An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
An enzyme of the oxidoreductase class that catalyzes the formation of L-TYROSINE, dihydrobiopterin, and water from L-PHENYLALANINE, tetrahydrobiopterin, and oxygen. Deficiency of this enzyme may cause PHENYLKETONURIAS and PHENYLKETONURIA, MATERNAL. EC
An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.
A group of autosomal recessive disorders marked by a deficiency of the hepatic enzyme PHENYLALANINE HYDROXYLASE or less frequently by reduced activity of DIHYDROPTERIDINE REDUCTASE (i.e., atypical phenylketonuria). Classical phenylketonuria is caused by a severe deficiency of phenylalanine hydroxylase and presents in infancy with developmental delay; SEIZURES; skin HYPOPIGMENTATION; ECZEMA; and demyelination in the central nervous system. (From Adams et al., Principles of Neurology, 6th ed, p952).
A group of compounds that are derivatives of phenylpyruvic acid which has the general formula C6H5CH2COCOOH, and is a metabolite of phenylalanine. (From Dorland, 28th ed)
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC
A natural product that has been considered as a growth factor for some insects.
Compounds based on 2-amino-4-hydroxypteridine.
The rate dynamics in chemical or physical systems.
An essential branched-chain amino acid important for hemoglobin formation.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Amino acids containing an aromatic side chain.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An enzyme that activates phenylalanine with its specific transfer RNA. EC
A condition occurring in untreated or partially treated females with PHENYLKETONURIA when they become pregnant. This may result in damages to the FETUS, including MICROCEPHALY; MENTAL RETARDATION; congenital heart disease; FETAL GROWTH RETARDATION; and CRANIOFACIAL ABNORMALITIES. (From Am J Med Genet 1997 Mar 3;69(1):89-95)
A selective and irreversible inhibitor of tryptophan hydroxylase, a rate-limiting enzyme in the biosynthesis of serotonin (5-HYDROXYTRYPTAMINE). Fenclonine acts pharmacologically to deplete endogenous levels of serotonin.
An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Flavoring agent sweeter than sugar, metabolized as PHENYLALANINE and ASPARTIC ACID.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.
An enzyme that catalyzes the formation of 7-phospho-2-keto-3-deoxy-D-arabinoheptonate from phosphoenolpyruvate and D-erythrose-4-phosphate. It is one of the first enzymes in the biosynthesis of TYROSINE and PHENYLALANINE. This enzyme was formerly listed as EC
A species of ANABAENA that can form SPORES called akinetes.
A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.
The amounts of various substances in food needed by an organism to sustain healthy life.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Derivatives of phenylacetic acid. Included under this heading are a variety of acid forms, salts, esters, and amides that contain the benzeneacetic acid structure. Note that this class of compounds should not be confused with derivatives of phenyl acetate, which contain the PHENOL ester of ACETIC ACID.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.
Food and dietary formulations including elemental (chemically defined formula) diets, synthetic and semisynthetic diets, space diets, weight-reduction formulas, tube-feeding diets, complete liquid diets, and supplemental liquid and solid diets.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria occurring in soil and water. Its organisms are generally nonpathogenic, but some species do cause infections of mammals, including humans.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
An essential amino acid. It is often added to animal feed.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Proteins prepared by recombinant DNA technology.
A sulfur-containing essential L-amino acid that is important in many body functions.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.
A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.
Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Amino acids which have a branched carbon chain.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC
A nonmetallic, diatomic gas that is a trace element and member of the halogen family. It is used in dentistry as flouride (FLUORIDES) to prevent dental caries.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A large and heterogenous group of fungi whose common characteristic is the absence of a sexual state. Many of the pathogenic fungi in humans belong to this group.
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.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Amino acids with uncharged R groups or side chains.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
An enzyme that catalyzes the conversion of L-TYROSINE and 2-oxoglutarate to 4-hydroxyphenylpyruvate and L-GLUTAMATE. It is a pyridoxal-phosphate protein. L-PHENYLALANINE is hydroxylated to L-tyrosine. The mitochondrial enzyme may be identical with ASPARTATE AMINOTRANSFERASES (EC Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC
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 and EC
A plant genus of the family APIACEAE used for flavoring food.
Peptides composed of two amino acid units.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Established cell cultures that have the potential to propagate indefinitely.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The sum of the weight of all the atoms in a molecule.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Radioactive substances added in minute amounts to the reacting elements or compounds in a chemical process and traced through the process by appropriate detection methods, e.g., Geiger counter. Compounds containing tracers are often said to be tagged or labeled. (Hawley's Condensed Chemical Dictionary, 12th ed)
An enzyme that catalyzes the hydroxylation of TRYPTOPHAN to 5-HYDROXYTRYPTOPHAN in the presence of NADPH and molecular oxygen. It is important in the biosynthesis of SEROTONIN.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Phenylalanine is an essential amino acid 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 ...
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Phenylalanine is an essential amino acid. This means that it must be obtained through the diet in adequate quantities to meet the bodys needs.
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 ...
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 ...
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 ...
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 report, Boc-3-(trifluoromethyl)-D-phenylalanine MSDS safety technical specifications search, Boc-3-(trifluoromethyl)-D-phenylalanine safety information specifications ect.
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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 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 ...
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.
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 ...
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 ...
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: 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 ...
Learn detail information about the benefits, uses, dosage and side effects of Phenylalanine on humans Health-Dietary supplement database
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Structure, properties, spectra, suppliers and links for: L-(-)-Phenylalanine, Phenylalanine, L-Phenylalanine, 63-91-2, C6H5CH2CH(NH2)COOH.
1. The rate of protein synthesis in quadriceps muscle of healthy subjects estimated from the incorporation of l-[1-13C]leucine given by continuous infusion was 1.1%/day. The estimate of protein synthesis from the incorporation of a flooding amount of labelled leucine was 1.8%/day (sd 0.65). The possibility that the higher rate obtained with the flooding technique arose from stimulation of protein synthesis by the large amount of leucine is unlikely.. 2. The same rate of protein synthesis (1.7%/day, sd 0.3) was obtained with a flooding amount (0.05 g/kg) of a different amino acid, l-[1-13C]phenylalanine, as was obtained with leucine.. 3. Incorporation of l-[1-13C]phenylalanine was not affected by simultaneous injection of leucine (1.7%/day, sd 0.7) or valine (1.6%/day, sd 0.4).. 4. Protein synthesis, assessed in a completely different way from the proportion of polyribosomes isolated from the skeletal muscle, was unaltered by the injection of 0.05 g of l-leucine/kg (44.6%, sd 8.5 versus 43.8%, sd ...
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
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. ...
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 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.
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.
[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...
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.
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 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 ...
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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.
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 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.
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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.
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 is a precursor to key neurotransmitters. Learn the risks and potential benefits of supplementation + best food sources.
Utilisation du ω-undécylènoyl phenylalanine, commercialisée sous le nom de marque SEPIWHITE™ MSH, en association avec un actif éclaircissant comme par ...
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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.
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. 2. 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. ... offer top selection of l-phenylalanine, big blend, l tyrosine, l arginine, amino, tyrosine, dietary supplement, nutrition
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An essential aromatic amino acid that is a precursor of melanin; dopamine; noradrenalin (norepinephrine), and thyroxine. [PubChem]
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 | 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-/ACM70663568 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
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 ...
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)): a somatostatin receptor subtype 4 agonist
Phenylalanine is an absolutely necessary amino acid in the human body. It is a rich source of protein. Phenylalanine cannot be made in the body, it must be consumed from the food. Phenylalanine can be found in mothers milk and is available in a number of foods like meat, milk, fish, peanuts, poultry, etc. Phenylalanine has a pleasant and distinctive smell. There are three types of phenylalanine D-phenylalanine, L- phenylalanine and the combined form that is DL-phenylalanine. The L- phenylalanine is a natural source of phenylalanine and it is available in the food. It is the only amino acid which essential and obtained in proteins. D-phenylalanine is used as a pain killer. Phenylalanine is used in treating many health issues and disorders like Parkinson disease, depression, attention deficit-hyperactivity disorder, etc. It is used in the pharmaceutical industry on a large scale. It is used in multiple food items. As pharmaceutical & food industries are growing rapidly, the demand for ...
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 ...
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 ...
TY - JOUR. T1 - Bony Changes of PKU Neonates Unrelated to Phenylalanine Levels. AU - Weisberg, Sanford. AU - Fisch, R O. AU - Fienberg, S. AU - Day, D. PY - 1991. Y1 - 1991. M3 - Article. VL - 14. SP - 890. EP - 895. JO - The American Journal of Diseases of Children. JF - The American Journal of Diseases of Children. ER - ...
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 ...
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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Bacteria that produce phenylalanine deaminase are able to remove the amino group from the amino acid phenylalanine yielding ammonia and phenylpyruvic acid
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 ...
PubMed Central Canada (PMC Canada) provides free access to a stable and permanent online digital archive of full-text, peer-reviewed health and life sciences research publications. It builds on PubMed Central (PMC), the U.S. National Institutes of Health (NIH) free digital archive of biomedical and life sciences journal literature and is a member of the broader PMC International (PMCI) network of e-repositories.
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 ...
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 ...
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 - Phenylalanine 4 hydroxylase or Phenylalanine hydroxylase is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine...
Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). Learn more about this test or book an appointment today.
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. ...
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
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 ...
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.
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 ...
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. ...
Dr. Anna Kate Shoveller received her PhD in Nutrition and Metabolism at the University of Alberta in 2004 and is currently an Assistant Professor in the Department of Animal Biosciences, University of Guelph. From 2007-2015 she was employed by Procter & Gamble and Mars Pet Care where she added to the knowledge of dog and cat nutrition through investigation in the areas of energy metabolism and nutrient budgets of dogs and cats using indirect calorimetry and applying the indicator amino acid oxidation technique to quantify amino acids requirements in adult dogs. Shoveller has taken this experience and returned to academia where she teaches companion animal nutrition and runs an active comparative nutrition research group. Overall, Shovellers laboratory focuses on optimizing nutrition across mammalian species for health and longevity without compromising the future of our food chain. She has published over 50 peer-reviewed papers, contributed to multiple book chapters, applied for multiple ...
TY - JOUR. T1 - Effects of tyrosine/phenylalanine depletion on electrophysiological correlates of memory in healthy volunteers. AU - Linssen, A.M.W.. AU - Riedel, W.J.. AU - Sambeth, A.. PY - 2011/2. Y1 - 2011/2. N2 - Dopamine is well known for involvement in reinforcement, motor control and frontal lobe functions, such as attention and memory. Tyrosine/phenylalanine depletion (TPD) lowers dopamine synthesis and can therefore be used as a model to study the effects of low dopamine levels. This is the first study to assess the effect of TPD on memory performance and its electrophysiological correlates. In a double blind placebo (PLA)-controlled crossover design, 17 healthy volunteers (six males, 11 females) aged between 18 and 25 were tested after TPD and PLA. Working memory was assessed using a Sternberg memory scanning task (SMS) and episodic memory using the Visual Verbal Learning Test (VVLT). Simultaneously, event-related potentials (ERPs) were measured. The tyrosine and phenylalanine ratio ...
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 ...
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. ...
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,...
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: a melanocortin-3 receptor agonist
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 ...
Tyrosine is a non-essential amino acid synthesized in the body from the essential amino acid phenylalanine. The typical dietary amount provided by a 3 oz portion of animal protein ranges from 0.3 g to 1 g of tyrosine. Tyrosine is the precursor amino acid from which the body makes dopamine (with vitamin B6 as a cofactor), which is then converted to norepinephrine (with vitamin C as a cofactor) and then to epinephrine (with SAMe as a cofactor).. Made with non-GMO ingredients.. ...
This form of the essential amino acid Phenylalanine is made of equal parts D (synthetic) and L (natural). DLPA activates endorphins which are hormones that trigger and intensify the bodys own natural painkilling ability. DLPA can inhibit enzymes that breakdown these endorphins and allow them to do their job by restori
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: Download citation file:. ...
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.. ...
TY - CHAP. T1 - Importance of Phenylalanine Residue in Tethered Peptide Ligand for Self-Activation of Thrombin Receptor. AU - Nose, Takeru. AU - Shimohigashi, Yasuyuki. AU - Ohno, Motonori. AU - Ogino, Yoshio. AU - Costa, Tommaso. PY - 1993/3. Y1 - 1993/3. M3 - Chapter (peer-reviewed). SP - 362. EP - 363. BT - Peptide Chemistry 1992. ER - ...
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,
Semantic Scholar extracted view of The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase. by Gordon Guroff et al.
AN INCREASING number of phenylketonuric infants are being fed a low-phenylalanine diet with the aim of preventing the development of mental retardation. Severe
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.
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.
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.. ...
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). ...
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 ...
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
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Erythrose 4-phosphate and phosphoenolpyruvate: phenylalanine, tyrosine, and tryptophan[edit]. Phenylalanine, tyrosine, and ... Tyrosine and phenylalanine are biosynthesized from prephenate, which is converted to an amino acid-specific intermediate. This ... Tyrosine is synthesized by the hydroxylation of phenylalanine, an essential amino acid. The pathways for the biosynthesis of ... Each one of these has its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively. The rest of the ...
... and state that the product contains phenylalanine. Phenylalanine is one of the essential amino acids and is required for normal ... Phenylalanine is converted to its methyl ester and combined with the N-formyl aspartic anhydride; then the protecting group is ... Aspartame is a methyl ester of the dipeptide of the natural amino acids L-aspartic acid and L-phenylalanine. Under strongly ... "Phenylalanine". PubChem, National Library of Medicine, US National Institutes of Health. 17 August 2019. Retrieved 23 August ...
L-Phenylalanine. a naturally occurring amino acid (equilibrium dissociation constant (KB) from Schild regression is 573 μM). ... "Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations ...
Kaufman S (1962). "Phenylalanine hydroxylase". Methods Enzymol. 5: 809-816. doi:10.1016/s0076-6879(62)05317-3. Lind KE ( ... a controlled diet which is lacking in phenylalanine, well as supplementation of L-DOPA. Sepiapterin reductase Longo N (June ...
Phenylalanine Ergocornine. CH(CH3)2. CH(CH3)2. Valine alpha-Ergocryptine. CH(CH3)2. CH2CH(CH3)2. Leucine ...
Phenylalanine. 0.959 g. Tyrosine. 0.796 g. Valine. 1.199 g. Arginine. 1.545 g. ...
Phenylalanine. 0.713 g. Tyrosine. 0.454 g. Valine. 0.730 g. Arginine. 2.086 g. ...
Phenylalanine. 1.120 g. Tyrosine. 0.452 g. Valine. 0.817 g. Arginine. 2.446 g. ...
Phenylalanine. 0.497 g. Tyrosine. 0.381 g. Valine. 0.701 g. Arginine. 1.516 g. ...
Phenylalanine. 1.447 g. Tyrosine. 1.263 g. Valine. 1.777 g. Arginine. 4.550 g. ...
Phenylalanine. 0.668 g. Tyrosine. 0.513 g. Valine. 0.767 g. Arginine. 0.755 g. ...
Like all protein-rich foods, spirulina contains the essential amino acid phenylalanine (2.6-4.1 g/100 g),[5] which should be ... avoided by people who have phenylketonuria, a rare genetic disorder that prevents the body from metabolizing phenylalanine, ...
Phenylalanine. 0.102 g. Tyrosine. 0.067 g. Valine. 0.135 g. Arginine. 0.173 g. ...
Phenylalanine no change. Phenylalanine. Normal protein, normal function A point mutation causing a nonsynonymous substitution ... For example, the DNA codons TTT and TTC both code for the amino acid Phenylalanine, so a change from the third T to C makes no ...
Phenylalanine. 0.681 g. Tyrosine. 0.678 g. Valine. 0.949 g. Arginine. 1.099 g. ...
Phenylalanine. 0.169 g. Tyrosine. 0.103 g. Valine. 0.202 g. Arginine. 0.546 g. ...
Phenylalanine. 0.542 g. Tyrosine. 0.329 g. Valine. 0.679 g. Arginine. 1.060 g. ...
Phenylalanine MKHIPFFFAFFFTFP stop Lactis-leu-phe leader RNA motif Attenuation in eukaryotes[edit]. Research conducted on ... A similar attenuation mechanism regulates the synthesis of histidine, phenylalanine and threonine. ...
Phenylalanine Phe F MT-TF 577-647 L Proline Pro P MT-TP 15,956-16,023 H ...
May 2008). "Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and ... The 2,5-cyclohexene ring becomes a phenyl ring, and L-phenylalanine is formed. Certain forms of ADT have been shown to exhibit ... The systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in ... Arogenate dehydratase (ADT) (EC is an enzyme that catalyzes the chemical reaction L-arogenate → L-phenylalanine + H2O ...
Infants with PKU appear normal at birth, but are unable to metabolize the essential amino acid phenylalanine, resulting in ... Mitchell, J. J.; Trakadis, Y. J.; Scriver, C. R. (2011). "Phenylalanine hydroxylase deficiency". Genetics in Medicine. 13 (8): ... to measure phenylalanine levels in blood samples obtained by pricking a newborn baby's heel on the second day of life on filter ... Robert Guthrie developed a simple method using a bacterial inhibition assay that could detect high levels of phenylalanine in ...
... contains phenylalanine". In Canada, the ingredient listing reads: "carbonated water, caramel color, phosphoric acid, aspartame ... contains a source of phenylalanine". The initial formulation of Diet Pepsi was sweetened with the artificial sweetener ... 124 mg/355 ml, contains phenylalanine), sodium benzoate, caffeine, flavor, acesulfame potassium (32 mg/355ml), citric acid, ...
This compound on reduction gives access to phenylalanine. Variants of the azlactone synthesis in which analogues of azlactones ... "dl-β-Phenylalanine". Organic Syntheses.; Collective Volume, 2, p. 489 Alfred Hassner, Irishi Namboothiri (2011). Organic ...
Aspartame contains phenylalanine.) In addition to the standard lemon-lime flavor, Sprite Zero Sugar is also available in cherry ...
Phenylketonurics: Contains phenylalanine. Orange 7 Up: This flavor was available for a short time in Norway during the mid- ...
Mitchell, J. J.; Trakadis, Y. J.; Scriver, C. R. (2011). "Phenylalanine hydroxylase deficiency". Genetics in Medicine. 13 (8): ...
The enzyme phenylalanine hydroxylase normally converts the amino acid phenylalanine into the amino acid tyrosine. If this ... If phenylalanine is in excess in the blood, it will saturate the transporter. Excessive levels of phenylalanine tend to ... then phenylalanine levels in the blood will increase over time. Toxic levels of phenylalanine (and insufficient levels of ... are caused by a mutated gene for the enzyme phenylalanine hydroxylase (PAH), which converts the amino acid phenylalanine ("Phe ...
Phenylalanine Deaminase Negative Eosin-methylene blue Positive Glucose Fermentation Acid/Gas Lactose Fermentation Acid/Gas ...
phenylalanine ditbdms. 107715-95-7 C21H40. 4-nonylbicyclohexyl. 95135-87-8 ...
N-formylmethionine-leucyl-phenylalanine); b) complement components C5a and C3a which are chemotactic factors formed during the ...
phenylalanine (fĕn´əlăl´ənēn´), organic compound, one of the 22 α-amino acids [1] commonly found in animal proteins. Only the l ... phenylalanine An aromatic, non-polar amino acid.. Cite this article Pick a style below, and copy the text for your bibliography ... phenylalanine (fĕn´əlăl´ənēn´), organic compound, one of the 22 α-amino acids commonly found in animal proteins. Only the l- ... phenylalanine (fee-nyl-al-ă-neen) n. an essential amino acid that is readily converted to tyrosine. Blockade of this metabolic ...
... is enantiomer of D-phenylalanine (CHEBI:16998) L-phenylalanine (CHEBI:17295) is tautomer of L- ... L-phenylalanine (CHEBI:17295) is a phenylalanine (CHEBI:28044) L-phenylalanine (CHEBI:17295) is a proteinogenic amino acid ( ... D-phenylalanine (CHEBI:16998) is enantiomer of L-phenylalanine (CHEBI:17295). L-phenylalanine residue (CHEBI:29997) is ... L-phenylalanine (CHEBI:17295) has role plant metabolite (CHEBI:76924) L-phenylalanine (CHEBI:17295) is a L-α-amino acid (CHEBI: ...
Phenylalanine, an amino acid present in the mixture obtained upon hydrolysis of common proteins. Human hemoglobin (the oxygen- ... to lack of the enzyme phenylalanine hydroxylase, so that phenylalanine is converted not to tyrosine but to phenylpyruvic acid. ... Phenylalanine, an amino acid present in the mixture obtained upon hydrolysis of common proteins. Human hemoglobin (the oxygen- ... More About Phenylalanine. 11 references found in Britannica articles. Assorted References. *amino acids* In human nutrition: ...
... is enantiomer of D-phenylalanine zwitterion (CHEBI:57981) L-phenylalanine zwitterion ( ... D-phenylalanine zwitterion (CHEBI:57981) is enantiomer of L-phenylalanine zwitterion (CHEBI:58095). L-phenylalanine (CHEBI: ... CHEBI:58095 - L-phenylalanine zwitterion. Main. ChEBI Ontology. Automatic Xrefs. Reactions. Pathways. Models. ... An amino acid zwitterion arising from transfer of a proton from the carboxy to the amino group of L-phenylalanine; major ...
The test detects abnormally high levels of an amino acid called phenylalanine. ... Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). ... Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). The test detects ... The test paper is taken to the laboratory, where it is mixed with a type of bacteria that needs phenylalanine to grow. Another ...
Other names: DL-«beta»-Phenylalanine; «beta»-Phenylalanine, dl-; (.+/-.)-Phenylalanine; Alanine, phenyl-, DL-; DL-«alpha»-Amino ... beta»-phenylpropionic acid; DL-«beta»-Phenyl-«alpha»-alanine; DL-2-Amino-3-phenylpropanoic acid; DL-3-Phenylalanine; DLPA; 2- ...
FDAs Bacteriological Analytical Manual (the BAM) is the agencys preferred laboratory procedures for the detection in food and cosmetic products of pathogens (bacterial, viral, parasitic, plus yeast and mold) and of microbial toxins. The complete BAM is now available online and will be updated as needed.
Neurotransmitter deficiency disorders with normal blood phenylalanine levels span an increasingly complex spectrum of clinical ... an oral phenylalanine load, with serial serum phenylalanine levels over the following four to six hours, can help confirm the ... can be shown to have abnormal phenylalanine metabolism if stressed by administration of an oral phenylalanine load (100 mg/kg ... Phenylalanine loading is also valuable in confirming a suspected diagnosis, but is not specific to the disorder, as PKU ...
Categories Supplements Amino Acids Phenylalanine Categories Health Topics Depression Phenylalanine Categories Health Topics ...
Brands A-Z Source Naturals L-Phenylalanine Categories Supplements Amino Acids L-Phenylalanine ... Source Naturals, L-Phenylalanine 3 Results (showing 1 - 3) Visit Manufacturers Website » ...
Brands A-Z Now Foods L-Phenylalanine Categories Supplements Amino Acids L-Phenylalanine ... Now Foods, L-Phenylalanine 1 Results (showing 1 - 1) Visit Manufacturers Website » ...
The preparation of phenylalanine from cinnamic acid using immobilized cells having phenylalanine ammonia lyase activity is also ... A process is disclosed for preparing phenylalanine which comprises contacting phenylpyruvic acid or phenylpyruvate with ... The preparation of phenylalanine from cinnamic acid using immobilized cells having phenylalanine ammonia lyase activity is also ... 16) reviewed the production of phenylalanine from precursor keto acids. He noted a maximum yield of 63.5% phenylalanine was ...
This article reviews the benefits, side effects and food sources of phenylalanine. ... Phenylalanine is an amino acid used by your body to produce proteins and important molecules. ... What Is Phenylalanine?. Share on Pinterest. Phenylalanine is an amino acid, which are the building blocks of proteins in your ... This molecule exists in two forms or arrangements: L-phenylalanine and D-phenylalanine. Theyre nearly identical but have a ...
Dansyl-L-phenylalanine; CAS Number: 1104-36-5; EC Number: 214-165-3; Linear Formula: C21H22N2O4S; find Sigma-Aldrich-D1750 MSDS ...
Three isozymes of phenylalanine hydroxylase exist in adult rat liver. They are chromatographically unique. Partial ...
DL-Phenylalanine is a mixture of D-phenylalanine and L-phenylalanine. The reputed analgesic activity of DL-phenylalanine may be ... A small amount of D-phenylalanine appears to be converted to L-phenylalanine. D-Phenylalanine is distributed to the various ... Lignan is derived from phenylalanine and from tyrosine. Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ... who must ingest phenylalanine or phenylalanine-containing proteins. The first description of phenylalanine was made in 1879, ...
Phenylalanine , C9H11NO2 , CID 6140 - structure, chemical names, physical and chemical properties, classification, patents, ...
Types of phenylalanine. Phenylalanine is normally presented in three ways:. - L-Phenylalanine: The most common in food and that ... More information: Foods rich in phenylalanine. Poor foods in phenylalanine. Foods that contain little phenylalanine are fruits ... Properties of phenylalanine. Photo of a label of sweetener aspartame. The label reads: "Contains phenylalanine", so it is not ... What is phenylalanine?. Phenylalanine is an essential amino acid that the body can not synthesize and therefore must be ...
Learn more about PHENYLALANINE uses, effectiveness, possible side effects, interactions, dosage, user ratings and products that ... D-phenylalanine, L-phenylalanine, and the mix made in the laboratory called DL-phenylalanine. D-phenylalanine is not an ... Beta-phenyl-alanine, Bêta-phenyl-alanine, DLPA, D-Phenylalanine, D-Phénylalanine, DL-Phenylalanine, DL-Phénylalanine, D,L- ... L-Phenylalanine, L-Phénylalanine, Phenylalanine Ethyl Ester HCl, Phenylalanine Isovaleric Acid, Phenylalanine Methyl Ester HCl ...
Phenylalanine 4-monooxygenase definition at, a free online dictionary with pronunciation, synonyms and ...
Phenylalanine, a naturally occurring amino acid, is not present in chewing gum products on its own. Instead, it comes from the ... What are some of the dangers of phenylalanine?. A: As of 2015, while normal amounts of phenylalanine in foods are likely safe, ... How does phenylalanine in gum affect your health?. A: For individuals suffering from phenylketonuria, a genetic inability to ... Phenylalanine, a naturally occurring amino acid, is not present in chewing gum products on its own. Instead, it comes from the ...
A definition of the medical term "phenylalanine" is presented. Phenylalanine is an essential amino acid and is one of the two ... A definition of the term "hyperphenylalaninemia" is presented, which refers to an increased amount of phenylalanine in the ...
L-phenylalanine L-Phenylalanine L-phenylalanine L-Phenylalanine L-phenylalanine phenylalanine Phe PHENYLALANINE β-phenyl-L- ... PHENYLALANINE PubChem Notes: Phenylalanine An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; ...
DL-phenylalanine (50/50 blend of D-phenylalanine and L-phenylalanine) You can take phenylalanine as a capsule, powder, or ... L-phenylalanine, the natural form found in proteins. *D-phenylalanine (a mirror image of L-phenylalanine that is made in a ... DL-phenylalanine, a combination of the 2 forms The body changes phenylalanine into tyrosine, another amino acid that is needed ... Phenylalanine. Overview. Phenylalanine is an essential amino acid (a building block for proteins in the body), meaning the body ...
Find treatment reviews for L-Phenylalanine from other patients. Learn from their experiences about effectiveness, side effects ...
N-adenylyl-L-phenylalanine Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are ... L-phenylalanine adenylyltransferase. This enzyme is also called L-phenylalanine adenylyltransferase. Lerbs W, Luckner M (1985 ... In enzymology, a phenylalanine adenylyltransferase (EC is an enzyme that catalyzes the chemical reaction ATP + L- ... diphosphate and N-adenylyl-L-phenylalanine. This enzyme belongs to the family of transferases, specifically those transferring ...
Phenylalanine, Phenylalanine, L-Phenylalanine, 63-91-2, C6H5CH2CH(NH2)COOH. ... L-Phenylalanine is an antagonist at ?2? calcium channels with a Ki of 980 nM. MedChem Express HY-N0215. ... odourless Food and Agriculture Organization of the United Nations L-Phenylalanine. ...
Mutations in the phenylalanine hydroxylase (PAH) gene cause PAH deficiency with various phenotypes. A new hyperphenylalaninemia ... Mutations in the phenylalanine hydroxylase (PAH) gene cause PAH deficiency with various phenotypes. A new hyperphenylalaninemia ... The molecular basis of phenylalanine hydroxylase deficiency: Increasing evidence for a complex trait. *Gersting S ...
  • Phenylalanine can be degraded into simpler compounds by the enzymes of the body and is readily converted to the amino acid tyrosine . (
  • Phenylketonuria (PKU), an inherited disease that, if left untreated, results in retarded mental development in children, has been shown to be associated with the lack of activity of the enzyme that converts phenylalanine to tyrosine. (
  • Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin. (
  • For phenylalanine plus tyrosine, for adults 19 years and older, 33 mg/kg body weight/day. (
  • L-Phenylalanine is biologically converted into L-tyrosine, another one of the DNA-encoded amino acids. (
  • Lignan is derived from phenylalanine and from tyrosine. (
  • Summary Phenylalanine can be converted to the amino acid tyrosine, which is then used to produce important signaling molecules. (
  • Phenylalanine is a precursor of tyrosine , an amino acid involved in the production of neurohormones and some chemicals such as norepinephrine, tyramine, epinephrine, dopamine, thyroxine, or cholecystokinin (CCK). (
  • Phenylalanine and tyrosine are essential to produce thyroxine, a hormone responsible for the proper functioning of the thyroid gland , which controls the body's metabolism . (
  • People with cancer should avoid this amino acid supplement without medical advice, especially if suffering melanoma (Phenylalanine is degraded into tyrosine, which in turn stimulates the synthesis of melanin and may affect skin cancer). (
  • An enzyme that catalyzes the oxidation of phenylalanine to tyrosine. (
  • The body changes phenylalanine into tyrosine, another amino acid that is needed to make proteins and brain chemicals, including L-dopa, epinephrine, norepinephrine, and thyroid hormones. (
  • People with PKU must eat a diet that avoids phenylalanine and take tyrosine supplements for optimal brain development and growth. (
  • As a building block of protein, phenylalanine is changed into tyrosine that helps the brain stay balanced. (
  • Determination of Phenylalanine and Tyrosine by Liquid Chromatogra. (
  • Throughout life, they must control their blood levels of phenylalanine ( Phe ) and consume a diet containing adequate amounts of Phe and tyrosine ( Tyr ). (
  • Phenylketonuria (PKU) is a rare autosomal recessive disorder caused by deficiency of the phenylalanine hydroxylase enzyme leading to an impaired conversion of the amino acid phenylalanine (Phe) to tyrosine. (
  • Phenylalanine is converted to the nonessential amino acid tyrosine, then to dihydroxyphenylalanine (DOPA). (
  • Tetrahydrobiopterin is required to convert phenylalanine to tyrosine, but it is also required to convert tyrosine to DOPA which in turn is converted to dopamine. (
  • If a person cannot convert phenylalanine to tyrosine, and tyrosine into DOPA, because of the lack of PAH or BH 4 then they will have difficulty in producing dopamine in the correct amounts, as there will be insufficient DOPA in their system. (
  • The aromatic amino acids tryptophan, phenylalanine, and tyrosine are important as precursors of 5-hydroxytryptamine (5-HT) and the catecholamines. (
  • The purpose of this chapter is to follow tryptophan, phenylalanine, and tyrosine from the diet through the periphery to the brain, to review some of the metabolic processes that occur there, and to indicate to some extent what the significance of these processes may be. (
  • EC ), the enzyme catalyzing conversion of the essential amino acid nutrient phenylalanine to tyrosine. (
  • It is inherited in an autosomal recessive manner and is caused by a defect in the enzyme phenylalanine hydroxylase (PAH), which converts the essential amino acid phenylalanine to tyrosine. (
  • Deficiency of PAH results in decreased levels of tyrosine and an accumulation of phenylalanine in blood and tissues. (
  • Tyrosine is a nonessential amino acid that derives from dietary sources, the hydroxylation of phenylalanine, or protein breakdown. (
  • Measurement of the phenylalanine:tyrosine ratio is helpful in monitoring appropriate dietary intake. (
  • The quantitative results of phenylalanine and tyrosine with age-dependent reference values are reported without added interpretation. (
  • The shikimate pathway provides carbon skeletons for the aromatic amino acids L -tryptophan, L -phenylalanine, and L -tyrosine. (
  • Kuvan is the synthetic form of 6R-BH4, a naturally occurring co-factor that works in conjunction with the enzyme phenylalanine hydroxylase (PAH) to metabolize phenylalanine into tyrosine. (
  • As a precursor to the amino acid tyrosine‚ l-Phenylalanine may end up increasing levels of some important neurotransmitters. (
  • Phenylalanine is used to form tyrosine. (
  • Because your body can't reconvert tyrosine to phenylalanine, you must get this nutrient amino from your diet. (
  • This is because L-phenylalanine is utilized by the body to produce L-tyrosine, a biochemical precursor in the synthesis of the neurotransmitters, epinephrine, norepinephrine and dopamine, and the skin pigment melanin. (
  • No such association existed between neopterin and tyrosine concentrations (r (s) = -0.018), but neopterin concentrations correlated to the phenylalanine to tyrosine ratio (r (s) = 0.328, p = 0.001). (
  • This assumption is further supported by the correlation found between higher neopterin concentrations and higher phenylalanine to tyrosine ratio, which estimates efficacy of PAH. (
  • L-phenylalanine can be converted to L-tyrosine and subsequently to L-dopa, norepinephrine , and epinephrine. (
  • D-phenylalanine (DPA) is not normally found in the body and cannot be converted to L-tyrosine, L-dopa, or norepinephrine . (
  • Both low blood pressure and elevated blood pressure have been normalized by administration of therapeutic doses of phenylalanine and tyrosine to animals. (
  • Phenylalanine can be converted to tyrosine by way of an enzyme called phenylalanine hydroxylase. (
  • Like tyrosine, phenylalanine is a precursor for the formation of neurotransmitters such as dopamine, epinephrine and norepinephrine as well as tyramine and the very important catecholamine. (
  • An enzyme of the oxidoreductase class that catalyzes the formation of L-TYROSINE, dihydrobiopterin, and water from L-PHENYLALANINE, tetrahydrobiopterin, and oxygen. (
  • which catalyzes the conversion of phenylalanine to tyrosine) and thus lead to elevated phenylalanine levels and reduced tyrosine levels. (
  • Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). (
  • The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase. (
  • Lab results may report phenylalanine levels using either mg/dL and μmol/L. One mg/dL of phenylalanine is approximately equivalent to 60 μmol/L. A (rare) "variant form" of phenylketonuria called hyperphenylalaninemia is caused by the inability to synthesize a cofactor called tetrahydrobiopterin, which can be supplemented. (
  • Warning labels on chewing gum that indicate the presence of phenylalanine are there for the benefit of some people whose bodies cannot easily digest the chemical due to a disease called phenylketonuria. (
  • The label reads: "Contains phenylalanine", so it is not suitable for phenylketonuria. (
  • A diet rich in foods that contain lots phenylalanine are not suitable for people with phenylketonuria. (
  • For pregnant patients who have high levels of phenylalanine, such as those with a condition called phenylketonuria (PKU), even normal food amounts are UNSAFE . (
  • For individuals suffering from phenylketonuria, a genetic inability to digest phenylalanine, chewing gum containing aspartame can lead to serious side effe. (
  • On the other hand, a rare metabolic disorder called phenylketonuria (PKU) occurs in people who are missing an enzyme that the body needs to use phenylalanine. (
  • People with phenylketonuria (PKU), and women who are breastfeeding or are pregnant, should not take phenylalanine supplements. (
  • Those born with a disorder known as PKU, or phenylketonuria, have a buildup of phenylalanine due to a metabolic predisposition that prevents them from using it for energy. (
  • L-phenylalanine may induce severe side effects in people who have a medical condition called phenylketonuria. (
  • Phenylketonuria, also called PKU, is an inherited genetic condition that prevents the body from synthesizing the enzyme required to break down phenylalanine. (
  • Mutations of the phenylalanine hydroxylase gene in Iranian patients with phenylketonuria. (
  • Phenylketonuria (PKU) is an autosomal recessive disease which results from mutations in the phenylalanine hydroxylase (PAH) gene. (
  • Phenylalanine is dangerous to those born with phenylketonuria (PKU), an inherited disease that stops phenylalanine from being dealt with properly in the body. (
  • a deficiency of either phenylalanine 4-monooxyenase or dihydropteridine reductase will result in phenylketonuria. (
  • 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). (
  • People with phenylketonuria must not supplement phenylalanine . (
  • People who have with phenylketonuria (PKU, a condition in which the body cannot break down phenylalanine) should follow a strict phenylalanine-restricted diet. (
  • Phenylalanine has been studied for phenylketonuria, with negative effects reported in terms of mood and brain function. (
  • Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. (
  • The preparation of phenylalanine from cinnamic acid using immobilized cells having phenylalanine ammonia lyase activity is also disclosed. (
  • 16. A process for preparing phenylalanine which comprises contacting cinnamic acid with immobilized cells having phenylalanine ammonia lyase actibity, said cells being immobilized with a polyazetidine polymer. (
  • It was our purpose to investigate the localization of the key phenylpropanoid enzyme, phenylalanine ammonia-lyase, within the tapetum and the other anther tissues. (
  • Phenylalanine ammonia-lyase (PAL) catalyzes the first step in phenylpropanoid synthesis. (
  • Source Naturals DL-Phenylalanine, or DLPA, is a 50/50 blend of the D- and L- forms of the amino acid phenylalanine (phenylalanine is one of the few amino acids that can be utilized in its D- form). (
  • It was discovered that d- and dl-Phenylalanine (DLPA), but not l-Phenylalanine, inhibit several of the enzymes responsible for endorphin destruction. (
  • Has anyone here tried DL- Phenylalanine (DLPA) ? (
  • The DL-Phenylalanine (DLPA) is a combination of the D and L forms of the amino acid‚ Phenylalanine. (
  • Classical PKU is caused by a mutated gene that deals with the creation of the enzyme phenylalanine hydroxylase (PAH). (
  • phenylalanine (fĕn´əlăl´ənēn´) , organic compound, one of the 22 α- amino acids commonly found in animal proteins. (
  • Phenylalanine contributes to the structure of proteins into which it has been incorporated by the tendency of its side chain to participate in hydrophobic interactions (see isoleucine ). (
  • Phenylalanine , an amino acid present in the mixture obtained upon hydrolysis of common proteins . (
  • As an essential amino acid, phenylalanine is not synthesized de novo in humans and other animals, who must ingest phenylalanine or phenylalanine-containing proteins. (
  • Phenylalanine is an amino acid found in many foods and used by your body to produce proteins and other important molecules. (
  • Phenylalanine is an amino acid, which are the building blocks of proteins in your body . (
  • Summary Phenylalanine is an essential amino acid that is used to produce proteins and signaling molecules. (
  • Your body needs phenylalanine and other amino acids to make proteins. (
  • It is the only form of phenylalanine found in proteins. (
  • Phenylalanine is an essential amino acid (a building block for proteins in the body), meaning the body needs it for health but cannot make it. (
  • Phenylalanine is a type of amino acid that your body uses to generate proteins and certain types of chemicals in the brain. (
  • Phenylalanine is a building block that the body uses to make proteins. (
  • L-phenylalanine is an essential amino acid used by cells to synthesize proteins. (
  • L-phenylalanine (LPA) serves as a building block for the various proteins that are produced in the body. (
  • L-phenylalanine is an essential amino acid in humans, and proteins contain only this form. (
  • Phenylalanine, a proteinogenic amino acid, contributes to the formation of important endogenous proteins, hormones and neurotransmitters , which include insulin, papain, tryptophan, the thyroid hormone thyroxine and the skin pigment melanin. (
  • There are three forms of phenylalanine: D-phenylalanine, L-phenylalanine, and the mix made in the laboratory called DL-phenylalanine. (
  • Because norepinephrine affects mood, different forms of phenylalanine have been proposed to treat depression. (
  • When phenylalanine was examined in the treatment of depression, Tufts Medical Center reports, both D and DL forms of phenylalanine were shown to be as effective as the antidepressant imipramine. (
  • Select studies have shown that L-Phenylalanine is potentially a precursor to dopamine and other related neurotransmitters‚ while the D- Phenylalanine may possibly slow the metabolic breakdown of endogenous opioids‚ thus encouraging an alert state. (
  • Phenylalanine serves in the body as a precursor to the catecholamine family of hormones. (
  • Other studies have reported that adding phenylalanine supplements to ultraviolet (UV) light exposure may improve skin pigmentation in individuals with this condition ( 13 , 14 ). (
  • Pregnant women or people suffering from liver and kidney should not take phenylalanine supplements. (
  • Phenylalanine supplements, in any form, should NOT be taken for more than two or three consecutive weeks . (
  • Phenylalanine supplements may raise blood pressure by its stimulating production role of epinephrine and norepinephrine, so that is not recommended for people with hypertension , or people with a family history of hypertension. (
  • In case of illness should avoid taking supplements of phenylalanine or other amino acid without medical supervision. (
  • For patients who process phenylalanine normally and have normal levels, it is probably fine to get the amount of phenylalanine found in food, but supplements should be avoided. (
  • For example, Life Extension, a neutraceutical company, promotes the use of DL-phenylalanine supplements to block pain receptors in the brain, to initiate the body's own analgesic processes and to reduce inflammation. (
  • According to University of Maryland Medical Center, the two known studies that examined the role of D-phenylalanine supplements for pain were positive in their results but lacked scientific reliability. (
  • Pigmentation disorders such as vitiligo, or patches of white skin and discoloration, may also benefit from the use of phenylalanine supplements. (
  • Additional side effects may occur following treatment with supplements that contain DL-phenylalanine. (
  • Children receiving DL-phenylalanine supplements may appear unusually hyperactive or anxious, UMMC reports. (
  • Treatment may include administration of BH4, L-dopa (and carbidopa) 5-hydroxytryptophan supplements, and a low phenylalanine diet. (
  • Avoid using phenylalanine supplements, and reduce high-phenylalanine containing foods like meat and dairy products if you have lupus. (
  • the metabolism of aspartame produces phenylalanine as one of the compound's metabolites. (
  • medical citation needed] A non-food source of phenylalanine is the artificial sweetener aspartame. (
  • The breakdown problems phenylketonurics have with the buildup of phenylalanine in the body also occurs with the ingestion of aspartame, although to a lesser degree. (
  • Several countries require indicating the presence of phenylalanine in gums that have been sweetened with aspartame. (
  • Phenylalanine is an essential amino acid and is one of the two linked amino acids in the sugar substitute Aspartame. (
  • The artificial sweetener aspartame is also high in phenylalanine. (
  • Aspartame, found in artificial sweeteners such as Nutrasweet, is a source of phenylalanine. (
  • ADHD and PKU linked through Phenylalanine and Aspartame? (
  • This article looks at a possible link of ADHD with Aspartame, a disease known as PKU and the effects of chemical processes involved with phenylalanine. (
  • Upon ingestion, aspartame breaks down into its components, including phenylalanine and methanol. (
  • Thus the higher level of phenylalanine from the aspartame triggers the worse hyperactive state, but eventually returns to the (normal but high)level as it is slowly converted and made into dopamine. (
  • The sweetener aspartame contains phenylalanine as part of its chemical makeup. (
  • Neurotransmitter deficiency disorders with normal blood phenylalanine levels span an increasingly complex spectrum of clinical phenotypes, ranging from ataxia and mental retardation to spastic diplegia to exercise-induced dystonia. (
  • Mutations in the phenylalanine hydroxylase (PAH) gene cause PAH deficiency with various phenotypes. (
  • Normally inherited defects in BH4 metabolism are detected at the time of newborn screening, as BH4 is also required for the activity of phenylalanine hydroxylase in the liver and a deficiency of the cofactor leads to hyperphenylalaninemia (14). (
  • 4]] Kuvan is indicated in patients of all ages with tetrahydrobiopterin (BH4) deficiency, and in those aged 4 years and above with PKU (due phenylalanine hydroxylase enzyme deficiency) who are responsive to Kuvan. (
  • PKU is caused by a deficiency of hepatic phenylalanine hydroxylase (1). (
  • Although rare, individuals whose diets are very low in protein may develop a deficiency of L-phenylalanine. (
  • Very limited evidence suggests that phenylalanine may be beneficial in treating Parkinson's disease, but more studies are needed ( 24 ). (
  • In addition to its role in protein production, phenylalanine is used to make other important molecules in your body, several of which send signals between different parts of your body ( 6 ). (
  • Phenylalanine is an amino acid , a "building block" of protein. (
  • The two remaining forms, L-phenylalanine from protein food sources and DL-phenylalanine, which is a combination of the synthetic and protein food source, have not been thoroughly evaluated. (
  • In addition, two closed ligand-bound structures of the same protein are presented, a phenylalanine-bound form at 1.8 A and a leucine-bound structure at a nominal resolution of 2.4 A. These structures show the basis of this protein's ligand specificity, as well as illustrating the conformational changes that are associated with ligand binding. (
  • We show that the protein lacking this N-terminal sequence does not require activation by phenylalanine, shows an altered structural response to phenylalanine, and is not inhibited by BH(4). (
  • Phenylalanine plays a key role in the biosynthesis of other amino acids and some neurotransmitters. (
  • Phenylalanine ammonialyase (PAL) catalyzes the first step in the biosynthesis of phenylpropanoids, and is usually encoded by a multi-gene family. (
  • 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. (
  • Valine and phenylalanine as precursors in the biosynthesis of alkamides in Acmella radicans. (
  • 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. (
  • This results in the buildup of phenylalanine in the blood, an event leading to several pathological consequences. (
  • Phenylalanine uses the same active transport channel as tryptophan to cross the blood-brain barrier. (
  • Phenylalanine cooperates, along with tryptophan in appetite control . (
  • Phenylalanine is known to be the antagonist of tryptophan. (
  • Whereas tryptophan has been used to induce sleep, phenylalanine has been used to increase states of arousal. (
  • After all baseline measurements were recorded, the participants were randomized to ingest either the phenylalanine capsules or a placebo-an empty cellulose capsule made by Matsutani-with a cup of tap water. (
  • Wheat germs, pumpkin seeds, walnuts and whole grain products contain phenylalanine as well. (
  • PAH is needed to process phenylalanine, although other, non-PAH gene mutations can also cause PKU. (
  • Some research suggests that tardive dyskinesia patients may process phenylalanine abnormally. (
  • Phenylalanine has been studied as a treatment for several medical conditions, including skin disorders, depression and pain ( 3 ). (
  • 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 ). (
  • Thus, food intake with phenylalanine may help reduce the symptoms of depression and Alzheimer's . (
  • Limited clinical research performed in the 1970s and 1980s suggests L-phenylalanine or DL-phenylalanine might be useful for depression . (
  • Taking D-phenylalanine does not appear to improve symptoms of depression . (
  • One animal study suggests that D-phenylalanine may improve rigidity, walking disabilities, speech difficulties, and depression associated with Parkinson disease. (
  • 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. (
  • More research is needed to tell whether phenylalanine has any real effect on depression. (
  • 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. (
  • 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. (
  • DL-Phenylalanine is used to relieve cases of minor depression and other mood issues as well as and physical discomforts and pain. (
  • Phenylalanine can affect depression via three separate pathways. (
  • Therapeutic doses of phenylalanine may have useful roles in the management of blood pressure disorders and the control of certain forms of depression. (
  • Depression is a common use for L-phenylalanine or DL-phenylalanine. (
  • L-phenylalanine has been found to improve mood in people who have major depression. (
  • DL-phenylalanine and D-phenylalanine have also been studied for depression, although the results are unclear. (
  • Phenylalanine can be used to produce the molecule dopamine . (
  • Researchers think this is because phenylalanine increases production of brain chemicals, such as dopamine and norepinephrine. (
  • Phenylalanine is transformed into norepinephrine in the body through a variety of metabolic steps, as well as to other active chemicals, such as epinephrine, dopamine, and tyramine. (
  • 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. (
  • The test detects abnormally high levels of an amino acid called phenylalanine. (
  • 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. (
  • Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula C 9H 11NO 2. (
  • Phenylalanine, a naturally occurring amino acid, is not present in chewing gum products on its own. (
  • 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. (
  • 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. (
  • 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. (
  • 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. (
  • 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 ). (
  • This amino acid is produced directly from phenylalanine. (
  • Phenylalanine is an essential amino acid that the body can not synthesize and therefore must be provided by the diet. (
  • D-phenylalanine is not an essential amino acid. (
  • L-phenylalanine is an essential amino acid. (
  • Phenylalanine is an essential amino acid that must be supplemented through diet. (
  • D-phenylalanine is a synthetic form of this amino acid created in a laboratory. (
  • and DL-phenylalanine, a combination of the first two forms of this amino acid. (
  • It is made by our bodies from phenylalanine, which is an essential amino acid and must be consumed daily. (
  • 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. (
  • 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. (
  • PAL, a robust enzyme without need for a cofactor, converts phenylalanine to trans-cinnamic acid, a harmless metabolite. (
  • 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. (
  • 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. (
  • 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. (
  • 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. (
  • The aim of this research is to investigate the inhibitive effect of amino acid such as DL-phenylalanine. (
  • C9H11NO2 amino acid Phenylalanine molecule isolated on white. (
  • 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. (
  • 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. (
  • 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. (
  • Present treatment relies on the observation that a (semisynthetic) diet low in phenylalanine ( 3 - 5 ) will prevent HPA and thus the disease. (
  • Treatment includes the early introduction of a diet low in phenylalanine. (
  • Preliminary studies suggest that L-phenylalanine (oral and topical) strengthens the effect of UVA radiation for people with vitiligo. (
  • 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. (
  • 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). (
  • 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. (
  • L-phenylalanine is LIKELY SAFE when consumed in amounts commonly found in foods by pregnant patients who have normal phenylalanine levels. (
  • If PKU is not detected early, increasing phenylalanine levels in the baby will cause intellectual disability. (
  • Phenylalanine is found in many foods and generally does not warrant supplementation except in special circumstances. (
  • This led the researchers to hypothesize that glucagon secretion following phenylalanine supplementation may lead to fat oxidation. (
  • Until more is known, it makes sense for people with this condition to avoid phenylalanine supplementation. (
  • Contraindications of phenylalanine supplementation are in those individuals who display a hyper-functioning nervous state (anxiety) that may be aggravated by adrenaline. (
  • Supplementation with phenylalanine in these people can actually amplify the problem. (
  • Phenylalanine supplementation should be discontinued if headaches result. (
  • You can take phenylalanine as a capsule, powder, or tablet. (
  • 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. (
  • The capsule of phenylalanine came from ingredient manufacturer Kyowa Hakko, which is owned by the beverage giant Kirin Holdings. (
  • At the recommended dosage‚ each 90-capsule bottle of Pure Encapsulations' dl-Phenylalanine should last for about 15 to 22 days. (
  • Douglas Labs L-Phenylalanine 90 caps supplies 500 mg of pure L-Phenylalanine in each capsule. (
  • 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. (
  • Limited research suggests taking D-phenylalanine might decrease symptoms of Parkinson disease. (
  • Research database Health Notes Online suggests the use of L-phenylalanine while patients are undergoing ultraviolet radiation therapy. (
  • Certain researchers suggests the possibility that D-Phenylalanine may inhibit the action of enzymes that break down endorphins (the feel-good hormone) and enkephalins. (
  • The MP Diagnostics ImmuChem Phenylalanine ELISA Kit is designed for the quantitative determination of phenylalanine in neonatal blood spots. (
  • Phenylalanine hydroxylase is an enzyme involved in the metabolism of phenylalanine (Phe). (
  • They found that the respiratory exchange ratio-the amount of carbon dioxide produced in metabolism per oxygen used-decreased significantly following ingestion of phenylalanine compared to placebo. (
  • Food with a high phenylalanine content are meat products or animal-based products in general such as poultry, eggs and milk. (
  • The test paper is taken to the laboratory, where it is mixed with a type of bacteria that needs phenylalanine to grow. (
  • Other studies suggest that elevated phenylalanine concentrations are linked to mood swings. (
  • Carbon steel specimens in triplicate were immersed in 100 mL of well water (Table 1 ) and various concentrations of DL-phenylalanine in the presence and absence of Zn 2+ (as ZnSO 4 7H 2 O) for a period of seven days. (
  • Increased blood concentrations of phenylalanine in patients with trauma and sepsis are common but unexplained. (
  • We examined the potential relationship between serum concentrations of phenylalanine and the immune activation marker neopterin in 84 specimens of 18 patients (14 males and 4 females) post-trauma during 12-14 days of follow up. (
  • In enzymology, a phenylalanine adenylyltransferase (EC 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. (
  • Animal foods are those that contain more phenylalanine, for example cheese. (
  • L-phenylalanine is LIKELY SAFE for most people when taken in amounts commonly found in foods. (
  • As of 2015, while normal amounts of phenylalanine in foods are likely safe, too much phenylalanine in a pregnant woman's system creates a risk for birth de. (
  • Phenylalanine naturally occurs in many foods, but not so concentrated. (
  • However, taking phenylalanine by mouth does not seem to have any effect on ADHD symptoms . (
  • DL-phenylalanine should not be used in people taking antipsychotic drugs, as it may cause or worsen symptoms of tardive dyskinesia (TD). (
  • PKU symptoms can be managed by reducing and controlling the amount of phenylalanine your infant consumes. (
  • DL-phenylalanine is commonly used to reduce the symptoms of brain fog and fatigue while increasing energy. (
  • D-phenylalanine in combination with other agents may help reduce symptoms of alcohol withdrawal. (
  • A definition of the medical term "phenylalanine" is presented. (
  • A definition of the term "hyperphenylalaninemia" is presented, which refers to an increased amount of phenylalanine in the blood. (
  • The dietary supplement from Source Naturals‚ DL-Phenylalanine 750 mg 60 Tablets‚ may possibly help in the support of an alert state of mind. (
  • Phenylalanine is available as a dietary supplement in the form of L-phenylalanine, D-phenylalanine, and DL-phenylalanine. (
  • The relevance of phenylalanine metabolic pathways in wood formation, the biotic interactions, and ultraviolet protection is discussed. (