title: Molecular basis of human MAO A and B.
abstract: 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.
authors.affiliation: School of Pharmacy, University of Southern California, Los Angeles 90033.
authors.forename: J C
authors.initials: JC
authors.lastname: Shih
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D006801:Humans; D007527:Isoenzymes / Q000235:genetics*; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D014162:Transfection; D014960:X Chromosome
chemical_list: D007527:Isoenzymes; D008995:Monoamine Oxidase