Molecular Determinants of Enzyme Cold Adaptation: Comparative Structural and Computational Studies of Cold- and Warm-Adapted Enzymes

Author(s): Elena Papaleo, Matteo Tiberti, Gaetano Invernizzi, Marco Pasi, Valeria Ranzani

Journal Name: Current Protein & Peptide Science

Volume 12 , Issue 7 , 2011

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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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Article Details

Year: 2011
Published on: 01 March, 2012
Page: [657 - 683]
Pages: 27
DOI: 10.2174/1389203711109070657
Price: $65

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