Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine
Other name(s): RMT2 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-N5-methyl-L-arginine-forming)
Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the δ-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC 220.127.116.119, type I protein arginine methyltransferase, EC 18.104.22.1680, type II protein arginine methyltransferase, and EC 22.214.171.1241, type III protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
1. Niewmierzycka, A. and Clarke, S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274 (1999) 814-824. [PMID: 9873020]
2. Chern, M.K., Chang, K.N., Liu, L.F., Tam, T.C., Liu, Y.C., Liang, Y.L. and Tam, M.F. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J. Biol. Chem. 277 (2002) 15345-15353. [PMID: 11856739]
3. Olsson, I., Berrez, J.M., Leipus, A., Ostlund, C. and Mutvei, A. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Exp Cell Res 313 (2007) 1778-1789. [PMID: 17448464]