MAOA:FAD oxidatively deaminates of 5HT

Stable Identifier
R-HSA-141186
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Amine oxidase (flavin-containing) A (MAOA) catalyses the oxidative deamination of biogenic and dietary amines, the regulation of which is critical for mental state homeostasis. MAOA, located on the mitochondrial outer membrane and requiring FAD as cofactor (Weyler 1989), preferentially oxidises biogenic amines such as 5-hydroxytryptamine (5HT), dopamine, noradrenaline and adrenaline (latter three not shown here). 5HT is deaminated to 5-hydroxyindolacetaldehyde (5HIALD).

Literature References
PubMed ID Title Journal Year
2764901 Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit

Weyler, W

Biochem. J. 1989
6408492 The deamination of dopamine by human brain monoamine oxidase. Specificity for the two enzyme forms in seven brain regions

O'Carroll, AM, Fowler, CJ, Phillips, JP, Tobbia, I, Tipton, KF

Naunyn Schmiedebergs Arch Pharmacol 1983
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
primary amine oxidase activity of MAOA:FAD [mitochondrial outer membrane]
Physical Entity
Activity
Orthologous Events
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Created