Phenylalanine. Medical search

An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.

An enzyme of the oxidoreductase class that catalyzes the formation of L-TYROSINE, dihydrobiopterin, and water from L-PHENYLALANINE, tetrahydrobiopterin, and oxygen. Deficiency of this enzyme may cause PHENYLKETONURIAS and PHENYLKETONURIA, MATERNAL. EC 1.14.16.1.

An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.

A group of autosomal recessive disorders marked by a deficiency of the hepatic enzyme PHENYLALANINE HYDROXYLASE or less frequently by reduced activity of DIHYDROPTERIDINE REDUCTASE (i.e., atypical phenylketonuria). Classical phenylketonuria is caused by a severe deficiency of phenylalanine hydroxylase and presents in infancy with developmental delay; SEIZURES; skin HYPOPIGMENTATION; ECZEMA; and demyelination in the central nervous system. (From Adams et al., Principles of Neurology, 6th ed, p952).

A group of compounds that are derivatives of phenylpyruvic acid which has the general formula C6H5CH2COCOOH, and is a metabolite of phenylalanine. (From Dorland, 28th ed)

A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.

An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.

A natural product that has been considered as a growth factor for some insects.

Compounds based on 2-amino-4-hydroxypteridine.

The rate dynamics in chemical or physical systems.

An essential branched-chain amino acid important for hemoglobin formation.

An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Amino acids containing an aromatic side chain.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.

A condition occurring in untreated or partially treated females with PHENYLKETONURIA when they become pregnant. This may result in damages to the FETUS, including MICROCEPHALY; MENTAL RETARDATION; congenital heart disease; FETAL GROWTH RETARDATION; and CRANIOFACIAL ABNORMALITIES. (From Am J Med Genet 1997 Mar 3;69(1):89-95)

A selective and irreversible inhibitor of tryptophan hydroxylase, a rate-limiting enzyme in the biosynthesis of serotonin (5-HYDROXYTRYPTAMINE). Fenclonine acts pharmacologically to deplete endogenous levels of serotonin.

3-(p-Fluorophenyl)-alanine.

An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.

Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Flavoring agent sweeter than sugar, metabolized as PHENYLALANINE and ASPARTIC ACID.

Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)

Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.

An enzyme that catalyzes the formation of 7-phospho-2-keto-3-deoxy-D-arabinoheptonate from phosphoenolpyruvate and D-erythrose-4-phosphate. It is one of the first enzymes in the biosynthesis of TYROSINE and PHENYLALANINE. This enzyme was formerly listed as EC 4.1.2.15.

A species of ANABAENA that can form SPORES called akinetes.

A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.

The amounts of various substances in food needed by an organism to sustain healthy life.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Derivatives of phenylacetic acid. Included under this heading are a variety of acid forms, salts, esters, and amides that contain the benzeneacetic acid structure. Note that this class of compounds should not be confused with derivatives of phenyl acetate, which contain the PHENOL ester of ACETIC ACID.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.

Food and dietary formulations including elemental (chemically defined formula) diets, synthetic and semisynthetic diets, space diets, weight-reduction formulas, tube-feeding diets, complete liquid diets, and supplemental liquid and solid diets.

A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.

A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria occurring in soil and water. Its organisms are generally nonpathogenic, but some species do cause infections of mammals, including humans.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.

An essential amino acid. It is often added to animal feed.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

Proteins prepared by recombinant DNA technology.

A sulfur-containing essential L-amino acid that is important in many body functions.

The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.

Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.

The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.

A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.

Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

Amino acids which have a branched carbon chain.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC 1.6.99.7.

A nonmetallic, diatomic gas that is a trace element and member of the halogen family. It is used in dentistry as flouride (FLUORIDES) to prevent dental caries.

A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A large and heterogenous group of fungi whose common characteristic is the absence of a sexual state. Many of the pathogenic fungi in humans belong to this group.

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 2.6.1.1.). Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC 2.6.1.5.

A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE. Deficiency in the enzyme causes ALKAPTONURIA, an autosomal recessive disorder, characterized by homogentisic aciduria, OCHRONOSIS and ARTHRITIS. This enzyme was formerly characterized as EC 1.13.1.5 and EC 1.99.2.5.

A plant genus of the family APIACEAE used for flavoring food.

Peptides composed of two amino acid units.

A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Established cell cultures that have the potential to propagate indefinitely.

Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).

Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.

The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

The sum of the weight of all the atoms in a molecule.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

Radioactive substances added in minute amounts to the reacting elements or compounds in a chemical process and traced through the process by appropriate detection methods, e.g., Geiger counter. Compounds containing tracers are often said to be tagged or labeled. (Hawley's Condensed Chemical Dictionary, 12th ed)

An enzyme that catalyzes the hydroxylation of TRYPTOPHAN to 5-HYDROXYTRYPTOPHAN in the presence of NADPH and molecular oxygen. It is important in the biosynthesis of SEROTONIN.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

There are several types of PKU, including classic PKU, mild PKU, and hyperphenylalaninemia (HPA). Classic PKU is the most severe form of the disorder and is characterized by a complete deficiency of the enzyme phenylalanine hydroxylase (PAH), which is necessary for the breakdown of Phe. Mild PKU is characterized by a partial deficiency of PAH, while HPA is caused by a variety of other genetic defects that affect the breakdown of Phe.

Symptoms of PKU can vary depending on the severity of the disorder, but may include developmental delays, intellectual disability, seizures, and behavioral problems. If left untreated, PKU can lead to serious health complications such as brain damage, seizures, and even death.

The primary treatment for PKU is a strict diet that limits the intake of Phe. This typically involves avoiding foods that are high in Phe, such as meat, fish, eggs, and dairy products, and consuming specialized medical foods that are low in Phe. In some cases, medication may also be prescribed to help manage symptoms.

PKU is an autosomal recessive disorder, which means that it is inherited in an unusual way. Both parents must carry the genetic mutation that causes PKU, and each child has a 25% chance of inheriting the disorder. PKU can be diagnosed through newborn screening, which is typically performed soon after birth. Early diagnosis and treatment can help prevent or minimize the symptoms of PKU and improve quality of life for individuals with the disorder.

When a pregnant woman has PKU, her body may not be able to properly metabolize Phe, leading to an accumulation of this amino acid in her blood and tissues. This can cause a range of health problems for the mother and her unborn baby.

If left untreated, PKU during pregnancy can lead to:

1. Preterm birth: Women with untreated PKU are at risk of giving birth prematurely, which can increase the risk of health problems for the baby.
2. Low birth weight: Babies born to mothers with PKU may have a lower birth weight than expected, which can increase their risk of health problems.
3. Intellectual disability: Untreated PKU during pregnancy can increase the risk of intellectual disability in the baby.
4. Heart defects: PKU can increase the risk of heart defects in the developing fetus.
5. Other health problems: PKU can also increase the risk of other health problems in the baby, such as seizures and developmental delays.

To manage PKU during pregnancy, women with the condition typically need to follow a strict diet that limits their intake of phenylalanine. This may involve avoiding certain foods that are high in Phe, such as meat, fish, eggs, and dairy products, and instead eating foods that are low in Phe, such as fruits, vegetables, and grains. In some cases, women with PKU may also need to take supplements or medications to help manage their condition during pregnancy.

It is important for pregnant women with PKU to work closely with their healthcare provider to manage their condition and ensure the best possible outcome for their baby. Regular monitoring of Phe levels and close follow-up with a metabolic specialist can help to minimize the risk of complications and ensure that the baby is receiving the appropriate nutrients for growth and development.

DL-Phenylalanine is a mixture of D-phenylalanine and L-phenylalanine. The reputed analgesic activity of DL-phenylalanine may be ... Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. Phenylalanine is biosynthesized via the ... A small amount of D-phenylalanine appears to be converted to L-phenylalanine. D-Phenylalanine is distributed to the various ... ISBN 978-3-540-48595-7. Wikimedia Commons has media related to L-Phenylalanine. Phenylalanine mass spectrum Phenylalanine at ...

https://en.wikipedia.org/wiki/Phenylalanine

N-adenylyl-L-phenylalanine Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are ... L-phenylalanine adenylyltransferase. This enzyme is also called L-phenylalanine adenylyltransferase. Lerbs W, Luckner M (1985 ... In enzymology, a phenylalanine adenylyltransferase (EC 2.7.7.54) is an enzyme that catalyzes the chemical reaction ATP + L- ... diphosphate and N-adenylyl-L-phenylalanine. This enzyme belongs to the family of transferases, specifically those transferring ...

https://en.wikipedia.org/wiki/Phenylalanine_adenylyltransferase

The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction L-phenylalanine ⇌ {\displaystyle \ ... and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal ... The systematic name of this enzyme class is L-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use ... include L-phenylalanine decarboxylase, aromatic L-amino acid decarboxylase, ...

https://en.wikipedia.org/wiki/Phenylalanine_decarboxylase

The Pah-KO mouse model presented high blood phenylalanine and low tyrosine levels, hypocholesterolemia, high phenylalanine and ... GeneReviews/NCBI/NIH/UW entry on Phenylalanine Hydroxylase Deficiency Locus-specific database of the human phenylalanine ... "Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase". Archives of Biochemistry and ... "The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for ...

https://en.wikipedia.org/wiki/Phenylalanine_hydroxylase

In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction L-phenylalanine + ... This enzyme participates in phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. As of late 2007, ... Asano Y, Nakazawa A, Endo K, Hibino Y, Ohmori M, Numao N, Kondo K (1987). "Phenylalanine dehydrogenase of Bacillus badius. ... The systematic name of this enzyme class is L-phenylalanine:NAD+ oxidoreductase (deaminating). Other names in common use ...

https://en.wikipedia.org/wiki/Phenylalanine_dehydrogenase

Other names in common use include phenylalanine (histidine) aminotransferase, phenylalanine(histidine):pyruvate ... In enzymology, a phenylalanine(histidine) transaminase (EC 2.6.1.58) is an enzyme that catalyzes the chemical reaction L- ... Minatogawa Y, Noguchi T, Kido R (January 1977). "Species distribution and properties of hepatic phenylalanine (histidine): ... The systematic name of this enzyme class is L-phenylalanine:pyruvate aminotransferase. ...

https://en.wikipedia.org/wiki/Phenylalanine(histidine)_transaminase

... and L-phenylalanine ammonia-lyase. Phenylalanine ammonia lyase is specific for L-phenylalanine, and to a lesser extent, L- ... The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic ... phenylalanine ammonia-lyases), EC 4.3.1.25 (tyrosine ammonia-lyases), and EC 4.3.1.26 (phenylalanine/tyrosine ammonia-lyases). ... Phenylalanine ammonia lyase is found widely in plants, as well as some bacteria, yeast, and fungi, with isoenzymes existing ...

https://en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase

This enzyme is also called acetyl-CoA-L-phenylalanine alpha-N-acetyltransferase. This enzyme participates in phenylalanine ... N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. ...

https://en.wikipedia.org/wiki/Phenylalanine_N-acetyltransferase

a EINECS number 200-568-1 (phenylalanine) ^a CID 994 from PubChem (phenylalanine) ^a CID 71567 from PubChem (D-phenylalanine) ^ ... a CID 6140 from PubChem (L-phenylalanine) (Articles with short description, Short description matches Wikidata, PubChem ID (CID ...

https://en.wikipedia.org/wiki/Phenylalanine_(data_page)

This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis. Phenylalanine- ... In enzymology, a phenylalanine-tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction ATP + L- ... The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include ... L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNAPhe. This enzyme belongs to ...

https://en.wikipedia.org/wiki/Phenylalanine—tRNA_ligase

... (EC 1.14.13.124, phenylalanine N-hydroxylase, CYP79A2) is an enzyme with systematic name L- ... N-hydroxy-L-phenylalanine + O2 + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } N,N-dihydroxy-L-phenylalanine + NADP+ + H2O ( ... L-phenylalanine + O2 + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } N-hydroxy-L-phenylalanine + NADP+ + H2O: (1b) ... 1c) N,N-dihydroxy-L-phenylalanine ⇌ {\displaystyle \rightleftharpoons } (E)-phenylacetaldoxime + CO2 + H2O Phenylalanine N- ...

https://en.wikipedia.org/wiki/Phenylalanine_N-monooxygenase

In enzymology, a phenylalanine 2-monooxygenase (EC 1.13.12.9) is an enzyme that catalyzes the chemical reaction L-phenylalanine ... Koyama H (1984). "A simple and rapid enzymatic determination of L-phenylalanine with a novel L-phenylalanine oxidase ( ... and phenylalanine (deaminating, decarboxylating)oxidase. This enzyme participates in phenylalanine metabolism. Koyama H ( ... Koyama H (August 1984). "Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and ...

https://en.wikipedia.org/wiki/Phenylalanine_2-monooxygenase

The enzyme phenylalanine racemase (EC 5.1.1.11, phenylalanine racemase, phenylalanine racemase (adenosine triphosphate- ... phenylalanine racemase phenylalanine racemase (adenosine triphosphate-hydrolysing) gramicidin S synthetase I Phenylalanine ... Biology portal Phenylalanine Racemase Phenylketonuria Takahashi H, Sato E, Kurahashi K (1971). "Racemization of phenylalanine ... Phenylalanine Pyridoxal-phosphate (active form of vitamin B6) Problems in the digestion of phenylalanine (phe) to tyrosine (tyr ...

https://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolysing)

N-Formylmethionyl-leucyl-phenylalanine (fMLF, fMLP or N-formyl-met-leu-phe) is an N-formylated tripeptide and sometimes simply ... N-Formylmethionine Leucyl-Phenylalanine at the US National Library of Medicine Medical Subject Headings (MeSH) (CS1 errors: ... n-formylmethionine leucyl-phenylalanine, Cancerweb Panaro MA, Mitolo V (Aug 1999). "Cellular responses to fMLF challenging: a ...

https://en.wikipedia.org/wiki/N-Formylmethionine-leucyl-phenylalanine

... 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 ...

https://en.wikipedia.org/wiki/Aspartame

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 ...

https://en.wikipedia.org/wiki/NMDA_receptor_antagonist

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 ...

https://en.wikipedia.org/wiki/6,7-dihydropteridine_reductase

May 2008). "Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and ... The 2,5-cyclohexene ring becomes a phenyl ring, and L-phenylalanine is formed. Certain forms of ADT have been shown to exhibit ... The systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in ... Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction L-arogenate → L phenylalanine + H2O ...

https://en.wikipedia.org/wiki/Arogenate_dehydratase

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 ...

https://en.wikipedia.org/wiki/Newborn_screening

... 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, ...

https://en.wikipedia.org/wiki/Diet_Pepsi

5, p. 946 H. B. Gillespie, H. R. Snyder (1934). "dl-β-Phenylalanine". Organic Syntheses.; Collective Volume, vol. 2, p. 489 ... This compound on reduction gives access to phenylalanine. Variants of the azlactone synthesis in which analogues of azlactones ...

https://en.wikipedia.org/wiki/Erlenmeyer–Plöchl_azlactone_and_amino-acid_synthesis

Aspartame contains phenylalanine.) Comparing Sprite Zero Sugar to other popular lemon-lime sodas. Sprite (soft drink) Coca-Cola ...

https://en.wikipedia.org/wiki/Sprite_Zero_Sugar

Phenylketonurics: Contains phenylalanine. Diet Cherry 7 Up was rebranded as Cherry 7 Up Zero Sugar in late 2020. Orange 7 Up: ...

https://en.wikipedia.org/wiki/7_Up

Mitchell, J. J.; Trakadis, Y. J.; Scriver, C. R. (2011). "Phenylalanine hydroxylase deficiency". Genetics in Medicine. 13 (8): ...

https://en.wikipedia.org/wiki/Newborn_Screening_Saves_Lives_Reauthorization_Act_of_2013

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 ...

https://en.wikipedia.org/wiki/Phenylketonuria

N-formylmethionine-leucyl-phenylalanine); b) complement components C5a and C3a which are chemotactic factors formed during the ...

https://en.wikipedia.org/wiki/Specialized_pro-resolving_mediators

Strecker degradation of phenylalanine. Phenylacetaldehyde is often contaminated with polystyrene oxide polymer because of the ... Phenylacetaldehyde occurs extensively in nature because it can be biosynthetically derived from the amino acid phenylalanine. ... Historically, before biotechnology approaches were developed, phenylacetaldehyde was also used to produce phenylalanine via the ...

https://en.wikipedia.org/wiki/Phenylacetaldehyde

Phenylalanine and Tyrosine are grouped together because one of them can be synthesized from the other using the enzyme ... Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, ... "Phenylalanine and Tyrosine Metabolism". National Center for Biotechnology Information PubChem. 18 May 2022. Retrieved 21 ... Tyrosine is synthesized by the hydroxylation of phenylalanine, an essential amino acid. Estimating the daily requirement for ...

https://en.wikipedia.org/wiki/Essential_amino_acid

Phenylalanine, a common amino acid. Biphenyl, consisting of two phenyl groups. The two rings tend not to be coplanar. ... Most common among natural products is the amino acid phenylalanine, which contains a phenyl group. A major product of the ...

https://en.wikipedia.org/wiki/Phenyl_group

A formulation containing lofepramine and the amino acid phenylalanine is under investigation as a treatment for fatigue as of ... "Lofepramine/phenylalanine - MultiCell Technologies - AdisInsight". AdisInsight. Springer International Publishing AG. Retrieved ...

https://en.wikipedia.org/wiki/Lofepramine

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 ...

http://www.nlm.nih.gov/medlineplus/ency/article/003362.htm

https://medlineplus.gov/ency/article/003362.htm

SEARCH RESULTS for: Phenylalanine Hydroxylase Activator [Drug Class] (11 results) *Share : JavaScript needed for Sharing tools ...

https://dailymed.nlm.nih.gov/dailymed/search.cfm?query=Phenylalanine%20Hydroxylase%20Activator&searchdb=class

L-Phenylalanine reagent grade, ≥98%; CAS Number: 63-91-2; EC Number: 200-568-1; Synonyms: (S)-2-Amino-3-phenylpropionic acid; ... L-Phenylalanine is an essential aromatic amino acid.. It has a role in metabolism as it forms a starting point for many ... L-Phenylalanine has been used in Fluo-4 Ca2+-assay in a study to demonstrate that G-protein coupled receptor 139 reference ... surrogate agonists 1a and 7c and L-phenylalanine share a common binding site.. It has also been used to spike blood samples to ...

https://www.sigmaaldrich.com/RU/en/product/sial/p2126

Level of blood phenylalanine (Phe). Patients with Phe blood levels ,=600 µmol/L (10 mg/dL) on a normal diet must be treated ... Diamond A. Phenylalanine levels of 6-10 mg/dl may not be as benign as once thought. Acta Pædiatr Suppl 1994;407:89-91. ... Recommendations of the German Working Group for Metabolic Diseases for Control of Phenylalanine in Phenylketonuria The content ... Griffiths P, Paterson L, Harvie A. Neuropsychologic effects of subsequent exposure to phenylalanine in adolescents and young ...

https://www.nichd.nih.gov/publications/pubs/pku/Pages/sub19.aspx

SC-49992, a mimetic of the peptide arginine-glycine-aspartic acid-phenylalanine that blocks platelet aggregation, enhances ... SC-49992, a mimetic of the peptide arginine-glycine-aspartic acid-phenylalanine that blocks platelet aggregation, enhances ... SC-49992, a mimetic of the peptide arginine-glycine-aspartic acid-phenylalanine that blocks platelet aggregation, enhances ... SC-49992, a mimetic of the peptide arginine-glycine-aspartic acid-phenylalanine that blocks platelet aggregation, enhances ...

https://jpet.aspetjournals.org/content/267/3/1191

Discovery of phenylalanine derivatives as potent HIV-1 capsid inhibitors from click chemistry-based compound library. ... Discovery of phenylalanine derivatives as potent HIV-1 capsid inhibitors from click chemistry-based compound library. Journal ... We report the design, parallel synthesis, and anti-HIV-1 activity evaluation of a series of novel phenylalanine derivatives as ...

https://scholars.duke.edu/display/pub1350499

Haaveissa maraton tai juoksun aloittaminen? Täältä löydät kaiken tarvitsemasi juoksuharrastuksen tueksi!

https://maisematiemaraton.fi/p/gaam-phenylalanine-60-caps/

Learn about the claims, recommended intake, and side effects of phenylalanine.

https://myhealth.ucsd.edu/library/diseasesconditions/adult/bone/19,Phenylalanine

Learn about the claims, recommended intake, and side effects of phenylalanine.

https://healthlibrary.bvhealthsystem.org/RelatedItems/19,Phenylalanine

Tag: phenylalanine. Phenylketonuria aka PKU. May 17, 2017. May 18, 2017. by DreaEatsWell, posted in DEW, Drea Eats Well, PKU, ... Tagged Amino Acids, Formula, newborn screening, phenylalanine, Phenylketonuria, PKULeave a comment ...

https://dreaeatswell.com/tag/phenylalanine/

Your body naturally converts L-Phenylalanine into the amino acid L-Tyrosine which is then ... Phenylalanine is a highly bio-available essential amino acid. ... Type of Phenylalanine to buy. L-Phenylalanine is available in ... D-Phenylalanine is a mirror image of L-Phenylalanine that is made in the lab. And DL-Phenylalanine is a combination of the two ... L-Phenylalanine vs. D-Phenylalanine: Whats the Difference?. L-Phenylalanine is an essential amino acid which means you must ...

https://nootropicsexpert.com/phenylalanine/comment-page-2/?replytocom=29288

Phenylalanine is an essential amino acid found in meat, dairy, and beans. It has been used to treat chronic pain and ease ... Phenylalanine can be taken as a pill or powder. It can also be applied to the skin as a cream. ... It is likely safe for most adults to take L-phenylalanine in small doses for a short time. Not enough studies have been done to ... Women who are pregnant or trying to become pregnant or who are breastfeeding should not take high amounts of phenylalanine. ...

https://therapy.epnet.com/GetContent.aspx?token=b07cead8-3508-47b4-a855-614f3d8eb5ee&chunkiid=21664

Learn about the claims, recommended intake, and side effects of phenylalanine.

https://healthlibrary.osfhealthcare.org/Wellness/BackandNeck/19,Phenylalanine

Phenylalanine is an amino acid found in many foods and used by your body to produce proteins and other important molecules. It ...

https://www.vitajoy-biotech.com/ingredients/phenylalanine/

Learn about the claims, recommended intake, and side effects of phenylalanine.

https://encyclopedia.nm.org/Library/Wellness/DiseasesConditions/19,Phenylalanine

Phenylalanine is an essential amino acid found in meat, dairy, and beans. It has been used to treat chronic pain and ease ... Phenylalanine. Home , Health Information Center , Natural & Alternative Treatments , Herbs & Supplements , Article. ... Phenylalanine can be taken as a pill or powder. It can also be applied to the skin as a cream. ... It is likely safe for most adults to take L-phenylalanine in small doses for a short time. Not enough studies have been done to ...

https://health.cvs.com/GetContent.aspx?token=f75979d3-9c7c-4b16-af56-3e122a3f19e3%20=222857&chunkiid=21664

What is L-phenylalanine?. The amino acid L-phenylalanine belongs to the essential amino acids, i.e. those that are vital and ... Natural L-Phenylalanine from Switzerland. L-phenylalanine is on the one hand needed for muscle building and is further needed ... How does L-Phenylalanine work in the body?. Phenylalanine has been known since 1879 and has been continuously researched in ... What sources contain L-phenylalanine?. L-phenylalanine is supplied to the human organism mainly with the intake of animal foods ...

https://www.kingnature.de/ar/supplements-ar/amino-acids-ar/l-phenylalanine-ar/

... and of phenylalanine in particular, are rate-limiting in production of these metabolites. In contrast, increased phenylalanine ... and of phenylalanine in particular, are rate-limiting in production of these metabolites. In contrast, increased phenylalanine ... and of phenylalanine in particular, are rate-limiting in production of these metabolites. In contrast, increased phenylalanine ... and of phenylalanine in particular, are rate-limiting in production of these metabolites. In contrast, increased phenylalanine ...

https://cris.bgu.ac.il/en/publications/phenylalanine-and-tyrosine-levels-are-rate-limiting-factors-in-pr

This website uses cookies to improve your experience while you navigate through the website. Out of these, the cookies that are categorized as necessary are stored on your browser as they are essential for the working of basic functionalities of the website. We also use third-party cookies that help us analyze and understand how you use this website. These cookies will be stored in your browser only with your consent. You also have the option to opt-out of these cookies. But opting out of some of these cookies may affect your browsing experience ...

https://esferadourada.com/ingredients/phenylalanine-en/

SEARCH RESULTS for: Phenylalanine Hydroxylase Activator [Drug Class] (11 results) *Share : JavaScript needed for Sharing tools ...

https://www.dailymed.nlm.nih.gov/dailymed/search.cfm?query=Phenylalanine%20Hydroxylase%20Activator&searchdb=class

Undecylenoyl phenylalanine has good skin affinity and can control the combination of α-MSH (melanocyte stimulating hormone) and ... Undecylenoyl Phenylalanine Powder Purity ≧98% , Cas# 175357-18-3 , C20H29NO3 , White Powder , ... UNDECYLENOYLPHENYLALANINE, L-Phenylalanine,N-(1-oxo-10-undecen-1-yl)-, N-(1-Oxo-10-undecen-1-yl)-L-phenylalanine. LGBUP, (S,E)- ... Undecylenoyl Phenylalanine Powder Purity ≧98% , Cas# 175357-18-3 , C20H29NO3 , White Powder , Undecylenoyl phenylalanine has ...

https://www.cosmetics-add.com/product/undecylenoyl-phenylalanine/

Mmetụta Phenylalanine. Na onye ahụike, phenylalanine na-etinye obi ya dum. Mgbe ị na-eri nri bara ọgaranya na phenylalanine, ị ... Nri nri Phenylalanine bara ọgaranya:. Njirimara nozuzu nke phenylalanine. Phenylalanine bụ amino acid aromatic nke bụ akụkụ ... Phenylalanine maka ịma mma na ahụ ike. Phenylalanine a na-akpọkwa ezigbo ọnọdụ amino acid. Ma onye nọ nọnọdụ dị mma na-adọta ... Njirimara bara uru nke phenylalanine na mmetụta ya na ahụ:. Notu oge na ahụ anyị, phenylalanine nwere ike inye aka ọ bụghị ...

https://ig.healthy-food-near-me.com/phenylalanine/

... catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine. Inherited mutations that result in PAH enzyme ... The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I- ... Allosteric Regulation, Binding Sites, Humans, Ligands, Models, Molecular, Phenylalanine, Phenylalanine Hydroxylase, Protein ... Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain. Share Share Share ...

https://www.ndm.ox.ac.uk/publications/616195?f3b84282-00ad-11ee-9762-06ee384a3ad0

or phenylalanine-transport, PAH, PCBD, QDPR and tyrosine-degradation. *Comment: Phenylalanine can be catabolized via ... or phenylalanine-transport, ARO8, phenylpyruvate-decarboxylase, pad-dh and phenylacetate-degradation. *or phenylalanine- ... L-phenylalanine ABC transporter, ATPase component 1 (LivF). BT3837. BT0562. livG. L-phenylalanine ABC transporter, ATPase ... L-phenylalanine ABC transporter, permease component 1 (LivH). livJ. L-phenylalanine ABC transporter, substrate-binding ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&path=phenylalanine&orgId=FitnessBrowser__Btheta

Phenylketonuria (PKU) is an autosomal recessive inborn error of metabolism where high phenylalanine (Phe) concentrations cause ... Machine Learning Model Reveals an Association with Phenylalanine Concentrations in Dried Blood Spots. ...

https://pesquisa.bvsalud.org/portal/resource/pt/mdl-37367836

A small amount of D-phenylalanine may be converted to L-phenylalanine in the body. D-phenylalanine is reported ... D- and L-phenylalanine are structural mirror images of each other. ... Dietary Supplement Vegan Non-GMO Gluten Free D-phenylalanine is a non-protein amino acid related to the essential amino acid L- ... D-phenylalanine is a non-protein amino acid related to the essential amino acid L-phenylalanine. D- and L-phenylalanine are ...

https://betterhealthinternational.org/products/doctors-best-best-d-phenylalanine-500-mg-60-veggie-caps

Phenylalanine *Valine OTHER. The following are examples of ingredients that would be classified as other: *an electrolyte (eg ...

https://wwwn.cdc.gov/Nchs/Nnyfs/DSII.htm

phenylalanine. *lysine. Health benefits. Many cultures use Capsicum in traditional medicine. In addition, studies indicate it ...

https://www.medicalnewstoday.com/articles/capsicum?utm_source=ReadNext

Phenylalanine* * Protein Folding * Protein Transport / genetics * Receptor Protein-Tyrosine Kinases / chemistry* * Receptor ...

https://pubmed.ncbi.nlm.nih.gov/21242967/

Your body naturally converts L-Phenylalanine into the amino acid L-Tyrosine which is then converted into L-DOPA . (nootropicsexpert.com)
The enzyme phenylalanine hydroxylase converts Phenylalanine in your liver into the amino acid L-Tyrosine . (nootropicsexpert.com)
L-Phenylalanine (LPA) is converted into the amino acid L-Tyrosine in your liver. (nootropicsexpert.com)
Phenylalanine and tyrosine levels are rate-limiting factors in production of health promoting metabolites in Vitis vinifera cv. (bgu.ac.il)
The presence of AroG* protein led to elevated levels of primary metabolites in the shikimate and AAA pathways including phenylalanine and tyrosine, and to a dramatic increase in phenylpropanoids. (bgu.ac.il)
N'ihi ọrịa a, phenylalanine enweghị ike ịtụgharị na tyrosine, nke nwere mmetụta na-adịghị mma na usoro ụjọ ahụ dum na ụbụrụ ọkachasị. (healthy-food-near-me.com)
The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine. (ox.ac.uk)
Overview: Phenylalanine utilization in GapMind is based on MetaCyc pathway L-phenylalanine degradation I (aerobic, via tyrosine, link ), pathway II (anaerobic, via phenylacetaldehyde dehydrogenase, link ), degradation via phenylpyruvate:ferredoxin oxidoreductase ( PMC3346364 ), or degradation via phenylacetaldehyde:ferredoxin oxidoreductase ( PMID:24214948 ). (lbl.gov)
Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine. (nih.gov)
Reduction of phenylalanine and tyrosine has reportedly reduced homogentisic acid excretion. (medscape.com)
Reduction of phenylalanine and tyrosine reportedly reduced homogentisic acid excretion in the urine of a child. (medscape.com)
However, people do not need all the phenyalanine they eat, so the body converts extra phenylalanine to another harmless amino acid, tyrosine. (nih.gov)
People with PKU cannot properly break down the extra phenylalanine to convert it to tyrosine. (nih.gov)

Serum phenylalanine screening is a blood test to look for signs of the disease phenylketonuria (PKU). (nih.gov)
Mgbe ị na-eri nri bara ọgaranya na phenylalanine, ị kwesịrị ịkpachara anya maka ndị ahụ nwere nsogbu sitere na amino acid metabolism, nke a na-akpọ phenylketonuria. (healthy-food-near-me.com)
Risk of Developing Insulin Resistance in Adult Subjects with Phenylketonuria: Machine Learning Model Reveals an Association with Phenylalanine Concentrations in Dried Blood Spots. (bvsalud.org)
Phenylketonuria (PKU) is an autosomal recessive inborn error of metabolism where high phenylalanine (Phe) concentrations cause irreversible intellectual disability that can be prevented by newborn screening and early treatment . (bvsalud.org)
Caution: Phenylalanine supplements should not be taken by individuals with phenylketonuria (PKU), children, pregnant or lactating women, people with high blood pressure, and anyone taking anti-psychotic medications or MAO inhibitors. (betterhealthinternational.org)
Structural studies on phenylalanine hydroxylase and implications toward understanding and treating phenylketonuria. (nih.gov)
Phenylketonuria [‏PKU]‏ is an autosomal recessive genetic disorder caused by defects in the phenylalanine hydroxylase [‏PAH]‏ system. (who.int)
Chen, L., & Woo, S.L.C. ``Complete and persistent phenotypic correction of phenylketonuria in mice by site-specific genome integration of murine phenylalanine hydroxylase cDNA. (nih.gov)
Phenylketonuria (PKU) is a genetic metabolic disorder that increases the body's levels of phenylalanine. (nih.gov)

L-phenylalanine is on the one hand needed for muscle building and is further needed for the building of other amino acids and the production of hormones. (kingnature.de)
The amino acid L-phenylalanine belongs to the essential amino acids , i.e. those that are vital and maintain the body's functions. (kingnature.de)
Phenylalanine has been known since 1879 and has been continuously researched in connection with other amino acids and proteins ever since. (kingnature.de)
Most of the variants that cause PKU change single amino acids in phenylalanine hydroxylase. (nih.gov)
Phenylalanine is one of the building blocks (amino acids) of proteins. (nih.gov)

Blau N, Erlandsen H. The metabolic and molecular bases of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. (nih.gov)
Phenylalanine Hydroxylase Deficiency. (nih.gov)

D-phenylalanine is reported to inhibit an enzyme that degrades enkephalins, which are naturally occurring substances In the body that belong to the class of compounds known as "endorphins. (betterhealthinternational.org)
The PAH gene provides instructions for making an enzyme called phenylalanine hydroxylase. (nih.gov)
This enzyme helps process phenylalanine, which is a building block of proteins (amino acid). (nih.gov)

Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain. (ox.ac.uk)
D- and L-phenylalanine are structural mirror images of each other. (betterhealthinternational.org)

L-Phenylalanine is the natural form found in proteins. (nootropicsexpert.com)
Phenylalanine is an amino acid found in many foods and used by your body to produce proteins and other important molecules. (vitajoy-biotech.com)

L-Phenylalanine can be a highly effective nootropic for boosting cognitive function because it boosts norepinephrine and dopamine production. (nootropicsexpert.com)
L-Phenylalanine helps produce the catecholamine-triad of neurotransmitters dopamine , norepinephrine and epinephrine . (nootropicsexpert.com)
Phenylalanine is a necessary precursor for dopamine , norepinephrine and epinephrine . (nootropicsexpert.com)
These are based on the fact that L-phenylalanine is considered a precursor for dopamine and norepinephrine in the body. (kingnature.de)

Other PAH gene variants delete small amounts of DNA from the gene or disrupt the way the gene's instructions are used to make phenylalanine hydroxylase. (nih.gov)
PAH gene variants reduce the activity of phenylalanine hydroxylase, preventing it from processing phenylalanine effectively. (nih.gov)

8-Guanidino-octanoyl-aspartic acid-phenylalanine (SC-49992), a mimetic of the tetrapeptide arginine-glycine-aspartic acid-phenylalanine, is a potent inhibitor of platelet aggregation. (aspetjournals.org)
For example, the most common variant in many populations replaces the amino acid arginine with the amino acid tryptophan at position 408 (written as Arg408Trp or R408W) in phenylalanine hydroxylase. (nih.gov)

L-Phenylalanine also stimulates the production of thyroid hormones T3 (triiodothyronine) and T4 (thyroxine) which are crucial in maintaining both overall physical and cognitive health. (nootropicsexpert.com)

Discovery of phenylalanine derivatives as potent HIV-1 capsid inhibitors from click chemistry-based compound library. (duke.edu)

L-Phenylalanine is an essential aromatic amino acid. (sigmaaldrich.com)
Phenylalanine bụ amino acid aromatic nke bụ akụkụ nke protein, ma dịkwa na ahụ na ụdị n'efu. (healthy-food-near-me.com)

This suggests that concentrations of AAAs, and of phenylalanine in particular, are rate-limiting in production of these metabolites. (bgu.ac.il)
In contrast, increased phenylalanine production did not lead to elevated concentrations of anthocyanins, even though they are also phenylpropanoid metabolites. (bgu.ac.il)

If PKU is not detected early, increasing phenylalanine levels in the baby will cause intellectual disability. (nih.gov)
If PKU is not treated, phenylalanine can build up to harmful levels, causing intellectual disability and other serious health problems. (nih.gov)
Mothers who have PKU and no longer follow a phenylalanine-restricted diet have an increased risk of having children with an intellectual disability, because their children may be exposed to very high levels of phenylalanine before birth. (nih.gov)

In addition to the supply in food, dietary supplements exist that contain L-phenylalanine as a nutrient. (kingnature.de)

To exploit the full potential that L-phenylalanine offers the body, it is recommended to take vitamins B3, B6 and C. Vitamin B6 in particular contributes to normal energy metabolism and normal functioning of the nervous system. (kingnature.de)

According to some clinical trials, Undecylenoyl Phenylalanine (MoreWhiteUChemicalbookP) does reduce pigmentation spots. (cosmetics-add.com)

Women who are pregnant or trying to become pregnant or who are breastfeeding should not take high amounts of phenylalanine. (epnet.com)
Because nerve cells in the brain are particularly sensitive to phenylalanine levels, excessive amounts of this substance can cause brain damage. (nih.gov)

L-Phenylalanine can be an effective treatment for some with ADHD symptoms. (nootropicsexpert.com)

L-Phenylalanine works in synergy with pharmaceutical drugs like Ritalin and Adderall by boosting extracellular levels of dopamine. (nootropicsexpert.com)

Another substance that blocks phenylalanine from reacting with anything else is added. (nih.gov)
This test is done to screen infants for PKU, a fairly rare condition that occurs when the body lacks a substance needed to breakdown the amino acid phenylalanine. (nih.gov)

The test detects abnormally high levels of an amino acid called phenylalanine. (nih.gov)
A normal test result means that phenylalanine levels are normal and the child does not have PKU. (nih.gov)
Further testing will be done if the phenylalanine levels in your baby's blood are too high. (nih.gov)
Many neurohackers prefer L-Phenylalanine over other catecholamine precursors because it supports neurotransmitter production without directly increasing neurotransmitter levels. (nootropicsexpert.com)
This condition increase the levels of phenylalanine in the blood. (nih.gov)
Classic PKU, the most severe form of the disorder, occurs in people who have very low levels of phenylalanine hydroxylase activity or who have no phenylalanine hydroxylase activity at all. (nih.gov)
People with untreated classic PKU have levels of phenylalanine high enough to cause severe brain damage and other serious medical problems. (nih.gov)

The artificial sweetener aspartame also contains Phenylalanine. (nootropicsexpert.com)

Effects attributed to phenylalanine, first and foremost the alleviation of depression, have not yet been demonstrated by reliable data from clinical studies. (kingnature.de)

D-Phenylalanine (but not L-Phenylalanine) has been used to treat chronic pain although the clinical research in this area is sparse. (nootropicsexpert.com)

In this way, L-phenylalanine indirectly helps with healthy weight reduction in the context of diets aimed at lowering the body fat percentage. (kingnature.de)

Green Stone Swiss Co ., Limited has always focused on the supply of beauty, nutritional, and healthy ingredients (Undecylenoyl Phenylalanine supply). (cosmetics-add.com)

Phenylalanine is a highly bio-available essential amino acid. (nootropicsexpert.com)
L-Phenylalanine is an essential amino acid that you get from food or a supplement. (nootropicsexpert.com)
L-Phenylalanine is an essential amino acid which means you must get if from food. (nootropicsexpert.com)
Phenylalanine is an essential amino acid found in meat, dairy, and beans. (epnet.com)
D-phenylalanine is a non-protein amino acid related to the essential amino acid L-phenylalanine. (betterhealthinternational.org)
CNDP2 synthesizes Lac-Phe by combining the essential amino acid phenylalanine with lactate. (nih.gov)

D-Phenylalanine (DPA) slows the action of the enzymes carboxypeptidase A or endorphinase and enkephalinase . (nootropicsexpert.com)
N'otu oge na ahụ anyị, phenylalanine na-arụkọ ọrụ na ogige dịka mmiri, enzymes digestive, na amino acid ndị ọzọ. (healthy-food-near-me.com)

Phenylalanine can be taken as a pill or powder. (epnet.com)
Undecylenoyl phenylalanine (MoreWhiteUP) is a white powder. (cosmetics-add.com)

L-phenylalanine also plays a not insignificant role in the formation of the thyroid hormone thyroxine. (kingnature.de)
It is also recognized that L-phenylalanine exerts an influence on hormone control. (kingnature.de)
Undecylenoyl phenylalanine has good skin affinity and can control the combination of α-MSH (melanocyte stimulating hormone) and melanin production factor, thereby blocking the process of melanin formation. (cosmetics-add.com)
Undecylenoyl phenylalanine, also known as acylamide, is a melanin-stimulating hormone (α-MSH) receptor antagonist. (cosmetics-add.com)

As a nootropic supplement, you may find several different forms of Phenylalanine available. (nootropicsexpert.com)

Your body cannot synthesize Phenylalanine on its own. (nootropicsexpert.com)
How does L-Phenylalanine work in the body? (kingnature.de)
A small amount of D-phenylalanine may be converted to L-phenylalanine in the body. (betterhealthinternational.org)
This means phenylalanine builds up in the person's blood, urine, and body. (nih.gov)

The team found that the largest exercise-induced increase was in a compound called N -lactoyl-phenylalanine, or Lac-Phe. (nih.gov)

L-Phenylalanine has been used in Fluo-4 Ca 2+ -assay in a study to demonstrate that G-protein coupled receptor 139 reference surrogate agonists 1a and 7c and L-phenylalanine share a common binding site. (sigmaaldrich.com)

It is likely safe for most adults to take L-phenylalanine in small doses for a short time. (epnet.com)

L-Phenylalanine is also well suited for athletes who want to support their demanding training sessions with micronutrients. (kingnature.de)

Learn more about the amino acid L-phenylalanine in the following text and enrich your knowledge. (kingnature.de)

The test paper is taken to the laboratory, where it is mixed with a type of bacteria that needs phenylalanine to grow. (nih.gov)

D-Phenylalanine is a mirror image of L-Phenylalanine that is made in the lab. (nootropicsexpert.com)
D-Phenylalanine (DPA) is a synthetic version of, and mirror image of L-Phenylalanine created in the lab. (nootropicsexpert.com)

Anatomy2

Organisms7

Diseases2

Chemicals and Drugs55

Analytical, Diagnostic and Therapeutic Techniques and Equipment9

Phenomena and Processes23

Technology, Industry, Agriculture2

Information Science3

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

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

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)

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

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

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

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

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)

Phenylalanine

Phenylalanine Hydroxylase

Phenylalanine Ammonia-Lyase

Phenylketonurias

Phenylpyruvic Acids

Tyrosine

Amino Acids

Ammonia-Lyases

Prephenate Dehydratase

Biopterin

Pterins

Kinetics

Leucine

Tryptophan

Molecular Sequence Data

Amino Acids, Aromatic

Amino Acid Sequence

Phenylalanine-tRNA Ligase

Phenylketonuria, Maternal

Fenclonine

p-Fluorophenylalanine

Chorismate Mutase

Mutagenesis, Site-Directed

Mutation

Amino Acids, Essential

Carbon Isotopes

Binding Sites

Aspartame

Hydroxylation

Pteridines

3-Deoxy-7-Phosphoheptulonate Synthase

Anabaena variabilis

Rhodotorula

Nutritional Requirements

Liver

Hydro-Lyases

Deuterium

Base Sequence

Escherichia coli

Isoleucine

Models, Molecular

Phenylacetates

Structure-Activity Relationship

Amino Acid Substitution

Alanine

Muscle Proteins

Protein Conformation

RNA, Transfer, Phe

Food, Formulated

Valine

Substrate Specificity

Leucine Dehydrogenase

Chromobacterium

Protein Binding

Aldehyde-Lyases

Lysine

Oxidation-Reduction

Recombinant Proteins

Methionine

Protein Biosynthesis

Dietary Proteins

RNA, Transfer

Shikimic Acid

RNA, Transfer, Amino Acyl

Tetroses

Phosphorylation

Amino Acids, Branched-Chain

Hydrogen-Ion Concentration

Dihydropteridine Reductase

Fluorine

Glycine

Protein Structure, Tertiary

Catalysis

Mitosporic Fungi

Protein Hydrolysates

Cloning, Molecular

Cinnamates

Point Mutation

Transaminases

Amino Acids, Neutral