期刊
CHEMICAL COMMUNICATIONS
卷 54, 期 50, 页码 6622-6634出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cc02426j
关键词
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资金
- Spanish MINECO [BES-2015-074964, CTQ2014-59212-P]
- Generalitat de Catalunya [2017-FI-B-00118, 2015-FI-B-00165]
- European Community for Marie Curie fellowship [H2020-MSCA-IF-2016-753045]
- Ramon y Cajal contract [RYC-2014-16846]
- European Community for CIG project [PCIG14-GA-2013-630978]
- European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program [ERC-2015-StG-679001]
The free energy landscape concept that describes enzymes as an ensemble of differently populated conformational sub-states in dynamic equilibrium is key for evaluating enzyme activity, enantioselectivity, and specificity. Mutations introduced in the enzyme sequence can alter the populations of the pre-existing conformational states, thus strongly modifying the enzyme ability to accommodate alternative substrates, revert its enantiopreferences, and even increase the activity for some residual promiscuous reactions. In this feature article, we present an overview of the current experimental and computational strategies to explore the conformational free energy landscape of enzymes. We provide a series of recent publications that highlight the key role of conformational dynamics for the enzyme evolution towards new functions and substrates, and provide some perspectives on how conformational dynamism should be considered in future computational enzyme design protocols.
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