Structural highlights
Function
AOFB_HUMAN Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
Publication Abstract from PubMed
The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 +/- 0.3 muM), of rat MAO B (K(i) = 2.9 +/- 0.5 muM), and of zebrafish MAO (K(i) = 30.8 +/- 5.3 muM). No inhibition is observed with purified human or rat MAO A. The 1.8 A structure of the MAO B complex demonstrates that it binds within the substrate cavity.
Interactions of Monoamine Oxidases with the Antiepileptic Drug Zonisamide: Specificity of Inhibition and Structure of the Human Monoamine Oxidase B Complex.,Binda C, Aldeco M, Mattevi A, Edmondson DE J Med Chem. 2010 Dec 22. PMID:21175212[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Binda C, Aldeco M, Mattevi A, Edmondson DE. Interactions of Monoamine Oxidases with the Antiepileptic Drug Zonisamide: Specificity of Inhibition and Structure of the Human Monoamine Oxidase B Complex. J Med Chem. 2010 Dec 22. PMID:21175212 doi:10.1021/jm101359c
