Publication
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 C alpha 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.
Tamar Kohn, Aleksandar Antanasijevic, Kiruthika Kumar, Shotaro Torii
Luc Reymond, Fabien Kuttler, Milena Maria Schuhmacher, Manon Sandra Bardyn, Daria Korotkova, Triana Amen
Nako Nakatsuka, Xinyu Zhang, Haiying Hu