MAOB:FAD oxidatively deaminates TYR

Stable Identifier
R-HSA-141202
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, mitochondrial outer membrane
ReviewStatus
5/5
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MAOB:FAD oxidatively deaminates TYR
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Monoamine oxidases (MAOA and B), present in the outer mitochondrial membrane, catalyse the oxidation of biogenic amines, releasing hydrogen peroxide (H2O2). H2O2 produced during the oxidative deamination of these amines appears to be involved in the progress of neurodegenerative disorders such as Parkinson disease, presumably via oxidative damage to the mitochondrial membrane. MAOB (also MAOA but not show here), with FAD as cofactor, can deaminate tyramine (TYR), a naturally-occuring monoamine that can act as a catecholamine releasing agent (Pearce & Roth 1985).
Literature References
PubMed ID Title Journal Year
4016087 Human brain monoamine oxidase type B: mechanism of deamination as probed by steady-state methods

Pearce, LB, Roth, JA

Biochemistry 1985
Participants
Input
Output
Participates
as an event of
Catalyst Activity

primary methylamine oxidase activity of MAOB:FAD [mitochondrial outer membrane]

Physical Entity
MAOB:FAD [mitochondrial outer membrane] (Homo sapiens)
Activity
primary methylamine oxidase activity (GO:0008131)
Orthologous Events
MAOB:FAD oxidatively deaminates TYR (Bos taurus)
MAOB:FAD oxidatively deaminates TYR (Dictyostelium discoideum)
MAOB:FAD oxidatively deaminates TYR (Mus musculus)
MAOB:FAD oxidatively deaminates TYR (Rattus norvegicus)
MAOB:FAD oxidatively deaminates TYR (Sus scrofa)
Cross References
RHEA
Authored
Jassal, B  (2008-05-19)
Reviewed
D'Eustachio, P  (2008-05-28)
Created
Jassal, B  (2004-09-03)
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