适应(眼睛)
计算生物学
酶
超家族
生物
灵活性(工程)
遗传学
生物化学
基因
数学
统计
神经科学
作者
Elena Papaleo,Matteo Tiberti,Gaetano Invernizzi,Marco Pasi,Valeria Ranzani
出处
期刊:Current Protein & Peptide Science
[Bentham Science]
日期:2011-11-01
卷期号:12 (7): 657-683
被引量:46
标识
DOI:10.2174/1389203711109070657
摘要
The identification of molecular mechanisms underlying enzyme cold adaptation is a hot-topic both for fundamental research and industrial applications. In the present contribution, we review the last decades of structural computational investigations on cold-adapted enzymes in comparison to their warm-adapted counterparts. Comparative sequence and structural studies allow the definition of a multitude of adaptation strategies. Different enzymes carried out diverse mechanisms to adapt to low temperatures, so that a general theory for enzyme cold adaptation cannot be formulated. However, some common features can be traced in dynamic and flexibility properties of these enzymes, as well as in their intra- and inter-molecular interaction networks. Interestingly, the current data suggest that a family-centered point of view is necessary in the comparative analyses of cold- and warm-adapted enzymes. In fact, enzymes belonging to the same family or superfamily, thus sharing at least the three-dimensional fold and common features of the functional sites, have evolved similar structural and dynamic patterns to overcome the detrimental effects of low temperatures. Keywords: Molecular dynamics, flexibility, electrostatic interactions, cold-adapted enzyme, psychrophilic enzyme, cold adaptation, extremophilic enzyme, Enzyme Cold Adaptation, Warm-Adapted Enzymes, stability
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