Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.

ABSTRACT: The past decade has brought major advances in our knowledge of the structures and mechanisms of MAO A and MAO B, which are pharmacological targets for specific inhibitors. In both enzymes, crystallographic and biochemical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mitochondrial membrane. Pulsed EPR data show both enzymes are dimeric in their membrane-bound forms with agreement between distances measured in their crystalline forms. Distances measured between active site-directed spin-labels in membrane preparations show excellent agreement with those estimated from crystallographic data. Our knowledge of requirements for development of specific reversible MAO B inhibitors is in a fairly mature status. Less is known regarding the structural re

SUBMITTER: Edmondson DE 

PROVIDER: S-EPMC2710584 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature