Despite the quinone-dependent copper amine oxidases being described as having the ability to metabolize unbranched primary amines to the corresponding aldehydes, we previously showed that the secondary amines 3-pyrrolines are metabolized as mechanism-based inactivators of bovine plasma amine oxidase (BPAO), and that the 3-(3-nitro-4-methoxyphenyl)-substituted analog was a particularly potent and efficient inactivator. We now show that additional 3-aryl-3-pyrrolines containing highly electron-withdrawing aryl groups (pyridyl, quinolyl, isoquinolyl, and pentafluorophenyl) are some of the most potent inactivators of BPAO reported to date. We also provide mass spectroscopic confirmation of the proposed mechanism of inhibition involving pyrrolylation of the active-site cofactor, through identification by MALDI-TOF and LC-ESI-MS/MS of the (3-arylpyrrol-1-yl)resorcinol derivatives of the cofactor-containing thermolytic peptides. © 2006 Elsevier Ltd. All rights reserved.
Mendeley saves you time finding and organizing research
Choose a citation style from the tabs below