Open AccessLinkage of nanosecond protein motion with enzymatic methyl transfer by nicotinamide N-methyltransferase
Author(s) -
Yahui Jing,
Yiting Cheng,
Fangya Li,
Yuping Li,
Fan Liu,
Jianyu Zhang
Publication year - 2021
Publication title -
turkish journal of biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.323
H-Index - 38
eISSN - 1303-6092
pISSN - 1300-0152
DOI - 10.3906/biy-2101-54
Subject(s) - nicotinamide , methyltransferase , enzyme , tryptophan , methionine , methylation , biochemistry , biology , mutation , dna , chemistry , amino acid , gene
Nicotinamide N-methyltransferase (NNMT), a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide (NCA) N 1 -methylation through S-adenosyl-L-methionine (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.