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  2. Phenylalanine (data page) - Wikipedia

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

    Structure. Crystal data: ... data relate to Standard temperature and ... ^a EINECS number 200-568-1 (phenylalanine) ^a CID 994 from PubChem (phenylalanine) ^a CID ...

  3. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Tyrosine ball and stick model spinning. L-Tyrosine or tyrosine (symbol Tyr or Y) [2] or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group.

  4. Phenylalanine - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine

    Phenylalanine ball and stick model spinning. Phenylalanine (symbol Phe or F) [3] is an essential α-amino acid with the formula C 9 H 11 NO 2.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.

  5. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    Tyrosine is semi-essential; therefore, it can be synthesized by the animal, but only from phenylalanine. Phenylketonuria, a genetic disorder that occurs as a result of the inability to breakdown phenylalanine, is due to a lack of the enzyme phenylalanine hydroxylase. A dietary lack of tryptophan can cause stunted skeletal development. [9]

  6. 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 ...

  7. Catecholamine - Wikipedia

    en.wikipedia.org/wiki/Catecholamine

    Tyrosine is created from phenylalanine by hydroxylation by the enzyme phenylalanine hydroxylase. Tyrosine is also ingested directly from dietary protein. Catecholamine-secreting cells use several reactions to convert tyrosine serially to L-DOPA and then to dopamine. Depending on the cell type, dopamine may be further converted to norepinephrine ...

  8. Biopterin-dependent aromatic amino acid hydroxylase - Wikipedia

    en.wikipedia.org/wiki/Biopterin-dependent...

    These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively. The AAAH enzymes are functionally and structurally related proteins which act as rate-limiting catalysts for important metabolic pathways . [ 1 ]

  9. 4-Hydroxyphenylpyruvic acid - Wikipedia

    en.wikipedia.org/wiki/4-Hydroxyphenylpyruvic_acid

    4-Hydroxyphenylpyruvic acid (4-HPPA) is an intermediate in the metabolism of the amino acid phenylalanine. The aromatic side chain of phenylalanine is hydroxylated by the enzyme phenylalanine hydroxylase to form tyrosine. The conversion from tyrosine to 4-HPPA is in turn catalyzed by tyrosine aminotransferase. [2]