Molecular basis of human MAO A and B.
Molecular basis of human MAO A and B.
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发表时间：
1991
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通讯作者：
J. Shih
中科院分区：
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作者：
J. Shih
单胺氧化酶A和B （MAO A和B）催化许多具有不同底物和抑制剂特异性的生物胺和外源胺的氧化脱胺作用。近年来，已分离出编码人肝脏MAO A和B的cDNA克隆。推导出的氨基酸序列的比较表明，它们同源性为70%，似乎来自不同的基因。通过瞬时转染cdna表达的功能酶提供了明确的证据，证明MAO A和B的不同催化活性存在于它们的一级氨基酸序列中。这两个位于X染色体上的基因Xp11.23在一些诺里病患者中缺失。MAO基因对许多疾病的可能作用或联系现在可以进行研究。
Monoamine oxidase A and B (MAO A and B) catalyze the oxidative deamination of a number of biogenic and xenobiotic amines with different substrate and inhibitor specificities. Recently, cDNA clones that encode the human liver MAO A and B have been isolated. Comparison of the deduced amino acid sequences shows that they are 70% homologous and they appear to be derived from separate genes. Expression of functional enzymes by transient transfection of the cDNAs provide unequivocal evidence that the different catalytic activities of MAO A and B reside in their primary amino acid sequences. These two genes located on the X chromosome, Xp11.23, are deleted in some patients with Norrie disease. The possible role or the linkage of MAO genes to a number of diseases can now be investigated.