Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions
Xinjian Ji1, Wan-Qiu Liu2, Shuguang Yuan3
1Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
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.
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