WordNet

an essential amino acid found in proteins and needed for growth of children and for protein metabolism in children and adults; abundant in milk and eggs; it is normally converted to tyrosine in the human body
the 6th letter of the Roman alphabet (同)f

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/05/01 01:41:44」(JST)

wiki ja

フェニルアラニン (phenylalanine) はアミノ酸の一種で、側鎖にベンジル基を持つ。略号は Phe または F。アラニンの側鎖の水素原子が1つフェニル基で置き換えられた構造を持つことが名称の由来である。室温では白色の粉末性固体である。

性質

タンパク質構成アミノ酸で、牛乳、卵、肉などの食品中のたんぱく質に多く含まれている必須アミノ酸の1つ。非極性側鎖アミノ酸で、芳香族アミノ酸。糖原性を持つ。

他のアミノ酸と同じく、D体とL体の2つのエナンチオマーを持つ。L-フェニルアラニン (LPA) は天然に存在する化合物であり、DNAによってコードされ、タンパク質を構成する。D-フェニルアラニン (DPA) は化学合成によって人工的に作り出される化合物である。

L-フェニルアラニンは生体内で L-チロシンに変換され、さらに L-ドーパとなる。これがさらにドーパミンやノルアドレナリン、アドレナリンへと誘導される。D-フェニルアラニンはフェネチルアミンに変換されるのみである。

8万人に1人と言われるフェニルケトン尿症では、このフェニルアラニンをチロシンに変化させる酵素、フェニルアラニン-4-モノオキシゲナーゼ (EC 1.14.16.1) の遺伝子の完全欠損により、血中にフェニルアラニンが異常に蓄積される。そのためフェニルアラニンの摂取を控えねばならない。シュガーレスガムなど多くの食品に含まれ、「フェニルアラニンを含む」旨の注意書きが表示されている。実際にはフェニルアラニンそのものが添加されているわけではなく、体内で分解されてフェニルアラニンを生成させる化合物を含む場合にこの表示が付される。例えば甘味料のアスパルテームは加水分解によってフェニルアラニン、アスパラギン酸、メタノールとなる。

コドンの中ではフェニルアラニンのものが最初に発見された。マーシャル・ニーレンバーグ (Marshall Warren Nirenberg) が発見者である。連続したウラシルからなる mRNA をバクテリア E. coli に挿入すると、そのバクテリアはフェニルアラニンのみを繰り返し単位とする新規なタンパク質を生産することを見出した。

フェニルアラニンは血液脳関門を通過する際にトリプトファンと同じチャネルを使用しており、大量に存在するとセロトニンの生成を阻害する。

合成によって作り出されるラセミ体の DL-フェニルアラニン (DLPA) はサプリメントとして利用される。DLPA は慢性疼痛やうつ病、あるいは月経前症候群による情緒不安定に有効な場合があるとされる。また、ADHD（注意欠陥多動性障害）の発症者の活力や注意力・集中力を増進させるという調査結果がある。

生合成

動物はフェニルアラニンを体内で作り出すことができないため、食物から摂取する必要がある。植物や大部分の微生物においてはシキミ酸経路によってプレフェン酸から生合成される。

プレフェン酸が脱炭酸されると同時にヒドロキシ基を失い、フェニルピルビン酸となる。これがグルタミン酸を窒素源とするアミノ基転移を受け、フェニルアラニンと α-ケトグルタル酸を与える。

出典

^ Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959.

外部リンク

フェニルアラニン - 「健康食品」の安全性・有効性情報（国立健康・栄養研究所）

wiki en

[Wiki en表示]

Phenylalanine (US: /ˌfɛnəlˈæləniːn/, UK: /ˌfiːnaɪlˈæləniːn/; abbreviated as Phe or F)^[2] is an α-amino acid with the formula C₆H₅CH₂CH(NH₂)COOH. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins, coded for by DNA. The codons for L-phenylalanine are UUU and UUC. Phenylalanine is a precursor for tyrosine; the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline); and the skin pigment melanin.

Phenylalanine is found naturally in the breast milk of mammals. It is used in the manufacture of food and drink products and sold as a nutritional supplement for its reputed analgesic and antidepressant effects. It is a direct precursor to the neuromodulator phenethylamine, a commonly used dietary supplement.

History

The first description of phenylalanine was made in 1879, when Schulze and Barbieri identified a compound with the empirical formula, C₉H₁₁NO₂, in yellow lupine (Lupinus luteus) seedlings. In 1882, Erlenmeyer and Lipp first synthesized phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia.^[3]^[4]

The genetic codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W. Nirenberg in 1961. They showed that by using mRNA to insert multiple uracil repeats into the genome of the bacterium E. coli, they could cause the bacterium to produce a polypeptide consisting solely of repeated phenylalanine amino acids. This discovery helped to establish the nature of the coding relationship that links information stored in genomic nucleic acid with protein expression in the living cell.

Biosynthesis

As an essential amino acid, phenylalanine is not synthesized de novo in humans and other animals, who must ingest phenylalanine or phenylalanine-containing proteins.

Dietary sources

Good sources of phenylalanine are eggs, chicken, liver, beef, milk, and soybeans.^[5] Other sources include spinach and leafy greens, tofu, amaranth leaves, and lupin seeds.

Other biological roles

L-Phenylalanine is biologically converted into L-tyrosine, another one of the DNA-encoded amino acids. L-tyrosine in turn is converted into L-DOPA, which is further converted into dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline). The latter three are known as the catecholamines.

Phenylalanine uses the same active transport channel as tryptophan to cross the blood–brain barrier. In excessive quantities, supplementation can interfere with the production of serotonin and other aromatic amino acids as well as nitric oxide due to the overuse (eventually, limited availability) of the associated cofactors, iron or tetrahydrobiopterin. Phenylalanine, which is found in the synthetic chemical aspartame (a sugar substitute) can, as a constituent of high doses of aspartame, occasionally cause seizures, according to MSN Health and Fitness, though there is only some evidence to support that theory, and it is mixed and the risk is small.^[6] The corresponding enzymes in for those compounds are the aromatic amino acid hydroxylase family and nitric oxide synthase.

Human biosynthesis pathway for trace amines and catecholamines^[7]^[8]

L-Phenylalanine

L-Tyrosine

L-Dopa

Epinephrine

Phenethylamine

p-Tyramine

Dopamine

Norepinephrine

N-Methylphenethylamine

N-Methyltyramine

p-Octopamine

Synephrine

3-Methoxytyramine

AADC

PNMT

AAAH

COMT

DBH

Phenylalanine in humans may ultimately be metabolized into a range of different substances.

In plants

Phenylalanine is the starting compound used in the synthesis of flavonoids. Lignan is derived from phenylalanine and from tyrosine. Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase.^[9]

Phenylketonuria

The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase. Individuals with this disorder are known as "phenylketonurics" and must regulate their intake of phenylalanine. A (rare) "variant form" of phenylketonuria called hyperphenylalaninemia is caused by the inability to synthesize a cofactor called tetrahydrobiopterin, which can be supplemented. Pregnant women with hyperphenylalaninemia may show similar symptoms of the disorder (high levels of phenylalanine in blood) but these indicators will usually disappear at the end of gestation. Pregnant women with PKU must control their blood phenylalanine levels even if the fetus is heterozygus for the defective gene because the fetus could be adversely affected due to hepatic immaturity.^{[medical citation needed]} Individuals who cannot metabolize phenylalanine must monitor their intake of protein to control the buildup of phenylalanine as their bodies convert protein into its component amino acids.

Phenylketonurics often use blood tests to monitor the amount of phenylalanine in their blood. Lab results may report phenylalanine levels in different units, including mg/dL and μmol/L. One mg/dL of phenylalanine is approximately equivalent to 60 μmol/L.

A non-food source of phenylalanine is the artificial sweetener aspartame. This compound, sold under the trade names Equal and NutraSweet, is metabolized by the body into several chemical byproducts including phenylalanine. The breakdown problems phenylketonurics have with protein and the attendant buildup of phenylalanine in the body also occurs with the ingestion of aspartame, although to a lesser degree. Accordingly, all products in Australia, the U.S. and Canada that contain aspartame must be labeled: "Phenylketonurics: Contains phenylalanine." In the UK, foods containing aspartame must carry ingredient panels that refer to the presence of "aspartame or E951"^[10] and they must be labeled with a warning "Contains a source of phenylalanine." In Brazil, the label "Contém Fenilalanina" (Portuguese for "Contains Phenylalanine") is also mandatory in products which contain it. These warnings are placed to aid individuals who have been diagnosed with PKU so that they can avoid such foods.

Geneticists have recently sequenced the genome of macaques. Their investigations have found "some instances where the normal form of the macaque protein looks like the diseased human protein" including markers for PKU.^[11]

D-, L- and DL-phenylalanine

The stereoisomer D-phenylalanine (DPA) can be produced by conventional organic synthesis, either as a single enantiomer or as a component of the racemic mixture. It does not participate in protein biosynthesis although it is found in proteins in small amounts - particularly aged proteins and food proteins that have been processed. The biological functions of D-amino acids remain unclear, although D-phenylalanine has pharmacological activity at niacin receptor 2.^[12]

DL-Phenylalanine (DLPA) is marketed as a nutritional supplement for its supposed analgesic and antidepressant activities. DL-Phenylalanine is a mixture of D-phenylalanine and L-phenylalanine. The reputed analgesic activity of DL-phenylalanine may be explained by the possible blockage by D-phenylalanine of enkephalin degradation by the enzyme carboxypeptidase A.^[13] The mechanism of DL-phenylalanine's supposed antidepressant activity may be accounted for by the precursor role of L-phenylalanine in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated brain levels of norepinephrine and dopamine are thought to have an antidepressant effect. D-Phenylalanine is absorbed from the small intestine and transported to the liver via the portal circulation. A small amount of D-phenylalanine appears to be converted to L-phenylalanine. D-Phenylalanine is distributed to the various tissues of the body via the systemic circulation. It appears to cross the blood–brain barrier less efficiently than L-phenylalanine, and so a small amount of an ingested dose of D-phenylalanine is excreted in the urine without penetrating the central nervous system.^{[citation needed]}

L-Phenylalanine is an antagonist at α2δ Ca²⁺ calcium channels with a K_i of 980 nM.^[14] At higher doses, this may play a role in its analgesic and antidepressant properties.

In the brain, L-phenylalanine is a competitive antagonist at the glycine binding site of NMDA receptor^[15] and at the glutamate binding site of AMPA receptor.^[16] At the glycine binding site of NMDA receptor L-phenylalanine has an apparent equilibrium dissociation constant (K_B) of 573 µM estimated by Schild regression^[17] which is considerably lower than brain L-phenylalanine concentration observed in untreated human phenylketonuria.^[18] L-Phenylalanine also inhibits neurotransmitter release at glutamatergic synapses in hippocampus and cortex with IC₅₀ of 980 µM, a brain concentration seen in classical phenylketonuria, whereas D-phenylalanine has a significantly smaller effect.^[16]

Commercial synthesis

L-Phenylalanine is produced for medical, feed, and nutritional applications, such as aspartame, in large quantities by utilizing the bacterium Escherichia coli, which naturally produces aromatic amino acids like phenylalanine. The quantity of L-phenylalanine produced commercially has been increased by genetically engineering E. coli, such as by altering the regulatory promoters or amplifying the number of genes controlling enzymes responsible for the synthesis of the amino acid.^[19]

Derivatives

Boronophenylalanine (BPA) is a dihydroxyboryl derivative of phenylalanine, used in neutron capture therapy.

References

^ Dawson, R. M. C.; et al. (1959). Data for Biochemical Research. Oxford: Clarendon Press.
^ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (1983). "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17.
^ Thorpe, T. E. (1913). A Dictionary of Applied Chemistry. Longmans, Green, and Co. pp. 191–193. Retrieved 2012-06-04.
^ Plimmer, R. H. A. (1912) [1908]. Plimmer, R. H. A.; Hopkins, F. G., ed. The Chemical Composition of the Proteins. Monographs on Biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. pp. 93–97. Retrieved 2012-06-04.
^ Harvey M. Ross; June Roth (1 April 1991). The Mood Control Diet: 21 Days to Conquering Depression and Fatigue. Simon & Schuster. p. 59. ISBN 978-0-13-590449-7.
^ http://www.msn.com/en-us/health/medical/15-reasons-why-drinking-diet-soda-and-alcohol-can-kill-you/ss-BBpp9X4#image=13
^ Broadley KJ (March 2010). "The vascular effects of trace amines and amphetamines". Pharmacol. Ther. 125 (3): 363–375. doi:10.1016/j.pharmthera.2009.11.005. PMID 19948186.
^ Lindemann L, Hoener MC (May 2005). "A renaissance in trace amines inspired by a novel GPCR family". Trends Pharmacol. Sci. 26 (5): 274–281. doi:10.1016/j.tips.2005.03.007. PMID 15860375.
^ Nelson, D. L.; Cox, M. M. (2000). Lehninger, Principles of Biochemistry (3rd ed.). New York: Worth Publishing. ISBN 1-57259-153-6.
^ "Aspartame". UK: Food Standards Agency.
^ Gibbs, R. A.; et al. (2007). "Evolutionary and Biomedical Insights from the Rhesus Macaque Genome" (pdf). Science 316 (5822): 222–234. doi:10.1126/science.1139247. PMID 17431167.
^ "D-phenylalanine". IUPHAR. Retrieved 24 June 2014.
^ Christianson, D. W.; Mangani, S.; Shoham, G.; Lipscomb, W. N. (1989). "Binding of D-Phenylalanine and D-Tyrosine to Carboxypeptidase A" (pdf). Journal of Biological Chemistry 264 (22): 12849–12853. PMID 2568989.
^ Mortell KH, Anderson DJ, Lynch JJ, et al. (March 2006). "Structure-activity relationships of alpha-amino acid ligands for the alpha2delta subunit of voltage-gated calcium channels". Bioorganic & Medicinal Chemistry Letters 16 (5): 1138–41. doi:10.1016/j.bmcl.2005.11.108. PMID 16380257.
^ Glushakov, AV; Dennis, DM; Morey, TE; Sumners, C; Cucchiara, RF; Seubert, CN; Martynyuk, AE (2002). "Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations observed during phenylketonuria.". Molecular Psychiatry 7 (4): 359–67. doi:10.1038/sj.mp.4000976. PMID 11986979.
^ ^a ^b Glushakov, AV; Dennis, DM; Sumners, C; Seubert, CN; Martynyuk, AE (Apr 1, 2003). "L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses.". Journal of neuroscience research 72 (1): 116–24. doi:10.1002/jnr.10569. PMID 12645085.
^ Glushakov, AV; Glushakova, O; Varshney, M; Bajpai, LK; Sumners, C; Laipis, PJ; Embury, JE; Baker, SP; Otero, DH; Dennis, DM; Seubert, CN; Martynyuk, AE (February 2005). "Long-term changes in glutamatergic synaptic transmission in phenylketonuria.". Brain : a journal of neurology 128 (Pt 2): 300–7. doi:10.1093/brain/awh354. PMID 15634735.
^ Möller, HE; Weglage, J; Bick, U; Wiedermann, D; Feldmann, R; Ullrich, K (December 2003). "Brain imaging and proton magnetic resonance spectroscopy in patients with phenylketonuria.". Pediatrics 112 (6 Pt 2): 1580–3. PMID 14654669.
^ Sprenger, G. A. (2007). "Aromatic Amino Acids". Amino Acid Biosynthesis: Pathways, Regulation and Metabolic Engineering (1st ed.). Springer. pp. 106–113. ISBN 978-3-540-48595-7.

External links

Phenylalanine mass spectrum
Phenylalanine at ChemSynthesis
Food Sources of Phenylalanine

UpToDate Contents

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1. フェニルケトン尿症の概要 overview of phenylketonuria
2. チロシン代謝障害 disorders of tyrosine metabolism
3. 肝性脳症：病因 hepatic encephalopathy pathogenesis
4. アスリートにおけるオーバートレーニング症候群 overtraining syndrome in athletes
5. ガラクトース血症：臨床的特徴および診断 galactosemia clinical features and diagnosis

English Journal

Dual effects of slightly acidic electrolyzed water (SAEW) treatment on the accumulation of γ-aminobutyric acid (GABA) and rutin in germinated buckwheat.

Hao J1, Wu T1, Li H1, Wang W2, Liu H3.
Food chemistry.Food Chem.2016 Jun 15;201:87-93. doi: 10.1016/j.foodchem.2016.01.037. Epub 2016 Jan 11.
In the present study, the dual effects of slightly acidic electrolyzed water (SAEW) treatment on γ-aminobutyric acid (GABA) and rutin accumulation of germinated buckwheat were evaluated during germination. The results showed that SAEW treatment (pH 5.83, ACC of 20.3mg/L) could promote the accumulat
PMID 26868552

Chemical composition and nutritional evaluation of the seeds of Acacia tortilis (Forssk.) Hayne ssp. raddiana.

Embaby HE1, Rayan AM2.
Food chemistry.Food Chem.2016 Jun 1;200:62-8. doi: 10.1016/j.foodchem.2016.01.019. Epub 2016 Jan 7.
Chemical composition and nutritional evaluation as well as physicochemical and functional properties of seed flour of Acacia tortilis (Forssk.) Hayne ssp. raddiana were studied. The results indicated that seeds contained 5.30% moisture, 3.99% ash, 9.19% fat, 14.31% fiber, 27.21% protein and 45.30% c
PMID 26830561

Enhancing phytochemical levels, enzymatic and antioxidant activity of spinach leaves by chitosan treatment and an insight into the metabolic pathway using DART-MS technique.

Singh S1.
Food chemistry.Food Chem.2016 May 15;199:176-84. doi: 10.1016/j.foodchem.2015.11.127. Epub 2015 Nov 28.
Phytochemicals are health promoting compounds, synthesized by the plants to protect them against biotic or abiotic stress. The metabolic pathways leading to the synthesis of these phytochemicals are highly inducible; therefore methods could be developed to enhance their production by the exogenous a
PMID 26775959

Japanese Journal

血漿中の乳糜およびビリルビンがHPLC-ESI/MS によるアミノ酸濃度分析に与える影響

CHROMATOGRAPHY advpub(0), 2016
NAID 130005144675

Enantioselective Determination of Phenylalanine, Tyrosine and 3,4-Dihydroxyphenylalanine in the Urine of D-Amino Acid Oxidase Deficient Mice Using Two-Dimensional High-Performance Liquid Chromatography

CHROMATOGRAPHY 37(1), 15-22, 2016
NAID 130005133691

Development of Spray-Freeze-Dried Powders for Inhalation with High Inhalation Performance and Antihygroscopic Property

Chemical and Pharmaceutical Bulletin 64(3), 239-245, 2016
NAID 130005131586

Related Pictures

★リンクテーブル★

リンク元	「フェニルアラニン」「L-phenylalanine」「F」
拡張検索	「3,4-dihydroxyphenylalanine」「p-fluorophenylalanine」「phenylalanine hydroxylase」「L-dihydroxyphenylalanine」

「フェニルアラニン」

Phenylalanine
	; L-Phenylalanine
	; L-Phenylalanine at physiological pH
Names
	IUPAC name Phenylalanine
	Other names 2-Amino-3-phenylpropanoic acid
Identifiers
CAS Number	150-30-1 (DL) ; 63-91-2 (L)
ChEBI	CHEBI:58095
ChEMBL	ChEMBL301523
ChemSpider	5910
DrugBank	DB00120
IUPHAR/BPS	3313
KEGG	D00021
PubChem	994
UNII	8P946UF12S
	InChI InChI=1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1 Key: COLNVLDHVKWLRT-QMMMGPOBSA-N ; InChI=1/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1 Key: COLNVLDHVKWLRT-QMMMGPOBBC ;
Properties
Chemical formula	C6H5CH2CH(NH2)COOH
Acidity (pKa)	1.83 (carboxyl), 9.13 (amino)
Hazards
Safety data sheet	See: data page
NFPA 704	1 2 0
Supplementary data page
Structure and; properties	Refractive index (n),; Dielectric constant (εr), etc.
Thermodynamic; data	Phase behaviour; solid–liquid–gas
Spectral data	UV, IR, NMR, MS
	verify (what is ?)
	Infobox references

フェニルアラニン
	IUPAC名 Phenylalanine
	別称 2-Amino-3-phenylpropanoic acid
識別情報
CAS登録番号	150-30-1 (DL) , 63-91-2 (L)
PubChem	994
ChemSpider	5910
UNII	8P946UF12S
DrugBank	DB00120
KEGG	D00021
ChEMBL	CHEMBL301523
	SMILES c1ccc(cc1)C[C@@H](C(=O)O)N;
	InChI InChI=1S/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1 ; Key: COLNVLDHVKWLRT-QMMMGPOBSA-N InChI=1/C9H11NO2/c10-8(9(11)12)6-7-4-2-1-3-5-7/h1-5,8H,6,10H2,(H,11,12)/t8-/m0/s1; Key: COLNVLDHVKWLRT-QMMMGPOBBC;
特性
化学式	C9H11NO2
モル質量	165.19 g mol−1
酸解離定数 pKa	1.83 (カルボキシル基), 9.13 (アミノ基)
	特記なき場合、データは常温 (25 °C)・常圧 (100 kPa) におけるものである。

　　[★]

英: phenylalanine, Phe, F
関: アミノ酸

胃でガストリン分泌↑

無電荷、無極性

-CH2-C6H5

アラニンにフェニル基(-C6H5)を付けたもの

「L-phenylalanine」

　　[★]

L-フェニルアラニン

関: phenylalanine

「F」

　　[★] フェニルアラニン phenylalanine 　

「3,4-dihydroxyphenylalanine」

　　[★]

3、ジヒドロキシフェニルアラニン、ドーパ

関: dihydroxyphenylalanine、DOPA

「p-fluorophenylalanine」

　　[★]

p-フルオロフェニルアラニン、パラフルオロフェニルアラニン

「phenylalanine hydroxylase」

　　[★] フェニルアラニン水酸化酵素

「L-dihydroxyphenylalanine」

　　[★]

関: Levodopa

同: L-DOPA

[1] Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959.

[1] Dawson, R. M. C.; et al. (1959). Data for Biochemical Research. Oxford: Clarendon Press.

[2] IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (1983). "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17.

[3] Thorpe, T. E. (1913). A Dictionary of Applied Chemistry. Longmans, Green, and Co. pp. 191–193. Retrieved 2012-06-04.

[4] Plimmer, R. H. A. (1912) [1908]. Plimmer, R. H. A.; Hopkins, F. G., ed. The Chemical Composition of the Proteins. Monographs on Biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. pp. 93–97. Retrieved 2012-06-04.

[RossRoth1991-5] Harvey M. Ross; June Roth (1 April 1991). The Mood Control Diet: 21 Days to Conquering Depression and Fatigue. Simon & Schuster. p. 59. ISBN 978-0-13-590449-7.

[6] ttp://www.msn.com/en-us/health/medical/15-reasons-why-drinking-diet-soda-and-alcohol-can-kill-you/ss-BBpp9X4#image=13

[Trace_amine_template_1-7] Broadley KJ (March 2010). "The vascular effects of trace amines and amphetamines". Pharmacol. Ther. 125 (3): 363–375. doi:10.1016/j.pharmthera.2009.11.005. PMID 19948186.

[Trace_amine_template_2-8] Lindemann L, Hoener MC (May 2005). "A renaissance in trace amines inspired by a novel GPCR family". Trends Pharmacol. Sci. 26 (5): 274–281. doi:10.1016/j.tips.2005.03.007. PMID 15860375.

[Nelson-9] Nelson, D. L.; Cox, M. M. (2000). Lehninger, Principles of Biochemistry (3rd ed.). New York: Worth Publishing. ISBN 1-57259-153-6.

[10] "Aspartame". UK: Food Standards Agency.

[11] Gibbs, R. A.; et al. (2007). "Evolutionary and Biomedical Insights from the Rhesus Macaque Genome" (pdf). Science 316 (5822): 222–234. doi:10.1126/science.1139247. PMID 17431167.

[12] "D-phenylalanine". IUPHAR. Retrieved 24 June 2014.

[13] Christianson, D. W.; Mangani, S.; Shoham, G.; Lipscomb, W. N. (1989). "Binding of D-Phenylalanine and D-Tyrosine to Carboxypeptidase A" (pdf). Journal of Biological Chemistry 264 (22): 12849–12853. PMID 2568989.

[pmid16380257-14] Mortell KH, Anderson DJ, Lynch JJ, et al. (March 2006). "Structure-activity relationships of alpha-amino acid ligands for the alpha2delta subunit of voltage-gated calcium channels". Bioorganic & Medicinal Chemistry Letters 16 (5): 1138–41. doi:10.1016/j.bmcl.2005.11.108. PMID 16380257.

[15] Glushakov, AV; Dennis, DM; Morey, TE; Sumners, C; Cucchiara, RF; Seubert, CN; Martynyuk, AE (2002). "Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations observed during phenylketonuria.". Molecular Psychiatry 7 (4): 359–67. doi:10.1038/sj.mp.4000976. PMID 11986979.

[Glushakov_116.E2.80.9324-16] Glushakov, AV; Dennis, DM; Sumners, C; Seubert, CN; Martynyuk, AE (Apr 1, 2003). "L-phenylalanine selectively depresses currents at glutamatergic excitatory synapses.". Journal of neuroscience research 72 (1): 116–24. doi:10.1002/jnr.10569. PMID 12645085.

[17] Glushakov, AV; Glushakova, O; Varshney, M; Bajpai, LK; Sumners, C; Laipis, PJ; Embury, JE; Baker, SP; Otero, DH; Dennis, DM; Seubert, CN; Martynyuk, AE (February 2005). "Long-term changes in glutamatergic synaptic transmission in phenylketonuria.". Brain : a journal of neurology 128 (Pt 2): 300–7. doi:10.1093/brain/awh354. PMID 15634735.

[18] Möller, HE; Weglage, J; Bick, U; Wiedermann, D; Feldmann, R; Ullrich, K (December 2003). "Brain imaging and proton magnetic resonance spectroscopy in patients with phenylketonuria.". Pediatrics 112 (6 Pt 2): 1580–3. PMID 14654669.

[19] Sprenger, G. A. (2007). "Aromatic Amino Acids". Amino Acid Biosynthesis: Pathways, Regulation and Metabolic Engineering (1st ed.). Springer. pp. 106–113. ISBN 978-3-540-48595-7.

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phenylalanine