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首页> 外文期刊>Biological chemistry >Human butyrylcholinesterase components differ in aryl acylamidase activity
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Human butyrylcholinesterase components differ in aryl acylamidase activity

机译：人丁酰胆碱酯酶成分的芳基酰化酶活性不同

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摘要

Apart from its esterase activity, butyrylcholinesterase (BuChE) displays aryl acylamidase (AAA) activity able to hydrolyze o-nitroacetanilide (ONA) and its trifluoro-derivative (F-ONA). We report here that, despite amidase and esterase sites residing in the same protein, in human samples depleted of acetylcholinesterase the ratio of amidase to esterase activity varied depending on the source of BuChE. The much faster degradation of ONA and F-ONA by BuChE monomers (G,) of colon and kidney than by the tetramers (G(4)) suggests aggregation-driven differences in the AAA site between single and polymerized subunits. The similar ratio of F-ONA to butyrylthiocholine hydrolysis by serum G, and G, forms support structural differences in the amidase site according to the source of BuChE. The changing ratios of amidase to esterase activities in the human sources probably arise from post-translational modifications in BuChE subunits, the specific proportion of monomers and oligomers and the variable capacity of the tetramers for degrading ONA and F-ONA. The elevated amidase activity of BuChE monomers and the scant activity of the tetramers justify the occurrence of single BuChE subunits in cells as a means to sustain the AAA activity of BuChE which otherwise could be lost by tetramerization.
机译：除了其酯酶活性外，丁酰胆碱酯酶（BuChE）还具有能够水解邻硝基乙酰苯胺（ONA）及其三氟衍生物（F-ONA）的芳基酰化酶（AAA）活性。我们在这里报告说，尽管酰胺酶和酯酶位点驻留在同一蛋白质中，但在人体样品中乙酰胆碱酯酶消耗的情况下，酰胺酶与酯酶活性的比率因BuChE的来源而异。结肠和肾脏的BuChE单体（G）比四聚体（G（4））降解ONA和F-ONA的快得多，这表明由聚合驱动的单个和聚合亚基之间的AAA位点的差异。根据BuChE的来源，血清G和G的F-ONA与丁酰硫代胆碱水解的相似比例形成了酰胺酶位点的支持结构差异。人源中酰胺酶与酯酶活性比率的变化可能源自BuChE亚基的翻译后修饰，单体和低聚物的特定比例以及四聚物降解ONA和F-ONA的可变能力。 BuChE单体的酰胺酶活性升高，四聚体的活性低，证明了细胞中单个BuChE亚基的出现是维持BuChE AAA活性的一种手段，否则可能会因四聚作用而丧失。

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