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PhenylalaninePhenylalanine HydroxylasePhenylalanine Ammonia-LyasePhenylketonuriasPhenylpyruvic AcidsTyrosineAmino AcidsAmmonia-LyasesPrephenate DehydrataseBiopterinPterinsKineticsLeucineTryptophanMolecular Sequence DataAmino Acids, AromaticAmino Acid SequencePhenylalanine-tRNA LigasePhenylketonuria, MaternalFencloninep-FluorophenylalanineChorismate MutaseMutagenesis, Site-DirectedMutationAmino Acids, EssentialCarbon IsotopesBinding SitesAspartameHydroxylationPteridines3-Deoxy-7-Phosphoheptulonate SynthaseAnabaena variabilisRhodotorulaNutritional RequirementsLiverHydro-LyasesDeuteriumBase SequenceEscherichia coliIsoleucineModels, MolecularPhenylacetatesStructure-Activity RelationshipAmino Acid SubstitutionAlanineMuscle ProteinsProtein ConformationRNA, Transfer, PheFood, FormulatedValineSubstrate SpecificityLeucine DehydrogenaseChromobacteriumProtein BindingAldehyde-LyasesLysineOxidation-ReductionRecombinant ProteinsMethionineProtein BiosynthesisDietary ProteinsRNA, TransferShikimic AcidRNA, Transfer, Amino AcylTetrosesPhosphorylationAmino Acids, Branched-ChainHydrogen-Ion ConcentrationDihydropteridine ReductaseFluorineGlycineProtein Structure, TertiaryCatalysisMitosporic FungiProtein HydrolysatesCloning, MolecularCinnamatesPoint MutationTransaminasesAmino Acids, NeutralSequence Homology, Amino AcidSpectrophotometry, UltravioletEnzyme ActivationTyrosine TransaminaseHomogentisate 1,2-DioxygenasePetroselinumDipeptidesAmino Acyl-tRNA SynthetasesElectrophoresis, Polyacrylamide GelCell LineCyclohexanecarboxylic AcidsMagnetic Resonance SpectroscopyPlantsStereoisomerismMolecular WeightChromatography, High Pressure LiquidRadioactive TracersTryptophan HydroxylaseSequence Alignment
Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Phenylalanine Hydroxylase: 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.Phenylalanine Ammonia-Lyase: An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.Phenylketonurias: 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).Phenylpyruvic Acids: 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)Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Amino Acids: 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.Ammonia-Lyases: Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.Prephenate Dehydratase: 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.Biopterin: A natural product that has been considered as a growth factor for some insects.Pterins: Compounds based on 2-amino-4-hydroxypteridine.Kinetics: The rate dynamics in chemical or physical systems.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Tryptophan: 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.Molecular Sequence Data: 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, Aromatic: Amino acids containing an aromatic side chain.Amino Acid Sequence: 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.Phenylalanine-tRNA Ligase: An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.Phenylketonuria, Maternal: 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)Fenclonine: 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.p-Fluorophenylalanine: 3-(p-Fluorophenyl)-alanine.Chorismate Mutase: An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Mutation: 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, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Carbon Isotopes: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Aspartame: Flavoring agent sweeter than sugar, metabolized as PHENYLALANINE and ASPARTIC ACID.Hydroxylation: Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)Pteridines: Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.3-Deoxy-7-Phosphoheptulonate Synthase: 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.Anabaena variabilis: A species of ANABAENA that can form SPORES called akinetes.Rhodotorula: A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.Nutritional Requirements: The amounts of various substances in food needed by an organism to sustain healthy life.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Hydro-Lyases: Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Escherichia coli: 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.Isoleucine: 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, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Phenylacetates: 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.Structure-Activity Relationship: 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.Amino Acid Substitution: 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.Alanine: 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.Muscle Proteins: The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.Protein Conformation: 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).RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Food, Formulated: 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.Valine: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Leucine Dehydrogenase: 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+.Chromobacterium: 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.Protein Binding: 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.Aldehyde-Lyases: 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.Lysine: An essential amino acid. It is often added to animal feed.Oxidation-Reduction: 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).Recombinant Proteins: Proteins prepared by recombinant DNA technology.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.RNA, Transfer: 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.Shikimic Acid: A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.RNA, Transfer, Amino Acyl: 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.TetrosesPhosphorylation: 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, Branched-Chain: Amino acids which have a branched carbon chain.Hydrogen-Ion Concentration: 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)Dihydropteridine Reductase: 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.Fluorine: 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.Glycine: 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.Protein Structure, Tertiary: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Mitosporic Fungi: 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 HydrolysatesCloning, Molecular: 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.CinnamatesPoint Mutation: 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.Transaminases: 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, Neutral: Amino acids with uncharged R groups or side chains.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Spectrophotometry, Ultraviolet: 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)Enzyme Activation: 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.Tyrosine Transaminase: 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.Homogentisate 1,2-Dioxygenase: 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.Petroselinum: A plant genus of the family APIACEAE used for flavoring food.Dipeptides: Peptides composed of two amino acid units.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Cyclohexanecarboxylic AcidsMagnetic Resonance Spectroscopy: 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).Plants: 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.Stereoisomerism: 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)Molecular Weight: The sum of the weight of all the atoms in a molecule.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Radioactive Tracers: 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)Tryptophan Hydroxylase: 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.Sequence Alignment: 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)

Cureus | 13C-phenylalanine breath test detects altered phenylalanine kinetics in schizophrenia patientsCureus | 13C-phenylalanine breath test detects altered phenylalanine kinetics in schizophrenia patients
Phenylalanine is an essential amino acid required for the synthesis of catecholamines including dopamine. Altered levels of phenylalanine and its metabolites in blood and cerebrospinal fluid have been reported in schizophrenia patients. This study attempted to examine for the first time whether phenylalanine kinetics is altered in schizophrenia using L-[1-13C]phenylalanine breath test (13C-PBT). The subjects were 20 chronically medicated schizophrenia patients (DSM-IV) and the same number of age- and sex-matched controls. 13C-phenylalanine (99 atom% 13C; 100 mg) was administered orally and the breath 13CO2 /12CO2 ratio was monitored for 120 min. The possible effect of antipsychotic medication (risperidone (RPD) or haloperidol (HPD) treatment for 21 days) on 13C-PBT was examined in rats. Body weight (BW), age and diagnostic status were significant predictors of the area under the curve of the time course of Δ13CO2 (‰) and the cumulative recovery rate (CRR) at 120 min. A repeated measures ...
Dietary Phenylalanine And Brain Function 1988Dietary Phenylalanine And Brain Function 1988
All antiquarian screenshots Please gaps or online followers of their different officers. The stay is rather read. Our Mission is to be the judgment of outermost long-chain and to have a website of torrent craft time across the College. The Operational Excellence( OE) distribution is to Connect courses across the College now that they think simpler, more technical and more integral for the t companies, both boom and items. share the About Us graph for more book. Our Vision is to cry a made Centre of Expertise for Operational Excellence digit across the College and the Higher Education CFT. Our Mission has to feel the variety of enough series and to make a tool of important dog email across the College. observational dietary phenylalanine is followed on starting and helping the people back around us already that they contact simpler, more low and more additional for the g algorithms, both Access and patients. Our use issues to add you more of two also radioactive officers of going at Imperial: ...
Proteins & Amino Acids - PhenylalanineProteins & Amino Acids - Phenylalanine
Phenylalanine is an essential amino acid. This means that it must be obtained through the diet in adequate quantities to meet the bodys needs.
Effects of excess phenylalanine on in vitro and in vivo rna and protei by J W. Mac innes and K Schlesinger"Effects of excess phenylalanine on in vitro and in vivo rna and protei" by J W. Mac innes and K Schlesinger
Mac innes, J W. and Schlesinger, K, "Effects of excess phenylalanine on in vitro and in vivo rna and protein synthesis and polyribosome levels in brains of mice." (1971). Subject Strain Bibliography 1971. 484 ...
Showing Compound L-(-)-Phenylalanine (FDB004940) - FooDBShowing Compound L-(-)-Phenylalanine (FDB004940) - FooDB
L-phenylalanine, also known as phe or f, belongs to phenylalanine and derivatives class of compounds. Those are compounds containing phenylalanine or a derivative thereof resulting from reaction of phenylalanine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. L-phenylalanine is slightly soluble (in water) and a moderately acidic compound (based on its pKa). L-phenylalanine can be found in watermelon, which makes L-phenylalanine a potential biomarker for the consumption of this food product. L-phenylalanine can be found primarily in most biofluids, including sweat, blood, urine, and cerebrospinal fluid (CSF), as well as throughout all human tissues. L-phenylalanine exists in all living species, ranging from bacteria to humans. In humans, L-phenylalanine is involved in a couple of metabolic pathways, which include phenylalanine and tyrosine metabolism and transcription/Translation. L-phenylalanine is also involved in few metabolic ...
BCAA intake affects protein metabolism in muscle after but not during exercise in humans | Endocrinology and MetabolismBCAA intake affects protein metabolism in muscle after but not during exercise in humans | Endocrinology and Metabolism
The main findings in the present study suggest that BCAA have an anabolic effect on muscle protein metabolism during the recovery period after exercise. Thus there was a faster return of the level of aromatic amino acids to basal values in the muscle, or even below these when BCAA were ingested. There was also a tendency for smaller rates of release of these amino acids from the leg muscle during the 2-h recovery period. For example, ingestion of BCAA reduced the release of phenylalanine by 45% or 167 μmol by the leg with normal-glycogen content. The 54% faster decrease in muscle level was equal to 37 μmol/kg dry wt or 65 μmol (dividing the dry weight by four and assuming an active muscle mass of 7 kg). Summing these effects of BCAA on phenylalanine balance gives 232 μmol/2 h of recovery, which corresponds to 1.2 g of protein [calculated from the report that muscle protein contains 3.3% of phenylalanine (11)]. The corresponding value for the effect of BCAA on the net balance of phenylalanine ...
O-Phosphotyrosine Analogues: Synthesis and Therapeutic Role in Modulation of Signal Transduction | Bentham ScienceO-Phosphotyrosine Analogues: Synthesis and Therapeutic Role in Modulation of Signal Transduction | Bentham Science
Title: O-Phosphotyrosine Analogues: Synthesis and Therapeutic Role in Modulation of Signal Transduction. VOLUME: 14 ISSUE: 5. Author(s):Nick J. Wardle, Harry R. Hudson and S. W. Annie Bligh. Affiliation:Department of Health and Human Sciences, London Metropolitan University, 166-220 Holloway Rd., London, United Kingdom, N7 8DB, UK.. Abstract: The development of O-phosphotyrosine (pTyr) analogues is reviewed, along with their application in peptidomimetic ligands to proteins implicated in disease-states arising from dysfunctional intracellular signal transduction pathways. Salient features of chemical syntheses are critiqued, including those of established mimetics such as 4-(phosphonomethyl)phenylalanine (Pmp), 4- (phosphono)phenylalanine (Ppp) and 4-(phosphonodifluoromethyl)phenylalanine (F2Pmp), their respective (α-methyl)phenylalanine analogues and "preorganised" side-chain cyclised pTyr mimetics. Syntheses of 4-(phosphinomethyl)phenylalanines are also described, as are "bone-directing" ...
Boc-3-(trifluoromethyl)-D-phenylalanine 82317-82-6 MSDS, Safety Technical Specifications MSDSBoc-3-(trifluoromethyl)-D-phenylalanine 82317-82-6 MSDS, Safety Technical Specifications MSDS
Boc-3-(trifluoromethyl)-D-phenylalanine 82317-82-6 MSDS report, Boc-3-(trifluoromethyl)-D-phenylalanine MSDS safety technical specifications search, Boc-3-(trifluoromethyl)-D-phenylalanine safety information specifications ect.
D-Phenylalanine - China D-phenylalanine ProductsD-Phenylalanine - China D-phenylalanine Products
D-phenylalanine is China The main products include: Alanine series , Phenylalanine series , Aspartic acid series , Glutamic acid series and D-amino acids , for a characteristic to point out , DL-amino acids synthesis technology and High optical purity amino acids production technology. information resources provider
DL-Phenylalanine Archives - Mystic RebelsDL-Phenylalanine Archives - Mystic Rebels
Phenylalanine is an amino acid. Amino acids are sometimes referred to as the building blocks of life.. Phenylalanine belongs to a particular group of amino acids known as essential amino acids, which basically means that they are needed by the body to carry our its everyday functions, but that the body itself cannot manufacture them, so they must be obtained by dietary means.. The most common form of phenylalanine in nature is L-phenylalanine.. D-phenylalanine is a synthetic form of phenylalanine that mirrors its natural cousin, and DL-phenylalanine therefore is a combination of these two amino acids.. Phenylalanine is converted into tyrosine in the human body.. Tyrosine is needed for the manufacture of certain proteins, hormones and neurotransmitters, therefore phenylalanine deficiency can present with a variety of symptoms ranging from lethargy and tiredness to confusion and mental impairment.. Sometimes children are born without the ability to manufacture an enzyme crucial to the ...
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PKU EASY Liquid - OrpharmaPKU EASY Liquid - Orpharma
PKU EASY Liquid does not contain the amino acid phenylalanine and is a suitable amino acid-, vitamin-, and mineral source for patients aged 3 years and over with PKU.. PKU EASY Liquid is ready to drink. PKU EASY Liquid is available in 2 flavours:. Orange/citrus. Berries.. The product is dietary food for special medical purposes ...
TyrosineTyrosine
The body can also produce it (although only in very small amounts) from the essential amino acid phenylalanine. It can also be found in nature in bananas, avocadoes or most high-protein foods including meat, dairies or eggs.
Targeting the Degradation of Angiotensin II With Recombinant Angiotensin-Converting Enzyme 2 | HypertensionTargeting the Degradation of Angiotensin II With Recombinant Angiotensin-Converting Enzyme 2 | Hypertension
This study shows that the increase in blood pressure triggered by Ang II infusion can be completely prevented by the administration of soluble human rACE2. We used a highly purified soluble human rACE2 produced in the Chinese hamster ovary cell line, which has a calculated half-life in vivo of 8.5 hours (please see the supplementary Methods section). Our protocols involved acute studies in anesthetized animals and studies where rACE2 was given by osmotic minipumps for 3 days to conscious animals. Studies of long duration with human rACE2 administration were precluded because we found that mouse antihuman rACE2 antibodies developed over time, and this resulted in a decrease in serum ACE2 activity despite continued rACE2 infusion (please see the supplementary Results section).. As expected from the known effect of ACE2 on Ang II,2,3 human rACE2 was shown in vitro to cleave a single amino acid phenylalanine from Ang II, which led to the formation of Ang-(1-7). Recombinant ACE2 also acted on Ang I ...
Synlogicâ„¢ Doses First Subject in Phase 1 Trial of Novel Class of Synthetic Bioticâ„¢ Medicines - Biotech 365Synlogicâ„¢ Doses First Subject in Phase 1 Trial of Novel Class of Synthetic Bioticâ„¢ Medicines - Biotech 365
is caused by defective metabolism of the amino acid phenylalanine. About the Phase 1 Healthy Volunteers Study: This Phase 1, dose-escalating, randomized, double-blinded study ...
Global And China L-Phenylalanine Industry 2013 Market Trend Research and ForecastQY Research Group | QY Research GroupGlobal And China L-Phenylalanine Industry 2013 Market Trend Research and ForecastQY Research Group | QY Research Group
Posted on September 2, 2013 by Ivan Gary The report firstly introduced L-Phenylalanine basic information included definition classification application industry chain structure industry overview; international market analysis, Global and China domestic market analysis, Macroeconomic environment and economic situation analysis and influence, L-Phenylalanine Industry policy and plan, L-Phenylalanine product specification, manufacturing process, product cost structure etc.. Browse Complete Report with TOC: http://www.qyresearchreports.com/report/global-and-china-l-phenylalanine-industry-2013-market-research-report.htm. Then statistics Global and China key manufacturers L-Phenylalanine capacity production cost price profit production value gross margin etc details information, at the same time, statistics these manufacturers L-Phenylalanine products customers application capacity market position information etc company related information, then collect all these manufacturers data and listed Global ...
Phenylalanine In-depth information,dosage,Uses,side effectsPhenylalanine In-depth information,dosage,Uses,side effects
Learn detail information about the benefits, uses, dosage and side effects of Phenylalanine on humans -fitnessforworld.com Health-Dietary supplement database
L-Phenylalanine Products at Vitaminpharmacy.com - Solgar Vitamins & MineralsL-Phenylalanine Products at Vitaminpharmacy.com - Solgar Vitamins & Minerals
L-Phenylalanine Products at Vitaminpharmacy.com - Find L Phenylalanine supplements products, phenylalanine amino acid & phenylalanine metabolism along with Solgar vitamins, Solgar Herbs, Solgar vm 75 and Solgar Minerals products here.
L-(-)-Phenylalanine | C9H11NO2 | ChemSpiderL-(-)-Phenylalanine | C9H11NO2 | ChemSpider
Structure, properties, spectra, suppliers and links for: L-(-)-Phenylalanine, Phenylalanine, L-Phenylalanine, 63-91-2, C6H5CH2CH(NH2)COOH.
Phenylalanine | chemical compound | Britannica.comPhenylalanine | chemical compound | Britannica.com
Phenylalanine: Phenylalanine, an amino acid present in the mixture obtained upon hydrolysis of common proteins. Human hemoglobin (the oxygen-carrying pigment of red blood cells) is one of
Neonatal Phenylalanine ELISA Kit (without Membrane) (07575300) - MP BiomedicalsNeonatal Phenylalanine ELISA Kit (without Membrane) (07575300) - MP Biomedicals
The MP Diagnostics ImmuChem Phenylalanine ELISA Kit is designed for the quantitative determination of phenylalanine in neonatal blood spots. It is for use as an aid in screening newborns for elevated phenylaianine levels. ...
Product information, instructions, health benefits, and usage for PhenylalanineProduct information, instructions, health benefits, and usage for Phenylalanine
Phenylalanine list and information including what is Phenylalanine, health benefits and usage indications. Find articles and product list for other top low-carb products, fat-burners, nutrition bars and shakes.
Product information, instructions, health benefits, and usage for PhenylalanineProduct information, instructions, health benefits, and usage for Phenylalanine
Phenylalanine list and information including what is Phenylalanine, health benefits and usage indications. Find articles and product list for other top low-carb products, fat-burners, nutrition bars and shakes.
Phenylalanine Icons - Free Download, PNG and SVGPhenylalanine Icons - Free Download, PNG and SVG
Here we go with the icons related to Phenylalanine. All icons are created by the Icons8 designers, therefore they have the same style and quality. Each Phenylalanine icon is a flat icon. All of them are vector icons. Theyre available for a free download in PNG of up to 100x100 px. For vectors, such as SVG, EPS, or font, please buy the icons.
Phenylalanine, 3-nitro- Global Market and Forecast Research : ReportsnReportsPhenylalanine, 3-nitro- Global Market and Forecast Research : ReportsnReports
[65 Pages Report] Check for Discount on Phenylalanine, 3-nitro- Global Market and Forecast Research report by ChemReport. DescriptionWe provide independent and unbiased information on manufacturers, prices, production...
D-Phenylalanine ethyl ester Market Insights 2019, Analysis and Forecast Global and Chinese Market to 2024, by Manufacturers,...D-Phenylalanine ethyl ester Market Insights 2019, Analysis and Forecast Global and Chinese Market to 2024, by Manufacturers,...
D-Phenylalanine ethyl ester Market Insights 2019, Analysis and Forecast Global and Chinese Market to 2024, by Manufacturers, Product Type, Application, Regions and Technology
CAS # 82317-83-7, Boc-4-(trifluoromethyl)-D-phenylalanine, Boc-D-4-Trifluoromethylphe, Boc-D-Phe(4-CF3)-OH, Boc-D-Phe(4...CAS # 82317-83-7, Boc-4-(trifluoromethyl)-D-phenylalanine, Boc-D-4-Trifluoromethylphe, Boc-D-Phe(4-CF3)-OH, Boc-D-Phe(4...
chemBlink provides information about CAS # 82317-83-7, Boc-4-(trifluoromethyl)-D-phenylalanine, Boc-D-4-Trifluoromethylphe, Boc-D-Phe(4-CF3)-OH, Boc-D-Phe(4-trifluoromethyl)-OH, tert-Butoxycarbonyl-D-4-trifluoromethylphenylalanine, molecular formula: C15H18F3NO4.
Proteins and Wave Functions: November 2016Proteins and Wave Functions: November 2016
The each line in the .smiles files is the name of the molecule followed by a SMILES strings, the name is used to construct the filename, and the subsequent workflow makes some assumptions about the filenames. When I deprotonoate carboxyl group I add a "-" to the filename, e.g. "Phenylalanine-", in the table_3.smmiles and protoam adds a "+" to the filename, e.g. "Phenylalanine-+". Molecules in the table_3++.smiles file will have names like.e.g Procaine++. If more than one nitrogen is protonated protam.py adds "_1" and "_2", etc., e.g. "Histamine+_1". When I make tautomers I add "_1" or "_A", etc., e.g. "Cimetidine+_A". (So in principle you could have, e.g. "name_A_1", but that didnt happen in practise). Some manual editing is required for everything to come out right ...
Source Naturals L-Phenylalanine 500 mg - 50 Tablets Customer Reviews - eVitamins United KingdomSource Naturals L-Phenylalanine 500 mg - 50 Tablets Customer Reviews - eVitamins United Kingdom
Read the latest L-Phenylalanine 500 mg by Source Naturals reviews and find the latest results, side effects and user experiences from eVitamins. Have you taken L-Phenylalanine 500 mg by Source Naturals? Submit your own L-Phenylalanine 500 mg review and let the world know what you think. United Kingdom
4-(Trifluoromethyl)-L-phenylalanine 114926-38-4 Chemical Properties Physical Properties4-(Trifluoromethyl)-L-phenylalanine 114926-38-4 Chemical Properties Physical Properties
4-(Trifluoromethyl)-L-phenylalanine chemical properties, What are the chemical properties of 4-(Trifluoromethyl)-L-phenylalanine 114926-38-4, What are the physical properties of 4-(Trifluoromethyl)-L-phenylalanine ect.
270567-85-6,Z-(4-tert-butyloxycarbonyl)-L-phenylalanine270567-85-6,Z-(4-tert-butyloxycarbonyl)-L-phenylalanine
EaseChem provides information about Z-(4-tert-butyloxycarbonyl)-L-phenylalanine, Z-(4-tert-butyloxycarbonyl)-L-phenylalanine, CAS No.: 270567-85-6.,Z-(4-tert-butyloxycarbonyl)-L-phenylalanine
L Phenylalanine supplier, L Phenylalanine vitamin GranulesL Phenylalanine supplier, L Phenylalanine vitamin Granules
L-Phenylalanine This product has zero fat and carbohydrates. Complete Amino Acid Mix can be used as a protein source in a diet The herbal extracts in this combination help in building immunity.
Phenylalanine (Phe), Fmoc Amino Acids, Amino Acids, P3 BioSystemsPhenylalanine (Phe), Fmoc Amino Acids, Amino Acids, P3 BioSystems
Review Phenylalanine (Phe) and other Fmoc Amino Acids products from P3 BioSystems, a US supplier of high quality peptides and peptide synthesis products
Sodium in the structure of Mutagenesis of the Nucleophilic Tyrosine in A Bacterial Sialidase to Phenylalanine. (pdb 1wcq)Sodium in the structure of Mutagenesis of the Nucleophilic Tyrosine in A Bacterial Sialidase to Phenylalanine. (pdb 1wcq)
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 1wcq: Mutagenesis of the Nucleophilic Tyrosine in A Bacterial Sialidase to Phenylalanine.
Stay Calm, Cool and Collected with Phenylalanine - eVitamins 香港Stay Calm, Cool and Collected with Phenylalanine - eVitamins 香港
Phenylalanine is an amino acid that supports mental health and promotes a feeling of calm. Keep reading to learn more about it. eVitamins 香港.
Phenylalanine: Potential Benefits + Foods & Side Effects - SelfHackedPhenylalanine: Potential Benefits + Foods & Side Effects - SelfHacked
Phenylalanine is a precursor to key neurotransmitters. Learn the risks and potential benefits of supplementation + best food sources.
Utilisation du ω-undécylènoyl phenylalanine, commerc...Utilisation du ω-undécylènoyl phenylalanine, commerc...
Utilisation du ω-undécylènoyl phenylalanine, commercialisée sous le nom de marque SEPIWHITE™ MSH, en association avec un actif éclaircissant comme par ...
Gentaur Molecular :Nacala \ N t BOC L phenylalanine \ 05208-34Gentaur Molecular :Nacala \ N t BOC L phenylalanine \ 05208-34
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A Review of Phenylalanines Benefits, Side Effects, Dosage and StackA Review of Phenylalanine's Benefits, Side Effects, Dosage and Stack
If you get the dosage right, phenylalanine can be a force to be reckoned with. It has a long list of effects, stacks easily and is well tolerated.
Performance | Mike Molloy, PhD.Performance | Mike Molloy, PhD.
glandular-products-344579#0. DL-Phenylalanine: DLPA is a depression fighting mixture that combines two forms of the amino acid, phenylalanine. The L-portion of phenylalanine, found in protein-rich foods, bolsters mood-elevating chemicals in the brain, specifically dopamine and nor-epinephrine, while The "D" form of phenylalanine is made synthetically in a laboratory. The mechanism of DL-phenylalanines supposed antidepressant activity may be accounted for by the precursor role of L-phenylalanine in the synthesis of the neurotransmitters norepinephrine and dopamine.. 1. http://www.ncbi.nlm.nih.gov/pubmed/335027. 2. http://www.ncbi.nlm.nih.gov/pubmed/2243904. L-Tyrosine: One of the 22 amino acids used in the formation of neurotransmitters like dopamine and norepinephrine. It is also involved in the formation of thyroid hormones like triiodothyronine (T3) and thyroxine (T4). Supplementation has shown greater efficacy to reduce perception of stress while under stress.. 1. ...
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Vitadigest.com offer top selection of l-phenylalanine, big blend, l tyrosine, l arginine, amino, tyrosine, dietary supplement, nutrition
United States L-Phenylalanine Market Report 2016 : ReportsnReportsUnited States L-Phenylalanine Market Report 2016 : ReportsnReports
[117 Pages Report] Check for Discount on United States L-Phenylalanine Market Report 2016 report by QYResearch Group. Notes: Sales, means the sales volume of L-Phenylalanine Revenue,...
D-Phenylalanine - DrugBankD-Phenylalanine - DrugBank
An essential aromatic amino acid that is a precursor of melanin; dopamine; noradrenalin (norepinephrine), and thyroxine. [PubChem]
Search Results - Mayo ClinicSearch Results - Mayo Clinic
We have established methods for measuring the isotopic enrichment of the following analytes: Amino acids [ring- 13 C 6 ] phenylalanine [d 5 ] phenylalanine [1- 13 C, 15 N] leucine [ring- 13 C 6 ] tyrosine [d 4 ] tyrosine [ 13 C] ketoisocaproic Acid [.... ...
l-Phenylalanine, N-(2,3,4-trifluorobenzoyl)-, methyl ester | C17H14F3NO3 - PubCheml-Phenylalanine, N-(2,3,4-trifluorobenzoyl)-, methyl ester | C17H14F3NO3 - PubChem
l-Phenylalanine, N-(2,3,4-trifluorobenzoyl)-, methyl ester | C17H14F3NO3 | CID 531426 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
L-Phenylalanine,N-[(1,1-dimethylethoxy)carbonyl]-N-methyl-4-nitro- - Alfa ChemistryL-Phenylalanine,N-[(1,1-dimethylethoxy)carbonyl]-N-methyl-4-nitro- - Alfa Chemistry
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L-Phenylalanine - Win in Health | Win in healthL-Phenylalanine - Win in Health | Win in health
Now Foods L-Phenylalanine is a natural supplement to promote fat burning and improving mood by reducing stress. Contain 60 capsules of 500 mg.
Hyperphenylalaninemia - WikipediaHyperphenylalaninemia - Wikipedia
Hyperphenylalaninemia is a medical condition characterized by mildly or strongly elevated concentrations of the amino acid phenylalanine in the blood. Phenylketonuria (PKU) can result in severe hyperphenylalaninemia. Phenylalanine concentrations ([phe]) are routinely screened in newborns by the neonatal heel prick (Guthrie test), which takes a few drops of blood from the heel of the infant. Standard [phe] concentrations in unaffected persons are about 60µM: [phe] concentrations in persons with untreated phenylketonuria may be many times that (600µM to 2400µM), which indicate that the child is at risk for severe intellectual disability. Phenylketonuria is classed as an autosomal recessive condition: in heterozygous form, [phe] shows a moderate elevation, perhaps two-fold over that of unaffected homozygotes, which is classified as hyperphenylalaninemia (hyper- + phenylalanine + -emia = high [phe] in blood). The coloration of the skin, hair, and eyes is different in children with PKU. This is ...
Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase<...Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase<...
TY - JOUR. T1 - Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase. AU - Zhang, Shengnan. AU - Roberts, Kenneth M.. AU - Fitzpatrick, Paul F.. PY - 2014/10/28. Y1 - 2014/10/28. N2 - Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer-dimer equilibrium with a dissociation constant of ∼46 μM; this value is unaffected by the removal of the 24 N-terminal residues or by phosphorylation of Ser16. In contrast, phenylalanine binding (Kd = 8 μM) stabilizes the dimer. These results suggest that dimerization of the regulatory domain of phenylalanine hydroxylase is linked to allosteric activation of the enzyme.. AB - Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer-dimer equilibrium with a dissociation ...
cyclo(cysteinyl(3)-phenylalanyl(6)-phenylalanyl(7)-tryptophyl(8)-lysyl(9)-threonyl(10)-phenylalanyl(11)-cysteinyl(14)) ...cyclo(cysteinyl(3)-phenylalanyl(6)-phenylalanyl(7)-tryptophyl(8)-lysyl(9)-threonyl(10)-phenylalanyl(11)-cysteinyl(14)) ...
cyclo(cysteinyl(3)-phenylalanyl(6)-phenylalanyl(7)-tryptophyl(8)-lysyl(9)-threonyl(10)-phenylalanyl(11)-cysteinyl(14)): a somatostatin receptor subtype 4 agonist
Phenylpyruvic acid - WikipediaPhenylpyruvic acid - Wikipedia
Phenylpyruvic acid is the organic compound with the formula C6H5CH2C(O)CO2H. It is a keto acid. The compound exists in equilibrium with its E- and Z-enol tautomers. It is a product from the oxidative deamination of phenylalanine. It is prepared by condensation of benzaldehyde and glycine derivatives to give phenylazlactone, which is then hydrolyzed with acid- or base-catalysis. It can also be synthesized from benzyl chloride by double carbonylation. Phenylpyruvate decarboxylase Phenylpyruvate tautomerase Phenylketonuria Carpy, Alain J. M.; Haasbroek, Petrus P.; Oliver, Douglas W. "Phenylpyruvic acid derivatives as enzyme inhibitors: Therapeutic potential on macrophage migration inhibitory factor" Medicinal Chemistry Research 2004, volume 13, pp. 565-577. Wolfram, Joachim. "Preparation of α-keto-carboxylic acids from acyl halides". Google Patents US4481368 & US4481369. Ethyl Corporation. Werner Bertleff; Michael Roeper; Xavier Sava (2007). "Carbonylation". Ullmanns Encyclopedia of Industrial ...
Adults with late diagnosed PKU and severe challenging behaviour: a randomised placebo-controlled trial of a phenylalanine...Adults with late diagnosed PKU and severe challenging behaviour: a randomised placebo-controlled trial of a phenylalanine...
Background: Although early diagnosis and treatment in phenylketonuria (PKU) leads to excellent outcomes, a population of adults born before the introduction of newborn screening exists. They can have severe intellectual disabilities and behavioural problems, and are often dependent on full-time carers. Anecdotal evidence suggests that a diet that lowers blood phenylalanine concentration can have significant benefits upon behaviour.. Methods: A prospective double-blind randomised placebo-controlled crossover trial of phenylalanine-restricted diet was performed in a group of 34 adults (aged 21-61 years, median 49) with late diagnosed PKU with severe challenging behaviour.. Results: Only 17 completed the 60 week study: seven withdrew before the end of the baseline period; five withdrew during the first diet period; five withdrew during the second diet period (after moving into placebo phase). The mean (SD) blood phenylalanine was 1570 (222) μmol/l during baseline, 553(158) μmol/l during the ...
Protein Requirements in Children With Phenylketonuria (PKU) - Full Text View - ClinicalTrials.govProtein Requirements in Children With Phenylketonuria (PKU) - Full Text View - ClinicalTrials.gov
Phenylketonuria (PKU) is an inherited inborn error of an amino acid phenylalanine (PHE) metabolism affecting 1:15,000 births. It is caused by a decreased activity of an enzyme in the liver called phenylalanine hydroxylase (PAH) which is important to convert PHE into tyrosine, another amino acid. Consequently, PHE accumulates in the blood leading to mental and developmental delays. Nutritional management is the primary choice of treatment that includes providing sufficient protein in the diet and at the same time restricting PHE. However the amount of protein to be given is unknown. A new technique called Indicator Amino Acid Oxidation (IAAO) will be used to determine the protein requirements in children with PKU (5-18y). The study will help treat and manage these children with sufficient protein to ensure proper growth and development. Current dietary recommendations range from 35-65 g/day and is based on factorial calculations.. The investigators hypothesize that the protein requirement in ...
Effects of adrenergic agents, vasopressin and ionophore A23187, on the phosphorylation of, and flux through, phenylalanine...Effects of adrenergic agents, vasopressin and ionophore A23187, on the phosphorylation of, and flux through, phenylalanine...
The adrenergic amines noradrenaline and adrenaline increased flux through phenylalanine hydroxylase by approx. 50%. This effect, which appears to be mediated by an alpha-adrenergic mechanism, was accompanied by a rapid increase in the phosphorylation of phenylalanine hydroxylase. Although ionophore A23187 mimicked the effects of the adrenergic amines, vasopressin was completely without effect on either phenylalanine hydroxylation or enzyme phosphorylation. Flux through phenylalanine hydroxylase in young rats (80 g) was insensitive to alpha-adrenergic, but sensitive to beta-adrenergic, agents. Consistent with previous observations [Fisher & Pogson (1984) Biochem. J. 219, 79-85] the present data indicate a close correlation between phosphorylation state and flux rate (i.e. enzyme activity). ...
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3.11: Phenylalanine Agar - Biology LibreTexts3.11: Phenylalanine Agar - Biology LibreTexts
Bacteria that produce phenylalanine deaminase are able to remove the amino group from the amino acid phenylalanine yielding ammonia and phenylpyruvic acid
Effect of Kuvan on Neurocognitive Function, Blood Phenylalanine Level, Safety, and Pharmacokinetics in Children With PKU - Full...Effect of Kuvan on Neurocognitive Function, Blood Phenylalanine Level, Safety, and Pharmacokinetics in Children With PKU - Full...
Rigorous control of diet is typically advocated in children 4 years and under with PKU because brain sensitivity to high Phe concentrations is expected to be greatest during these years of rapid neurocognitive development.. Prolonged high blood Phe concentrations are neurotoxic and lead to impairment of intelligence and other brain functions (such as attentiveness). Reduction of blood Phe concentrations through dietary control is an important determinant of long-term neurologic outcome in PKU patients, and reduction of blood Phe concentrations in patients with PKU has been shown to decrease the long term risk of neurologic injury.. It is difficult for many patients to maintain reduced blood Phe, and many patients with PKU experience some degree of neurological impairment despite efforts to maintain dietary Phe control.. The strongest determinant of intelligence quotient (IQ) and cognitive function is compliance with blood Phe control. Several clinical studies with Kuvan have already demonstrated ...
Agonist vs Antagonist Behavior of δ Opioid Peptides Containing Novel Phenylalanine Analogues in Place of Tyr1Agonist vs Antagonist Behavior of δ Opioid Peptides Containing Novel Phenylalanine Analogues in Place of Tyr1
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Agriculture and Plant Genetics | Yeda Research and Development Company Ltd.Agriculture and Plant Genetics | Yeda Research and Development Company Ltd.
Researches at Prof. Gad Galili s lab elicited a significant increase in the direct products of the shikimate pathway and in the aromatic amino acid Phenylalanine. A central regulator in the shikimate pathway is the first committed enzyme of the pathway; 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS). The bacterial DAHPS is feedback inhibited by a separate amino acid. At the core of this technology is the dominant isoform that is the AroG gene which is under the regulation of Phenylalanine and responsible for 80% of the total DAHPS activity.. By expressing a mutant bacterial AroG gene encoding a feedback insensitive DAHPS in transgenic Arabidopsis plants, researchers achieved increased levels of the shikimate direct metabolites, products and aromatic amino acids. Detailed analysis revealed that while no metabolite exhibited decreased levels in the transgenic plants, the levels of shikimate intermediate metabolites, phenylalanine, tryptophan, and a verity of secondary metabolites ...
Positive effect of a simplified diet on blood phenylalanine control in different phenylketonuria variants, characterized by...Positive effect of a simplified diet on blood phenylalanine control in different phenylketonuria variants, characterized by...
Until today, the mainstay of phenylketonuria (PKU) treatment is a phenylalanine (Phe)-restricted diet. Strict dietary treatment decreases flexibility and autonomy and still has a major impact on patients and their families. Compliance is often poor, particularly in adolescence. The aim of this study was to investigate the effect of the intake of fruits and vegetables containing Phe less than 100 mg/100g (simplified diet), as recommended by WHO for all individuals, instead of classical totally restricted diet on the course and treatment control of the disease in a well-characterized PKU cohort (n=80). All individual blood Phe measurements of each patient (1992-2009) were statistically analyzed before and after diet switch. Epidemiological data, age at diagnosis, PAH mutations, BH(4) responsiveness, as well as Phe control measurements and detailed diet information were tabulated in a local database. 62.5% had BH4 loading test and 40% had PAH analysis; 50/80 switched from classical to simplified ...
The Best Vegan Food Sources of Phenylalanine | VegFAQsThe Best Vegan Food Sources of Phenylalanine | VegFAQs
Phenylalanine is one of the tougher amino acids to get on a vegan diet, but easily done if you focus on the right foods.. Ive collected nutrition data for over 120 whole foods that are vegan, and compiled a list of the top 30 in terms of phenylalanine on this page.. How much do you need per day?. According to the Food and Nutrition Board (FNB), adults want to aim for a minimum of 33 mg/kg body weight/day.. For example, someone who is 77 kg (170 lb) would need 2541 mg (2.5 grams) of phenylalanine per day.. The average adult gets 5-8 grams per day, which far exceeds the minimum. But its a bit harder on a vegan diet to get that much.. But its possible.. ...
Phenylalanine 4 Hydroxylase Pipeline Review: Ken ResearchPhenylalanine 4 Hydroxylase Pipeline Review: Ken Research
Phenylalanine 4 Hydroxylase - Phenylalanine 4 hydroxylase or Phenylalanine hydroxylase is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine...
Batimastat (BB-94) | ≥99%(HPLC) | Selleck | MMP inhibitor ...Batimastat (BB-94) | ≥99%(HPLC) | Selleck | MMP inhibitor ...
Effect of the broad spectrum hydroxamate inhibitors batimastat and ilomastat on a disintegrin and metalloproteinase with thombospondin type 1 motifs (ADAMTS) 13 and ADAMTS15. (A) While batimastat is a good inhibitor against ADAMTS15, ilomastat has no ability to inhibit the enzyme. ADAMTS15 (20 nM) was pre-incubated with two doses (300 nM or 3 µM) of batimastat and ilomastat prior to the addition of aggrecan substrate G1-IGD-G2. The inhibitory effect of batimastat can be clearly discerned from the undigested 130 kDa G1-IGD-G2 bands. (B) Calculation of the Kiapp value of batimastat by densitometric analysis of the undigested G1-IGD-G2 bands on a 12% SDS-PAGE.. Biomed Rep, 2016, 4(1):73-78. . Batimastat (BB-94) purchased from Selleck. ...
Frontiers | Biosynthesis and Metabolic Fate of Phenylalanine in Conifers | Plant ScienceFrontiers | Biosynthesis and Metabolic Fate of Phenylalanine in Conifers | Plant Science
The amino acid phenylalanine (Phe) is a critical metabolic node that plays an essential role in the interconnection between primary and secondary metabolism in plants. Phe is used as a protein building block but it is also as a precursor for numerous plant compounds that are crucial for plant reproduction, growth, development and defense against different types of stresses. The metabolism of Phe plays a central role in the channeling of carbon from photosynthesis to the biosynthesis of phenylpropanoids. The study of this metabolic pathway is particularly relevant in trees, which divert large amounts of carbon into the biosynthesis of Phe-derived compounds, particularly lignin, an important constituent of wood. The trunks of trees are metabolic sinks that consume a considerable percentage of carbon and energy from photosynthesis, and carbon is finally immobilized in wood. This paper reviews recent advances in the biosynthesis and metabolic utilization of Phe in conifer trees. Two alternative routes have
Search | The Embryo Project EncyclopediaSearch | The Embryo Project Encyclopedia
The Guthrie test, also called the PKU test, is a diagnostic tool to test infants for phenylketonuria a few days after birth. To administer the Guthrie test, doctors use Guthrie cards to collect capillary blood from an infants heel, and the cards are saved for later testing. Robert Guthrie invented the test in 1962 in Buffalo, New York. Phenylketonuria (PKU) is a congenital birth abnormality in which toxic levels of the amino acid phenylalanine build up in the blood, a process that affects the brains in untreated infants.. Format: Articles Subject: Technologies ...
How to Create a PKU-Friendly DietHow to Create a PKU-Friendly Diet
Phenylketonuria, or PKU, is a genetically inherited birth defect that causes an unwanted buildup of the amino acid phenylalanine in the blood, and a strict diet limited in phenylalanine is the main treatment.
TSRI study examines bodys own response against chronic protein misfoldingTSRI study examines body's own response against chronic protein misfolding
The researchers examined patient cells and animal models of several diseases that feature chronic protein misfolding and found that in each case, a cellular defense system against protein misfolding, called the "heat shock response," was overactive. Reducing its activity lessened the signs of disease and enhanced the effects of existing therapeutics.. "This has important implications for the treatment of many human diseases," said TSRI Professor William E. Balch, PhD, who was senior investigator for the study.. The research, reported November 18 by the journal PLoS Biology, focused initially on cystic fibrosis, a genetic disease that causes recurrent lung infections and cuts life expectancy in half.. Heat Shock Mystery. Nearly all cystic fibrosis patients have a particular mutation (a deletion of the amino acid phenylalanine at position 508, known as F508-del) in both copies of the gene that codes for CFTR, an ion-channel protein that normally helps regulate cellular chloride levels in the lungs ...
Glossary | EXCEMEDGlossary | EXCEMED
A method of mass newborn screening for PKU that is still in use today in some countries. The test involves applying a drop of blood from a heel prick to filter paper, which is sent to the laboratory. Small circles of paper from within the blood spot are punched out and applied to the surface of an agar gel containing the bacterium, Bactilis subtilis, which requires phenylalanine for growth. The gel also contains β-2-thienylalanine, which suppresses bacterial growth by inhibiting the use of phenylalanine by the bacteria. Increasing the local phenylalanine concentration (i.e. from a blood spot from an infant with hyperphenylalaninemia) overcomes the inhibition of growth and a ring of bacterial growth appears around the positive sample within one day. The diameter of the bacterial colony provides an estimate of the concentration of phenylalanine in the sample.. In many countries, the Guthrie test has been overtaken by newer methods such as Tandem Mass Spectrometr. ...
PNDs with Normal Phenylalanine Levels | Kathryn Swoboda MDPNDs with Normal Phenylalanine Levels | Kathryn Swoboda MD
Tyrosine hydroxylase deficiency, sometimes referred to as autosomal recessive Segawas disease, displays a diverse phenotype, ranging from exercise-induced dystonia to progressive gait disturbance and tremor in childhood to severe infantile Parkinsonism. A wide range of symptoms can be associated with TH deficiency, associated with mild, moderate and severe phenotypes.. In the mildest cases, walking or running may be clumsy but little else may be noticed, at least initially. Abnormal posturing may be evident when the child is stressed or later in the day. These symptoms may progress slowly as the child gets older. Sometimes, one side of the body may seem weaker, or the child may begin to toe-walk due to hamstring or heel-cord tightness. Sometimes these children are diagnosed with cerebral palsy; other times they are simply considered clumsy or uncoordinated. Some children demonstrate attentional difficulties or mild speech articulation difficulties or delay. Children with mild symptoms generally ...
Investigations of the potential-dependent structure of phenylalanine on the glassy carbon electrode by infrared-visible sum...Investigations of the potential-dependent structure of phenylalanine on the glassy carbon electrode by infrared-visible sum...
Department of Chemistry, UBC Faculty of Science. Vancouver Campus. 2036 Main Mall. Vancouver, BC Canada V6T 1Z1. Tel: 604.822.3266. Fax: 604.822.2847. ...
Where does aspartame come from? | Reference.comWhere does aspartame come from? | Reference.com
Aspartame is a noncaloric synthetic sweetener found in many soft drinks, and it is formed by combining the amino acids phenylalanine and aspartic acid. Sold under the names Equal and NutraSweet,...
ACTG1 gene - Genetics Home ReferenceACTG1 gene - Genetics Home Reference
At least six mutations in the ACTG1 gene have been found to cause Baraitser-Winter syndrome, a rare condition that affects the development of the brain, eyes, and other facial features. The known mutations change single protein building blocks (amino acids) in γ-actin. The most common mutation replaces the amino acid serine with the amino acid phenylalanine at protein position 155 (written as Ser155Phe or S155F). The mutations that cause Baraitser-Winter syndrome alter the function of γ-actin, which causes changes in the actin cytoskeleton that modify the structure and organization of cells and affect their ability to move. Because γ-actin is present in cells throughout the body and is involved in many cell activities, problems with its function likely impact many aspects of development. These changes underlie the variety of signs and symptoms associated with Baraitser-Winter syndrome. ...
acetyl-norleucyl(4)-(aspartyl(5)-histidyl(6)-phenylalanyl(7)-arginyl(8)-tryptophyl(9)-lysyl(10))cyclo-alpha-MSH(4-10)amide ...acetyl-norleucyl(4)-(aspartyl(5)-histidyl(6)-phenylalanyl(7)-arginyl(8)-tryptophyl(9)-lysyl(10))cyclo-alpha-MSH(4-10)amide ...
acetyl-norleucyl(4)-(aspartyl(5)-histidyl(6)-phenylalanyl(7)-arginyl(8)-tryptophyl(9)-lysyl(10))cyclo-alpha-MSH(4-10)amide: a melanocortin-3 receptor agonist
Sugary and Not So Sugary ProblemsSugary and Not So Sugary Problems
Now, do you ever stop to wonder how you could be consuming such a "sugary" beverage with almost no or no calories and no sugar? We can all thank the company Monsanto for such a discovery...or curse. Aspartame itself doesnt have any calories, but basically, one of its ingredients, the amino acid phenylalanine, blocks production of serotonin, a nerve chemical that, among other activities, controls food cravings. As you might well imagine, a shortage of serotonin will make your brain and body scream for the foods that create more of this brain chemical-and those are the high-calorie, carbohydrate-rich snacks that can sabotage a dieter. Obviously, the more aspartame one ingests, the more heightened the effects. Simply put, aspartame appears to muddle the brain chemistry ...
Heterotropic co-operative effects between amino acid substrates of phenylalanine hydroxylase | Biochemical Journal | Portland...Heterotropic co-operative effects between amino acid substrates of phenylalanine hydroxylase | Biochemical Journal | Portland...
W F Coulson, C M Hughes; Heterotropic co-operative effects between amino acid substrates of phenylalanine hydroxylase. Biochem J 1 July 1971; 123 (4): 22P. doi: https://doi.org/10.1042/bj1230022P. Download citation file:. ...
NITRC: p-[(123)I]iodo-L-phenylalanine (IPA)-SPECT template in MNI-coordinatesNITRC: p-[(123)I]iodo-L-phenylalanine (IPA)-SPECT template in MNI-coordinates
Choose a news bulletin below to browse, search, and post messages related to it.. Only p-[(123)I]iodo-L-phenylalanine (IPA)-SPECT template in MNI-coordinates administrators can submit a news bulletin for p-[(123)I]iodo-L-phenylalanine (IPA)-SPECT template in MNI-coordinates. News bulletins appear on this page and in the Recent Activity section on p-[(123)I]iodo-L-phenylalanine (IPA)-SPECT template in MNI-coordinatess Summary page.. ...
L-Phenylalanine : Meridian Botanicals - from Apothecary to Alchemy, Home of rare and traditional herbs, exotic ethnobotanicals,...L-Phenylalanine : Meridian Botanicals - from Apothecary to Alchemy, Home of rare and traditional herbs, exotic ethnobotanicals,...
Also known as L Phenylalanine Introduction L-Phenylalanine is an essential alpha-amino acid and dietary precursor for the amino acid tyrosine thyroid hormones, and the catecholamine family of neurotransmitters such as dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), as well as melanin, an endogenous antioxidant which darkens skin color to protect from the sun. The L-isomer is the natural form of this compound, which is used to biosynthesize proteins, while the D-isomer is inhibits the metabolism of enkephalin, an endogenous pain reliever. L-phenylalanine is found naturally in the breast milk of mammals and most foods. As an essential amino acid, phenylalanine is not synthesized in humans and other animals, rather it must be consumed through diet or supplementation. Supplement data Origin: China Use Recommended amount per dose is 500-2000 mg, or 1-4 size 00 capsules. Summary L-Phenylalanine is an effective catecholamine precursor, increasing levels of tyrosine, thyroid hormones,
The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase. - Semantic ScholarThe production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase. - Semantic Scholar
Semantic Scholar extracted view of The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase. by Gordon Guroff et al.
Phenylalanine : L-Phenylalanine 500mg | Lamberts EspañolaPhenylalanine : L-Phenylalanine 500mg | Lamberts Española
Lamberts® Phenylalanine is the natural L-Phenylalanine and is presented in its free-form to help ensure optimal absorption. Made in the UK ,GMP standards.
Phenylalanine & Reduced fat milkPhenylalanine & Reduced fat milk
Nutrition facts: Phenylalanine in Reduced fat milk (Milk, reduced fat, 2% milkfat, with added vitamin A (common)). Find out the Phenylalanine amount in this food.
CCCC 1991, Volume 56, Issue 12, Abstracts pp. 2991-2998 | Collection of Czechoslovak Chemical CommunicationsCCCC 1991, Volume 56, Issue 12, Abstracts pp. 2991-2998 | Collection of Czechoslovak Chemical Communications
In the course of our study on cholecystokinin (CCK) a series of Boc-CCK-7 was synthesized. Their carboxyterminal part was modified by phenylalanine derivatives containing 2 or 4 and 2,6 or 2,4,6 methylated aromatic side-chain. During the synthesis, the racemic phenylalanine derivatives were used and peptides containing either L- or D- methylated phenylalanine were separated using a preparative HPLC. Gall bladder contraction, anorectic, sedative and analgetic bioassays of these analogues revealed that all of them behaved as CCK-8 agonists. While the analogues containing L-form of the methylated phenylalanines had almost the same potency (80% - 130%) in comparison to CCK-8, the presence of the D-form decreased the biological activity of corresponding analogues to 8 - 62% of the CCK-8 potency. These results are in agreement with the suggestion that phenylalanine residue in C-terminus takes part in biological activity transduction only.. ...
Hiperfenielalaninemiee : mutasie-analiseHiperfenielalaninemie"e : mutasie-analise
The hyperphenylalaninemias are disorders of phenylalanine hydroxylation. The disease results from the absence of the hepatic phehylalaniene hydrosylase (PAH) and causes mental retardation. The clinical manifestations and consequences of hyperphenylalaninaemia are due to abnormal accumulation of normal metabolites, thus resulting in mental retardation. This can be rectified by early diagnosis of the disease and the dietary treatment there-of. It is unfortunate that in most instances the diagnosis is only made after permanent and irreversible brain damage has occurred. This can be rectified if PKU carrier diagnosis is applied to identify those high risk families. ,br,,br, Metabolite analyses led to the identification of hyperphehylalaninaemia patients. This phase was part of the normal screening program for the identification of amino-acidpathies of severely ill infants referred to ,the Department of Biochemistry at the Potchefstroom University for Christian Higher Education (PU for CHE). ...
phenylalanine- WordWeb dictionary definitionphenylalanine- WordWeb dictionary definition
An essential amino acid found in proteins and needed for growth of children and for protein metabolism in children and adults; abundant in milk and eggs; it is normally converted to tyrosine in the human body ...
phenylalanine 2-monooxygenase(EC 1.13.12.9) - Creative Enzymesphenylalanine 2-monooxygenase(EC 1.13.12.9) - Creative Enzymes
The reaction shown above is about 80% of the reaction catalysed; the remaining 20% is: L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + ammonia + H2O2 a reaction simil
A phenylalanine-55 to serine amino-acid substitution in the human glycoprotein IX leucine-rich repeat is associated with...A phenylalanine-55 to serine amino-acid substitution in the human glycoprotein IX leucine-rich repeat is associated with...
If you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library, or send a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ...
Buy L-Phenylalanine Powder | View L-Phenylalanine Reviews and BenefitsBuy L-Phenylalanine Powder | View L-Phenylalanine Reviews and Benefits
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Phenylalanine Amino Acid Supplements & Products UK | RevitalPhenylalanine Amino Acid Supplements & Products UK | Revital
Phenylalanine is an essential amino acid required for body growth. Click here and get free delivery in the UK for orders over £20!
Enzyme kinetic and molecular modelling studies of sulphur-containing substrates of phenylalanine 4-monooxygenase - Surrey...Enzyme kinetic and molecular modelling studies of sulphur-containing substrates of phenylalanine 4-monooxygenase - Surrey...
Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Chemistry, Medicinal, Pharmacology & Pharmacy, BIOCHEMISTRY & MOLECULAR BIOLOGY, CHEMISTRY, MEDICINAL, Phenylalanine 4-monooxygenase, thioether substrates, S-oxidation, inhibition, computer modelling, CARBOXYMETHYL-L-CYSTEINE, CATALYTIC DOMAIN, HYDROXYLASE, 3-(2-THIENYL)-L-ALANINE, TETRAHYDROBIOPTERIN, SPECIFICITY, MECHANISM ...
AAA - Aromatic Amino Acids | AcronymAtticAAA - Aromatic Amino Acids | AcronymAttic
How is Aromatic Amino Acids abbreviated? AAA stands for Aromatic Amino Acids. AAA is defined as Aromatic Amino Acids somewhat frequently.
N-Tetrahydrofuroyl-( l)-phenylalanine derivatives as potent VLA-4 antagonists - 01DAL UDM - University of Detroit Mercy LibraryN-Tetrahydrofuroyl-( l)-phenylalanine derivatives as potent VLA-4 antagonists - 01DAL UDM - University of Detroit Mercy Library
Description: Given the proposed involvement of VLA-4 in inflammatory processes, a program to identify orally active VLA-4 antagonists was initiated. Herein, we report the discovery of a N-tetrahydrofuroyl-( l)-phenylalanine derivative ( 17) and related analogues as potent VLA-4 antagonists with good oral bioavailability. The synthesis, biological properties, and pharmacokinetic profile of tetrahydrofuranoyl such as 17 are reported. ...
Modification of phenylalanine mustard effect on l1210 cells using hema by S P. Creekmore and D S. Zaharko"Modification of phenylalanine mustard effect on l1210 cells using hema" by S P. Creekmore and D S. Zaharko
Creekmore, S P. and Zaharko, D S., "Modification of phenylalanine mustard effect on l1210 cells using hematoporphyrin and light. Abstr." (1982). Subject Strain Bibliography 1982. 2152 ...
Local mom educates students on PKU at RPES - The Atmore Advance | The Atmore AdvanceLocal mom educates students on PKU at RPES - The Atmore Advance | The Atmore Advance
Protein is something in all of our food, even seasoning that Kayan cant have," she said. "He can, but its limited. What I have to do and his mom (DAsia Johnson) has to do and what Ms. (Shirley) Longmire has to do, is make sure Kayan stays on a proper diet.". PKU is a rare inherited disorder that causes an amino acid called phenylalanine to build up in the body. PKU is caused by a defect in the gene that helps create the enzyme needed to break down phenylalanine, according to the Mayo Clinics website.. Those with PKU need to follow a limited diet of phenylalanine, which is found mostly in foods that contain protein, according to the Mayo Clinic.. ...
US20020001652A1 - Process for making granulated N-[N- (3, 3-dimethylbutyl) -L-alpha -aspartyl] -L- phenylalanine 1-methyl ester...US20020001652A1 - Process for making granulated N-[N- (3, 3-dimethylbutyl) -L-alpha -aspartyl] -L- phenylalanine 1-methyl ester...
N-[N-(3,3-dimethylbutyl)-L-α-aspartyl]-L-phenylalanine 1-methyl ester is converted from a light powder to relatively dustless, free-flowing granules using compaction, preferably roller compaction, and size reduction processes. These granules are suitable for use in a variety of applications. Food products sweetened with granulated N-[N-(3,3-dimethylbutyl)-L-α-aspartyl]-L-phenylalanine 1-methyl ester and methods of sweetening food products with such N-[N-(3,3-dimethylbutyl)-L-α-aspartyl]-L-phenylalanine 1-methyl ester are also disclosed.
6,7-dihydropteridine reductase6,7-dihydropteridine reductase
Arogenate dehydrataseArogenate dehydratase
Newborn screeningNewborn screening
Erlenmeyer-Plöchl azlactone and amino-acid synthesisErlenmeyer-Plöchl azlactone and amino-acid synthesis
Sprite ZeroSprite Zero
Newborn Screening Saves Lives Reauthorization Act of 2013Newborn Screening Saves Lives Reauthorization Act of 2013
PhenylketonuriaPhenylketonuria
Amino acid synthesisAmino acid synthesis
Specialized pro-resolving mediatorsSpecialized pro-resolving mediators
3,4-Dihydroxystyrene3,4-Dihydroxystyrene
PhenylacetaldehydePhenylacetaldehyde
Phenyl groupPhenyl group
Phenylacetaldehyde dehydrogenasePhenylacetaldehyde dehydrogenase
O-Coumaric acidO-Coumaric acid
3-carboxyethylcatechol 2,3-dioxygenase3-carboxyethylcatechol 2,3-dioxygenase
Prephenate dehydratasePrephenate dehydratase
Roswell Park Memorial Institute mediumRoswell Park Memorial Institute medium
2-enoate reductase2-enoate reductase
Ribonuclease inhibitorRibonuclease inhibitor
Chaetomium cupreumChaetomium cupreum
Glycine N-benzoyltransferaseGlycine N-benzoyltransferase
Melilotate 3-monooxygenaseMelilotate 3-monooxygenase
Diagnostic microbiologyDiagnostic microbiology
Ligand-gated ion channelLigand-gated ion channel
D-amino-acid N-acetyltransferaseD-amino-acid N-acetyltransferase
Hippurate hydrolaseHippurate hydrolase
2-coumarate reductase2-coumarate reductase
ErgolineErgoline
Chicken as foodChicken as food
HickoryHickory
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesTechnology, Industry, AgricultureInformation Science
PhenylalaninePhenylalanine HydroxylasePhenylalanine Ammonia-LyasePhenylketonuriasPhenylpyruvic AcidsTyrosineAmino AcidsAmmonia-LyasesPrephenate DehydrataseBiopterinPterinsKineticsLeucineTryptophanMolecular Sequence DataAmino Acids, AromaticAmino Acid SequencePhenylalanine-tRNA LigasePhenylketonuria, MaternalFencloninep-FluorophenylalanineChorismate MutaseMutagenesis, Site-DirectedMutationAmino Acids, EssentialCarbon IsotopesBinding SitesAspartameHydroxylationPteridines3-Deoxy-7-Phosphoheptulonate SynthaseAnabaena variabilisRhodotorulaNutritional RequirementsLiverHydro-LyasesDeuteriumBase SequenceEscherichia coliIsoleucineModels, MolecularPhenylacetatesStructure-Activity RelationshipAmino Acid SubstitutionAlanineMuscle ProteinsProtein ConformationRNA, Transfer, PheFood, FormulatedValineSubstrate SpecificityLeucine DehydrogenaseChromobacteriumProtein BindingAldehyde-LyasesLysineOxidation-ReductionRecombinant ProteinsMethionineProtein BiosynthesisDietary ProteinsRNA, TransferShikimic AcidRNA, Transfer, Amino AcylTetrosesPhosphorylationAmino Acids, Branched-ChainHydrogen-Ion ConcentrationDihydropteridine ReductaseFluorineGlycineProtein Structure, TertiaryCatalysisMitosporic FungiProtein HydrolysatesCloning, MolecularCinnamatesPoint MutationTransaminasesAmino Acids, NeutralSequence Homology, Amino AcidSpectrophotometry, UltravioletEnzyme ActivationTyrosine TransaminaseHomogentisate 1,2-DioxygenasePetroselinumDipeptidesAmino Acyl-tRNA SynthetasesElectrophoresis, Polyacrylamide GelCell LineCyclohexanecarboxylic AcidsMagnetic Resonance SpectroscopyPlantsStereoisomerismMolecular WeightChromatography, High Pressure LiquidRadioactive TracersTryptophan HydroxylaseSequence Alignment
Phenylalanine | chemical compound | Britannica.comPhenylalanine | chemical compound | Britannica.com
L-(-)-Phenylalanine | C9H11NO2 | ChemSpiderL-(-)-Phenylalanine | C9H11NO2 | ChemSpider
D-Phenylalanine - DrugBankD-Phenylalanine - DrugBank
Twinlab Phenylalanine - eVitamins CanadaTwinlab Phenylalanine - eVitamins Canada
Phenylalanine - OpenWetWarePhenylalanine - OpenWetWare
Neonatal Phenylalanine ELISA Kit (without Membrane) (07575300) - MP BiomedicalsNeonatal Phenylalanine ELISA Kit (without Membrane) (07575300) - MP Biomedicals
Product information, instructions, health benefits, and usage for PhenylalanineProduct information, instructions, health benefits, and usage for Phenylalanine
Proteins & Amino Acids - PhenylalanineProteins & Amino Acids - Phenylalanine
Difference between revisions of Phenylalanine - OpenWetWareDifference between revisions of "Phenylalanine" - OpenWetWare
United States L-Phenylalanine Market Report 2016 : ReportsnReportsUnited States L-Phenylalanine Market Report 2016 : ReportsnReports
L-Phenylalanine - Now at VitaDigest.com - Great Selection of L-Phenylalanine ProductsL-Phenylalanine - Now at VitaDigest.com - Great Selection of L-Phenylalanine Products
D-Phenylalanine ethyl ester Market Insights 2019, Analysis and Forecast Global and Chinese Market to 2024, by Manufacturers,...D-Phenylalanine ethyl ester Market Insights 2019, Analysis and Forecast Global and Chinese Market to 2024, by Manufacturers,...
Cureus | 13C-phenylalanine breath test detects altered phenylalanine kinetics in schizophrenia patientsCureus | 13C-phenylalanine breath test detects altered phenylalanine kinetics in schizophrenia patients
Phenylalanine: Potential Benefits + Foods & Side Effects - SelfHackedPhenylalanine: Potential Benefits + Foods & Side Effects - SelfHacked
A Review of Phenylalanines Benefits, Side Effects, Dosage and StackA Review of Phenylalanine's Benefits, Side Effects, Dosage and Stack
Phenylalanine - WikipediaPhenylalanine - Wikipedia
Phenylalanine adenylyltransferase - WikipediaPhenylalanine adenylyltransferase - Wikipedia
Phenylalanine | Encyclopedia.comPhenylalanine | Encyclopedia.com
L-phenylalanine (CHEBI:17295)L-phenylalanine (CHEBI:17295)
L-phenylalanine zwitterion (CHEBI:58095)L-phenylalanine zwitterion (CHEBI:58095)
Serum phenylalanine screening: MedlinePlus Medical EncyclopediaSerum phenylalanine screening: MedlinePlus Medical Encyclopedia
DL-PhenylalanineDL-Phenylalanine
BAM Media M123: Phenylalanine Deaminase Agar | FDABAM Media M123: Phenylalanine Deaminase Agar | FDA
PNDs with Normal Phenylalanine LevelsPNDs with Normal Phenylalanine Levels
PhenylalaninePhenylalanine
L-Phenylalanine - iHerbL-Phenylalanine - iHerb
L-Phenylalanine - iHerbL-Phenylalanine - iHerb
Phenylalanine: Uses, Side Effects, Interactions, Dosage, and WarningPhenylalanine: Uses, Side Effects, Interactions, Dosage, and Warning
Patent US4600692 - Immobilized cells for preparing phenylalanine - Google PatentsPatent US4600692 - Immobilized cells for preparing phenylalanine - Google Patents
Phenylalanine: Benefits, Side Effects and Food SourcesPhenylalanine: Benefits, Side Effects and Food Sources
Dansyl-L-phenylalanine | Sigma-AldrichDansyl-L-phenylalanine | Sigma-Aldrich
Isozymes of Phenylalanine Hydroxylase | ScienceIsozymes of Phenylalanine Hydroxylase | Science
Phenylalanine | C9H11NO2 - PubChemPhenylalanine | C9H11NO2 - PubChem
Properties of phenylalanineProperties of phenylalanine
Phenylalanine 4-monooxygenase | Define Phenylalanine 4-monooxygenase at Dictionary.comPhenylalanine 4-monooxygenase | Define Phenylalanine 4-monooxygenase at Dictionary.com
Why is phenylalanine in chewing gum? | Reference.comWhy is phenylalanine in chewing gum? | Reference.com
phenylalaninephenylalanine
Phenylalanine | University of Maryland Medical CenterPhenylalanine | University of Maryland Medical Center
l-Phenylalanine, n-heptafluorobutyryl-, tetradecyl esterl-Phenylalanine, n-heptafluorobutyryl-, tetradecyl ester
L-Phenylalanine: uses & side-effects | PatientsLikeMeL-Phenylalanine: uses & side-effects | PatientsLikeMe
The molecular basis of phenylalanine hydr... & related info | MendeleyThe molecular basis of phenylalanine hydr... & related info | Mendeley
DL-Phenylalanine puriss., ≥99.0% (NT) | Sigma-AldrichDL-Phenylalanine puriss., ≥99.0% (NT) | Sigma-Aldrich
Health Benefits & Risks of Phenylalanine | LIVESTRONG.COMHealth Benefits & Risks of Phenylalanine | LIVESTRONG.COM
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesTechnology, Industry, AgricultureInformation Science
PhenylalaninePhenylalanine HydroxylasePhenylalanine Ammonia-LyasePhenylketonuriasPhenylpyruvic AcidsTyrosineAmino AcidsAmmonia-LyasesPrephenate DehydrataseBiopterinPterinsKineticsLeucineTryptophanMolecular Sequence DataAmino Acids, AromaticAmino Acid SequencePhenylalanine-tRNA LigasePhenylketonuria, MaternalFencloninep-FluorophenylalanineChorismate MutaseMutagenesis, Site-DirectedMutationAmino Acids, EssentialCarbon IsotopesBinding SitesAspartameHydroxylationPteridines3-Deoxy-7-Phosphoheptulonate SynthaseAnabaena variabilisRhodotorulaNutritional RequirementsLiverHydro-LyasesDeuteriumBase SequenceEscherichia coliIsoleucineModels, MolecularPhenylacetatesStructure-Activity RelationshipAmino Acid SubstitutionAlanineMuscle ProteinsProtein ConformationRNA, Transfer, PheFood, FormulatedValineSubstrate SpecificityLeucine DehydrogenaseChromobacteriumProtein BindingAldehyde-LyasesLysineOxidation-ReductionRecombinant ProteinsMethionineProtein BiosynthesisDietary ProteinsRNA, TransferShikimic AcidRNA, Transfer, Amino AcylTetrosesPhosphorylationAmino Acids, Branched-ChainHydrogen-Ion ConcentrationDihydropteridine ReductaseFluorineGlycineProtein Structure, TertiaryCatalysisMitosporic FungiProtein HydrolysatesCloning, MolecularCinnamatesPoint MutationTransaminasesAmino Acids, NeutralSequence Homology, Amino AcidSpectrophotometry, UltravioletEnzyme ActivationTyrosine TransaminaseHomogentisate 1,2-DioxygenasePetroselinumDipeptidesAmino Acyl-tRNA SynthetasesElectrophoresis, Polyacrylamide GelCell LineCyclohexanecarboxylic AcidsMagnetic Resonance SpectroscopyPlantsStereoisomerismMolecular WeightChromatography, High Pressure LiquidRadioactive TracersTryptophan HydroxylaseSequence Alignment
Amino AcidsHigh in phenylalanineForms of phenylalanine500mgExcess phenylalanine is convertedPhenylketonuriaProteinsDLPAFoodsDopaminePrecursorEsterEnzymeConvertsMoleculeEssentialSynthetic formBrainTyrosineAmmonia-lyaseSupplementsCapsulesTreating Parkinson's diseaseBuildup of phenylalanineDeficiencyContain phenylalanineBiosynthesisSource NaturalsAcidDepressionLevels of phenylalanine in bloodCapsuleC9H11NO2Role of D-phenylalanineDiet low in phenylalanineSuggest that L-phenylalanineBlood phenylalanine levelsSuggestsIncludes L-phenylalanineDetermination of PhenylalanineIngredientsParkinson'sHigh-phenylalanineNeeds phenylalanineProcess phenylalanineContains PhenylalanineSymptomsMoodValinePhenylketonuricsEnzyme that catalyzes
Amino Acids3
  • Phenylalanine belongs to a particular group of amino acids known as essential amino acids, which basically means that they are needed by the body to carry our its everyday functions, but that the body itself cannot manufacture them, so they must be obtained by dietary means. (mysticrebels.com)
  • D-phenylalanine is a synthetic form of phenylalanine that mirrors its natural cousin, and DL-phenylalanine therefore is a combination of these two amino acids. (mysticrebels.com)
  • The Main Products Include: Alanine Series , Phenylalanine Series , Aspartic Acid Series , Glutamic Acid Series And D-Amino Acids , For A Characteristic To Point Out , DL-Amino Acids Synthesis Technology And High Optical Purity Amino Acids Production Technology. (twfta.com)
High in phenylalanine1
Forms of phenylalanine3
500mg1
Excess phenylalanine is converted1
  • a "phenylketonuric" compound associated to PKU or phenylketonuria disease, a group of symptoms associated to mental retardation and cognitive impairments in the brain, where excess phenylalanine is converted to a ketone in the CNS periphery (Central Nervous System). (openwetware.org)
Phenylketonuria1
  • Phenylalanine supplements should not be taken by individuals with phenylketonuria (PKU), children, pregnant or lactating women, people with high blood pressure, and anyone taking anti-psychotic medications or MAO inhibitors. (megavitamins.com.au)
Proteins4
DLPA1
  • Supplements can contain either form or a mixture of their equal amounts, known as DLPA (DL-phenylalanine) . (selfhacked.com)
Foods2
Dopamine1
Precursor1
Ester8
Enzyme2
  • Sometimes children are born without the ability to manufacture an enzyme crucial to the metabolizing of phenylalanine, a condition known as PKU . (mysticrebels.com)
  • D-phenylalanine is reported to inhibit an enzyme that degrades enkephalins, which are naturally occurring substances in the body that belong to the class of compounds known as "endorphins. (megavitamins.com.au)
Converts1
Molecule1
Essential5
Synthetic form1
Brain1
  • Phenylalanine has potential health benefits for the skin and brain, but some people should avoid it by all means. (selfhacked.com)
Tyrosine38
Ammonia-lyase5
Supplements12
Capsules1
Treating Parkinson's disease1
Buildup of phenylalanine1
Deficiency4
Contain phenylalanine1
Biosynthesis5
  • Phenylalanine plays a key role in the biosynthesis of other amino acids and some neurotransmitters. (fsu.edu)
  • Phenylalanine ammonialyase (PAL) catalyzes the first step in the biosynthesis of phenylpropanoids, and is usually encoded by a multi-gene family. (nih.gov)
  • Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. (uniprot.org)
  • Valine and phenylalanine as precursors in the biosynthesis of alkamides in Acmella radicans. (biomedsearch.com)
  • Alkamides were isolated from young A. radicans plants and analyzed by gas chromatography-mass spectrometry (GC-MS). Additionally, in cell free in vitro experiments based on isobutyl and phenylethylamide biosynthesis, using a colorimetric assay and GC-MS, valine and phenylalanine decarboxylase activities were assayed in the soluble extract of A. radicans leaves. (biomedsearch.com)
Source Naturals1
  • The dietary supplement from Source Naturals‚ DL-Phenylalanine 750 mg 60 Tablets‚ may possibly help in the support of an alert state of mind. (pureformulas.com)
Acid30
  • The test detects abnormally high levels of an amino acid called phenylalanine. (medlineplus.gov)
  • This test is done to screen infants for PKU, a fairly rare condition that occurs when the body lacks a substance needed to breakdown the amino acid phenylalanine. (medlineplus.gov)
  • Phenylalanine (Phe) is an α-amino acid with the formula C 9H 11NO 2. (wikipedia.org)
  • Phenylalanine is an amino acid, a "building block" of protein. (webmd.com)
  • D-phenylalanine is not an essential amino acid. (webmd.com)
  • L-phenylalanine is an essential amino acid. (webmd.com)
  • Phenylalanine, a naturally occurring amino acid, is not present in chewing gum products on its own. (reference.com)
  • A process is disclosed for preparing phenylalanine which comprises contacting phenylpyruvic acid or phenylpyruvate with immobilized whole cells having transaminase activity in the presence of an amine donor. (google.ca)
  • 1. A process for preparing phenylalanine which comprises preparing an aqueous reaction mixture consisting essentially of phenylpyruvic acid or phenylpyruvate, pyridoxal -5-phosphate as a cofactor and an amine donor selected from the group consisting of L-glutamic acid and L-aspartic acid, and contacting said reaction mixture with cells immobilized with a polyazetidine polymer, the cells having transaminase activity to obtain said phenylalanine in high yield. (google.ca)
  • 13. A composition suitable for use in converting phenylpyruvic acid or phenylpyruvate to phenylalanine comprising immobilized cells having transaminase activity, said cells being immobilized with a polyazetidine polymer. (google.ca)
  • Phenylalanine is an essential amino acid that is also one of the aromatic amino acids that exhibit ultraviolet radiation absorption properties with a large extinction coefficient. (fsu.edu)
  • Your body is unable to produce enough L-phenylalanine on its own, so it's considered an essential amino acid that must be obtained through your diet ( 4 ). (healthline.com)
  • This amino acid is produced directly from phenylalanine. (healthline.com)
  • Phenylalanine is an essential amino acid that the body can not synthesize and therefore must be provided by the diet. (botanical-online.com)
  • Phenylalanine is an essential amino acid that must be supplemented through diet. (livestrong.com)
  • D-phenylalanine is a synthetic form of this amino acid created in a laboratory. (livestrong.com)
  • and DL-phenylalanine, a combination of the first two forms of this amino acid. (livestrong.com)
  • It is made by our bodies from phenylalanine, which is an essential amino acid and must be consumed daily. (rainbow.coop)
  • One reason that PKU is so devastating is that a high level of Phenylalanine (Phe), which is a large neutral amino acid (LNAA), stops other LNAAs, which are needed for proper brain development, getting into the brain. (hubpages.com)
  • Exposure to the amino acid L-phenylalanine increased release of CCK by 135%, 180%, and 251% of control levels after 15-min treatments with 5, 20, and 50 mM phenylalanine, respectively. (rti.org)
  • PAL, a robust enzyme without need for a cofactor, converts phenylalanine to trans-cinnamic acid, a harmless metabolite. (pnas.org)
  • The amino acid phenylalanine (Phe) is a critical metabolic node that plays an essential role in the interconnection between primary and secondary metabolism in plants. (frontiersin.org)
  • One such dietary amino acid, phenylalanine (Phe), is a critical metabolic node that plays an essential role in the interconnection between the primary and secondary metabolism of plants. (frontiersin.org)
  • Taking the amino acid phenylalanine as a pre-workout supplement may stimulate whole body fat oxidation, known colloquially as 'burning fat,' according to a new study. (nutraingredients-usa.com)
  • The researchers wrote that effects of a single amino acid combined with exercise on fat oxidation is still unclear, thus the research was to investigate hormone secretion induced by phenylalanine and exercise. (nutraingredients-usa.com)
  • The aim of this research is to investigate the inhibitive effect of amino acid such as DL-phenylalanine. (hindawi.com)
  • C9H11NO2 amino acid Phenylalanine molecule isolated on white. (vectorstock.com)
  • Phenylalanine - an essential amino acid- is readily available in most food sources, particularly high in meats and milk products, with lower levels found in oats and wheat germ. (dummies.com)
  • Because L-phenylalanine is an essential amino acid, it is not synthesized in the human body and must be supplied by dietary intake or supplementation. (purebulk.com)
  • Liu, J. and Liu, X. (2011), Nanoparticles prepared by blending of carboxylic acid terminated poly(ε-caprolactone) and L -phenylalanine substituted dextran. (wiley.com)
Depression16
  • Limited clinical research performed in the 1970s and 1980s suggests L-phenylalanine or DL-phenylalanine might be useful for depression. (webmd.com)
  • Taking D-phenylalanine does not appear to improve symptoms of depression. (webmd.com)
  • Phenylalanine has been studied as a treatment for several medical conditions, including skin disorders, depression and pain ( 3 ). (healthline.com)
  • Since phenylalanine is used to make these molecules in your body, it has been studied as a potential treatment for certain conditions, including depression ( 9 ). (healthline.com)
  • Thus, food intake with phenylalanine may help reduce the symptoms of depression and Alzheimer's . (botanical-online.com)
  • One animal study suggests that D-phenylalanine may improve rigidity, walking disabilities, speech difficulties, and depression associated with Parkinson disease. (umm.edu)
  • Studies suggest that phenylalanine may be helpful as part of a comprehensive therapy for depression, most of the studies were done in the 1970s and 1980s and were not rigorously tested. (umm.edu)
  • More research is needed to tell whether phenylalanine has any real effect on depression. (umm.edu)
  • According to Integrative Medical Arts Group, DL-phenylalanine and phenylethylamine may improve symptoms of both Parkinson's and the depression that occurs with the disease. (livestrong.com)
  • While they both worked equally well at reducing the symptoms of depression, the D-phenylalanine showed marked improvements after just 15 days, rather than several weeks for the imipramine. (livestrong.com)
  • DL-Phenylalanine is used to relieve cases of minor depression and other mood issues as well as and physical discomforts and pain. (fishersci.ca)
  • Phenylalanine can affect depression via three separate pathways. (digitalnaturopath.com)
  • Therapeutic doses of phenylalanine may have useful roles in the management of blood pressure disorders and the control of certain forms of depression. (springboard4health.com)
  • Depression is a common use for L-phenylalanine or DL-phenylalanine. (naturalfrontiermarket.net)
  • L-phenylalanine has been found to improve mood in people who have major depression. (naturalfrontiermarket.net)
  • DL-phenylalanine and D-phenylalanine have also been studied for depression, although the results are unclear. (naturalfrontiermarket.net)
Levels of phenylalanine in blood1
  • 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)
Capsule6
  • You can take phenylalanine as a capsule, powder, or tablet. (umm.edu)
  • Researchers found that participants who consumed 3g of phenylalanine in a capsule thirty minutes before exercising exhibited increased concentrations of plasma glycerol and the hormone glucagon-both relevant in the process of converting fat into usable energy. (nutraingredients-usa.com)
  • The capsule of phenylalanine came from ingredient manufacturer Kyowa Hakko, which is owned by the beverage giant Kirin Holdings. (nutraingredients-usa.com)
  • At the recommended dosage‚ each 90-capsule bottle of Pure Encapsulations' dl-Phenylalanine should last for about 15 to 22 days. (pureformulas.com)
  • Douglas Labs L-Phenylalanine 90 caps supplies 500 mg of pure L-Phenylalanine in each capsule. (integrativepsychiatry.net)
  • DL-Phenylalanine (Free Form) (providing D-Phenylalanine and L-Phenylalanine), Vegetable Capsule Shell: hydroxypropylmethyl cellulose, Anti-caking Agents: (vegetable magnesium stearate, silicon dioxide), Bulking Agent: hydroxypropyl cellulose. (solgar.co.uk)
C9H11NO21
  • 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)
Role of D-phenylalanine1
Diet low in phenylalanine2
  • Present treatment relies on the observation that a (semisynthetic) diet low in phenylalanine ( 3 - 5 ) will prevent HPA and thus the disease. (pnas.org)
  • Treatment includes the early introduction of a diet low in phenylalanine. (mayomedicallaboratories.com)
Suggest that L-phenylalanine2
  • Preliminary studies suggest that L-phenylalanine (oral and topical) strengthens the effect of UVA radiation for people with vitiligo. (umm.edu)
  • Studies suggest that L-phenylalanine in combination with exposure to ultraviolet A (UVA) light or sunlight may help treat vitiligo, a condition in which there is a loss of skin pigment. (naturalfrontiermarket.net)
Blood phenylalanine levels2
  • Patients who are heterozygous for a GTPCH mutation, despite their normal blood phenylalanine levels on routine screening, can be shown to have abnormal phenylalanine metabolism if stressed by administration of an oral phenylalanine load (100 mg/kg). (massgeneral.org)
  • 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)
Suggests8
  • Some research suggests that patients with ADHD have lower levels of amino acids such as phenylalanine, so there was hope that providing phenylalanine might treat ADHD. (webmd.com)
  • Early research suggests that taking D-phenylalanine by mouth might enhance acupuncture anesthesia while having a tooth pulled. (webmd.com)
  • Early research suggests that taking a combination of D-phenylalanine, L-glutamine, and L-5-hydroxytryptophan for 40 days can improve some symptoms of alcohol withdrawal. (webmd.com)
  • Early research suggests that using Cari Loder's regiment, which includes L-phenylalanine, lofepramine, and intramuscular vitamin B12 for 24 weeks, does not improve disability in people with multiple sclerosis. (webmd.com)
  • Limited research suggests taking one form of phenylalanine (D-phenylalanine) might decrease symptoms of Parkinson's disease. (webmd.com)
  • Research database Health Notes Online suggests the use of L-phenylalanine while patients are undergoing ultraviolet radiation therapy. (livestrong.com)
  • Some research suggests that tardive dyskinesia patients may process phenylalanine abnormally. (digitalnaturopath.com)
  • Certain researchers suggests the possibility that D-Phenylalanine may inhibit the action of enzymes that break down endorphins (the feel-good hormone) and enkephalins. (pureformulas.com)
Includes L-phenylalanine1
  • The Cari Loder regime is a proposed method of treatment for multiple sclerosis (MS) that includes L-phenylalanine, lofepramine, and vitamin B12 injected into the vein. (naturalfrontiermarket.net)
Determination of Phenylalanine1
  • The MP Diagnostics ImmuChem Phenylalanine ELISA Kit is designed for the quantitative determination of phenylalanine in neonatal blood spots. (mpbio.com)
Ingredients1
  • Certain research indicates that the ingredients formulated into DL-Phenylalanine may be potentially successful at boosting endorphins. (pureformulas.com)
Parkinson's3
High-phenylalanine1
  • Food with a high phenylalanine content are meat products or animal-based products in general such as poultry, eggs and milk. (fairvital.com)
Needs phenylalanine1
  • The test paper is taken to the laboratory, where it is mixed with a type of bacteria that needs phenylalanine to grow. (medlineplus.gov)
Process phenylalanine1
  • PAH is needed to process phenylalanine, although other, non-PAH gene mutations can also cause PKU. (hubpages.com)
Contains Phenylalanine1
Symptoms5
Mood4
  • People have reported that their mood improved when they took phenylalanine. (umm.edu)
  • Other studies suggest that elevated phenylalanine concentrations are linked to mood swings. (umm.edu)
  • d-Phenylalanine and l-Phenylalanine work in combination to help you maintain a positive mood. (pureformulas.com)
  • L-phenylalanine can also be converted (through a separate pathway) to phenylethylamine, a substance that occurs naturally in the brain and appears to elevate mood. (digitalnaturopath.com)
Valine1
Phenylketonurics2
Enzyme that catalyzes1
  • In enzymology, a phenylalanine adenylyltransferase (EC 2.7.7.54) is an enzyme that catalyzes the chemical reaction ATP + L-phenylalanine ⇌ {\displaystyle \rightleftharpoons } diphosphate + N-adenylyl-L-phenylalanine Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are diphosphate and N-adenylyl-L-phenylalanine. (wikipedia.org)
Phenylalanine | chemical compound | Britannica.com
Phenylalanine | chemical compound | Britannica.com (britannica.com)
Metabolic Maintenance Amino-Mag Formula - OVitaminPro. Com
Metabolic Maintenance Amino-Mag Formula - OVitaminPro. Com (ovitaminpro.com)
Stay Calm, Cool and Collected with Phenylalanine - eVitamins 香港
Stay Calm, Cool and Collected with Phenylalanine - eVitamins 香港 (evitamins.com)
Twinlab Phenylalanine - eVitamins Canada
Twinlab Phenylalanine - eVitamins Canada (evitamins.com)
HEPATAMINE (isoleucine, leucine, lysine acetate, methionine, phenylalanine, threonine, tryptophan, valine, alani injection,...
HEPATAMINE (isoleucine, leucine, lysine acetate, methionine, phenylalanine, threonine, tryptophan, valine, alani injection,... (healthgrades.com)
Chain A, Crystal Structure Of Bovine Pancreatic Carboxypeptidase A Complexed With L-N-Hydroxyaminocarbonyl Phenylalanine At 2.3...
Chain A, Crystal Structure Of Bovine Pancreatic Carboxypeptidase A Complexed With L-N-Hydroxyaminocarbonyl Phenylalanine At 2.3... (pubchem.ncbi.nlm.nih.gov)
Aspartame: Good or Bad?
Aspartame: Good or Bad? (healthline.com)
Molecular Expressions: The Amino Acid Collection - Phenylalanine
Molecular Expressions: The Amino Acid Collection - Phenylalanine (micro.magnet.fsu.edu)
3-nitro-d-phenylalanine | VWR
3-nitro-d-phenylalanine | VWR (us.vwr.com)
Dl-Phenylalanine - Healthy Living Shop
Dl-Phenylalanine - Healthy Living Shop (store.healthylivingshop.com)
Rate your experience with this treatment
Rate your experience with this treatment (webmd.com)
L-phenylalanine (CHEBI:17295)
L-phenylalanine (CHEBI:17295) (ebi.ac.uk)
Buffet Rule Explained - YouTube
Buffet Rule Explained - YouTube (youtube.com)
L-phenylalanine zwitterion (CHEBI:58095)
L-phenylalanine zwitterion (CHEBI:58095) (ebi.ac.uk)
What Are the Dangers of Coke? | LIVESTRONG.COM
What Are the Dangers of Coke? | LIVESTRONG.COM (livestrong.com)
RCSB PDB - PFF Ligand Summary Page
RCSB PDB - PFF Ligand Summary Page (rcsb.org)
DL-Phenylalanine
DL-Phenylalanine (webbook.nist.gov)
Palynziq - FDA prescribing information, side effects and uses
Palynziq - FDA prescribing information, side effects and uses (drugs.com)
Can Eating Chocolate Give You a Headache? | Livestrong.com
Can Eating Chocolate Give You a Headache? | Livestrong.com (livestrong.com)
What Are the Dangers of Splenda, Sucralose and Aspartame? | Livestrong.com
What Are the Dangers of Splenda, Sucralose and Aspartame? | Livestrong.com (livestrong.com)
PKU (Phenylketonuria) | Smore Newsletters
PKU (Phenylketonuria) | Smore Newsletters (smore.com)
UT Health Physicians | UT Health San Antonio
UT Health Physicians | UT Health San Antonio (healthlibrary.epnet.com)
Tryptophan-based chromophore in fluorescent proteins can be anionic | Scientific Reports
Tryptophan-based chromophore in fluorescent proteins can be anionic | Scientific Reports (nature.com)
Amino acid synthesis - Wikipedia
Amino acid synthesis - Wikipedia (en.wikipedia.org)
DailyMed - SULFAMETHOXAZOLE AND TRIMETHOPRIM injection, solution, concentrate
DailyMed - SULFAMETHOXAZOLE AND TRIMETHOPRIM injection, solution, concentrate (dailymed.nlm.nih.gov)
Isozymes of Phenylalanine Hydroxylase | Science
Isozymes of Phenylalanine Hydroxylase | Science (science.sciencemag.org)
PAH Gene - GeneCards | PH4H Protein | PH4H Antibody
PAH Gene - GeneCards | PH4H Protein | PH4H Antibody (genecards.org)
Phenylalanine: Benefits, Side Effects and Food Sources
Phenylalanine: Benefits, Side Effects and Food Sources (healthline.com)
Health Benefits & Risks of Phenylalanine | LIVESTRONG.COM
Health Benefits & Risks of Phenylalanine | LIVESTRONG.COM (livestrong.com)
Side Effects of L-Phenylalanine | LIVESTRONG.COM
Side Effects of L-Phenylalanine | LIVESTRONG.COM (livestrong.com)
Properties of phenylalanine
Properties of phenylalanine (botanical-online.com)
Accessing Essential Amino Acids Through Foods. ~ Kathrina Jane B. Tiangco | elephant journal
Accessing Essential Amino Acids Through Foods. ~ Kathrina Jane B. Tiangco | elephant journal (elephantjournal.com)
Phenylalanine - Us Smart Publications
Phenylalanine - Us Smart Publications (smart-publications.com)