Silman Israel, Sussman Joel L
Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.
Chem Biol Interact. 2008 Sep 25;175(1-3):3-10. doi: 10.1016/j.cbi.2008.05.035. Epub 2008 Jun 6.
In accordance with its biological role, termination of neurotransmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine, acetylcholinesterase is one of nature's most efficient enzymes. Solution of its three-dimensional structure revealed that its active site is located at the bottom of a deep and narrow gorge. Such an architecture was unanticipated in view of its high turnover number. The present review examines how the highly specialized structure of acetylcholinesterase, with its sequestered active site, contributes to its catalytic efficacy, and discusses how the traffic of substrate and products to and from the active site is controlled.
根据其生物学作用，通过快速水解神经递质乙酰胆碱来终止胆碱能突触处的神经传递，乙酰胆碱酯酶是自然界中最有效的酶之一。其三维结构的解析表明，其活性位点位于一个深而窄的峡谷底部。鉴于其高周转率，这样的结构是出人意料的。本综述探讨了具有隐蔽活性位点的乙酰胆碱酯酶的高度专业化结构如何有助于其催化效率，并讨论了底物和产物进出活性位点的运输是如何被控制的。
