title: Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions.
abstract: The radical SAM enzyme NosL catalyzes the conversion of l-Trp to 3-methyl-2-indolic acid, and this reaction is initiated by the 5'-deoxyadenosyl (dAdo) radical-mediated hydrogen abstraction from the l-Trp amino group. We demonstrate here that when d-Trp was used in the NosL reaction, hydrogen abstraction occurs promiscuously at both the amino group and Cα of d-Trp. These results inspired us to establish the detailed mechanism of l-Trp amine dehydrogenation catalyzed by a NosL mutant, and to engineer a novel radical SAM-dependent l-Tyr amine dehydrogenase from the thiamine biosynthesis enzyme ThiH.
authors: Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
authors: Xinjian
authors: X
authors: Ji
authors: Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn and School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
authors: Wan-Qiu
authors: WQ
authors: Liu
authors: Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
authors: Shuguang
authors: S
authors: Yuan
authors: Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
authors: Yue
authors: Y
authors: Yin
authors: Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn and School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.
authors: Wei
authors: W
authors: Ding
authors: Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
authors: Qi
authors: Q
authors: Zhang