EEF1A lysine methyltransferase 1 (EEF1AKMT1)

EEF1A lysine methyltransferase 1 (EEF1AKMT1; sometimes referred to as N6AMT2) is a **protein-lysine N-methyltransferase enzyme** that catalyzes the methylation of lysine residues on target proteins, most notably on eukaryotic translation elongation factor 1 alpha (eEF1A)[1]. This post-translational modification may modulate eEF1A's role in protein synthesis and its non-canonical functions, including cytoskeletal regulation, RNA stability, and stress response[1][2][3][4]. While its alternative name "N6AMT2" suggests it could methylate DNA adenine (N6 position), this activity is not confirmed in higher eukaryotes and is likely a legacy of sequence homology to bacterial enzymes. EEF1AKMT1 is being studied for its roles in human biology, and abnormal methylation by related enzymes has been implicated in cancer[3]. Currently, no drugs directly and selectively target EEF1AKMT1, but it remains of scientific and therapeutic interest within the class of protein lysine methyltransferases. If you need further structured details, such as human gene/protein database identifiers or experimental validation references, please specify.

Other names

EEF1A lysine methyltransferase 1N6AMT2N(6)-adenine-specific DNA methyltransferase 2Protein-lysine N-methyltransferase N6AMT2eEF1A-KMTESP13

Inhibition of lysine methyltransferase activity leads to altered methylation of substrates such as elongation factors, potentially modifying protein synthesis, stability, or interactions. No approved drugs with direct, selective action; mechanisms derived from broader studies of methyltransferase inhibitors.