苏氨酸
ATP合酶
苯丙氨酸
残留物(化学)
生物化学
突变体
功能(生物学)
生物
计算生物学
氨基酸
磷酸化
丝氨酸
细胞生物学
酶
基因
作者
Fan Zhang,Yunpeng Wang,Jingyang Yue,Rong-Rong Zhang,Yonger Hu,Ruoshi Huang,Ai-jia Ji,B. Andes Hess,Zhongqiu Liu,Lixin Duan,Ruibo Wu
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2023-06-09
卷期号:9 (23)
被引量:2
标识
DOI:10.1126/sciadv.adh1418
摘要
Many functionally promiscuous plant 2,3-oxidosqualene cyclases (OSCs) have been found, but complete functional reshaping is rarely reported. In this study, we have identified two new plant OSCs: a unique protostadienol synthase (AoPDS) and a common cycloartenol synthase (AoCAS) from Alisma orientale (Sam.) Juzep. Multiscale simulations and mutagenesis experiments revealed that threonine-727 is an essential residue responsible for protosta-13 (17),24-dienol biosynthesis in AoPDS and that the F726T mutant completely reshapes the native function of AoCAS into a PDS function to yield almost exclusively protosta-13 (17),24-dienol. Unexpectedly, various native functions were uniformly reshaped into a PDS function by introducing the phenylalanine → threonine substitution at this conserved position in other plant and non-plant chair-boat-chair-type OSCs. Further computational modeling elaborated the trade-off mechanisms of the phenylalanine → threonine substitution that leads to the PDS activity. This study demonstrates a general strategy for functional reshaping by using a plastic residue based on the decipherment of the catalytic mechanism.
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