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tRNA N(3)-cytidine methyltransferase 2A (METTL2A) is an enzyme in humans that catalyzes the formation of 3-methylcytidine (m3C) at position 32 in the anticodon loop of specific tRNAs, notably tRNA^Thr and tRNA^Ser, using S-adenosylmethionine (SAM) as the methyl donor[1][2][3][5][7][9]. METTL2A is cytoplasmic and works independently or in coordination with protein cofactors to selectively recognize tRNA substrates, a process crucial for ensuring correct codon–anticodon pairing and translation fidelity[2]. While no direct pharmacological agents target METTL2A, changes in tRNA methylation (including m3C) have been related to translational stress, and abnormal activity of related enzymes has been linked to human disease[6]. There are no published drugs or biomarkers directly associated with METTL2A at present.
Inhibition or modulation of enzymatic methylation of tRNA cytidine at position 3 (potential, but no specific drugs described in available literature)
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