Jiabao Tang, Mengling Hao, Junxian Liu, Yaling Chen, Gulimire Wufuer, Jie Zhu, Xuejie Zhang, Tingquan Zheng, Mujin Fang, Shiyin Zhang, Tingdong Li, Shengxiang Ge, Jun Zhang, Ningshao Xia
Asparaginyl ligases have been extensively utilized as valuable tools for site-specific bioconjugation or surface-modification. However, the application is hindered by the laborious and poorly reproducible preparation processes, unstable activity and ambiguous substrate requirements. To address these limitations, this study employed a structure-based rational approach to obtain a high-yield and high-activity protein ligase called OaAEP1-C247A-aa55-351. It was observed that OaAEP1-C247A-aa55-351 exhibits appreciable catalytic activities across a wide pH range, and the addition of the Fe3+ metal ion effectively enhances the catalytic power...
April 18, 2024: Communications Chemistry