N6AMT1:TRMT112 transfers CH3 group from AdoMet to MMAIII

Stable Identifier
R-HSA-6800149
Type
Reaction
Species
Homo sapiens
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Inorganic arsenic (iAs) compounds are human carcinogens. The most toxic arsenic metabolite is monomethylarsonous acid (MMAIII). Arsenic (3+) methyltransferase (AS3MT) is the primary enzyme responsible for methylating MMAIII to the less toxic dimethylarsonic acid (DMAA). A human ortholog of yeast MTQ2, HemK methyltransferase family member 2 (aka N(6)-adenine-specific DNA methyltransferase 1, N6AMT1), is also able to methylate MMAIII using S-adenosyl L-methionine as methyl donor (Ren et al. 2011). N6AMT1 forms a heterodimer with multifunctional methyltransferase subunit TRM112-like protein (TRMT112) (Figaro et al. 2008).

Literature References
PubMed ID Title Journal Year
21193388 Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) in arsenic biomethylation and its role in arsenic-induced toxicity

Ren, X, Aleshin, M, Jo, WJ, Dills, R, Kalman, DA, Vulpe, CD, Smith, MT, Zhang, L

Environ. Health Perspect. 2011
18539146 HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1

Figaro, S, Scrima, N, Buckingham, RH, Heurgué-Hamard, V

FEBS Lett. 2008
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hasEvent
Catalyst Activity
Catalyst Activity
Title
methyltransferase activity of N6AMT1:TRMT112 [cytosol]
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Orthologous Events
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Rhea
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