Molecular Sequence Data
Amino Acid Sequence
Amino Acids, Essential
Amino Acid Substitution
RNA, Transfer, Phe
RNA, Transfer, Amino Acyl
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Amino Acyl-tRNA Synthetases
Electrophoresis, Polyacrylamide Gel
Magnetic Resonance Spectroscopy
Chromatography, High Pressure Liquid
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 . 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 188.8.131.52) to degrade phenylalanine, the harmful nutrient in PKU; in this treatment, PAL acts as a substitute for the enzyme phenylalanine monooxygenase (EC 184.108.40.206), 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.
Phenylalanine (data page)
Phenylalanine racemase (ATP-hydrolysing)
NMDA receptor antagonist
Erlenmeyer-Plöchl azlactone and amino-acid synthesis
Sprite Zero Sugar
Newborn Screening Saves Lives Reauthorization Act of 2013
Specialized pro-resolving mediators
Essential amino acid
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- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)