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In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature.
Phenylalanine (symbol Phe or F) [3] is an essential α-amino acid with the formula C 9 H 11 NO 2.It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine.
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]
Tyrosine (and its precursor phenylalanine) are precursors of the catecholamine neurotransmitters dopamine, epinephrine and norepinephrine and various trace amines. Phenylalanine is a precursor of phenethylamine and tyrosine in humans. In plants, it is a precursor of various phenylpropanoids, which are important in plant metabolism.
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
These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively. The AAAH enzymes are functionally and structurally related proteins which act as rate-limiting catalysts for important metabolic pathways. [1]
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