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Enhanced enzymatic activity exerted by a packed assembly of a single type of enzyme
Chemical Science ( IF 8.4 ) Pub Date : 2020-07-27 , DOI: 10.1039/d0sc03498c
Huyen Dinh 1 , Eiji Nakata 1 , Kaori Mutsuda-Zapater 1 , Masayuki Saimura 1 , Masahiro Kinoshita 1 , Takashi Morii 1
Affiliation  

In contrast to the dilute conditions employed for in vitro biochemical studies, enzymes are spatially organized at high density in cellular micro-compartments. In spite of being crucial for cellular functions, enzymatic reactions in such highly packed states have not been fully addressed. Here, we applied a protein adaptor to assemble a single type of monomeric enzyme on a DNA scaffold in the packed or dispersed states for carbonic anhydrase. The enzymatic reactions proceeded faster in the packed than in the dispersed state. Acceleration of the reaction in the packed assembly was more prominent for substrates with higher hydrophobicity. In addition, carbonic anhydrase is more tolerant of inhibitors in the packed assembly. Such an acceleration of the reaction in the packed state over the dispersed state was also observed for xylose reductase. We propose that the entropic force of water increases local substrate or cofactor concentration within the domain confined between enzyme surfaces, thus accelerating the reaction. Our system provides a reasonable model of enzymes in a packed state; this would help in engineering artificial metabolic systems.

中文翻译:

单一类型酶的紧密组装可增强酶活性

与体外生化研究所采用的稀释条件相反,酶在细胞微区室中以高密度空间组织。尽管对于细胞功能至关重要,但如此高度堆积状态下的酶反应尚未得到充分解决。在这里,我们应用蛋白质接头在 DNA 支架上以堆积或分散状态组装单一类型的单体酶,用于碳酸酐酶。酶促反应在堆积状态下比在分散状态下进行得更快。对于疏水性较高的基材,堆积组件中的反应加速更为显着。此外,碳酸酐酶对包装组件中的抑制剂具有更强的耐受性。对于木糖还原酶,也观察到堆积状态下的反应比分散状态下的反应加速。我们认为水的熵力增加了酶表面之间限制的区域内的局部底物或辅因子浓度,从而加速了反应。我们的系统提供了包装状态下酶的合理模型;这将有助于设计人工代谢系统。
更新日期:2020-09-03
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