Inhibition of Bovine Plasma Semicarbazide-Sensitive Amine Oxidase by Caffeine

被引:12
|
作者
Olivieri, A. [1 ]
Tipton, K. [1 ]
机构
[1] Trinity Coll Dublin, Sch Biochem & Immunol, Dublin 2, Ireland
关键词
Semicarbazide-Sensitive Amine Oxidase (SSAO); Caffeine; Enzyme Inhibition; Imidazoline Binding Sites; MONOAMINE OXIDASES; ENZYMES;
D O I
10.1002/jbt.20356
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. 0 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:26-27, 2011; View this article online at wileyonlinelibrary.com. DOI 10:1002/jbt.20356
引用
收藏
页码:26 / 27
页数:2
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