Adjusting Catalytic Activity of β-Amyrin Synthase GgBAS by Utilizing the Plasticity Residues of an Active Site

• DOI: 10.1021/acs.jcim.4c00297
• Publication Date: 2024-04-26T13:02:32Z
• Authors: Ying Zheng; Nianhang Chen; Zhongju Ji; Qiongyu Ye; Pingping Huang; Xiaodie Chen; Guanghong Cui; Lixin Duan; Fan Zhang
• Keywords: Catalytic Domain; Biocatalysis; Mutagenesis, Site-Directed; Molecular Dynamics Simulation; Intramolecular Transferases

β-Amyrin synthase (bAS) is a representative plant oxidosqualene cyclase (OSC), and previous studies have identified many functional residues mutants that can alter its catalytic activity. However, the regulatory mechanism of active site architecture for adjusting activity remains unclear. In this study, we investigate function key their effects on