DNA methyltransferase 2 (DNMT2)

DNA methyltransferase 2 (DNMT2) is a highly conserved enzyme initially classified as a DNA methyltransferase because of sequence homology to other cytosine-5 DNA methyltransferases; it contains all 10 conserved motifs characteristic of this enzyme family and binds S-adenosyl-L-methionine as the methyl donor[2][1]. However, despite its similarity to canonical DNA methyltransferases, DNMT2 exhibits only weak and often undetectable DNA methylation activity in vitro, instead primarily catalyzing the methylation of tRNA (notably cytosine-38 of tRNAAsp). DNMT2 binds DNA to form denaturant-resistant complexes, suggesting a role in epigenetic marking or genome surveillance, but its precise biological functions remain less well characterized than those of DNMT1 or DNMT3 family members. DNMT2 is present in multiple eukaryotic species, including humans, plants, and insects, and may participate in stress response, cellular differentiation, and possibly defense against viral infection, but its direct disease relevance is limited compared to other DNA methyltransferases[2][1][3].

Other names

DNA (cytosine-5)-methyltransferase 2Trm4 (in some species)tRNA methyltransferase homolog

Methyl group transfer from S-adenosyl-L-methionine (SAM) to the C5 position of cytosine (DNA or RNA substrate, though detectable DNA methylation activity is weak in vitro)[2][1]