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Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S‐adenosylmethionine
Author(s) -
Li Xiangli,
Geng Zhirong,
Wang Shuping,
Song Xiaoli,
Hu Xin,
Wang Zhilin
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.052
Subject(s) - methyltransferase , methylation , mutant , chemistry , arsenic , binding site , biochemistry , stereochemistry , dna , gene , organic chemistry
We prepared eight mutants (D76P, D76N, D84P, D84N, D102P, D102N, D150P and D150N) to investigate the functions of residues Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with the S‐adenosylmethionine (SAM)‐binding. The affinity of all the mutants for SAM were weakened. All the mutants except for D150N completely lost their methylation activities. Residues Asp76, 84, 102 and 150 greatly influenced hAS3MT catalytic activity via affecting SAM‐binding or methyl transfer. Asp76 and 84 were located in the SAM‐binding pocket, and Asp102 significantly affected SAM‐binding via forming hydrogen bonds with SAM.