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  2. 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.

  3. 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)

  4. 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.

  5. List of dopaminergic drugs - Wikipedia

    en.wikipedia.org/wiki/List_of_dopaminergic_drugs

    Dopamine receptors are a class of G protein-coupled receptors that are prominent in the vertebrate central nervous system (CNS) and are implicated in many neurological processes, including motivational and incentive salience, cognition, memory, learning, and fine motor control, as well as modulation of neuroendocrine signaling.

  6. Ketogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Ketogenic_amino_acid

    A ketogenic amino acid is an amino acid that can be degraded directly into acetyl-CoA, which is the precursor of ketone bodies and myelin, particularly during early childhood, when the developing brain requires high rates of myelin synthesis. [1] This is in contrast to the glucogenic amino acids, which are converted into glucose.

  7. 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]

  8. 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.

  9. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) from PEP/E4P, uses three isoenzymes AroF, AroG, and AroH. Each one of these has its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively.