Tyr393 and Tyr398 mutants of monoamine oxidase B

Abstract

Monoamine oxidase A and B (MAO A and B) are major neurotransmitter- and xenobiotic-metabolizing enzymes that are thought to play a role in psychiatric and neurological disorders. These isozymes have a high degree of identity in their nucleotide deduced amino acid sequences, but are encoded by different genes on the X-chromosome. Previous studies on MAO B have shown that FAD binds both noncovalently and covalently to specific amino acid residues that reside in highly conserved regions of MAO A and B. In the instant invention, it is demonstrated that the aromatic moieties at Tyr393 and Tyr398, which are located on each side of the covalent FAD binding residue (Cys397) participate in covalent FAD binding, and the generation of catalytically active MAO B.

Dependencies are inferred from the claim text.