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Article

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

Biochimie - 1 Dec 2014

Li Xiangli, Geng Zhirong, Chang Jiayin, Song Xiaoli, Wang Zhilin

Abstract excerpt

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,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 25447140
DOI: 10.1016/j.biochi.2014.10.014

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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