Phenylalanine

PheL-phenylalaninephenylalanine metabolism L -phenylalanineFD-phenylalanine D -phenylalanineD/DL-PhenylalanineP'''henylalaninephenylalanyl
Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula.wikipedia
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Essential amino acid

essential amino acidsessentialnon-essential amino acid
This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain.
Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine.

Tyrosine

Tyrtyrosine metabolismL-tyrosine
Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin. Lignan is derived from phenylalanine and from tyrosine.
While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine.

Dopamine

dopaminergic systemDAdopaminergic
Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin.
The direct precursor of dopamine, L -DOPA, can be synthesized indirectly from the essential amino acid phenylalanine or directly from the non-essential amino acid tyrosine.

Monoamine neurotransmitter

monoaminemonoaminesmonoamine neurotransmitters
Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin.
All monoamines are derived from aromatic amino acids like phenylalanine, tyrosine, and tryptophan by the action of aromatic amino acid decarboxylase enzymes.

Norepinephrine

noradrenalinenoradrenergicnoradrenalin
Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin.
Thus the direct precursor of norepinephrine is dopamine, which is synthesized indirectly from the essential amino acid phenylalanine or the non-essential amino acid tyrosine.

Phenethylamine

phenylethylaminephenylethylaminesβ-phenethylamine
It is a direct precursor to the neuromodulator phenethylamine, a commonly used dietary supplement.
In mammals, phenethylamine is produced from the amino acid L-phenylalanine by the enzyme aromatic L-amino acid decarboxylase via enzymatic decarboxylation.

Amino acid

amino acidsresiduesresidue
Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula.
Of the 20 standard amino acids, nine (His, Ile, Leu, Lys, Met, Phe, Thr, Trp and Val) are called essential amino acids because the human body cannot synthesize them from other compounds at the level needed for normal growth, so they must be obtained from food.

Phenylacetaldehyde

2-phenylacetaldehyde
In 1882, Erlenmeyer and Lipp first synthesized phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia.
Phenylacetaldehyde occurs extensively in nature because it can be biosynthetically derived from the amino acid phenylalanine.

Genetic code

codoncodonsencoded
It is encoded by the codons UUU and UUC. The genetic codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W. Nirenberg in 1961.
They used a cell-free system to translate a poly-uracil RNA sequence (i.e., UUUUU...) and discovered that the polypeptide that they had synthesized consisted of only the amino acid phenylalanine.

Aspartame

E951aspartam
Another common source of phenylalanine is anything sweetened with the artificial sweetener aspartame, such as diet drinks, diet foods and medication; the metabolism of aspartame produces phenylalanine as one of the compound's metabolites.
It is a methyl ester of the aspartic acid/phenylalanine dipeptide with the trade names, NutraSweet, Equal, and Canderel.

Phenyl group

phenylphenyl ringPh
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.
Most common among natural products is the amino acid phenylalanine, which contains a phenyl group.

Catecholamine

catecholaminescatecholamine synthesiscatecholamine systems
The latter three are known as the catecholamines.
Catecholamines are derived from the amino acid tyrosine, which is derived from dietary sources as well as synthesis from phenylalanine.

Tetrahydrobiopterin

BH4Sapropterinsapropterin dihydrochloride
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. A (rare) "variant form" of phenylketonuria called hyperphenylalaninemia is caused by the inability to synthesize a cofactor called tetrahydrobiopterin, which can be supplemented.
Tetrahydrobiopterin (BH 4, THB), also known as sapropterin, is a cofactor of the three aromatic amino acid hydroxylase enzymes, used in the degradation of amino acid phenylalanine and in the biosynthesis of the neurotransmitters serotonin (5-hydroxytryptamine, 5-HT), melatonin, dopamine, norepinephrine (noradrenaline), epinephrine (adrenaline), and is a cofactor for the production of nitric oxide (NO) by the nitric oxide synthases.

Phenylalanine ammonia-lyase

phenylalanine ammonia lyasephenylalanine deaminaseEC 4.3.1.24
Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase.
Phenylalanine ammonia lyase is an enzyme that catalyzes a reaction converting L -phenylalanine to ammonia and trans-cinnamic acid.

Phenylketonuria

PKUphenylketonuria, maternalphenylketonurias
The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase.
Phenylketonuria (PKU) is an inborn error of metabolism that results in decreased metabolism of the amino acid phenylalanine.

Adrenaline

epinephrineadrenaline junkieadrenalin
Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin.
Adrenaline is synthesized in the chromaffin cells of the adrenal medulla of the adrenal gland and a small number of neurons in the medulla oblongata in the brain through a metabolic pathway that converts the amino acids phenylalanine and tyrosine into a series of metabolic intermediates and, ultimately, adrenaline.

Lignan

lignansneolignanenterolignan
Lignan is derived from phenylalanine and from tyrosine.
Plant lignans are polyphenolic substances derived from phenylalanine via dimerization of substituted cinnamic alcohols (see cinnamic acid), known as monolignols, to a dibenzylbutane skeleton 2.

J. Heinrich Matthaei

Heinrich J. MatthaeiHeinrich MatthaeiHeinrick Matthaei
The genetic codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W. Nirenberg in 1961.
Whilst a post-doctoral visitor in the laboratory of Marshall Warren Nirenberg at the NIH in Bethesda, Maryland, he discovered that a synthetic RNA polynucleotide, composed of a repeating uridylic acid residue, coded for a polypeptide chain encoding just one kind of amino acid, phenylalanine.

Phenylalanine hydroxylase

PAHEC 1.14.16.1phenylalanine
The genetic disorder phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalanine hydroxylase.
Phenylalanine hydroxylase (PAH) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine.

Ernst Schulze (chemist)

Ernst SchulzeSchulze
The first description of phenylalanine was made in 1879, when Schulze and Barbieri identified a compound with the empirical formula, C 9 H 11 NO 2, in yellow lupine (Lupinus luteus) seedlings.
During his four decades at Zürich, Schulze concentrated on a variety of phytochemical studies, in the course of which he and his doctoral students discovered the amino acids Glutamine, Phenylalanine and Arginine, among many other organic compounds.

Hyperphenylalaninemia

Hyperphenylalanemia
A (rare) "variant form" of phenylketonuria called hyperphenylalaninemia is caused by the inability to synthesize a cofactor called tetrahydrobiopterin, which can be supplemented.
Hyperphenylalaninemia is a medical condition characterized by mildly or strongly elevated concentrations of the amino acid phenylalanine in the blood.

Biopterin-dependent aromatic amino acid hydroxylase

aromatic amino acid hydroxylasearomatic amino acid hydroxylasesbiopterin-dependent aromatic amino acid hydroxylases
The corresponding enzymes in for those compounds are the aromatic amino acid hydroxylase family and nitric oxide synthase.
These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively.

Cinnamic acid

trans-cinnamatecinnamatecinnamic
Phenylalanine is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase.
Its biosynthesis involves the action of the enzyme phenylalanine ammonia-lyase (PAL) on phenylalanine.

Diet drink

Dietdiet sodadiet drinks
Another common source of phenylalanine is anything sweetened with the artificial sweetener aspartame, such as diet drinks, diet foods and medication; the metabolism of aspartame produces phenylalanine as one of the compound's metabolites.
The newer aspartame-free drinks can also be safely consumed by phenylketonurics, because they do not contain phenylalanine.

Marshall Warren Nirenberg

Marshall NirenbergMarshall W. NirenbergDr. Marshall Nirenberg
The genetic codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W. Nirenberg in 1961.
Only in the extract containing the radioactively labeled phenylalanine, was the resulting protein also radioactive.