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Conformational Tinkering Drives Evolution of a Promiscuous Activity through Indirect Mutational Effects.

Biochemistry - 16 Aug 2016

Yang Gloria, Hong Nansook, Baier Florian, Jackson Colin J, Tokuriki Nobuhiko

Abstract excerpt

How remote mutations can lead to changes in enzyme function at a molecular level is a central question in evolutionary biochemistry and biophysics. Here, we combine laboratory evolution with biochemical, structural, genetic, and computational analysis to dissect the molecular basis for the functional optimization of phosphotriesterase activity in a bacterial lactonase (AiiA) from the metallo-β-lactamase (MBL)...

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Molecular Dynamics Simulation
Bacterial Proteins
Biocatalysis
Catalytic Domain
Directed Molecular Evolution

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Metalloendopeptidases

Molecular Docking Simulation

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PMID: 27444875
DOI: 10.1021/acs.biochem.6b00561

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