Abstract
Rational redesign of allosteric protein offers an efficient strategy to develop switchable biocatalysts. By combining the computational design and protein engineering, a glutathione peroxidase (GPx)-like active center that contains the catalytic selenocysteine (Sec) residue and substrate-binding Arg residue was precisely incorporated into the allosteric domain of adenylate kinase (AKe). The engineered selenoenzyme shows not only high GPx activity but also adenosine triphosphate (ATP)-responsive catalytic property, which is regulated by its opened to closed conformational change upon ATP binding. Theoretical and mutational analysis reveals that the synergistic effect of electrostatic interactions and van der Waals (vdW) interactions for substrate recognition is a major contribution to the high activity. The mitochondrial oxidative damage experiment further demonstrated its antioxidant ability at the subcellular level, offering a potential application toward controllable catalysis in vivo.
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