Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S-adenosylmethionine

被引：7

作者：

Li, Xiangli ^{[1
]}

Geng, Zhirong ^{[1
]}

Wang, Shuping ^{[1
]}

Song, Xiaoli ^{[2
]}

Hu, Xin ^{[3
]}

Wang, Zhilin ^{[1
]}

机构：

[1] Nanjing Univ, Sch Chem & Chem Engn, State Key Lab Coordinat Chem, Nanjing 210093, Jiangsu, Peoples R China

[2] Yangzhou Univ, Sch Chem & Chem Engn, Yangzhou 225002, Peoples R China

[3] Nanjing Univ, Modern Anal Ctr, Nanjing 210093, Jiangsu, Peoples R China

来源：

FEBS LETTERS | 2013年 / 587卷 / 14期

基金：

中国国家自然科学基金;

关键词：

Human arsenic(III) methyltransferase (hAS3MT); Mutants; S-adenosylmethionine; Hydrogen bond; OXIDATION-STATE METHYLTRANSFERASE; RAT GUANIDINOACETATE METHYLTRANSFERASE; CATECHOL O-METHYLTRANSFERASE; METHYL TRANSFER; MOLECULAR-DYNAMICS; ARSENITE; RESIDUES; BINDING; SITE; INSIGHTS;

D O I：

10.1016/j.febslet.2013.05.052

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2232 / 2240

页数：9

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