An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
An enzyme of the oxidoreductase class that catalyzes the formation of L-TYROSINE, dihydrobiopterin, and water from L-PHENYLALANINE, tetrahydrobiopterin, and oxygen. Deficiency of this enzyme may cause PHENYLKETONURIAS and PHENYLKETONURIA, MATERNAL. EC 1.14.16.1.
An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.
A group of autosomal recessive disorders marked by a deficiency of the hepatic enzyme PHENYLALANINE HYDROXYLASE or less frequently by reduced activity of DIHYDROPTERIDINE REDUCTASE (i.e., atypical phenylketonuria). Classical phenylketonuria is caused by a severe deficiency of phenylalanine hydroxylase and presents in infancy with developmental delay; SEIZURES; skin HYPOPIGMENTATION; ECZEMA; and demyelination in the central nervous system. (From Adams et al., Principles of Neurology, 6th ed, p952).
A group of compounds that are derivatives of phenylpyruvic acid which has the general formula C6H5CH2COCOOH, and is a metabolite of phenylalanine. (From Dorland, 28th ed)
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
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.
Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.
A natural product that has been considered as a growth factor for some insects.
Compounds based on 2-amino-4-hydroxypteridine.
The rate dynamics in chemical or physical systems.
An essential branched-chain amino acid important for hemoglobin formation.
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.
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.
Amino acids containing an aromatic side chain.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.
A condition occurring in untreated or partially treated females with PHENYLKETONURIA when they become pregnant. This may result in damages to the FETUS, including MICROCEPHALY; MENTAL RETARDATION; congenital heart disease; FETAL GROWTH RETARDATION; and CRANIOFACIAL ABNORMALITIES. (From Am J Med Genet 1997 Mar 3;69(1):89-95)
A selective and irreversible inhibitor of tryptophan hydroxylase, a rate-limiting enzyme in the biosynthesis of serotonin (5-HYDROXYTRYPTAMINE). Fenclonine acts pharmacologically to deplete endogenous levels of serotonin.
3-(p-Fluorophenyl)-alanine.
An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Flavoring agent sweeter than sugar, metabolized as PHENYLALANINE and ASPARTIC ACID.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.
An enzyme that catalyzes the formation of 7-phospho-2-keto-3-deoxy-D-arabinoheptonate from phosphoenolpyruvate and D-erythrose-4-phosphate. It is one of the first enzymes in the biosynthesis of TYROSINE and PHENYLALANINE. This enzyme was formerly listed as EC 4.1.2.15.
A species of ANABAENA that can form SPORES called akinetes.
A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.
The amounts of various substances in food needed by an organism to sustain healthy life.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Derivatives of phenylacetic acid. Included under this heading are a variety of acid forms, salts, esters, and amides that contain the benzeneacetic acid structure. Note that this class of compounds should not be confused with derivatives of phenyl acetate, which contain the PHENOL ester of ACETIC ACID.
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 naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.
Food and dietary formulations including elemental (chemically defined formula) diets, synthetic and semisynthetic diets, space diets, weight-reduction formulas, tube-feeding diets, complete liquid diets, and supplemental liquid and solid diets.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria occurring in soil and water. Its organisms are generally nonpathogenic, but some species do cause infections of mammals, including humans.
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.
Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
An essential amino acid. It is often added to animal feed.
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).
Proteins prepared by recombinant DNA technology.
A sulfur-containing essential L-amino acid that is important in many body functions.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.
A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.
Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.
Tetroses are uncommon sugars (monosaccharides) with four carbon atoms, having an aldehyde functional group at the first carbon atom, and forming ring structures in their cyclic forms, primarily found in complex carbohydrates and certain natural products.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Amino acids which have a branched carbon chain.
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)
An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC 1.6.99.7.
A nonmetallic, diatomic gas that is a trace element and member of the halogen family. It is used in dentistry as flouride (FLUORIDES) to prevent dental caries.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A large and heterogenous group of fungi whose common characteristic is the absence of a sexual state. Many of the pathogenic fungi in humans belong to this group.
Protein hydrolysates are defined as complex mixtures of peptides produced by the enzymatic or chemical breakdown of whole proteins, which can vary in their degree of hydrolysis and molecular weight, and are used in various medical and nutritional applications due to their improved digestibility and bioavailability compared to intact proteins.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Cinnamates are organic compounds that contain a cinnamic acid moiety, widely used in pharmaceutical and cosmetic industries as esters, with various applications ranging from UV absorbers to local anesthetics and antimicrobial agents.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
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.
Amino acids with uncharged R groups or side chains.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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)
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
An enzyme that catalyzes the conversion of L-TYROSINE and 2-oxoglutarate to 4-hydroxyphenylpyruvate and L-GLUTAMATE. It is a pyridoxal-phosphate protein. L-PHENYLALANINE is hydroxylated to L-tyrosine. The mitochondrial enzyme may be identical with ASPARTATE AMINOTRANSFERASES (EC 2.6.1.1.). Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC 2.6.1.5.
A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE. Deficiency in the enzyme causes ALKAPTONURIA, an autosomal recessive disorder, characterized by homogentisic aciduria, OCHRONOSIS and ARTHRITIS. This enzyme was formerly characterized as EC 1.13.1.5 and EC 1.99.2.5.
A plant genus of the family APIACEAE used for flavoring food.
Peptides composed of two amino acid units.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Established cell cultures that have the potential to propagate indefinitely.
Cyclohexanecarboxylic acids are organic compounds consisting of a cyclohexane ring substituted with a carboxylic acid group, typically represented by the structural formula C6H11COOH.
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).
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The sum of the weight of all the atoms in a molecule.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Radioactive substances added in minute amounts to the reacting elements or compounds in a chemical process and traced through the process by appropriate detection methods, e.g., Geiger counter. Compounds containing tracers are often said to be tagged or labeled. (Hawley's Condensed Chemical Dictionary, 12th ed)
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.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

Prior protein intake may affect phenylalanine kinetics measured in healthy adult volunteers consuming 1 g protein. kg-1. d-1. (1/4047)

Study of the amino acid metabolism of vulnerable groups, such as pregnant women, children and patients, is needed. Our existing protocol is preceded by 2 d of adaptation to a low 13C formula diet at a protein intake of 1 g. kg-1. d-1 to minimize variations in breath 13CO2 enrichment and protein metabolism. To expand on our potential study populations, a less invasive protocol needs to be developed. We have already established that a stable background 13CO2 enrichment can be achieved on the study day without prior adaptation to the low 13C formula. Therefore, this study investigates phenylalanine kinetics in response to variations in prior protein intake. Healthy adult subjects were each fed nutritionally adequate mixed diets containing 0.8, 1.4 and 2.0 g protein. kg-1. d-1 for 2 d. On d 3, subjects consumed an amino acid-based formula diet containing the equivalent of 1 g protein. kg-1. d-1 hourly for 10 h and primed hourly oral doses of L-[1-13C]phenylalanine for the final 6 h. Phenylalanine kinetics were calculated from plasma-free phenylalanine enrichment and breath 13CO2 excretion. A significant quadratic response of prior protein intake on phenylalanine flux (P = 0.012) and oxidation (P = 0.009) was identified, such that both variables were lower following adaptation to a protein intake of 1.4 g. kg-1. d-1. We conclude that variations in protein intake, between 0.8 and 2.0 g. kg-1. d-1, prior to the study day may affect amino acid kinetics and; therefore, it is prudent to continue to control protein intake prior to an amino acid kinetics study.  (+info)

Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. (2/4047)

Phe161 and Arg166 of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens belong to a newly discovered sequence motif in flavoprotein hydroxylases with a putative dual function in FAD and NADPH binding [1]. To study their role in more detail, Phe161 and Arg166 were selectively changed by site-directed mutagenesis. F161A and F161G are catalytically competent enzymes having a rather poor affinity for NADPH. The catalytic properties of R166K are similar to those of the native enzyme. R166S and R166E show impaired NADPH binding and R166E has lost the ability to bind FAD. The crystal structure of substrate complexed F161A at 2.2 A is indistinguishable from the native enzyme, except for small changes at the site of mutation. The crystal structure of substrate complexed R166S at 2.0 A revealed that Arg166 is important for providing an intimate contact between the FAD binding domain and a long excursion of the substrate binding domain. It is proposed that this interaction is essential for structural stability and for the recognition of the pyrophosphate moiety of NADPH.  (+info)

The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme. (3/4047)

The high-spin (S = 5/2) Fe(III) ion at the active site of recombinant human phenylalanine hydroxylase (PAH) has a paramagnetic effect on the longitudinal relaxation rate of water protons. This effect is proportional to the concentration of enzyme, with a paramagnetic molar-relaxivity value at 400 MHz and 25 degrees C of 1. 3 (+/- 0.03) x 10(3) s-1 M-1. The value of the Arrhenius activation energy (Ea) for the relaxation rate was -14.4 +/- 1.1 kJ/mol for the resting enzyme, indicating a fast exchange of water protons in the paramagnetic environment. The frequency dependence of the relaxation rate also supported this hypothesis. Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent. These findings may be related to the level of basal activity before activation for these enzymes, which is higher for human than for rat PAH. In the presence of saturating (5 mM) concentrations of the substrate L-Phe, the paramagnetic molar relaxivity for human PAH decreased to 0.72 (+/- 0.05) x 10(3) s-1 M-1 with no significant change in the Ea. Effective correlation times (tauC) of 1.8 (+/- 0.3) x 10(-10) and 1.25 (+/- 0.2) x 10(-10) s-1 were calculated for the enzyme and the enzyme-substrate complex, respectively, and most likely represent the electron spin relaxation rate (tauS) for Fe(III) in each case. Together with the paramagnetic molar-relaxivity values, the tauC values were used to estimate Fe(III)-water distances. It seems that at least one of the three water molecules coordinated to the iron in the resting rat and human enzymes is displaced from coordination on the binding of L-Phe at the active site.  (+info)

A different approach to treatment of phenylketonuria: phenylalanine degradation with recombinant phenylalanine ammonia lyase. (4/4047)

Phenylketonuria (PKU), with its associated hyperphenylalaninemia (HPA) and mental retardation, is a classic genetic disease and the first to have an identified chemical cause of impaired cognitive development. Treatment from birth with a low phenylalanine diet largely prevents the deviant cognitive phenotype by ameliorating HPA and is recognized as one of the first effective treatments of a genetic disease. However, compliance with dietary treatment is difficult and when it is for life, as now recommended by an internationally used set of guidelines, is probably unrealistic. Herein we describe experiments on a mouse model using another modality for treatment of PKU compatible with better compliance using ancillary phenylalanine ammonia lyase (PAL, EC 4.3.1.5) to degrade phenylalanine, the harmful nutrient in PKU; in this treatment, PAL acts as a substitute for the enzyme phenylalanine monooxygenase (EC 1.14.16.1), which is deficient in PKU. PAL, a robust enzyme without need for a cofactor, converts phenylalanine to trans-cinnamic acid, a harmless metabolite. We describe (i) an efficient recombinant approach to produce PAL enzyme, (ii) testing of PAL in orthologous N-ethyl-N'-nitrosourea (ENU) mutant mouse strains with HPA, and (iii) proofs of principle (PAL reduces HPA)-both pharmacologic (with a clear dose-response effect vs. HPA after PAL injection) and physiologic (protected enteral PAL is significantly effective vs. HPA). These findings open another way to facilitate treatment of this classic genetic disease.  (+info)

Rho family small G proteins play critical roles in mechanical stress-induced hypertrophic responses in cardiac myocytes. (5/4047)

-Mechanical stress induces a variety of hypertrophic responses, such as activation of protein kinases, reprogramming of gene expression, and an increase in protein synthesis. In the present study, to elucidate how mechanical stress induces such events, we examined the role of Rho family small GTP-binding proteins (G proteins) in mechanical stress-induced cardiac hypertrophy. Treatment of neonatal rat cardiomyocytes with the C3 exoenzyme, which abrogates Rho functions, suppressed stretch-induced activation of extracellular signal-regulated protein kinases (ERKs). Overexpression of the Rho GDP dissociation inhibitor (Rho-GDI), dominant-negative mutants of RhoA (DNRhoA), or DNRac1 significantly inhibited stretch-induced activation of transfected ERK2. Overexpression of constitutively active mutants of RhoA slightly activated ERK2 in cardiac myocytes. Overexpression of C-terminal Src kinase, which inhibits functions of the Src family of tyrosine kinases, or overexpression of DNRas had no effect on stretch-induced activation of transfected ERK2. The promoter activity of skeletal alpha-actin and c-fos genes was increased by stretch, and these increases were completely inhibited by either cotransfection of Rho-GDI or pretreatment with C3 exoenzyme. Mechanical stretch increased phenylalanine incorporation into cardiac myocytes by approximately 1.5-fold compared with control, and this increase was also significantly suppressed by pretreatment with C3 exoenzyme. Overexpression of Rho-GDI or DNRhoA did not affect angiotensin II-induced activation of ERK. ERKs were activated by culture media conditioned by stretch of cardiomyocytes without any treatment, but not of cardiomyocytes with pretreatment by C3 exoenzyme. These results suggest that the Rho family of small G proteins plays critical roles in mechanical stress-induced hypertrophic responses.  (+info)

Role of aromaticity of agonist switches of angiotensin II in the activation of the AT1 receptor. (6/4047)

We have shown previously that the octapeptide angiotensin II (Ang II) activates the AT1 receptor through an induced-fit mechanism (Noda, K., Feng, Y. H., Liu, X. P., Saad, Y., Husain, A., and Karnik, S. S. (1996) Biochemistry 35, 16435-16442). In this activation process, interactions between Tyr4 and Phe8 of Ang II with Asn111 and His256 of the AT1 receptor, respectively, are essential for agonism. Here we show that aromaticity, primarily, and size, secondarily, of the Tyr4 side chain are important in activating the receptor. Activation analysis of AT1 receptor position 111 mutants by various Ang II position 4 analogues suggests that an amino-aromatic bonding interaction operates between the residue Asn111 of the AT1 receptor and Tyr4 of Ang II. Degree and potency of AT1 receptor activation by Ang II can be recreated by a reciprocal exchange of aromatic and amide groups between positions 4 and 111 of Ang II and the AT1 receptor, respectively. In several other bonding combinations, set up between Ang II position 4 analogues and receptor mutants, the gain of affinity is not accompanied by gain of function. Activation analysis of position 256 receptor mutants by Ang II position 8 analogues suggests that aromaticity of Phe8 and His256 side chains is crucial for receptor activation; however, a stacked rather than an amino-aromatic interaction appears to operate at this switch locus. Interaction between these residues, unlike the Tyr4:Asn111 interaction, plays an insignificant role in ligand docking.  (+info)

Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. (7/4047)

Members of the hect domain protein family are characterized by sequence similarity of their C-terminal regions to the C terminus of E6-AP, an E3 ubiquitin-protein ligase. An essential intermediate step in E6-AP-dependent ubiquitination is the formation of a thioester complex between E6-AP and ubiquitin in the presence of distinct E2 ubiquitin-conjugating enzymes including human UbcH5, a member of the UBC4/UBC5 subfamily of E2s. Similarly, several hect domain proteins, including Saccharomyces cerevisiae RSP5, form ubiquitin thioester complexes, indicating that hect domain proteins in general have E3 activity. We show here, by the use of chimeric E2s generated between UbcH5 and other E2s, that a region of UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s, whereas the N-terminal 60 amino acids do not contribute significantly to the specificity of these interactions. The conservation of this phenylalanine residue throughout evolution underlines the importance of the ability to interact with hect domain proteins for the cellular function of UBC4/UBC5 subfamily members.  (+info)

Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. (8/4047)

Proteolytic processing of the amyloid precursor protein by beta-secretase yields A4CT (C99), which is cleaved further by the as yet unknown gamma-secretase, yielding the beta-amyloid (Abeta) peptide with 40 (Abeta40) or 42 residues (Abeta42). Because the position of gamma-secretase cleavage is crucial for the pathogenesis of Alzheimer's disease, we individually replaced all membrane-domain residues of A4CT outside the Abeta domain with phenylalanine, stably transfected the constructs in COS7 cells, and determined the effect of these mutations on the cleavage specificity of gamma-secretase (Abeta42/Abeta40 ratio). Compared with wild-type A4CT, mutations at Val-44, Ile-47, and Val-50 led to decreased Abeta42/Abeta40 ratios, whereas mutations at Thr-43, Ile-45, Val-46, Leu-49, and Met-51 led to increased Abeta42/Abeta40 ratios. A massive effect was observed for I45F (34-fold increase) making this construct important for the generation of animal models for Alzheimer's disease. Unlike the other mutations, A4CT-V44F was processed mainly to Abeta38, as determined by mass spectrometry. Our data provide a detailed model for the active site of gamma-secretase: gamma-secretase interacts with A4CT by binding to one side of the alpha-helical transmembrane domain of A4CT. Mutations in the transmembrane domain of A4CT interfere with the interaction between gamma-secretase and A4CT and, thus, alter the cleavage specificity of gamma-secretase.  (+info)

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.

Phenylalanine Hydroxylase (PAH) is an enzyme that plays a crucial role in the metabolism of the essential amino acid phenylalanine. This enzyme is primarily found in the liver and is responsible for converting phenylalanine into tyrosine, another amino acid. PAH requires a cofactor called tetrahydrobiopterin (BH4) to function properly.

Defects or mutations in the gene that encodes PAH can lead to a genetic disorder known as Phenylketonuria (PKU). In PKU, the activity of PAH is significantly reduced or absent, causing an accumulation of phenylalanine in the body. If left untreated, this condition can result in severe neurological damage and intellectual disability due to the toxic effects of high phenylalanine levels on the developing brain. A strict low-phenylalanine diet and regular monitoring of blood phenylalanine levels are essential for managing PKU and preventing associated complications.

Phenylalanine Ammonia-Lyase (PAL) is a enzyme that catalyzes the non-oxidative deamination of phenylalanine to trans-cinamic acid, releasing ammonia in the process. This reaction is a key step in the biosynthesis of various aromatic compounds in plants and microorganisms. In humans, PAL is not normally present, but its introduction through gene therapy has been studied as a potential treatment for phenylketonuria (PKU), a genetic disorder characterized by an inability to metabolize phenylalanine properly, leading to its accumulation in the body and potential neurological damage.

Phenylketonurias (PKU) is a genetic disorder characterized by the body's inability to properly metabolize the amino acid phenylalanine, due to a deficiency of the enzyme phenylalanine hydroxylase. This results in a buildup of phenylalanine in the blood and other tissues, which can cause serious neurological problems if left untreated.

The condition is typically detected through newborn screening and can be managed through a strict diet that limits the intake of phenylalanine. If left untreated, PKU can lead to intellectual disability, seizures, behavioral problems, and other serious health issues. In some cases, medication or a liver transplant may also be necessary to manage the condition.

Phenylpyruvic acid is not a medical condition, but rather a chemical compound that is produced in the body. It is a byproduct of phenylalanine metabolism, an essential amino acid that cannot be synthesized by the human body and must be obtained through dietary sources such as proteins.

In some rare genetic disorders, such as phenylketonuria (PKU), the body is unable to properly metabolize phenylalanine due to a deficiency or malfunction of the enzyme phenylalanine hydroxylase. As a result, phenylpyruvic acid and other toxic byproducts accumulate in the body, leading to various health problems such as intellectual disability, seizures, and behavioral issues.

Therefore, the medical relevance of phenylpyruvic acid lies in its association with certain metabolic disorders, particularly PKU, and its potential use as a diagnostic marker for these conditions.

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.

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).

Ammonia-lyases are a class of enzymes that catalyze the removal of an amino group from a substrate, releasing ammonia in the process. These enzymes play important roles in various biological pathways, including the biosynthesis and degradation of various metabolites such as amino acids, carbohydrates, and aromatic compounds.

The reaction catalyzed by ammonia-lyases typically involves the conversion of an alkyl or aryl group to a carbon-carbon double bond through the elimination of an amine group. This reaction is often reversible, allowing the enzyme to also catalyze the addition of an amino group to a double bond.

Ammonia-lyases are classified based on the type of substrate they act upon and the mechanism of the reaction they catalyze. Some examples of ammonia-lyases include aspartate ammonia-lyase, which catalyzes the conversion of aspartate to fumarate, and tyrosine ammonia-lyase, which converts tyrosine to p-coumaric acid.

These enzymes are important in both plant and animal metabolism and have potential applications in biotechnology and industrial processes.

Prephenate Dehydratase is not a medical term per se, but rather a biochemical term. It's a type of enzyme involved in the metabolic pathway known as the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in bacteria, fungi, and plants.

Prephenate Dehydratase specifically catalyzes the conversion of prephenate to phenylpyruvate and water in this pathway. This reaction is a key step in the synthesis of phenylalanine, one of the aromatic amino acids.

In a medical context, understanding the function of Prephenate Dehydratase may be relevant in fields such as microbiology or plant biochemistry, but it does not have direct clinical significance for human health diagnoses or treatments.

Biopterin is a type of pteridine compound that acts as a cofactor in various biological reactions, particularly in the metabolism of amino acids such as phenylalanine and tyrosine. It plays a crucial role in the production of neurotransmitters like dopamine, serotonin, and noradrenaline. Biopterin exists in two major forms: tetrahydrobiopterin (BH4) and dihydrobiopterin (BH2). BH4 is the active form that participates in enzymatic reactions, while BH2 is an oxidized form that can be reduced back to BH4 by the action of dihydrobiopterin reductase.

Deficiencies in biopterin metabolism have been linked to several neurological disorders, including phenylketonuria (PKU), dopamine-responsive dystonia, and certain forms of autism. In these conditions, the impaired synthesis or recycling of biopterin can lead to reduced levels of neurotransmitters, causing various neurological symptoms.

Pterins are a group of naturally occurring pigments that are derived from purines. They are widely distributed in various organisms, including bacteria, fungi, and animals. In humans, pterins are primarily found in the eye, skin, and hair. Some pterins have been found to play important roles as cofactors in enzymatic reactions and as electron carriers in metabolic pathways.

Abnormal levels of certain pterins can be indicative of genetic disorders or other medical conditions. For example, an excess of biopterin, a type of pterin, is associated with phenylketonuria (PKU), a genetic disorder that affects the body's ability to metabolize the amino acid phenylalanine. Similarly, low levels of neopterin, another type of pterin, can be indicative of immune system dysfunction or certain types of cancer.

Medical professionals may measure pterin levels in blood, urine, or other bodily fluids to help diagnose and monitor these conditions.

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.

Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.

Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.

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.

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.

Aromatic amino acids are a specific type of amino acids that contain an aromatic ring in their side chain. The three aromatic amino acids are phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp). These amino acids play important roles in various biological processes, including protein structure and function, neurotransmission, and enzyme catalysis.

The aromatic ring in these amino acids is composed of a planar six-membered carbon ring that contains alternating double bonds. This structure gives the side chains unique chemical properties, such as their ability to absorb ultraviolet light and participate in stacking interactions with other aromatic residues. These interactions can contribute to the stability and function of proteins and other biological molecules.

It's worth noting that while most amino acids are classified as either "hydrophobic" or "hydrophilic," depending on their chemical properties, aromatic amino acids exhibit characteristics of both groups. They can form hydrogen bonds with polar residues and also engage in hydrophobic interactions with nonpolar residues, making them versatile building blocks for protein structure and function.

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.

Phenylalanine-tRNA ligase, also known as Phe-tRNA synthetase, is an enzyme that plays a crucial role in protein synthesis. Its primary function is to catalyze the attachment of the amino acid phenylalanine to its corresponding transfer RNA (tRNA) molecule. This reaction forms a phenylalanine-tRNA complex, which is then used in the translation process to create proteins according to the genetic code. The systematic name for this enzyme is phenylalanyl-tRNA synthetase (EC 6.1.1.20). Any defects or mutations in the Phe-tRNA ligase can lead to various medical conditions, including neurological disorders and impaired growth.

Phenylketonuria, Maternal is not a medical condition itself but rather a term that refers to the potential effects of maternal phenylketonuria (PKU) on the unborn child. PKU is a genetic disorder characterized by an inability to metabolize the amino acid phenylalanine, leading to its accumulation in the body and causing intellectual disability and other neurological problems if left untreated.

If a woman with PKU becomes pregnant and does not maintain a strict low-phenylalanine diet during pregnancy, the high levels of phenylalanine in her blood can lead to abnormal fetal development. The unborn child may develop congenital heart defects, microcephaly (abnormally small head), intrauterine growth retardation, and intellectual disability. This is known as maternal PKU syndrome or fetal PKU.

Therefore, it's crucial for women with PKU who are planning to become pregnant or are already pregnant to adhere strictly to a low-phenylalanine diet and monitor their blood phenylalanine levels regularly to minimize the risk of maternal PKU syndrome.

Fenclonine is not a commonly used medical term or a medication in clinical practice. It's possible that you may have encountered this term in the context of research or scientific studies. Fenclonine is an experimental drug that has been investigated for its potential role as an inhibitor of bacterial enzymes, specifically the D-alanine:D-alanine ligase (DD-transpeptidase) involved in bacterial cell wall biosynthesis.

Inhibiting this enzyme can disrupt the integrity and growth of bacteria, making fenclonine a potential antibiotic agent. However, further research is required to establish its safety, efficacy, and therapeutic applications. As such, it's not currently used as a standard treatment option in human medicine.

For accurate information regarding medical definitions or treatments, consult with healthcare professionals or refer to reputable medical resources.

P-Fluorophenylalanine (p-FPA) is not a medical term, but a chemical compound used in research and medical fields. It's a type of amino acid that is used as a building block for proteins, similar to the naturally occurring amino acid phenylalanine. However, p-FPA has a fluorine atom attached to its para position (one of the possible positions on the phenyl ring).

This compound can be used in various research applications, including the study of protein synthesis and enzyme function. It's also been explored as a potential therapeutic agent for certain medical conditions, such as cancer and neurological disorders. However, more research is needed to establish its safety and efficacy for these uses.

Chorismate mutase is an important enzyme in the biosynthetic pathway of aromatic amino acids in bacteria, fungi, and plants. This enzyme catalyzes the conversion of chorismate to prephenate, which is a key step in the synthesis of phenylalanine, tyrosine, and tryptophan.

The reaction catalyzed by chorismate mutase is as follows:

chorismate → prephenate

Inhibition of this enzyme has been explored as a potential target for the development of antibiotics and herbicides, as interrupting the synthesis of aromatic amino acids can be lethal to bacteria and plants. In humans, the equivalent reaction is catalyzed by a different set of enzymes, so chorismate mutase inhibitors are not expected to have toxic effects on human cells.

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.

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.

Essential amino acids are a group of 9 out of the 20 standard amino acids that cannot be synthesized by the human body and must be obtained through diet. They include: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are essential for various biological processes such as protein synthesis, growth, and repair of body tissues. A deficiency in any of these essential amino acids can lead to impaired physical development and compromised immune function. Foods that provide all nine essential amino acids are considered complete proteins and include animal-derived products like meat, poultry, fish, eggs, and dairy, as well as soy and quinoa.

Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.

Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.

Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.

Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.

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.

Aspartame is a synthetic, low-calorie sweetener that is commonly used as a sugar substitute in foods and beverages. It is composed of two amino acids, aspartic acid and phenylalanine, and a methanol molecule. Aspartame is approximately 200 times sweeter than sugar, so only a small amount is needed to provide the same level of sweetness.

In the body, aspartame is broken down into its component parts during digestion. The aspartic acid and phenylalanine are absorbed and used for normal bodily functions, while the methanol is converted into formaldehyde and then formic acid, which are eliminated from the body.

Aspartame is approved for use in foods and beverages by many health authorities, including the U.S. Food and Drug Administration (FDA) and the European Food Safety Authority (EFSA). However, it has been the subject of some controversy, with some studies suggesting that it may be associated with health problems such as headaches, dizziness, and seizures. These claims have not been consistently supported by scientific research, and the FDA and EFSA consider aspartame to be safe for the general population when used in moderation.

It is important to note that people with a rare genetic disorder called phenylketonuria (PKU) must avoid aspartame because they are unable to metabolize phenylalanine, which can build up to toxic levels in their bodies. Foods and beverages containing aspartame must carry a warning label indicating its presence for this reason.

Hydroxylation is a biochemical process that involves the addition of a hydroxyl group (-OH) to a molecule, typically a steroid or xenobiotic compound. This process is primarily catalyzed by enzymes called hydroxylases, which are found in various tissues throughout the body.

In the context of medicine and biochemistry, hydroxylation can have several important functions:

1. Drug metabolism: Hydroxylation is a common way that the liver metabolizes drugs and other xenobiotic compounds. By adding a hydroxyl group to a drug molecule, it becomes more polar and water-soluble, which facilitates its excretion from the body.
2. Steroid hormone biosynthesis: Hydroxylation is an essential step in the biosynthesis of many steroid hormones, including cortisol, aldosterone, and the sex hormones estrogen and testosterone. These hormones are synthesized from cholesterol through a series of enzymatic reactions that involve hydroxylation at various steps.
3. Vitamin D activation: Hydroxylation is also necessary for the activation of vitamin D in the body. In order to become biologically active, vitamin D must undergo two successive hydroxylations, first in the liver and then in the kidneys.
4. Toxin degradation: Some toxic compounds can be rendered less harmful through hydroxylation. For example, phenol, a toxic compound found in cigarette smoke and some industrial chemicals, can be converted to a less toxic form through hydroxylation by enzymes in the liver.

Overall, hydroxylation is an important biochemical process that plays a critical role in various physiological functions, including drug metabolism, hormone biosynthesis, and toxin degradation.

Pteridines are a class of heterocyclic aromatic organic compounds that are structurally related to pterins, which contain a pyrimidine ring fused to a pyrazine ring. They are naturally occurring substances that can be found in various living organisms such as bacteria, fungi, plants, and animals.

Pteridines have several important biological functions. For instance, they play a crucial role in the synthesis of folate and biotin, which are essential cofactors for various metabolic reactions in the body. Additionally, some pteridines function as chromophores, contributing to the coloration of certain organisms such as butterflies and birds.

In medicine, pteridines have been studied for their potential therapeutic applications. For example, some synthetic pteridine derivatives have shown promising results in preclinical studies as antitumor, antiviral, and antibacterial agents. However, further research is needed to fully understand the medical implications of these compounds.

3-Deoxy-7-phosphoheptulonate synthase (DAH7PS) is an enzyme that catalyzes the first step in the synthesis of the aromatic amino acids, phenylalanine, tyrosine, and tryptophan. The reaction it catalyzes is the condensation of erythrose-4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-hept-2-ulose-7-phosphate (DAHP), also known as 3-deoxy-7-phosphoheptulonate.

The reaction catalyzed by DAH7PS is the first step in the shikimate pathway, which is a seven-step metabolic route used by bacteria, fungi, algae, parasites, and plants to produce aromatic amino acids and other important compounds. Mammals do not have this pathway, so enzymes of the shikimate pathway are potential targets for the development of antibiotics and herbicides.

DAH7PS is a regulatory enzyme in the shikimate pathway, and its activity is feedback inhibited by the aromatic amino acids phenylalanine and tyrosine. This helps to regulate the flow of carbon into the aromatic amino acid biosynthetic pathway based on the needs of the cell.

Anabaena variabilis is a species of cyanobacteria (blue-green algae) that can form filamentous colonies. It is capable of fixing atmospheric nitrogen, making it an important contributor to the nitrogen cycle in aquatic environments. The term 'variabilis' refers to the variable size and shape of its cells.

Here's a simple medical definition:

Anabaena variabilis: A species of filamentous cyanobacteria known for its ability to fix nitrogen, contributing to the nitrogen cycle in aquatic environments. Its cells can vary in size and shape.

Rhodotorula is a genus of unicellular, budding yeasts that are commonly found in the environment, particularly in damp and nutrient-rich places such as soil, water, and vegetation. They are characterized by their ability to produce carotenoid pigments, which give them a distinctive pinkish-red color.

While Rhodotorula species are not typically associated with human disease, they can occasionally cause infections in people with weakened immune systems or underlying medical conditions. These infections can occur in various parts of the body, including the respiratory tract, urinary tract, and skin.

Rhodotorula infections are usually treated with antifungal medications, such as fluconazole or amphotericin B. Preventing exposure to sources of Rhodotorula, such as contaminated medical equipment or water supplies, can also help reduce the risk of infection.

Nutritional requirements refer to the necessary amount of nutrients, including macronutrients (carbohydrates, proteins, and fats) and micronutrients (vitamins and minerals), that an individual requires to maintain good health, support normal growth and development, and promote optimal bodily functions. These requirements vary based on factors such as age, sex, body size, pregnancy status, and physical activity level. Meeting one's nutritional requirements typically involves consuming a balanced and varied diet, with additional consideration given to any specific dietary restrictions or medical conditions that may influence nutrient needs.

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.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

Deuterium is a stable and non-radioactive isotope of hydrogen. The atomic nucleus of deuterium, called a deuteron, contains one proton and one neutron, giving it an atomic weight of approximately 2.014 atomic mass units (amu). It is also known as heavy hydrogen or heavy water because its hydrogen atoms contain one neutron in addition to the usual one proton found in common hydrogen atoms.

Deuterium occurs naturally in trace amounts in water and other organic compounds, typically making up about 0.015% to 0.018% of all hydrogen atoms. It can be separated from regular hydrogen through various methods such as electrolysis or distillation, and it has many applications in scientific research, particularly in the fields of chemistry and physics.

In medical contexts, deuterium is sometimes used as a tracer to study metabolic processes in the body. By replacing hydrogen atoms in specific molecules with deuterium atoms, researchers can track the movement and transformation of those molecules within living organisms. This technique has been used to investigate various physiological processes, including drug metabolism, energy production, and lipid synthesis.

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.

'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.

Isoleucine is an essential branched-chain amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H13NO2. Isoleucine is crucial for muscle protein synthesis, hemoglobin formation, and energy regulation during exercise or fasting. It is found in various foods such as meat, fish, eggs, dairy products, legumes, and nuts. Deficiency of isoleucine may lead to various health issues like muscle wasting, fatigue, and mental confusion.

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.

Phenylacetates are a group of organic compounds that contain a phenyl group (a benzene ring with a hydroxyl group) and an acetic acid group. In the context of medicine, sodium phenylacetate is used in the treatment of certain metabolic disorders, such as urea cycle disorders, to help remove excess ammonia from the body. It does this by conjugating with glycine to form phenylacetylglutamine, which can then be excreted in the urine.

It is important to note that the use of phenylacetates should be under the supervision of a medical professional, as improper use or dosage can lead to serious side effects.

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.

An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.

Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.

Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.

In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.

Muscle proteins are a type of protein that are found in muscle tissue and are responsible for providing structure, strength, and functionality to muscles. The two major types of muscle proteins are:

1. Contractile proteins: These include actin and myosin, which are responsible for the contraction and relaxation of muscles. They work together to cause muscle movement by sliding along each other and shortening the muscle fibers.
2. Structural proteins: These include titin, nebulin, and desmin, which provide structural support and stability to muscle fibers. Titin is the largest protein in the human body and acts as a molecular spring that helps maintain the integrity of the sarcomere (the basic unit of muscle contraction). Nebulin helps regulate the length of the sarcomere, while desmin forms a network of filaments that connects adjacent muscle fibers together.

Overall, muscle proteins play a critical role in maintaining muscle health and function, and their dysregulation can lead to various muscle-related disorders such as muscular dystrophy, myopathies, and sarcopenia.

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.

Transfer RNA (tRNA) is a type of RNA molecule that helps translate genetic information from messenger RNA (mRNA) into proteins. Each tRNA carries a specific amino acid to the growing polypeptide chain during protein synthesis, based on the anticodon sequence in its variable loop region that recognizes and binds to a complementary codon sequence in the mRNA.

Phenylalanine (Phe) is one of the twenty standard amino acids found in proteins. It has a hydrophobic side chain, which means it tends to repel water and interact with other non-polar molecules. In tRNA, phenylalanine is attached to a specific tRNA molecule known as tRNAPhe. This tRNA recognizes the mRNA codons UUC and UUU, which specify phenylalanine during protein synthesis.

"Formulated food" is a term used in the field of clinical nutrition to refer to foods that are specially manufactured and designed to meet the nutritional needs of specific patient populations. These foods often come in the form of shakes, bars, or pouches and are intended to be used as a sole source or supplementary source of nutrition for individuals who have difficulty meeting their nutritional needs through traditional food sources alone.

Formulated foods may be indicated for patients who have medical conditions that affect their ability to eat or digest regular food, such as dysphagia (swallowing difficulties), malabsorption syndromes, or chronic inflammatory bowel disease. They may also be used in patients who require additional nutritional support during times of illness, injury, or recovery from surgery.

Formulated foods are typically designed to provide a balance of macronutrients (carbohydrates, proteins, and fats) and micronutrients (vitamins and minerals) that meet the recommended dietary intakes for specific patient populations. They may also contain additional ingredients such as fiber, probiotics, or other nutraceuticals to provide additional health benefits.

It is important to note that formulated foods should only be used under the guidance of a healthcare professional, such as a registered dietitian or physician, to ensure that they are appropriate for an individual's specific medical and nutritional needs.

Valine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet. It is a hydrophobic amino acid, with a branched side chain, and is necessary for the growth, repair, and maintenance of tissues in the body. Valine is also important for muscle metabolism, and is often used by athletes as a supplement to enhance physical performance. Like other essential amino acids, valine must be obtained through foods such as meat, fish, dairy products, and legumes.

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

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

Substrate specificity can be categorized as:

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

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

Leucine dehydrogenase (LDH) is an enzyme that catalyzes the reversible conversion of leucine to α-ketoisocaproate, while simultaneously reducing NAD+ to NADH. It plays a crucial role in the metabolism of branched-chain amino acids and is widely distributed in various tissues such as liver, kidney, heart, skeletal muscle, and brain.

In clinical settings, LDH is often measured in serum or plasma as a biomarker for tissue damage since it is released into the bloodstream upon cell death or injury. Elevated levels of LDH can be observed in various conditions such as myocardial infarction, hemolysis, liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific to a particular condition, and further diagnostic tests are usually required for accurate diagnosis.

'Chromobacterium' is a genus of gram-negative, aerobic or facultatively anaerobic bacteria that are commonly found in soil and water. The name "Chromobacterium" comes from the Greek words "chroma," meaning color, and "bakterion," meaning rod or staff. This refers to the fact that many species of this genus produce pigments that give them distinctive colors.

One of the most well-known species in this genus is Chromobacterium violaceum, which produces a characteristic violet-colored pigment called violacein. This bacterium can cause serious infections in humans, particularly in people with weakened immune systems. Other species in the genus include Chromobacterium aquaticum, Chromobacterium haemolyticum, and Chromobacterium piscinae, among others.

Chromobacterium species are known to be resistant to a variety of antibiotics, which can make them difficult to treat in clinical settings. They have also been studied for their potential industrial applications, such as the production of enzymes and other biomolecules with commercial value.

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.

Aldehyde-lyases are a class of enzymes that catalyze the breakdown or synthesis of molecules involving an aldehyde group through a reaction known as lyase cleavage. This type of reaction results in the removal of a molecule, typically water or carbon dioxide, from the substrate.

In the case of aldehyde-lyases, these enzymes specifically catalyze reactions that involve the conversion of an aldehyde into a carboxylic acid or vice versa. These enzymes are important in various metabolic pathways and play a crucial role in the biosynthesis and degradation of several biomolecules, including carbohydrates, amino acids, and lipids.

The systematic name for this class of enzymes is "ald(e)hyde-lyases." They are classified under EC number 4.3.1 in the Enzyme Commission (EC) system.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

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.

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.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:

1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.

Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.

Protein biosynthesis is the process by which cells generate new proteins. It involves two major steps: transcription and translation. Transcription is the process of creating a complementary RNA copy of a sequence of DNA. This RNA copy, or messenger RNA (mRNA), carries the genetic information to the site of protein synthesis, the ribosome. During translation, the mRNA is read by transfer RNA (tRNA) molecules, which bring specific amino acids to the ribosome based on the sequence of nucleotides in the mRNA. The ribosome then links these amino acids together in the correct order to form a polypeptide chain, which may then fold into a functional protein. Protein biosynthesis is essential for the growth and maintenance of all living organisms.

Dietary proteins are sources of protein that come from the foods we eat. Protein is an essential nutrient for the human body, required for various bodily functions such as growth, repair, and immune function. Dietary proteins are broken down into amino acids during digestion, which are then absorbed and used to synthesize new proteins in the body.

Dietary proteins can be classified as complete or incomplete based on their essential amino acid content. Complete proteins contain all nine essential amino acids that cannot be produced by the human body and must be obtained through the diet. Examples of complete protein sources include meat, poultry, fish, eggs, dairy products, soy, and quinoa.

Incomplete proteins lack one or more essential amino acids and are typically found in plant-based foods such as grains, legumes, nuts, and seeds. However, by combining different incomplete protein sources, it is possible to obtain all the essential amino acids needed for a complete protein diet. This concept is known as complementary proteins.

It's important to note that while dietary proteins are essential for good health, excessive protein intake can have negative effects on the body, such as increased stress on the kidneys and bones. Therefore, it's recommended to consume protein in moderation as part of a balanced and varied diet.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

Shikimic acid is not a medical term per se, but a chemical compound with significance in biochemistry and pharmacology. It is a cyclohexene derivative that plays a crucial role as an intermediate in the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) in plants and microorganisms.

Medically, shikimic acid is relevant due to its use as a precursor in the synthesis of antiviral drugs such as oseltamivir (Tamiflu), which is used for treating and preventing influenza A and B infections. It's important to note that shikimic acid itself does not have any direct medical applications, but its derivatives can be essential components in pharmaceutical products.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. It serves as the adaptor molecule that translates the genetic code present in messenger RNA (mRNA) into the corresponding amino acids, which are then linked together to form a polypeptide chain during protein synthesis.

Aminoacyl tRNA is a specific type of tRNA molecule that has been charged or activated with an amino acid. This process is called aminoacylation and is carried out by enzymes called aminoacyl-tRNA synthetases. Each synthetase specifically recognizes and attaches a particular amino acid to its corresponding tRNA, ensuring the fidelity of protein synthesis. Once an amino acid is attached to a tRNA, it forms an aminoacyl-tRNA complex, which can then participate in translation and contribute to the formation of a new protein.

Tetroses are a type of monosaccharides, which are simple sugars that cannot be broken down into simpler units by hydrolysis. Tetroses have four carbon atoms and are aldotetroses, meaning they contain an aldehyde functional group at the first carbon atom.

There are two naturally occurring tetroses: erythrose and threose. Erythrose has its hydroxyl groups on the second and fourth carbon atoms, while threose has its hydroxyl groups on the second and third carbon atoms. Tetroses can participate in various chemical reactions, including forming glycosidic bonds with other monosaccharides to create disaccharides or polysaccharides. However, tetroses are not as common as other monosaccharides, such as pentoses and hexoses.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

Branched-chain amino acids (BCAAs) are a group of three essential amino acids: leucine, isoleucine, and valine. They are called "branched-chain" because of their chemical structure, which has a side chain that branches off from the main part of the molecule.

BCAAs are essential because they cannot be produced by the human body and must be obtained through diet or supplementation. They are crucial for muscle growth and repair, and play a role in energy production during exercise. BCAAs are also important for maintaining proper immune function and can help to reduce muscle soreness and fatigue after exercise.

Foods that are good sources of BCAAs include meat, poultry, fish, eggs, dairy products, and legumes. BCAAs are also available as dietary supplements, which are often used by athletes and bodybuilders to enhance muscle growth and recovery. However, it is important to note that excessive intake of BCAAs may have adverse effects on liver function and insulin sensitivity, so it is recommended to consult with a healthcare provider before starting any new supplement regimen.

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.

Dihydropteridine reductase is an enzyme that plays a crucial role in the metabolism of certain amino acids, specifically phenylalanine and tyrosine. This enzyme is responsible for reducing dihydropteridines to tetrahydropteridines, which is a necessary step in the regeneration of tetrahydrobiopterin (BH4), an essential cofactor for the enzymes phenylalanine hydroxylase and tyrosine hydroxylase.

Phenylalanine hydroxylase and tyrosine hydroxylase are involved in the conversion of the amino acids phenylalanine and tyrosine to tyrosine and dopa, respectively. Without sufficient BH4, these enzymes cannot function properly, leading to an accumulation of phenylalanine and a decrease in the levels of important neurotransmitters such as dopamine, norepinephrine, and serotonin.

Deficiency in dihydropteridine reductase can lead to a rare genetic disorder known as dihydropteridine reductase deficiency (DPRD), which is characterized by elevated levels of phenylalanine and neurotransmitter imbalances, resulting in neurological symptoms such as developmental delay, seizures, and hypotonia. Treatment typically involves a low-phenylalanine diet and supplementation with BH4.

Fluorine is not a medical term itself, but it is a chemical element that is often discussed in the context of dental health. Here's a brief scientific/chemical definition:

Fluorine is a chemical element with the symbol F and atomic number 9. It is the most reactive and electronegative of all elements. Fluorine is never found in its free state in nature, but it is abundant in minerals such as fluorspar (calcium fluoride).

In dental health, fluoride, which is a compound containing fluorine, is used to help prevent tooth decay. It can be found in many water supplies, some foods, and various dental products like toothpaste and mouthwash. Fluoride works by strengthening the enamel on teeth, making them more resistant to acid attacks that can lead to cavities.

Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.

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.

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

Mitosporic fungi, also known as asexual fungi or anamorphic fungi, are a group of fungi that produce mitospores (also called conidia) during their asexual reproduction. Mitospores are produced from the tip of specialized hyphae called conidiophores and are used for dispersal and survival of the fungi in various environments. These fungi do not have a sexual reproductive stage or it has not been observed, making their taxonomic classification challenging. They are commonly found in soil, decaying organic matter, and water, and some of them can cause diseases in humans, animals, and plants. Examples of mitosporic fungi include Aspergillus, Penicillium, and Fusarium species.

Protein hydrolysates are defined as proteins that have been broken down into smaller peptide chains or individual amino acids through a process called hydrolysis. This process involves the use of water, enzymes, or acids to break the bonds between the amino acids in the protein molecule.

Protein hydrolysates are often used in medical and nutritional applications because they are easier to digest and absorb than intact proteins. They are also less likely to cause allergic reactions or digestive discomfort in individuals who have difficulty tolerating whole proteins. Protein hydrolysates can be derived from a variety of sources, including animal proteins such as collagen and casein, as well as plant proteins such as soy and wheat.

In addition to their use in medical and nutritional applications, protein hydrolysates are also used in the food industry as flavor enhancers, emulsifiers, and texturizers. They are commonly found in products such as infant formula, sports drinks, and clinical nutrition formulas.

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

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

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

Cinnamates are organic compounds that are derived from cinnamic acid. They contain a carbon ring with a double bond and a carboxylic acid group, making them aromatic acids. Cinnamates are widely used in the perfume industry due to their pleasant odor, and they also have various applications in the pharmaceutical and chemical industries.

In a medical context, cinnamates may be used as topical medications for the treatment of skin conditions such as fungal infections or inflammation. For example, cinnamate esters such as cinoxacin and ciclopirox are commonly used as antifungal agents in creams, lotions, and shampoos. These compounds work by disrupting the cell membranes of fungi, leading to their death.

Cinnamates may also have potential therapeutic benefits for other medical conditions. For instance, some studies suggest that cinnamate derivatives may have anti-inflammatory, antioxidant, and neuroprotective properties, making them promising candidates for the development of new drugs to treat diseases such as Alzheimer's and Parkinson's. However, more research is needed to confirm these effects and determine their safety and efficacy in humans.

A point mutation is a type of genetic mutation where a single nucleotide base (A, T, C, or G) in DNA is altered, deleted, or substituted with another nucleotide. Point mutations can have various effects on the organism, depending on the location of the mutation and whether it affects the function of any genes. Some point mutations may not have any noticeable effect, while others might lead to changes in the amino acids that make up proteins, potentially causing diseases or altering traits. Point mutations can occur spontaneously due to errors during DNA replication or be inherited from parents.

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.

Neutral amino acids are a type of amino acids that are characterized by the presence of a neutral side chain in their chemical structure. In other words, the side chain of these amino acids does not contain any ionizable groups, such as carboxyl or amino groups, which can give rise to positive or negative charges.

There are nine neutral amino acids in total, and they include:

1. Alanine (Ala) - has a methyl group (-CH3) as its side chain
2. Glycine (Gly) - has a hydrogen atom (-H) as its side chain
3. Valine (Val) - has an isopropyl group (-CH(CH3)2) as its side chain
4. Leucine (Leu) - has a branched alkyl group (-CH2CH(CH3)2) as its side chain
5. Isoleucine (Ile) - has a sec-butyl group (-CH(CH3)(CH2CH3)) as its side chain
6. Proline (Pro) - has a cyclic structure containing a secondary amino group (-NH-) as its side chain
7. Phenylalanine (Phe) - has an aromatic ring with a methyl group (-CH3) attached to it as its side chain
8. Tryptophan (Trp) - has an indole ring as its side chain
9. Methionine (Met) - has a sulfur-containing alkyl group (-CH2CH2SH) as its side chain

Neutral amino acids play important roles in various biological processes, such as protein synthesis, metabolism, and signaling pathways. They are also essential components of many dietary proteins and are required for the growth, development, and maintenance of tissues and organs in the body.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

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.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Tyrosine transaminase, also known as tyrosine aminotransferase or TAT, is an enzyme that plays a crucial role in the metabolism of the amino acid tyrosine. This enzyme catalyzes the transfer of an amino group from tyrosine to a ketoacid, such as alpha-ketoglutarate, resulting in the formation of a new amino acid, glutamate, and a ketone derivative of tyrosine.

Tyrosine transaminase is primarily found in the liver and its activity can be used as a biomarker for liver function. Increased levels of this enzyme in the blood may indicate liver damage or disease, such as hepatitis or cirrhosis. Therefore, measuring tyrosine transaminase activity is often part of routine liver function tests.

Homogentisate 1,2-dioxygenase (HGD) is an enzyme that plays a crucial role in the catabolism of tyrosine, an aromatic amino acid. This enzyme is involved in the third step of the tyrosine degradation pathway, also known as the tyrosine breakdown or catabolic pathway.

The homogentisate 1,2-dioxygenase enzyme catalyzes the conversion of homogentisic acid (HGA) into maleylacetoacetic acid. This reaction involves the cleavage of the aromatic ring of HGA and the introduction of oxygen, hence the name 'dioxygenase.' The reaction can be summarized as follows:

Homogentisate + O2 → Maleylacetoacetate

Deficiency or dysfunction in homogentisate 1,2-dioxygenase leads to a rare genetic disorder called alkaptonuria. In this condition, the body cannot break down tyrosine properly, resulting in an accumulation of HGA and its oxidation product, alkapton, which can cause damage to connective tissues and joints over time.

"Petroselinum" is the genus name for a group of plants that include several types of parsley. The most common variety is often used as a herb in cooking and is known as "Petroselinum crispum." It is native to the Mediterranean region and is now grown worldwide. Parsley has a bright, fresh flavor and is often used as a garnish or added to recipes for additional flavor. In addition to its use as a culinary herb, parsley has also been used in traditional medicine for its potential diuretic and digestive properties. However, it's important to note that the scientific evidence supporting these uses is limited, and more research is needed before any firm conclusions can be drawn.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) are a group of enzymes that play a crucial role in protein synthesis. They are responsible for attaching specific amino acids to their corresponding transfer RNAs (tRNAs), creating aminoacyl-tRNA complexes. These complexes are then used in the translation process to construct proteins according to the genetic code.

Each aminoacyl-tRNA synthetase is specific to a particular amino acid, and there are 20 different synthetases in total, one for each of the standard amino acids. The enzymes catalyze the reaction between an amino acid and ATP to form an aminoacyl-AMP intermediate, which then reacts with the appropriate tRNA to create the aminoacyl-tRNA complex. This two-step process ensures the fidelity of the translation process by preventing mismatching of amino acids with their corresponding tRNAs.

Defects in aminoacyl-tRNA synthetases can lead to various genetic disorders and diseases, such as Charcot-Marie-Tooth disease type 2D, distal spinal muscular atrophy, and leukoencephalopathy with brainstem and spinal cord involvement and lactate acidosis (LBSL).

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Cyclohexanecarboxylic acids are a type of organic compound that consists of a cyclohexane ring, which is a six-carbon saturated hydrocarbon, substituted with a carboxylic acid group (-COOH). This group contains a carbon atom double bonded to an oxygen atom and single bonded to a hydroxyl group (-OH).

The cyclohexane ring can be in various forms, including the chair, boat, or twist-boat conformations, depending on the orientation of its constituent atoms. The carboxylic acid group can ionize to form a carboxylate anion, which is negatively charged and has a deprotonated hydroxyl group.

Cyclohexanecarboxylic acids have various applications in industry and research, including as intermediates in the synthesis of other chemicals, solvents, and pharmaceuticals. They can also be found naturally in some plants and microorganisms.

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.

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

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

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Radioactive tracers are radioisotopes or radiolabeled compounds that are introduced into a biological system, such as the human body, in very small amounts to allow tracking or monitoring of specific physiological processes or locations. The radiation emitted by the tracer can be detected and measured, providing information about the distribution, metabolism, or binding of the compound within the body. This technique is widely used in medical imaging and research for diagnostic and therapeutic purposes. Examples of radioactive tracers include technetium-99m for bone scans, fluorine-18 for positron emission tomography (PET) scans, and iodine-131 for thyroid studies.

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.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

DL-Phenylalanine is a mixture of D-phenylalanine and L-phenylalanine. The reputed analgesic activity of DL-phenylalanine may be ... Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. Phenylalanine is biosynthesized via the ... A small amount of D-phenylalanine appears to be converted to L-phenylalanine. D-Phenylalanine is distributed to the various ... ISBN 978-3-540-48595-7. Wikimedia Commons has media related to L-Phenylalanine. Phenylalanine mass spectrum Phenylalanine at ...
N-adenylyl-L-phenylalanine Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are ... L-phenylalanine adenylyltransferase. This enzyme is also called L-phenylalanine adenylyltransferase. Lerbs W, Luckner M (1985 ... In enzymology, a phenylalanine adenylyltransferase (EC 2.7.7.54) is an enzyme that catalyzes the chemical reaction ATP + L- ... diphosphate and N-adenylyl-L-phenylalanine. This enzyme belongs to the family of transferases, specifically those transferring ...
The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction L-phenylalanine ⇌ {\displaystyle \ ... and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal ... The systematic name of this enzyme class is L-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use ... include L-phenylalanine decarboxylase, aromatic L-amino acid decarboxylase, ...
The Pah-KO mouse model presented high blood phenylalanine and low tyrosine levels, hypocholesterolemia, high phenylalanine and ... GeneReviews/NCBI/NIH/UW entry on Phenylalanine Hydroxylase Deficiency Locus-specific database of the human phenylalanine ... "Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase". Archives of Biochemistry and ... "The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for ...
In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction L-phenylalanine + ... This enzyme participates in phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. As of late 2007, ... Asano Y, Nakazawa A, Endo K, Hibino Y, Ohmori M, Numao N, Kondo K (1987). "Phenylalanine dehydrogenase of Bacillus badius. ... The systematic name of this enzyme class is L-phenylalanine:NAD+ oxidoreductase (deaminating). Other names in common use ...
Other names in common use include phenylalanine (histidine) aminotransferase, phenylalanine(histidine):pyruvate ... In enzymology, a phenylalanine(histidine) transaminase (EC 2.6.1.58) is an enzyme that catalyzes the chemical reaction L- ... Minatogawa Y, Noguchi T, Kido R (January 1977). "Species distribution and properties of hepatic phenylalanine (histidine): ... The systematic name of this enzyme class is L-phenylalanine:pyruvate aminotransferase. ...
... and L-phenylalanine ammonia-lyase. Phenylalanine ammonia lyase is specific for L-phenylalanine, and to a lesser extent, L- ... The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic ... phenylalanine ammonia-lyases), EC 4.3.1.25 (tyrosine ammonia-lyases), and EC 4.3.1.26 (phenylalanine/tyrosine ammonia-lyases). ... Phenylalanine ammonia lyase is found widely in plants, as well as some bacteria, yeast, and fungi, with isoenzymes existing ...
This enzyme is also called acetyl-CoA-L-phenylalanine alpha-N-acetyltransferase. This enzyme participates in phenylalanine ... N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. ...
a EINECS number 200-568-1 (phenylalanine) ^a CID 994 from PubChem (phenylalanine) ^a CID 71567 from PubChem (D-phenylalanine) ^ ... a CID 6140 from PubChem (L-phenylalanine) (Articles with short description, Short description matches Wikidata, PubChem ID (CID ...
This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis. Phenylalanine- ... In enzymology, a phenylalanine-tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction ATP + L- ... The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include ... L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNAPhe. This enzyme belongs to ...
... (EC 1.14.14.40, phenylalanine N-hydroxylase, CYP79A2) is an enzyme with systematic name L- ... N-hydroxy-L-phenylalanine + O2 + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } N,N-dihydroxy-L-phenylalanine + NADP+ + H2O ( ... L-phenylalanine + O2 + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } N-hydroxy-L-phenylalanine + NADP+ + H2O: (1b) ... 1c) N,N-dihydroxy-L-phenylalanine ⇌ {\displaystyle \rightleftharpoons } (E)-phenylacetaldoxime + CO2 + H2O Phenylalanine N- ...
In enzymology, a phenylalanine 2-monooxygenase (EC 1.13.12.9) is an enzyme that catalyzes the chemical reaction L-phenylalanine ... Koyama H (1984). "A simple and rapid enzymatic determination of L-phenylalanine with a novel L-phenylalanine oxidase ( ... and phenylalanine (deaminating, decarboxylating)oxidase. This enzyme participates in phenylalanine metabolism. Koyama H ( ... Koyama H (August 1984). "Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and ...
The enzyme phenylalanine racemase (EC 5.1.1.11, phenylalanine racemase, phenylalanine racemase (adenosine triphosphate- ... phenylalanine racemase phenylalanine racemase (adenosine triphosphate-hydrolysing) gramicidin S synthetase I Phenylalanine ... Biology portal Phenylalanine Racemase Phenylketonuria Takahashi H, Sato E, Kurahashi K (1971). "Racemization of phenylalanine ... Phenylalanine Pyridoxal-phosphate (active form of vitamin B6) Problems in the digestion of phenylalanine (phe) to tyrosine (tyr ...
N-Formylmethionyl-leucyl-phenylalanine (fMLF, fMLP or N-formyl-met-leu-phe) is an N-formylated tripeptide and sometimes simply ... N-Formylmethionine Leucyl-Phenylalanine at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (CS1 errors: ... n-formylmethionine leucyl-phenylalanine, Cancerweb Panaro MA, Mitolo V (Aug 1999). "Cellular responses to fMLF challenging: a ...
... and state that the product contains phenylalanine. Phenylalanine is one of the essential amino acids and is required for normal ... Phenylalanine is converted to its methyl ester and combined with the N-formyl aspartic anhydride; then the protecting group is ... Aspartame is a methyl ester of the dipeptide of the natural amino acids L-aspartic acid and L-phenylalanine. Under strongly ... As with methanol and phenylalanine, intake of aspartic acid from aspartame is less than would be expected from other dietary ...
L-Phenylalanine. a naturally occurring amino acid (equilibrium dissociation constant (KB) from Schild regression is 573 μM). ... "Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations ...
Kaufman S (1962). "Phenylalanine hydroxylase". Methods Enzymol. 5: 809-816. doi:10.1016/s0076-6879(62)05317-3. Lind KE ( ... a controlled diet which is lacking in phenylalanine, well as supplementation of L-DOPA. Sepiapterin reductase Longo N (June ...
May 2008). "Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and ... The 2,5-cyclohexene ring becomes a phenyl ring, and L-phenylalanine is formed. Certain forms of ADT have been shown to exhibit ... The systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in ... Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction L-arogenate → L phenylalanine + H2O ...
Infants with PKU appear normal at birth, but are unable to metabolize the essential amino acid phenylalanine, resulting in ... Mitchell, J. J.; Trakadis, Y. J.; Scriver, C. R. (2011). "Phenylalanine hydroxylase deficiency". Genetics in Medicine. 13 (8): ... to measure phenylalanine levels in blood samples obtained by pricking a newborn baby's heel on the second day of life on filter ... Robert Guthrie developed a simple method using a bacterial inhibition assay that could detect high levels of phenylalanine in ...
... contains phenylalanine". In Canada, the ingredient listing reads: "carbonated water, caramel color, phosphoric acid, aspartame ... contains a source of phenylalanine". The initial formulation of Diet Pepsi was sweetened with the artificial sweetener ... 124 mg/355 ml, contains phenylalanine), sodium benzoate, caffeine, flavor, acesulfame potassium (32 mg/355ml), citric acid, ...
5, p. 946 H. B. Gillespie, H. R. Snyder (1934). "dl-β-Phenylalanine". Organic Syntheses.; Collective Volume, vol. 2, p. 489 ... This compound on reduction gives access to phenylalanine. Variants of the azlactone synthesis in which analogues of azlactones ...
Aspartame contains phenylalanine.) Comparing Sprite Zero Sugar to other popular lemon-lime sodas: "Sprite Zero will become ...
Mitchell, J. J.; Trakadis, Y. J.; Scriver, C. R. (2011). "Phenylalanine hydroxylase deficiency". Genetics in Medicine. 13 (8): ...
The enzyme phenylalanine hydroxylase normally converts the amino acid phenylalanine into the amino acid tyrosine. If this ... If phenylalanine is in excess in the blood, it will saturate the transporter. Excessive levels of phenylalanine tend to ... then phenylalanine levels in the blood will increase over time. Toxic levels of phenylalanine (and insufficient levels of ... are caused by a mutated gene for the enzyme phenylalanine hydroxylase (PAH), which converts the amino acid phenylalanine ("Phe ...
N-formylmethionine-leucyl-phenylalanine); b) complement components C5a and C3a which are chemotactic factors formed during the ...
A formulation containing lofepramine and the amino acid phenylalanine is under investigation as a treatment for fatigue as of ... "Lofepramine/phenylalanine - MultiCell Technologies". AdisInsight. Springer International Publishing AG. Retrieved 3 August 2017 ...
Strecker degradation of phenylalanine. Phenylacetaldehyde is often contaminated with polystyrene oxide polymer because of the ... Phenylacetaldehyde occurs extensively in nature because it can be biosynthetically derived from the amino acid phenylalanine. ... Historically, before biotechnology approaches were developed, phenylacetaldehyde was also used to produce phenylalanine via the ...
Phenylalanine and tyrosine are grouped together because one of them can be synthesized from the other using the enzyme ... "Phenylalanine and Tyrosine Metabolism". National Center for Biotechnology Information PubChem. 18 May 2022. Retrieved 21 ... Tyrosine is synthesized by the hydroxylation of phenylalanine, which is an essential amino acid. Estimating the daily ... phenylalanine, leucine, isoleucine, methionine, valine, and arginine, in addition to threonine. Rose's later work showed that ...
Phenylalanine, a common amino acid. Biphenyl, consisting of two phenyl groups. The two rings tend not to be coplanar. ... Most common among natural products is the amino acid phenylalanine, which contains a phenyl group. A major product of the ...
... they are synthesized from phenylalanine. Floral scent emissions of most flowering plants vary predictably throughout the day, ...
DL-Phenylalanine is a mixture of D-phenylalanine and L-phenylalanine. The reputed analgesic activity of DL-phenylalanine may be ... Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. Phenylalanine is biosynthesized via the ... A small amount of D-phenylalanine appears to be converted to L-phenylalanine. D-Phenylalanine is distributed to the various ... ISBN 978-3-540-48595-7. Wikimedia Commons has media related to L-Phenylalanine. Phenylalanine mass spectrum Phenylalanine at ...
The test detects abnormally high levels of an amino acid called phenylalanine. ... The test detects abnormally high levels of an amino acid called phenylalanine. ... Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). ... Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). ...
1265 Phenylalanine Ca-Cb-Cc should be 113.6 (Geo) (Previous) (Back) (Next) # Species Formula ... PM7 Phenylalanine Ca-Cb-Cc should be 113.6 ,, ,,<C-C-C, GR=CCDC GWT=5 C 0.00000000 +0 0.0000000 +0 0.0000000 +0 0 0 0 C ...
Mechanism of the cleavage specificity of Alzheimers disease gamma-secretase identified by phenylalanine-scanning mutagenesis ...
Click the button below to add the L-Phenylalanine hydrazide 5 g to your wish list. ...
Learn about the claims, recommended intake, and side effects of phenylalanine.
Bourdillon, J. and Vanderlinde, R. E. "An Improved Screening Procedure For Blood Phenylalanine" vol. 81, no. 11, 1966. Export ... Bourdillon, J. and Vanderlinde, R. E. (1966). An Improved Screening Procedure For Blood Phenylalanine. 81(11). Bourdillon, J. ... Title : An Improved Screening Procedure For Blood Phenylalanine Personal Author(s) : Bourdillon, J.;Vanderlinde, R. E.; ... and Vanderlinde, R. E. "An Improved Screening Procedure For Blood Phenylalanine" 81, no. 11 (1966). ...
Phenylalanine is an amino acid that hydrates skin and helps reduce the appearance of uneven tone. Learn more at Paulas Choice. ... Phenylalanine description Phenylalanine is what is termed as an essential amino acid, meaning that it does not occur naturally ... Phenylalanine has been shown to be well-tolerated by skin, with no reports of adverse reactions. Usage levels of phenylalanine ... Products with Phenylalanine Routine step Step 5 Moisturiser PM: A nighttime moisturiser provides your skin with the right ...
This unusual amino acid helps increase endorphin levels in the brain and body, reducing physical and emotional pain. Our clinic experience supports the solid scientific research findings on this. INGREDIENTS: 500 mg D-Phenylalanine.
BOC-L-Phenylalanine Methyl Ester extrapure, 98%. https://gena.odoo.com/shop/51987-73-6-boc-l-phenylalanine-methyl-ester- ...
L-Phenylalanine LPA is not synthesized by the body. It must therefore be obtained from the diet. Phenylalanine is also used by ... L-Phenylalanine LPA is not synthesized by the body. It must therefore be obtained from the diet. Phenylalanine is also used by ... L-Phenylalanine, Vegetable HPMC capsule.. Directions. Take two capsules daily on an empty stomach or between the meals. Take in ... L-Phenylalanine 1000mg Capsules , MEMORY , ATTENTION , HEALTHY THYROID , PAIN RELIEF. Regular price £12.97 ...
eg UUU and UUC code for Phenylalanine. , Complete Degeneracy. Occur when any of the 4 bases can take third position in codon ... Nirenberg and his colleague Johann H Matthaei showed that a triplet of uracils (U) coded for the amino acid phenylalanine (F ... cell free content •The Poly-U Experiment • (UUUUUUUUU) →phenylalanine •The Poly-UC Experiment • Gobind Khorana (UCUCUCUCU) → ...
Phenylalanine. 2.63 g. 296. Proline. 2.66 g. Serine. 2.26 g. Threonine. 2.74 g. 282. ...
Low intensity cardio sessions on an empty stomach burn more fat if you take 3 g of the amino acid L-phenylalanine half an hour ... Low intensity cardio before breakfast burns more fat if you take some L-phenylalanine ... "In conclusion, pre-exercise ingestion of a phenylalanine supplement significantly accelerated secretion of glucagon during both ... http://www.ergo-log.com/cardio-before-breakfast-burns-more-fat-l-phenylalanine.html. ...
MCT10 is expressed within a selection of tissues such asAnd phenylalanine [50]. MCT10 is expressed inside a selection of ... And phenylalanine [50]. MCT10 is expressed within a selection of tissues such asAnd phenylalanine [50]. By .translation ... And phenylalanine [50]. MCT10 is expressed within a selection of tissues such as. And phenylalanine [50]. MCT10 is expressed ...
Phenylalanine 0.01 g ~ Data not available. Protein & Amino Acids Related. Protein Intake Calculator. Your daily protein chart ...
Phenylalanine. - Serine. - Threonine. - Tryptophan. - Valine. All of the amino acids perform vital functions in the body. They ...
Consider alternating highballs with delicious "mocktails" such as kombucha, ginger or hibiscus tea, strawberry-mint infused water, fresh-pressed fruit/veggie juices, green tea or stevia-sweetened lemonade. Bonus: these healthy, hydrating beverages help boost your natural radiance! Remember, habits that elevate your mental, physical and emotional well-being can also help you look and feel more beautiful for decades to come. Happy 2022![/vc_column_text][/vc_column][/vc_row][vc_row][vc_column][vc_text_separator title="Featured Products" border_width="2"][vc_row_inner equal_height="yes" content_placement="middle" gap="35"][vc_column_inner width="1/3"][vc_single_image image="171089" img_size="full" alignment="center" onclick="custom_link" img_link_target="_blank" css=".vc_custom_1701996824348{padding-right: 7% !important;padding-left: 7% !important;}" link="https://www.vitacost.com/jason-c-effects-powered-by-ester-c-creme"][/vc_column_inner][vc_column_inner width="1/3"][vc_single_image image="171088" ...
Coke Zero has no sugar and calories, but this doesnt mean its healthy. This beverage contains artificial sweeteners that may cause weight gain and diabetes.
Phenylalanine. 0.04 g. Proline. 0.11 g. Serine. 0.03 g. Threonine. 0.03 g. ...
Phenylalanine *Valine OTHER. The following are examples of ingredients that would be classified as other: *an electrolyte (eg ...
D-[(AMINO)CARBONYL]PHENYLALANINE. C10 H12 N2 O3. IPWQOZCSQLTKOI-QMMMGPOBSA-N. Interactions *Focus chain F [auth A] ... Both D- and L-isomers of N-(hydroxyaminocarbonyl)phenylalanine () were shown to have strong binding affinity towards ... Insight Into the Stereochemistry in the Inhibition of Carboxypeptidase a with N-(Hydroxyaminocarbonyl)Phenylalanine: Binding ...
Phenylalanine and tyrosine are flavonoid precursors via the shikimate pathway before condensing with the malonic acetate ... Balloon-type bubble bioreactor, Flavonoid, Gynura procumbens, Phenylalanine, Tyrosine. Subjects:. Q Science , Q Science ( ... The results show that supplementation of phenylalanine 200 mg/L could increase kaempferol (2233.33 mgL-1/g dry weight) and ... The aim of this research is to enhance flavonoid production of G. procumbens adventitious roots influenced by phenylalanine and ...
Gottschall, D. W., Dietrich, R. F., Benkovic, S. J., and Shiman, R. (1982). Phenylalanine hydroxylase. correlation of the iron ... phenylalanine hydroxylase (Gottschall et al., 1982), and tryptophan hydroxylase (Kuhn et al., 1980) that are involved in the ...
When aspartame is digested, the body breaks it down into its components, aspartic acid, phenylalanine and methanol. People ... Phenylketonuria, phenylalanine, PKU and aspartame. Methanol, Methyl Alcohol and aspartame. Lisa Sheas Library of Low Carb ... Phenylketonuria, phenylalanine, PKU and aspartame. As far as methanol goes, when it occurs naturally in foods, it is ... I will be posting more of my research shortly into aspartic acid, phenylalanine, methanol and formaldehyde, and how they affect ...
Table 6 Phenylalanine Market Size, By Region, 2014-2022 (USD Million). Table 7 Other Types Market Size, By Region, 2014-2022 ( ... Based on type, the market is segmented into glutamic acid, lysine, methionine, phenylalanine, tryptophan, and others. The ...
Noodles, egg, cooked, unenriched, with added salt from the USDA Nutrition Facts on RecipeTips.Com
  • Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin. (wikipedia.org)
  • For phenylalanine plus tyrosine, for adults 19 years and older, 33 mg/kg body weight/day. (wikipedia.org)
  • L-Phenylalanine is biologically converted into L-tyrosine, another one of the DNA-encoded amino acids. (wikipedia.org)
  • Lignan is derived from phenylalanine and from tyrosine. (wikipedia.org)
  • The assay was validated for precision by replicate analysis of DBS samples containing known concentrations of phenylalanine and tyrosine. (skemman.is)
  • Inter-assay precision was determined by replicate analysis (n = 5) of DBS samples for phenylalanine and tyrosine across two concentrations over five consecutive days. (skemman.is)
  • A method comparison study was performed by analysis of phenylalanine and tyrosine in DBS samples (n = 30) and their corresponding plasma samples using blood from PKU patients collected for routine blood phenylalanine monitoring. (skemman.is)
  • Results: Intra-assay precision, expressed as coefficient of variation (%CV), was 9.8% and 9.6% for phenylalanine and tyrosine, respectively. (skemman.is)
  • Inter-assay precision, also expressed as %CV was 15.6% for phenylalanine, and 13.8% for tyrosine. (skemman.is)
  • Linear regression analysis demonstrated excellent correlation between DBS and plasma for both phenylalanine (r2 =0.964) and tyrosine (r2 =0.918), with slope values of 0.15 and 0.115, respectively. (skemman.is)
  • Bland-Altman analysis revealed a clear negative proportional bias for both amino acids, with a mean bias of -197.9 for phenylalanine and -58.1 for tyrosine across the range of concentrations tested. (skemman.is)
  • Conclusions: The DBS method performs with acceptable precision for both phenylalanine and tyrosine across the range of clinically-relevant concentrations. (skemman.is)
  • Measurement of phenylalanine and tyrosine in DBS samples holds promise for clinical monitoring of PKU patients on treatment. (skemman.is)
  • Bespoke Biotics Noorpower-F L-Phenylalanine 1000 mg Vegetable Capsules is one of our premium-quality amino acid range products, containing L- Phenylalanine, an essential amino acid which functions as the precursor to Tyrosine which is used the create hormones such as epinephrine, norepinephrine, DOPA and dopamine. (bespokebiotics.co.uk)
  • In keeping my promise, this week article is about Phenylalanine +Tyrosine. (senyia.com)
  • Phenylalanine +Tyrosine support healing your body by regulating mood swings, helping memory, decreasing muscle and joint pain, and decreasing pain from arthritis. (senyia.com)
  • The most well-established human function of tetrahydrobiopterin (BH4) is as the cofactor for phenylalanine-4-hydroxylase (PAH), tyrosine-3-hydroxylase, and tryptophan-5-hydroxylase. (medscape.com)
  • As an essential amino acid, phenylalanine is not synthesized de novo in humans and other animals, who must ingest phenylalanine or phenylalanine-containing proteins. (wikipedia.org)
  • Phenylketonuria (PKU) is the most common IEM and is characterized by an inability to metabolize the essential amino acid (AA) phenylalanine. (skemman.is)
  • Phenylalanine is an essential amino acid. (stillwater-medical.org)
  • Phenylalanine is what is termed as an essential amino acid, meaning that it does not occur naturally in the human body and must be provided inobtained from food. (paulaschoice.co.uk)
  • Pregnant women with PKU must control their blood phenylalanine levels even if the fetus is heterozygous for the defective gene because the fetus could be adversely affected due to hepatic immaturity. (wikipedia.org)
  • PKU patients require lifelong monitoring of blood phenylalanine levels, which is usually performed by chromatographic analysis of plasma from venous blood. (skemman.is)
  • Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula C 9H 11NO 2. (wikipedia.org)
  • The test detects abnormally high levels of an amino acid called phenylalanine. (medlineplus.gov)
  • This test is done to screen infants for PKU, an uncommon condition that occurs when the body lacks a substance needed to breakdown the amino acid phenylalanine. (medlineplus.gov)
  • Bluebonnet's L-Phenylalanine 500 mg Capsules contain the free-form amino acid L-phenylalanine in its crystalline form. (thehealthshoppe.co)
  • Phenylalanine supplementation may help alleviate PD symptoms by increasing dopamine levels. (bespokebiotics.co.uk)
  • The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase. (wikipedia.org)
  • Recessive mutations in the phenylalanine hydroxylase (PAH) gene predispose to phenylketonuria (PKU) in conjunction with dietary exposure to phenylalanine. (nih.gov)
  • Pulmonary response of the guinea pig animal model to n-formyl- methionyl-leucyl-phenylalanine (FMLP) liquid aerosol. (cdc.gov)
  • Pulmonary responses to n-formyl-methionyl-leucyl-phenylalanine (59880976) (FMLP) were studied in guinea-pigs. (cdc.gov)
  • Response of an animal model to mixtures of endotoxin and N-formyl-methionyl-leucyl-phenylalanine (FMLP) aerosols. (cdc.gov)
  • Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. (alzforum.org)
  • Lichtenthaler SF, Wang R, Grimm H, Uljon SN, Masters CL, Beyreuther K . Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein . (alzforum.org)
  • Lab results may report phenylalanine levels using either mg/dL and μmol/L. One mg/dL of phenylalanine is approximately equivalent to 60 μmol/L. A (rare) "variant form" of phenylketonuria called hyperphenylalaninemia is caused by the inability to synthesize a cofactor called tetrahydrobiopterin, which can be supplemented. (wikipedia.org)
  • Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). (medlineplus.gov)
  • High levels of phenylalanine are linked with the genetic issue phenylketonuria. (stillwater-medical.org)
  • Pregnant people with the condition who don't stay away from phenylalanine during pregnancy may give birth to a baby with signs of phenylketonuria. (stillwater-medical.org)
  • Phenylalanine supplementation may be helpful in managing ADHD symptoms through increased neurotransmitter levels. (bespokebiotics.co.uk)
  • Enhanced neurotransmitter production, as a result of phenylalanine supplementation, may improve energy levels and reduce fatigue. (bespokebiotics.co.uk)
  • Phenylalanine may play a role in muscle recovery and reducing muscle soreness after exercise by supporting protein synthesis and neurotransmitter production. (bespokebiotics.co.uk)
  • the metabolism of aspartame produces phenylalanine as one of the compound's metabolites. (wikipedia.org)
  • Abnormality in phenylalanine metabolism has been useful in diagnosing DRD for most (50% of patients), but not all, patients. (medscape.com)
  • Individuals with this disorder are known as "phenylketonurics" and must regulate their intake of phenylalanine. (wikipedia.org)
  • Phenylalanine may help regulate appetite and promote a feeling of fullness, aiding in weight management. (bespokebiotics.co.uk)
  • If PKU is not detected early, increasing phenylalanine levels in the baby will cause intellectual disability. (medlineplus.gov)
  • High levels of phenylalanine cause intellectual problems in babies with this issue. (stillwater-medical.org)
  • Pregnant women with hyperphenylalaninemia may show similar symptoms of the disorder (high levels of phenylalanine in blood), but these indicators will usually disappear at the end of gestation. (wikipedia.org)
  • A normal test result means that phenylalanine levels are normal and the child does not have PKU. (medlineplus.gov)
  • Further testing will be done if the phenylalanine levels in your baby's blood are too high. (medlineplus.gov)
  • Usage levels of phenylalanine in cosmetics typically range from 0.00009-0.3% in rinse-off and leave-on formulas. (paulaschoice.co.uk)
  • The screening ciency the Delfia® time-resolved fluores- tests themselves but includes all of the protocol utilized a combination of MS/ cence application (Wallac Oy) was used elements essential for every neonate MS, molecular technologies and bio- to determine levels of phenylalanine to have access to a screening system chemical analysis. (who.int)
  • Phenylalanine has been used to treat vitiligo by stimulating melanin production, improving skin pigmentation. (bespokebiotics.co.uk)
  • The genetic codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W. Nirenberg in 1961. (wikipedia.org)
  • This unnatural L-phenylalanine derivative, 4-Azido-L-phenylalanine, is used e.g. for genetic code expansion in protein biosynthesis as it can be incorporated into the proteins. (baseclick.eu)
  • medical citation needed] A non-food source of phenylalanine is the artificial sweetener aspartame. (wikipedia.org)
  • Phenylalanine is used in some artificial sweeteners. (stillwater-medical.org)
  • Brain protein synthesis was measured using in vivo labeling with [2H5] phenylalanine. (lu.se)
  • The first description of phenylalanine was made in 1879, when Schulze and Barbieri identified a compound with the empirical formula, C9H11NO2, in yellow lupine (Lupinus luteus) seedlings. (wikipedia.org)
  • Phenylalanine is the starting compound used in the synthesis of flavonoids. (wikipedia.org)
  • This compound is metabolized by the body into several chemical byproducts including phenylalanine. (wikipedia.org)
  • In addition to its benefit when consumed, research shows phenylalanine also has value when applied topically. (paulaschoice.co.uk)
  • In DRD, BH4 deficiency results in accumulation of phenylalanine. (medscape.com)
  • The test paper is taken to the laboratory, where it is mixed with a type of bacteria that needs phenylalanine to grow. (medlineplus.gov)
  • The phenylalanine deaminase test is important to differentiate proteus and providendia from other enterobacteria and enterocolitis. (medicallabtechnology.com)
  • What is the Phenylalanine deaminase test used for? (medicallabtechnology.com)
  • Phenylalanine is found naturally in the milk of mammals. (wikipedia.org)
  • Phenylalanine is found in the seeds and sprouts of plants such as spinach, sunflowers, peanuts, and many varieties of beans. (paulaschoice.co.uk)
  • Studies also indicate that phenylalanine can aid in the reduction ohelp to visibly reducef the appearance of an uneven skin tone. (paulaschoice.co.uk)
  • Some enterobacteria members can form phenyl pyruvic acid from phenylalanine by oxidative deamination . (medicallabtechnology.com)
  • When this phenylalanine reacts with acidified ammonium sulfate OR 10 % ferric chloride solution to form phenyl pyruvic acid .This phenyl pyruvic acid gives green color . (medicallabtechnology.com)
  • Another substance that blocks phenylalanine from reacting with anything else is added. (medlineplus.gov)
  • Phenylalanine has been shown to be well-tolerated by skin, with no reports of adverse reactions. (paulaschoice.co.uk)
  • Tetrahydrobiopterin deficiencies are disorders that affect phenylalanine (Phe) homeostasis, as well as brain biosynthesis of catecholamine, serotonin, and (occasionally) nitric oxide. (medscape.com)
  • Phenylketonurics often use blood tests to monitor the amount of phenylalanine in their blood. (wikipedia.org)
  • Further analyses, including additional variations and environmental influences such as phenylalanine exposure are warranted. (nih.gov)
  • In this study, the impact of the length of the alkyl chain and of the cationic head group on the environmental biodegradability of l-phenylalanine ester (PheCn) derived ILs using the pyridinium (PyPheCn), imidazolium (ImPheCn) and cholinium (CholPheCn) head groups was systematically studied. (leuphana.de)