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Rat monoamine oxidase B expressed in Escherichia coli has a covalently-bound FAD.

Rat liver monoamine oxidase B (MAO B) was expressed in E. coli as catalytically active form, though inclusion bodies of the enzyme were also formed as a major protein in the cell. The active form of the recombinant MAO B exhibited similar properties as rat liver enzyme and localized in membrane of the bacteria. Covalent attachment of FAD to polypeptide chain of the recombinant enzyme was revealed by a labeling experiment with [3H]-pargyline, an irreversible mechanism-based inhibitor, indicating that the covalent linkage of FAD to the apoprotein was formed even in the prokaryotic cell. This observation suggests autocatalytic formation of the linkage in MAO B.