder. (wikipedia.org)
  • Outside the kynurenine pathway, tryptophan is also the precursor of serotonin and melatonin. (wikipathways.org)
  • Kinetic analysis of enzyme reactivation revealed an approximate doubling of enzyme Vmax with no change in enzyme affinity for either substrate, tryptophan, or pterin cofactor. (erowid.org)
  • Purification and properties of dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps. (brenda-enzymes.org)
  • The model includes mammalian data on enzyme kinetics and tryptophan transport from the intestinal lumen to liver, muscle, and brain. (duke.edu)
  • Fifteen hundred cases of eosinophilia-myalgia syndrome (EMS) and 37 deaths in patients taking l-tryptophan were reported in the late 1980s and early 1990s. (psychologytoday.com)
  • L-tryptophan and eosinophilia-myalgia syndrome in New Mexico. (cdc.gov)
  • L-tryptophan from a specific manufacturer caused hundreds of cases of a serious immune disorder, eosinophilia-myalgia syndrome (EMS), in the late 1980s. (consumerlab.com)
  • Non-L-tryptophan related eosinophilia-myalgia syndrome with hypoproteinemia and hypoalbuminemia. (jrheum.org)
  • No research has been done for the determination of plasma levels of tryptophan metabolites in patients of monopolar and bipolar depression. (scirp.org)
  • Ultra high-speed liquid chromatography/mass spectrometry has been used for the simultaneous determination of plasma levels of tryptophan metabolites in depressive patients. (scirp.org)
  • In patients of major monopolar depression age and gender differences of plasma levels of tryptophan metabolites disappear although significant differences are observed in healthy volunteers. (scirp.org)
  • Tomioka, H. , Masuda, J. , Takada, A. and Iwanami, A. (2020) Comparison of Age and Gender Differences of Tryptophan Metabolites in Patients of Major Monopolar and Bipolar Depression. (scirp.org)
  • How to take tryptophan? (consumerlab.com)
  • Patients who take tryptophan often report feeling less anxious and have fewer depressive symptoms. (naturalpedia.com)
  • The body uses tryptophan to help make melatonin and serotonin. (medlineplus.gov)
  • Editorial Note: On November 17, 1989, the Food and Drug Administration (FDA) recalled all dietary supplements that provided a daily dose of L-tryptophan (LT) greater than or equal to 100 mg. (cdc.gov)
  • Choose the Best L-Tryptophan and 5-HTP Supplements. (consumerlab.com)
  • Best choice for tryptophan supplements? (consumerlab.com)
  • Make sure you're choosing the best L-tryptophan or 5-HTP supplements approved in our tests! (consumerlab.com)
  • A few cohort studies have suggested that people addicted to smoking may benefit from taking tryptophan supplements. (naturalpedia.com)
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  • Both supplements are available, but tryptophan may require a doctor's prescription. (digitalnaturopath.com)
  • However, the presence of Peak X and its potential toxicity caused the FDA to ban L-tryptophan and 5-HTP dietary supplements until the mid-2000s, today more Health Care Providers are concerned of possible drug interactions between L-tryptophan supplements and select antidepressants that may cause serotonin syndrome, a life-threatening condition. (vumc.org)
  • however, in vitro a primary mechanism of cytotoxicity is through the depletion of tryptophan. (nih.gov)
  • Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. (wikipedia.org)
  • Amino acids, including tryptophan, are used as building blocks in protein biosynthesis, and proteins are required to sustain life. (wikipedia.org)
  • Binding of this repressor to the tryptophan operon prevents transcription of downstream DNA that codes for the enzymes involved in the biosynthesis of tryptophan. (wikipedia.org)
  • Oral supplementation of L-Tryptophan has a greater effect on increasing serotonin in the brain than tryptophan ingested from whole food sources. (naturalstacks.com)
  • The manuscript "Exploration of the close chemical space of tryptophan and tyrosine reveals importance of hydrophobicity in photo- CIDNP performance" describes experimental results of detecting CIDNP under continuous illumination for a set of ten compounds that are analogs of tyrosine or tryptophan. (copernicus.org)
  • For example, the pKa values of radicals (tryptophan and tyrosine) and the same molecules in the diamagnetic state differ by several units. (copernicus.org)
  • Source Naturals L-Tryptophan is extremely pure and is regularly tested to ensure the highest standards of quality. (fredmeyer.com)
  • 5-HTP is generally recommended over l-tryptophan because it crosses the blood-brain barrier at a higher rate, is converted into serotonin more efficiently than l-tryptophan, and has a more pronounced antidepressant effect. (psychologytoday.com)
  • Turkey does contain tryptophan, which does have a documented sleep-inducing effect as it is readily converted into serotonin by the body. (elitetrack.com)
  • Two enzymes, namely indoleamine 2,3-dioxygenase (IDO) in the immune system and the brain, and tryptophan 2,3-dioxygenase (TDO) in the liver, are responsible for the synthesis of kynurenine from tryptophan. (wikipedia.org)
  • So high levels of tryptophan prevent tryptophan synthesis through a negative feedback loop, and when the cell's tryptophan levels go down again, transcription from the trp operon resumes. (wikipedia.org)
  • The essential amino acid L-tryptophan is he precursor for the synthesis of melatonin and serotonin, a hormone and a neurotransmitter involved with mood and stress response. (fredmeyer.com)
  • Briefly, in mammalian cells, tryptophan is used mostly for protein synthesis. (wikipathways.org)
  • Multidimensional engineering of Escherichia coli for efficient synthesis of L-tryptophan. (bvsalud.org)
  • The disorder fructose malabsorption causes improper absorption of tryptophan in the intestine, reduced levels of tryptophan in the blood, and depression. (wikipedia.org)
  • It accomplishes this by facilitating absorption into muscle tissue of the amino acids that compete with tryptophan for access to the brain. (diagnose-me.com)
  • A novel route for early cataract diagnostics is investigated based on the excitation of tryptophan fluorescence (TF) at the red edge of its absorption band at 317 nm. (edinst.com)
  • tryptophan is diverted to form 5-hydroxytryptophan and serotonin) and in Hartnup disease (absorption of tryptophan by the intestine and kidneys is defective). (msdmanuals.com)
  • The work supports a role for chemical modification in the recognition and subsequent degradation of a key protein subunit of PSII by a bacterial-type protease, suggesting that tryptophan oxidation of components of the photosynthetic apparatus after high light stress plays a critical role in initiating the PSII repair system. (elifesciences.org)
  • November 11, 2022: Will the Tryptophan in Thanksgiving Turkey make you sleepy? (vumc.org)
  • In 2002, the U.S. Institute of Medicine set a Recommended Dietary Allowance (RDA) of 5 mg/kg body weight/day of Tryptophan for adults 19 years and over. (wikipedia.org)
  • Tryptophan is present in most protein-based foods or dietary proteins. (wikipedia.org)
  • Tryptophan is sold over the counter in the United States (after being banned to varying extents between 1989 and 2005) and the United Kingdom as a dietary supplement for use as an antidepressant, anxiolytic, and sleep aid. (wikipedia.org)
  • The richest dietary sources include fish, meat, dairy, eggs, nuts and wheat germ, but tryptophan tends to be deficient in most dietary proteins. (diagnose-me.com)
  • Tryptophan is the dietary amino acid precursor for production of serotonin in the body. (digitalnaturopath.com)
  • Tryptophan works better for acute insomnia than for chronic sleep problems. (diagnose-me.com)
  • In other words, it's unlikely to be enough tryptophan to increase serotonin levels to make you sleepy. (integrisok.com)
  • Does eating Thanksgiving turkey make you sleepy due to its tryptophan content? (vumc.org)
  • Tryptophan has an antidepressant effect and is particularly effective against manic depression and depression associated with menopause . (diagnose-me.com)
  • l-Tryptophan, 1 g, at bedtime reduces time to sleep onset in mild situational insomnia, and doses up to 15 g at bedtime may be necessary for severe insomnia. (psychologytoday.com)
  • Combining 2 g of l-tryptophan with 20 mg per day of fluoxetine resulted in more rapid response and improved sleep quality in depressed patients complaining of chronic insomnia. (psychologytoday.com)
  • L-tryptophan is used worldwide as an effective treatment for insomnia, anxiety, depression, and even severe cases of premenstrual syndrome (PMS). (naturalpedia.com)
  • If a patient has insomnia along with depression then tryptophan would appear to be even more effective, possibly because both conditions may be due to this deficiency. (diagnose-me.com)
  • Because tryptophan is converted into 5-hydroxytryptophan (5-HTP) which is then converted into the neurotransmitter serotonin, it has been proposed that consumption of tryptophan or 5-HTP may improve depression symptoms by increasing the level of serotonin in the brain. (wikipedia.org)
  • In 2001 a Cochrane review of the effect of 5-HTP and tryptophan on depression was published. (wikipedia.org)
  • Of 108 studies of 5-HTP and tryptophan on depression published between 1966 and 2000, only two met the authors' quality standards for inclusion, totaling 64 study participants. (wikipedia.org)
  • Tryptophan likewise reduces suicidal ideations brought about by severe depression. (naturalpedia.com)
  • 5HTP (5-hydroxy tryptophan) is considered by many to be more effective than tryptophan for depression . (diagnose-me.com)
  • In a group of 10 subjects with febrile convulsions, urinary elimination of kynurenines kynurenine, acetyl-kynurenine, and trioxykynurenine , both spontaneous and after ingestion of 1-tryptophan 5g per 1.73 sq, meters of body surface, was found to be greater than that measured in normal subjects, even allowing for pronounced behavioral variations among subjects. (dtic.mil)
  • This tryptophan tablet includes vitamin B6, which is required to convert tryptophan to serotonin. (fredmeyer.com)
  • Tryptophan is often given with vitamin B6 and magnesium in between meals with a small amount of carbohydrate to facilitate uptake by the brain. (diagnose-me.com)
  • Tryptophan, along with other aromatic amino acids, is also important in glycan-protein interactions. (wikipedia.org)
  • In bacteria that synthesize tryptophan, high cellular levels of this amino acid activate a repressor protein, which binds to the trp operon. (wikipedia.org)
  • Bradbury, JH & Norton, RS 1973, ' Carbon-13 NMR spectra of tryptophan, tryptophan peptides and of native and denatured proteins ', BBA - Protein Structure , vol. 328, no. 1, pp. 10-19. (monash.edu)
  • As you sink into your post-Thanksgiving food coma, the name of an amino acid might pop into your mind: tryptophan, a molecule found in high levels in turkey that's known to induce drowsiness. (go.com)
  • Transient mild adverse effects reported with l-tryptophan and 5-HTP include nausea, constipation, dry mouth, blurred vision, drowsiness, and decreased libido. (psychologytoday.com)
  • On this day that many of us Americans will consume copious amounts of Turkey I thought that this entry from wikipedia would be relevant and interesting: According to popular belief, tryptophan in turkey meat causes drowsiness. (elitetrack.com)
  • An equivalent dose of 5HTP (compared to 1gm of tryptophan ) is about 100mg. (diagnose-me.com)
  • An equivalent dose of 5HTP (compared to 1 gm of tryptophan ) is about 100 mg . (digitalnaturopath.com)
  • Foods rich in tryptophan include soybeans , cocoa powder, cashew nuts, peas , and oats . (naturalpedia.com)
  • Other foods, such as sunflower seeds and soybeans, are also high in tryptophan but people don't typically eat a large quantity in one sitting. (integrisok.com)
  • A systematic review of RCTs on 5-HTP or l-tryptophan in depressed mood identified 108 studies, but design problems and small study size limited analysis of findings to only two studies (N=64) that met inclusion criteria. (psychologytoday.com)
  • Those who are suffering from, or have a loved one currently diagnosed with, a mood disorder would have - most likely - heard of tryptophan. (naturalpedia.com)
  • Another way tryptophan helps patients with mood disorders is that it regulates sleep. (naturalpedia.com)
  • Tryptophan is an amino acid crucial in mood regulation . (naturalpedia.com)
  • Tryptophan is an essential amino acid that is used to alleviate symptoms of various mood disorders. (naturalpedia.com)
  • L-Tryptophan is an essential amino acid that the body uses to produce serotonin (a neurotransmitter responsible for regulating mood). (naturalstacks.com)
  • Tryptophan is among the less common amino acids found in proteins, but it plays important structural or functional roles whenever it occurs. (wikipedia.org)
  • Tryptophan is an amino acid needed for normal growth in infants and for the production and maintenance of the body's proteins, muscles, enzymes, and neurotransmitters. (medlineplus.gov)
  • L-Tryptophan Carma Complex is made from high-quality ingredients and is suitable for vegans and vegetarians. (troohealthcare.com)
  • In 2023, the emission spectrum of tryptophan was discovered in the interstellar gas of the star cluster IC 348. (wikipedia.org)
  • Tryptophan load simulations with and without vitamin B-6 deficiency showed altered metabolite concentrations consistent with published data. (duke.edu)
  • In the second paper, we investigated the ratio between the amino acid tryptophan and its metabolite kynurenine (KT ratio) in plasma from 249 individuals. (lu.se)
  • This permits tightly regulated and rapid responses to changes in the cell's internal and external tryptophan levels. (wikipedia.org)
  • There is evidence that blood tryptophan levels are unlikely to be altered by changing the diet, but consuming purified tryptophan increases the serotonin level in the brain, whereas eating foods containing tryptophan does not. (wikipedia.org)
  • In the new study, presented earlier this month at the Society for Neurosciences meeting in San Diego, half of the volunteers were given a drink that depleted their tryptophan levels prior to the start of the game, thereby decreasing serotonin levels in their brain. (go.com)
  • Increasing tryptophan levels normalizes sleep patterns which can aid in serotonin production. (naturalpedia.com)
  • Many depressed patients have low levels of tryptophan. (diagnose-me.com)
  • Results from 1211 samples of hair from healthy subjects (577 men and 634 women) show that tryptophan levels are significantly higher in males (37.83 +/- 3.45 microg/g dry hair) than in females (26.62 +/- 2.40 microg/g hair). (anagen.net)
  • Therefore, variations in tryptophan levels of human hair appear to be correlated with differences in hair colour in both sexes. (anagen.net)
  • Tryptophan also accumulates in hair during keratinization, as shown by the presence of high levels of this amino acid in grey and white hair. (anagen.net)
  • Other than meat and seafood, dairy, grains and nuts also contain moderate levels of tryptophan. (integrisok.com)
  • One study that attempted to separate the effectiveness of light therapy vs. tryptophan found that without adequate levels of tryptophan in the system, the light therapy alone did not provide relief. (digitalnaturopath.com)
  • Whereas supplemental 5-HTP can directly and freely influence serotonin production, the rate-limiting nature of L-tryptophan encourages balanced levels of serotonin. (naturalstacks.com)
  • Here, we synthesized two mechanistic probes to specifically test if the α-amino group of the substrate directly participates in a critical step of the O atom transfer during catalysis in human tryptophan 2,3-dioxygenase (TDO). (ku.edu)
  • This combined synthetic, biochemical, and biophysical study establishes the catalytic role of the α-amino group of the substrate during the O atom transfer reactions and thus represents a substantial advance to the mechanistic comprehension of the heme-based tryptophan dioxygenases. (ku.edu)
  • Tryptophan increases the amount of serotonin in the brain and blood which may lessen the severity of these conditions. (naturalpedia.com)
  • Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. (wikipedia.org)
  • L-tryptophan is an essential amino acid naturally found in meats and other foods. (consumerlab.com)
  • This essential amino acid, which is sometimes referred to as L-tryptophan, is used to regulate and mediate the production of various neurotransmitters , particularly serotonin. (naturalpedia.com)
  • An essential amino acid , tryptophan is the least abundant amino acid found in foods. (diagnose-me.com)
  • L-Tryptophan, referred to more commonly as just tryptophan, is an essential amino acid, meaning your body doesn't produce it. (integrisok.com)
  • The essential amino acid L-Tryptophan helps support relaxation, restful sleep, and feeling better. (food4less.com)
  • Tryptophan is an essential amino acid, meaning the body cannot produce it. (vumc.org)
  • L-Tryptophan is one the nine essential amino acids, but is one of the least plentiful found in the standard American diet. (naturalstacks.com)
  • Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. (wikipedia.org)
  • L-Tryptophan may help promote restful sleep, calm and relaxation. (naturalstacks.com)
  • Tryptophan is a chemical precursor to serotonin, one of the brain's most important signaling molecules and the target of the most commonly prescribed classes of antidepressants: selective serotonin reuptake inhibitors. (go.com)
  • In contrast, intensity of non-tryptophan emission with maximum at 435 nm exhibited an increase suggesting photochemical conversion of the tryptophan population to 435 nm emitting molecules. (edinst.com)
  • The following is a list of foods highest in tryptophan, according to data from the U.S. Department of Agriculture. (integrisok.com)
  • During the meeting, the work group discussed approving past meeting minutes, establishing meeting agendas, lessons learned, an update on the L-tryptophan video request, the cancer incidence assessment (CIA) communications plan, the summary document for the Toxic Substances Control Act (TSCA) Incinerator Public Health Assessment (PHA), and the summary document for the White Oak Creek (WOC) Radionuclide Releases PHA. (cdc.gov)
  • Contrary to the popular belief that cooked turkey contains an abundance of tryptophan, the tryptophan content in turkey is typical of poultry. (wikipedia.org)
  • While scientists say that the tryptophan in turkey is probably not the source of holiday fatigue, a possible new role for tryptophan has recently been uncovered. (go.com)
  • For years, tryptophan, an amino acid in turkey, garnered headlines in the media for making you sleepy. (integrisok.com)
  • A 1-cup (100 grams) serving of roasted turkey breast contains 318 mg of tryptophan, while roasted dark meat has 275 mg. (integrisok.com)
  • As you can see, tryptophan is one of the scarcest amino acids found in turkey - there are other amino acids in turkey competing with tryptophan once it enters the body. (integrisok.com)
  • Chicken, pork and ham, not turkey, all have higher amounts of tryptophan per serving. (integrisok.com)
  • Though the turkey myth has been debunked, as turkey contains no more tryptophan than any other common food or meat, there are other aspects of this myth that are worth exploring. (vumc.org)
  • However, there is still some risk with even pure L-tryptophan, particularly at high doses. (consumerlab.com)
  • L-tryptophan is taken for sleep at a dose of about 1 gram (1,000 mg) shortly before bedtime, while other uses have involved higher doses. (consumerlab.com)