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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.
Tyrosine ball and stick model spinning. L-Tyrosine or tyrosine (symbol Tyr or Y) [2] or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group.
Tyrosine is semi-essential; therefore, it can be synthesized by the animal, but only from phenylalanine. Phenylketonuria, a genetic disorder that occurs as a result of the inability to breakdown phenylalanine, is due to a lack of the enzyme phenylalanine hydroxylase. A dietary lack of tryptophan can cause stunted skeletal development. [9]
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.
Tyrosine is created from phenylalanine by hydroxylation by the enzyme phenylalanine hydroxylase. Tyrosine is also ingested directly from dietary protein. Catecholamine-secreting cells use several reactions to convert tyrosine serially to L-DOPA and then to dopamine. Depending on the cell type, dopamine may be further converted to norepinephrine ...
Tyrosine: Y Tyr Tyr behaves similarly to phenylalanine (precursor to tyrosine) and tryptophan, and is a precursor of melanin, epinephrine, and thyroid hormones. Naturally fluorescent, its fluorescence is usually quenched by energy transfer to tryptophans. Glutamic acid or glutamine: Z Glx A placeholder when either amino acid may occupy a position
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