Expression of Functional Human Monoamine Oxidase A and B cDNAs in Mammalian Cells

These results suggest that a single polypeptide of Monoamine oxidase A, existing as either a monomer or homodimer, is enzymatically active

Nancy C. Lan; Chonghong Chen; Jean C. Shih

2006

Scholarcy highlights

  • Previous studies had suggested that both Monoamine oxidase A and B consist of two subunits of molecular masses of 63 and 60 kilodaltons, respectively
  • The cDNAs encoding one subunit of human liver MAO A and B have been expressed in mammalian cells by transfection of the individual clones
  • The proteins expressed from these cDNAs are shown to be catalytically active
  • Similar to the endogenous enzymes, the expressed MAO A prefers serotonin as a substrate and is sensitive to the inhibitor clorgyline
  • The expressed MAO B prefers phenylethyl-amine as a substrate and is sensitive to the inhibitor deprenyl. These results suggest that a single polypeptide of MAO A, existing as either a monomer or homodimer, is enzymatically active
  • The ability to obtain functional Monoamine oxidase A and B from their respective cDNA clones allows us to study further the structure and function relationships of these important enzymes

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