Substrate tunnels in enzymes: structure-function relationships and computational methodology.
Substrate tunnels in enzymes: structure-function relationships and computational methodology.
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DOI：
10.1002/prot.24772
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发表时间：
2015-04
影响因子：
2.9
通讯作者：
Lill, Markus A.
中科院分区：
文献类型：
--
作者：
Kingsley, Laura J.;Lill, Markus A.
在酶中，活性位点是进入的底物化学转化为产物的位置。在一些酶中，这个位点深埋在蛋白质的核心，为了进入活性位点，底物必须通过一个隧道穿过蛋白质的主体。在许多系统中，这些通道充当过滤器，并被发现影响底物特异性和催化机制。在过去的几年里，由于蛋白质工程和药物设计等领域的影响，识别和理解这些通道如何发挥这种控制作用已经越来越引起人们的兴趣。这种日益增长的兴趣刺激了几种计算方法的发展，以识别和分析隧道以及配体如何通过这些隧道迁移。这篇综述的目的是概述隧道是如何影响底物特异性和催化效率的酶的隧道，并提供一个简短的总结用于识别和评估这些隧道的计算工具。
In enzymes, the active site is the location where incoming substrates are chemically converted to products. In some enzymes, this site is deeply buried within the core of the protein and in order to access the active site, substrates must pass through the body of the protein via a tunnel. In many systems, these tunnels act as filters and have been found to influence both substrate specificity and catalytic mechanism. Identifying and understanding how these tunnels exert such control has been of growing interest over the past several years due to implications in fields such as protein engineering and drug design. This growing interest has spurred the development of several computational methods to identify and analyze tunnels and how ligands migrate through these tunnels. The goal of this review is to outline how tunnels influence substrate specificity and catalytic efficiency in enzymes with tunnels and to provide a brief summary of the computational tools used to identify and evaluate these tunnels.
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影响因子：
8
作者：
Brocca, S;Secundo, F;Lotti, M
通讯作者：
Lotti, M
DOI：
10.1073/pnas.0807948105
发表时间：
2008-12-09
影响因子：
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作者：
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影响因子：
5.6
作者：
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通讯作者：
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