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Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC. Phenylalanine is found naturally in the milk of mammals.
Molecular diagram of L-phenylalanine. Items portrayed in this file depicts. creator. some value. author name string: NEUROtiker.
^a CID 71567 from PubChem (D-phenylalanine) ^a CID 6140 from PubChem (L-phenylalanine) This page was last edited on 12 January 2024, at 23:28 (UTC). Text is ...
Phenylalanine: F Phe Essential for humans, phenylalanine, tyrosine, and tryptophan contain a large, rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Phenylalanine can be converted into ...
Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine.PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH 4, a pteridine cofactor) and a non-heme iron for catalysis.
In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction. acetyl-CoA + L-phenylalanine CoA + N-acetyl-L-phenylalanine. Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products are CoA and N-acetyl-L-phenylalanine.
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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.