aromatic-L-amino-acid decarboxylase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-amino acid + H+ = R-H + CO2. [EC:4.1.1.28]

Aromatic-L-amino-acid decarboxylase activity refers to the enzymatic ability to catalyze the removal of a carboxyl group (COOH) from aromatic L-amino acids. This process involves decarboxylation, a chemical reaction where carbon dioxide (CO2) is released. Specifically, this activity targets amino acids with an aromatic ring, such as L-dopa (L-3,4-dihydroxyphenylalanine), L-tryptophan, and L-tyrosine.

The resulting products of this decarboxylation are biogenic amines, which are crucial signaling molecules in various physiological processes. For example, the decarboxylation of L-dopa yields dopamine, a neurotransmitter involved in movement, motivation, and reward. Similarly, decarboxylation of L-tryptophan produces serotonin, another neurotransmitter associated with mood, sleep, and appetite.

The enzyme responsible for aromatic-L-amino-acid decarboxylase activity is commonly known as aromatic L-amino acid decarboxylase (AADC). It is a pyridoxal phosphate-dependent enzyme, meaning it requires vitamin B6 (pyridoxine) as a cofactor for its catalytic activity.

AADC is found in various tissues, including the brain, adrenal glands, and peripheral nervous system. Its activity is critical for the synthesis of neurotransmitters and other bioactive molecules.

Mutations or deficiencies in AADC can lead to serious neurological disorders, such as dopa-responsive dystonia, a condition characterized by involuntary muscle contractions. This underscores the importance of AADC and its role in maintaining normal neurological function.'
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Proteins (1)

Compounds (4)