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  2. Phenylalanine (data page) - Wikipedia

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

    Download as PDF; Printable version; In other projects Wikidata item; Appearance. ... ^a EINECS number 200-568-1 (phenylalanine) ^a CID 994 from PubChem (phenylalanine)

  3. Hyperphenylalaninemia - Wikipedia

    en.wikipedia.org/wiki/Hyperphenylalaninemia

    A small subset of patients with hyperphenylalaninemia shows an appropriate reduction in plasma phenylalanine levels with dietary restriction of this amino acid; however, these patients still develop progressive neurologic symptoms and seizures and usually die within the first 2 years of life ("malignant" hyperphenylalaninemia).

  4. Phenylalanine - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine

    The biological functions of D-amino acids remain unclear, although D-phenylalanine has pharmacological activity at niacin receptor 2. [17] DL-Phenylalanine (DLPA) is marketed as a nutritional supplement for its purported analgesic and antidepressant activities, which have been supported by clinical trials.

  5. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Phenylalanine: F Phe Essential for humans, phenylalanine, tyrosine, and tryptophan contain a large, rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Phenylalanine can be converted into ...

  6. Catecholamine - Wikipedia

    en.wikipedia.org/wiki/Catecholamine

    The amino acids phenylalanine and tyrosine are precursors for catecholamines. Both amino acids are found in high concentrations in blood plasma and the brain. In mammals, tyrosine can be formed from dietary phenylalanine by the enzyme phenylalanine hydroxylase, found in large amounts in the liver.

  7. Tryptophan hydroxylase - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_hydroxylase

    Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin. Tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases.

  8. α-Methylphenylalanine - Wikipedia

    en.wikipedia.org/wiki/Α-Methylphenylalanine

    α-Methylphenylalanine (α-MePhe or AMPA) is an artificial amino acid and a phenethylamine and amphetamine derivative. [1] It is the α-methylated analogue of phenylalanine, the precursor of the catecholamine neurotransmitters, and the amino acid analogue of amphetamine (α-methylphenethylamine), a psychostimulant and monoamine releasing agent.

  9. Phenylethanolamine N-methyltransferase - Wikipedia

    en.wikipedia.org/wiki/Phenylethanolamine_N...

    The active site binding region for the cofactor SAM contains a rich number of pi bonds from phenylalanine and tyrosine residues in the active site help to keep it in its binding pocket through pi stacking. Among all known PNMT variants in nature there are 7 crucial aromatic residues conserved in the active site. [5]