Premium
Inhibition of bovine plasma semicarbazide‐sensitive amine oxidase by caffeine
Author(s) -
Olivieri A.,
Tipton K.
Publication year - 2011
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20356
Subject(s) - oxidative deamination , amine oxidase , chemistry , semicarbazide , benzylamine , methylamine , amine oxidase (copper containing) , amine gas treating , substrate (aquarium) , active site , enzyme , non competitive inhibition , biochemistry , diamine oxidase , stereochemistry , medicinal chemistry , organic chemistry , biology , ecology
Semicarbazide‐sensitive amine oxidase (SSAO) is a copper‐containing enzyme that catalyzes the oxidative deamination of endogenous and exogenous primary amines. SSAO exists in mammals both as a plasma‐soluble and as a membrane‐bound form, and its active site is able to come into contact with numerous xenobiotic, amine‐containing compounds. The kinetic studies performed in this work showed that caffeine inhibition of bovine serum amine oxidase was noncompetitive when benzylamine was used as substrate and mixed when the substrate used was methylamine. Since caffeine contains an imidazole ring, it cannot be excluded that it might bind to an inhibitory imidazoline‐binding site on SSAO. © 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:26–27 2011; View this article online at wileyonlinelibrary.com . DOI 10.1002/jbt.20356