N-terminal Xaa-Pro-Lys N-methyltransferase 2 (NTMT2)

N-terminal Xaa-Pro-Lys N-methyltransferase 2 (NTMT2) is an enzyme that catalyzes the methylation of the N-terminal α-amino group of protein substrates bearing the [Ala/Pro/Ser]-Pro-Lys motif following removal of the initiator methionine[7]. It is classified as a SAM-dependent class I methyltransferase of the Rossmann fold family, shares significant sequence and structural homology with NTMT1, and is primarily located in the nucleus[2][8]. NTMT2 was historically described as a mono-methyltransferase, but recent structural and biochemical studies demonstrate its ability to perform di- and tri-methylation, particularly for substrates with N-terminal glycine or proline[1][5]. NTMT2 is expressed largely in muscle tissues, suggesting tissue-specific biological roles[6][5]. The physiological substrates and the functional consequences of NTMT2-mediated methylation remain under investigation. No defined drugs are known to target NTMT2, and its links to human disease are not well-established.

Other names

NTMT2C1orf184METTL11BNRMT2NTM1BHOMT1BAlpha N-terminal protein methyltransferase 1BMethyltransferase-like protein 11BX-Pro-Lys N-terminal protein methyltransferase 1B

N-terminal methylation of substrates with compatible sequence motifs via transfer of methyl group from S-adenosyl-L-methionine (SAM)[1][2][4][5]. No drug-based mechanisms reported.