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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.
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Flavonoids are synthesized by the phenylpropanoid metabolic pathway in which the amino acid phenylalanine is used to produce 4-coumaroyl-CoA. [1] This can be combined with malonyl-CoA to yield the true backbone of flavonoids, a group of compounds called chalcones , which contain two phenyl rings.
Thus, the two substrates of this enzyme are L-phenylalanine and pyruvate, whereas its two products are phenylpyruvate and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-phenylalanine:pyruvate aminotransferase.
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In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction. L-phenylalanine + H 2 O + NAD + phenylpyruvate + NH 3 + NADH + H +. The 3 substrates of this enzyme are L-phenylalanine, H 2 O, and NAD +, whereas its 4 products are phenylpyruvate, NH 3, NADH, and H +.
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