Wiesner Jirí, Kriz Zdenek, Kuca Kamil, Jun Daniel, Koca Jaroslav
National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic.
J Enzyme Inhib Med Chem. 2007 Aug;22(4):417-24. doi: 10.1080/14756360701421294.
Acetylcholinesterase (AChE) is a widely spread enzyme playing a very important role in nerve signal transmission. As AChE controls key processes, its inhibition leads to the very fast death of an organism, including humans. However, when this feature is to be used for killing of unwanted organisms (i.e. mosquitoes), one is faced with the question - how much do AChEs differ between species and what are the differences? Here, a theoretical point of view was utilized to identify the structural basis for such differences. The various primary and tertiary alignments show that AChEs are very evolutionary conserved enzymes and this fact could lead to difficulties, for example, in the search for inhibitors specific for a particular species.
乙酰胆碱酯酶（AChE）是一种广泛分布的酶，在神经信号传递中起着非常重要的作用。由于AChE控制着关键过程，其抑制会导致生物体（包括人类）迅速死亡。然而，当要利用这一特性来杀死有害生物（如蚊子）时，就会面临一个问题——不同物种的AChE有多大差异以及差异是什么？在此，从理论角度来确定这种差异的结构基础。各种一级和三级比对表明，AChE是进化上非常保守的酶，这一事实可能会导致一些困难，例如，在寻找针对特定物种的抑制剂时。
