功能多样的酶超家族中新反应进化中的拓扑变化。
Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.
机构信息
Department of Pharmaceutical Chemistry, University of California, 600 16th Street, San Francisco, CA 94158-2517, USA.
出版信息
Curr Opin Struct Biol. 2011 Jun;21(3):391-7. doi: 10.1016/j.sbi.2011.03.007. Epub 2011 Apr 1.
Abstract
In functionally diverse enzyme superfamilies (SFs), conserved structural and active site features reflect catalytic capabilities 'hard-wired' in each SF architecture. Overlaid on this foundation, evolutionary changes in active site machinery, structural topology and other aspects of structural organization and interactions support the emergence of new reactions, mechanisms, and substrate specificity. This review connects topological with functional variation in each of the haloalkanoic acid dehalogenase (HAD) and vicinal oxygen chelate fold (VOC) SFs and a set of redox-active thioredoxin (Trx)-fold SFs to illustrate a few of the varied themes nature has used to evolve new functions from a limited set of structural scaffolds.
摘要
在功能多样的酶超家族（SFs）中，保守的结构和活性位点特征反映了每个 SF 结构中“硬连线”的催化能力。在此基础上，活性位点机制、结构拓扑和结构组织与相互作用的其他方面的进化变化支持了新反应、机制和底物特异性的出现。本综述将卤代烷酸脱卤酶（HAD）和毗邻氧螯合折叠（VOC）SF 以及一组氧化还原活性硫氧还蛋白（Trx）折叠 SF 中的拓扑与功能变化联系起来，说明了自然界从有限的结构支架进化新功能时使用的一些不同主题。
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