Loading...
research article
Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions
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.
Type
research article
Web of Science ID
WOS:000382120300023
Authors
Ji, Xinjian
•
Liu, Wan-Qiu
•
Yuan, Shuguang
•
Yin, Yue
•
Ding, Wei
•
Zhang, Qi
Publication date
2016
Publisher
Published in
Volume
52
Issue
69
Start page
10555
End page
10558
Peer reviewed
REVIEWED
EPFL units
Available on Infoscience
October 18, 2016
Use this identifier to reference this record