Aromatic L-amino acid decarboxylase
Aromatic L-amino acid decarboxylase (pronounced: a-ro-ma-tic el-a-mi-no a-cid de-car-box-y-lase), also known as DOPA decarboxylase or DDC, is an enzyme that plays a crucial role in the biosynthesis of several important neurotransmitters in the human body.
Etymology
The term "aromatic" refers to the presence of a benzene ring in the amino acids that this enzyme acts upon. "L-amino acid" refers to the configuration of the amino acids, which are left-handed (L) in most organisms. "Decarboxylase" refers to the type of reaction this enzyme catalyzes, which is the removal of a carboxyl group from the amino acids.
Function
Aromatic L-amino acid decarboxylase is responsible for the decarboxylation of L-DOPA to dopamine, 5-hydroxytryptophan to serotonin, and histidine to histamine. These neurotransmitters are essential for various physiological functions, including mood regulation, motor control, and immune response.
Related Terms
- Dopamine: A neurotransmitter produced by the decarboxylation of L-DOPA by aromatic L-amino acid decarboxylase.
- Serotonin: A neurotransmitter produced by the decarboxylation of 5-hydroxytryptophan by aromatic L-amino acid decarboxylase.
- Histamine: A neurotransmitter produced by the decarboxylation of histidine by aromatic L-amino acid decarboxylase.
- Decarboxylation: The chemical reaction that removes a carboxyl group from a molecule, which is catalyzed by enzymes like aromatic L-amino acid decarboxylase.
See Also
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