Linkage of nanosecond protein motion with enzymatic methyl transfer by nicotinamide N-methyltransferase

Authors : Yahui JING, Yiting CHENG, Fangya LI, Yuping LI, Fan LIU, Jianyu ZHANG

Pages : 333-341

View : 13 | Download : 7

Publication Date : 2021-12-01

Article Type : Research Paper

Abstract :Nicotinamide N-methyltransferase insert ignore into journalissuearticles values(NNMT);, a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide insert ignore into journalissuearticles values(NCA); N1-methylation through S-adenosyl-L-methionine insert ignore into journalissuearticles values(SAM); as a methyl donor, which has been linked to many diseases. Although extensive studies have concerned about the biological aspect, the detailed mechanism study of the enzyme function, especially in the part of protein dynamics is lacking. Here, wild-type nicotinamide N-methyltransferase together with the mutation at position 20 with Y20F, Y20G, and free tryptophan were carried out to explore the connection between protein dynamics and catalysis using time-resolved fluorescence lifetimes. The results show that wild-type nicotinamide N-methyltransferase prefers to adapt a less flexible protein conformation to achieve enzyme catalysis.
Keywords : Protein dynamics, nicotinamide N methyltransferase, methyl transfer, time resolved fluorescence