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Last Updated: 2023-10-25
Phenylalanine is one of the 22 proteinogenic amino acids present in organisms, specifically its L-isomer. It is an alpha-amino acid, meaning the side chain is present on the first, or alpha, carbon of the compound. In this case, the side chain is a benzyl group, and as this is inert and hydrophobic, leading the amino acid itself to be neutral and non-polar. Phenylalanine is also an essential amino acid in zebrafish, meaning that they can not be synthesized de novo by the organism, and instead must be obtained from food sources, including supplements if necessary. L-henylalanine can come from phenylalanine biosynthesis, and can be converted by phenylalanine hydroxylase to L-tyrosine. L-tyrosine can then be used in tyrosine metabolism. L-phenylalanine can also be converted to and from phenylpyruvic acid in the mitochondria by either aspartae aminotransferase or tyrosine transaminase. It can also be converted to phenylpyruvic acid in a non-reversible reaction catalyzed by amine oxidase. Phenylpyruvic acid can be converted to ortho-hydroxyphenylacetc acid by 4-hydroxyphenylpyruvate dioxygenase which removes a carbon atom from the structure and alters some bonds. It can also be reversibly converted to enol-phenylpyruvate by phenylpyruvate tautomerase. Finally, L-phenylalanine can be converted to phenylethylamine by aromatic-L-amino-acid decarboxylase, which removes a carbon dioxide molecule. From here, phenylethylamine is converted reversibly to phenylacetaldehyde by either a primary amine oxidase or monoamine oxidase. Phenylacetaldehyde is then converted reversibly to phenylacetic acid by aldehyde dehydrogenase, forming the final product of the pathway.
Phenylalanine Metabolism References
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