Abstract
Due to their importance in age‐related degenerative diseases, mammalian monoamine oxidases A and B (MAO A and B) have been the object of extensive studies. The mechanistic description for the MAO‐catalyzed oxidation of amines is controversial resulting in three different proposed mechanism including a hydride ion abstraction (Fitzpatrick, 2010), a proton abstraction involving an intermediate covalent adduct on the flavin (Miller and Edmondson, 1999), or a proton abstraction following a radical pair formation (Lu et al., 2002). It is largely assumed that MAO A and MAO B follow the same mechanistic pathway. Comparison of the influence of para substituents on reaction rates by steady‐state and stopped‐flow kinetic analysis has been used to determine electronic effects of various benzylamine analogs. Human MAO A exhibits a positive ρ (+1.4) characteristic of a H+ abstraction while human MAO B exhibits a negative ρ (−0.9) characteristic of a Habstraction. These results suggest the two enzymes follow differing catalytic mechanisms thus demonstrating the assumption they follow identical mechanisms is not correct.Supported by grant GM‐29344 from the NIH.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
