Tag: Aromatic amino acids

Over 500 naturally occurring amino acids exist, but only 20 are commonly used to build proteins in the human body. The answer to "Do phenylalanine tryptophan and tyrosine belong to the amino acids?" is an unequivocal yes, with each playing a distinct and crucial role.

Aromatic L-amino acid decarboxylase (AADC) deficiency, a key cause behind a deficiency of aromatic acids, is a rare neurometabolic disorder with typical onset within the first six months of life. This critical deficiency has a domino effect on the body, disrupting the synthesis of vital neurotransmitters and causing a cascade of severe health problems.

Approximately 75% of a human's body mass is composed of protein, and among the 20 standard amino acids that form these proteins are a special subset known as the natural aromatic amino acids. These unique amino acids contain an aromatic ring structure, which plays a pivotal role in the function of many proteins and serves as a precursor for numerous important biological molecules.

Over 95% of tryptophan is metabolized via the kynurenine pathway in mammals, a testament to the crucial role of aromatic amino acids in our bodies. These essential compounds, including phenylalanine, tryptophan, and tyrosine, must be obtained through a balanced diet, as the human body cannot produce them.

Approximately 70% of ingested phenylalanine is converted to tyrosine in the liver, highlighting their close metabolic relationship. The amino acid most similar to tyrosine, both structurally and functionally, is phenylalanine, primarily due to their shared aromatic ring structure.