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D-Phenylalanine is distributed to the various tissues of the body via the systemic circulation. It appears to cross the blood–brain barrier less efficiently than L -phenylalanine, and so a small amount of an ingested dose of D -phenylalanine is excreted in the urine without penetrating the central nervous system.
Tyrosine is a conditionally essential amino acid for PKU patients because without PAH it cannot be produced in the body through the breakdown of phenylalanine. [ citation needed ] PAH deficiency causes a spectrum of disorders, including classic phenylketonuria (PKU) and mild hyperphenylalaninemia (also known as "hyperphe" or "mild HPA"), [ 24 ...
Hyperphenylalaninemia is a recessive hereditary metabolic disorder that is caused by the body's failure to convert phenylalanine to tyrosine as a result of the entire or partial absence of the enzyme phenylalanine hydroxylase. [3]
“The body naturally can make tyrosine from [another amino acid] phenylalanine, and it can be obtained directly through diet from a variety of foods,” says Pumper.
This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral l-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency. [11] l-Phenylalanine, l-tyrosine, and l-DOPA are all precursors to the biological pigment melanin.
In mammals it is created from -lactate and L-phenylalanine by the cytosol nonspecific dipeptidase (CNDP2) protein. [1] It is classified as N-acyl-alpha-amino acid and pseudodipeptide. [11] It has also been reported that as an additive, N-L-lactoyl phenylalanine improves the taste of food, conferring an umami flavor [12].