Engineering Rieske oxygenase activity one piece at a time.
Engineering Rieske oxygenase activity one piece at a time.
复制标题
DOI：
10.1016/j.cbpa.2022.102227
复制
发表时间：
2023-03
影响因子：
7.8
通讯作者：
中科院分区：
文献类型：
--
作者：
酶工程在生物技术、化学和制药制造以及环境修复的生物催化剂开发中发挥着核心作用。蛋白质的合理设计历来依赖于靶向活性位点残基来赋予蛋白质所需的催化特性。然而，已知在活动站点之外还存在其他“热点”。亚基-亚基相互作用、入口隧道和柔性环等结构元素影响酶催化，并成为工程的潜在“热点”。对于使用 Rieske 簇和单核铁中心催化一系列具有挑战性的反应的 Rieske 加氧酶来说，活性位点区域之外的这些反应越来越多地被证明可以驱动催化结果。因此，在这里，我们重点介绍最近关于 Rieske 加氧酶结构特征的工作，这些工作表明活性位点内部和外部的结构片段是催化的关键决定因素，我们建议这些特征可能值得在 Rieske 加氧酶工程的努力中引起关注。
Enzyme engineering plays a central role in the development of biocatalysts for biotechnology, chemical and pharmaceutical manufacturing, and environmental remediation. Rational design of proteins has historically relied on targeting active site residues to confer a protein with desirable catalytic properties. However, additional “hotspots” are also known to exist beyond the active site. Structural elements such as subunit–subunit interactions, entrance tunnels, and flexible loops influence enzyme catalysis and serve as potential “hotspots” for engineering. For the Rieske oxygenases, which use a Rieske cluster and mononuclear iron center to catalyze a challenging set of reactions, these outside of the active site regions are increasingly being shown to drive catalytic outcomes. Therefore, here, we highlight recent work on structurally characterized Rieske oxygenases that implicates architectural pieces inside and outside of the active site as key dictators of catalysis, and we suggest that these features may warrant attention in efforts aimed at Rieske oxygenase engineering.
登录
查看更多内容
影响因子：
5.6
作者：
Dumitru, Razvan;Jiang, Wen Zhi;Weeks, Donald P.;Wilson, Mark A.
通讯作者：
Wilson, Mark A.
影响因子：
5.7
作者：
Kauppi, B;Lee, K;Ramaswamy, S
通讯作者：
Ramaswamy, S
影响因子：
3.2
作者：
Chebrou, H;Hurtubise, Y;Sylvestre, M
通讯作者：
Sylvestre, M
影响因子：
--
作者：
Ferraro, Daniel J.;Brown, Eric N.;Ramaswamy, S.
通讯作者：
Ramaswamy, S.
影响因子：
5.7
作者：
Ashikawa, Yuji;Fujimoto, Zui;Nojiri, Hideaki
通讯作者：
Nojiri, Hideaki