Description
2種類のモノアミンオキシダーゼアイソザイム（MAOAとMAOB）がX染色体上に近接してあり、ミトコンドリア外膜に局在して発現する。2つの酵素は神経伝達物質と栄養素としてのアミンを酸化し、正常な精神状態を保つ。MAOAはセロトニン、ノルアドレナリン、ドーパミンを良い基質とする一方、MAOBはフェニルエチルアミンを代謝する。
- Two monoamine oxidase (EC 1.4.3.4) isoenzymes, MAOA and MAOB (309860), are closely linked in opposite orientation on the X chromosome and are expressed in the outer mitochondrial membrane. MAOA and MAOB oxidize neurotransmitters and dietary amines, the regulation of which is important in maintaining normal mental states. MAOA prefers serotonin, norepinephrine, and dopamine as substrates, whereas MAOB prefers phenylethylamine. Low levels of MAO activity and mutations in the MAOA gene have been associated with violent, criminal, or impulsive behavior (Chen et al., 2004).
- The MAOB gene encodes monoamine oxidase B. Two monoamine oxidase (EC 1.4.3.4) isoenzymes, MAOA (309850) and MAOB, catalyze the oxidative deamination of neuroactive and vasoactive amines, as well as the oxidation of several xenobiotics. MAOA and MAOB are present in the outer mitochondrial membrane in the central nervous system and peripheral tissues. MAOA, the primary type in fibroblasts, preferentially degrades serotonin and norepinephrine. MAOB, the primary type found in platelets and leukocytes, preferentially degrades phenylethylamine and benzylamine (summary by Bach et al., 1988).
Function
アミンの酸化的脱アミノ化を触媒し、中枢神経系、末梢組織で神経伝達物質や血管作動生アミンの代謝に重要。
MAOAは5-ヒドロキシトリプタミン、ノルアドレナリン、アドレナリンを基質とする。
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine. (MAOA)
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. (MAOB)
Catalytic activity
RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.
Cofactor
FAD.
Subunit structure
Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer By similarity.
Subcellular location
Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Tissue specificity
Heart, liver, duodenum, blood vessels and kidney.
Sequence similarities
Belongs to the flavin monoamine oxidase family.
