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Genetically encoded Nδ-vinyl histidine for the evolution of enzyme catalytic center
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Genetically encoded Nδ-vinyl histidine for the evolution of enzyme catalytic center
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Journal Article
Genetically encoded Nδ-vinyl histidine for the evolution of enzyme catalytic center
2024
Overview
Genetic code expansion has emerged as a powerful tool for precisely introducing unnatural chemical structures into proteins to improve their catalytic functions. Given the high catalytic propensity of histidine in the enzyme pocket, increasing the chemical diversity of catalytic histidine could result in new characteristics of biocatalysts. Herein, we report the genetically encoded Nδ-Vinyl Histidine (δVin-H) and achieve the wild-type-like incorporation efficiency by the evolution of pyrrolysyl tRNA synthetase. As histidine usually acts as the nucleophile or the metal ligand in the catalytic center, we replace these two types of catalytic histidine to δVin-H to improve the performance of the histidine-involved catalytic center. Additionally, we further demonstrate the improvements of the hydrolysis activity of a previously reported organocatalytic esterase (the OE1.3 variant) in the acidic condition and myoglobin (Mb) catalyzed carbene transfer reactions under the aerobic condition. As histidine is one of the most frequently used residues in the enzyme catalytic center, the derivatization of the catalytic histidine by δVin-H holds a great potential to promote the performance of biocatalysts.
Genetic code expansion enables precisely introducing chemical structures into proteins to improve their catalytic functions. In this study, the authors report the incorporation of genetically encoded Nδ-Vinyl Histidine (δVin-H) into an organocatalytic esterase and myoglobin, and improve the performance of the hydrolysis reaction and carbene transfer reactions catalyzed by the respective enzymes.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
