Mutation of the eunicellane synthase Bnd4 alters its product profile and expands its prenylation ability.
Mutation of the eunicellane synthase Bnd4 alters its product profile and expands its prenylation ability.
复制标题
DOI:
10.1039/d2ob01931k
复制
发表时间:
2022-11-23
影响因子:
3.2
通讯作者:
中科院分区:
文献类型:
--
作者:
Bnd4 catalyzes the first committed step in the biosynthesis of the bacterial diterpenoid benditerpenoic acid and was the first eunicellane synthase identified from nature. We investigated the catalytic roles of the aromatic residues in the active site of Bnd4 through a series of mutation studies. These experiments revealed that large hydrophobic or aromatic side chains are required at F162 and Y197 for eunicellane formation and that selected mutations at W316 converted Bnd4 into a cembrane synthase. In addition, the Bnd4Y197A variant expanded the native prenylation ability of Bnd4 from accepting C5 and C10 prenyl donors to C15. This study supports the mechanism of eunicellane formation by Bnd4 and encourages further engineering of terpene synthases into practical and efficient prenyltransferases.
登录
查看更多内容
影响因子:
2.9
作者:
Ronnebaum TA;Gardner SM;Christianson DW
通讯作者:
Christianson DW
影响因子:
3.2
作者:
Meguro, Ayuko;Tomita, Takeo;Nishiyama, Makoto;Kuzuyama, Tomohisa
通讯作者:
Kuzuyama, Tomohisa
影响因子:
11.9
作者:
Rudolf JD;Alsup TA;Xu B;Li Z
通讯作者:
Li Z
影响因子:
5.2
作者:
Williams, PG;Yoshida, WY;Paul, VJ
通讯作者:
Paul, VJ
影响因子:
16.6
作者:
通讯作者:
--