Tyr393 and Tyr398 mutants of monoamine oxidase B
US6440714B2 · kind B2 · utility
Assignee
Inventors
Key dates
| Filing date | Mar 30, 2001 |
| Grant date | Aug 27, 2002 |
| Priority date | — |
| Expiry date | Mar 30, 2021 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC12N9/0022
- WIPO fieldBiotechnology
- WIPO sectorChemistry
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.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.