InterProInterPro Protein Domain record

Flavin amine oxidase
http://metadb.riken.jp/db/SciNetS_rib124i/crib124s1rib124u1613i

Flavin amine oxidase

InterPro Protein Domain record

description
  • <p>Monoamine oxidases (MAO) A and B are encoded by two genes derived from a common ancestral gene [<cite idref="PUB00003462"/>]. The enzymes catalyse the oxidative deamination of biogenic and xenobiotic amines and have important roles in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues [<cite idref="PUB00003451"/>]. MAO-A preferentially oxidises biogenic amines such as 5-hydroxytryptamine, norepinephrine and epinephrine. MAO-A deficiency has been linked to Brunner's syndrome, a form of X-linked nondysmorphic mild mental retardation [<cite idref="PUB00003451"/>].</p><p>The protein contains two similarly-sized subunits, one of which contains covalently-bound flavin adenine dinucleotide (FAD). The FAD binding site lies near the C terminus; at the N terminus are features characteristic of the ADP-binding fold, suggesting that this region is also involved in FAD binding [<cite idref="PUB00003451"/>]. The A and B forms of the enzyme share 70% sequence identity; both contain the pentapeptide Ser-Gly-Gly-Cys-Tyr, the cysteine of which binds FAD [<cite idref="PUB00004658"/>].</p>
label
  • Flavin amine oxidase
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type
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Os_RAPDB_Locus