当前位置： SCI文献检索 > BIOCHIMIE期刊下所有文献 > Mutational analysis of residues in human arsenic (III) methyltransferase (hAS3MT) belonging to 5 Å around S-adenosylmethionine (SAM).

Mutational analysis of residues in human arsenic (III) methyltransferase (hAS3MT) belonging to 5 Å around S-adenosylmethionine (SAM).

Abstract：

:The functions of residues 57-RY-58, G60, L77, 80-GSGR-83, I101, T104, 134-GY-135, N155, V157 and 160-LV-161 in human arsenic (III) methyltransferase (hAS3MT) 5 Å around S-adenosylmethionine (SAM) have not been studied. Herein, sixteen mutants were designed by substituting these residues with Ala. Mutants G60A, G80A, I101A, N155A and L160A were completely inactive. Only MMA was detected when mutants R57A, Y58A, G82A and T104A were used as the enzymes, which suggested that their catalytic activities were seriously impaired compared with that of wild type (WT). The catalytic capacities of other mutants were also lower than that of WT-hAS3MT. The KM(SAM) values of mutants were 1.9–8.7 times that of WT, suggesting their affinities to SAM were weakened. As evidenced by the experimental data herein, earlier literature and the model of hAS3MT-SAM, 57-RYYG-60, G78, G80, G82 and 155-NCV-157 interacted with the methionine of SAM, and 101-IDMT-104 and 135-YIE-137 were associated with the nucleotide adenosine of SAM. Since C156 and L160 were the common residues between 5 Å around SAM and 5 Å around As, and C156S and L160A were inactive, we proposed that C156 and L160 functioned in the methyl transfer process. G78, G80 and G82 belonging to the consensus GxGxG were located in a loop connecting the first β-strand and α-helix in the Rossmann fold core. Y59, N155, C156 and L160 oriented S(+)-CH(3) during its approach to the arsenic lone pair, and further activated methyl transfer. G78, D102, M103, T104, I136 and N155 formed hydrogen bonds with SAM.

journal_name

Biochimie

journal_title

Biochimie

authors

Li X,Geng Z,Chang J,Song X,Wang Z

doi

10.1016/j.biochi.2014.10.014

subject

Has Abstract

pub_date

2014-12-01 00:00:00

pages

396-405

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(14)00300-9

journal_volume

107 Pt B

pub_type

杂志文章

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