Aromatic L-amino acid decarboxylase
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| dopa decarboxylase (aromatic L-amino acid decarboxylase)
| |
| Identifiers | |
| Symbol(s) | DDC |
| Entrez | 1644 |
| OMIM | 107930 |
| RefSeq | NM_000790 |
| UniProt | P20711 |
| Other data | |
| EC number | 4.1.1.28 |
| Locus | Chr. 7 p11 |
Aromatic L-amino acid decarboxylase (EC 4.1.1.28, synonyms: DOPA decarboxylase, tryptophan decarboxylase, 5-hydroxytryptophan decarboxylase, AAAD) is an enzyme catalyzing the decarboxylation of L-DOPA or 5-HTP to yield the neurotransmitters dopamine and serotonin (5-HT), respectively. The enzyme uses pyridoxal phosphate as a cofactor. In normal dopamine and 5-HT neurotransmitter synthesis, AAAD is not the rate-limiting step of in either reaction. However, AAAD becomes the rate-limiting step of dopamine formation in Parkinson's Disease patients treated with L-DOPA.
AAAD is the rate-limiting enzyme in the formation of biogenic trace amines.
The same enzyme is also able to the decarboxylate the amino acid tryptophan to tryptamine, a precursor to many alkaloids found in plants and animals.
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