Aromatic L-amino acid decarboxylase

• OMIM: 107930
• UniProt: P20711

Aromatic L- amino acid decarboxylase ( AADC ), also known as dopa decarboxylase ( DDC), is the name given to enzymes in chordates that catalyze the biosynthesis of dopamine, serotonin and tryptamine using decarboxylation. As explorers applies the German pharmacologist Peter Holtz.

Mutations at the corresponding DDC gene and subsequent lack of the enzyme lead to lack of the appropriate neurotransmitters and catecholamines. AADC is the target gene therapy for the treatment of Parkinson's disease; Phase I trials have been successfully completed in 2008. Patients with polyendokriner autoimmune disease type I ( APS1 ) partly show autoantibodies to AADC. Some variants of the AADC are associated with nicotine dependence.

Catalyzed reactions

⇒ CO2

L- DOPA is decarboxylated to dopamine ( catecholamine synthesis).

⇒ CO2

5-Hydroxy- L-tryptophan is decarboxylated to serotonin.

⇒ CO2

L- tryptophan is decarboxylated to tryptamine.

⇒ CO2

L- histidine is decarboxylated to histamine.

⇒ CO2

L- tyrosine is decarboxylated to tyramine ( tyrosine degradation).

⇒ CO2

L- phenylalanine to phenethylamine decarboxylated (L -Phe- degradation).

Other Features

Although ubiquitous in the body, a study with mice, particularly high levels of AADC in kidney and intestine, and differences found in the renal concentration between males and females could be responsible for such gender differences in sodium balance. It is important for the development of the taste buds in mice.

AADC plays a role in the signal path of the androgen receptor.