Phenylalanine is converted to tyrosine by phenylalanine hydroxylase; tyrosine is a precursor for dopamine, norepinephrine, epinephrine, and thyroid hormones. Tryptophan serves as precursor for serotonin and the kynurenine pathway. All three aromatic amino acids are exclusively glucogenic, with carbon skeletons entering the citric acid cycle.
From your study of amino acid degradation, you know the general strategy: remove the amino group (via transamination or oxidative deamination), then channel the remaining carbon skeleton into central metabolic intermediates. The aromatic amino acids — phenylalanine, tyrosine, and tryptophan — follow this same logic, but their bulky aromatic rings make their degradation pathways more elaborate and biochemically distinctive. These three amino acids are also unique because their catabolic intermediates serve as precursors to some of the body's most important signaling molecules.
The most clinically significant pathway begins with phenylalanine. The enzyme phenylalanine hydroxylase (PAH) adds a hydroxyl group to phenylalanine's aromatic ring, converting it to tyrosine. This reaction requires molecular oxygen and the cofactor tetrahydrobiopterin (BH4), which gets oxidized in the process and must be regenerated by dihydrobiopterin reductase. This single reaction is so important that its failure — through mutations in PAH or BH4 metabolism — causes phenylketonuria (PKU), one of the most well-known inborn errors of metabolism. Because phenylalanine is converted to tyrosine before further degradation, tyrosine is the true hub of aromatic amino acid catabolism: both phenylalanine and tyrosine converge on the same downstream pathway.
Tyrosine degradation proceeds through a five-step pathway that ultimately yields fumarate (a citric acid cycle intermediate) and acetoacetate (a ketone body). This makes tyrosine both glucogenic and ketogenic. But tyrosine's metabolic significance extends far beyond its degradation. In specialized tissues, tyrosine is hydroxylated to form L-DOPA, which is decarboxylated to dopamine — the neurotransmitter central to motor control, reward, and motivation. Dopamine is further hydroxylated to norepinephrine and then methylated to epinephrine, forming the catecholamine signaling cascade. In the thyroid gland, tyrosine residues within thyroglobulin are iodinated and coupled to produce thyroid hormones (T3 and T4). In melanocytes, tyrosine is oxidized to form melanin pigments. No other amino acid feeds into as many physiologically critical biosynthetic pathways.
Tryptophan follows its own distinctive route. The major catabolic pathway is the kynurenine pathway, which opens the indole ring and ultimately produces alanine (glucogenic) and acetyl-CoA through a series of oxidative steps. Along the way, intermediates of this pathway include kynurenine and quinolinate, the latter being a precursor for NAD+ biosynthesis — making tryptophan the dietary source for de novo synthesis of this essential coenzyme. In a separate, quantitatively minor pathway, tryptophan is hydroxylated by tryptophan hydroxylase to form 5-hydroxytryptophan, which is then decarboxylated to produce serotonin — the neurotransmitter that regulates mood, sleep, and appetite. Serotonin can be further converted to melatonin in the pineal gland. The clinical importance of these branching pathways explains why aromatic amino acid metabolism appears so frequently in biochemistry and medical contexts.