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  2. 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]

  3. 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.

  4. Essential amino acid - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acid

    So, for convenience, sulfur-containing amino acids are sometimes considered a single pool of nutritionally equivalent amino acids as are the aromatic amino acid pair, phenylalanine and tyrosine. Likewise arginine , ornithine , and citrulline , which are interconvertible by the urea cycle , are considered a single group.

  5. Everything You Need To Know about Tyrosine - AOL

    www.aol.com/lifestyle/everything-know-tyrosine...

    Tyrosine is an amino acid made by the body. It may boost cognitive function, especially during periods of stress. Many foods contain tyrosine. Skip to main content. 24/7 Help. For premium support ...

  6. 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.

  7. 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]