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Phenylalanine and Tyrosine Biosynthesis
Last Updated: 2023-10-25
Phenylalanine and tyrosine are two of the 22 total amino acids, 21 of which are used in humans. Tyrosine is a non-essential amino acid, meaning that the body can produce enough of it as it needs without needing external sources. However, phenylalanine is an essential amino acid not produced by de-novo synthesis in animals, meaning that it is not synthesized from small molecules such as sugars, and can only be obtained from food, or by recycling other similar molecules. This pathway begins with L-phenylalanine, which can interact with amine oxidase to remove an amino group as well as add an oxygen molecule, forming phenylpyruvic acid. Phenylpyruvic acid can then be transformed to and from L-phenylalanine by either a Tat protein or aspartate aminotransferase, the latter of which exists in the mitochondria. L-phenylalanine can then interact with phenylalanine hydroxylase to add a hydroxyl group to its benzyl side chain, forming L-tyrosine. This can then interact with the same enzymes as L-phenylalanine, first amine oxidase to form 5-hydroxyphenylpyruvic acid. This can then interact with either the Tat protein or aspartate aminotransferase to reform, or be formed from L-tyrosine, with aspartate aminotransferase still existing in the mitochondria. L-phenylalanine can also be used in phenylalanine metabolism, while L-tyrosine can be used in tyrosine metabolism.
Phenylalanine and Tyrosine Biosynthesis References
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