The Enzyme Database

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Accepted name: type I protein arginine methyltransferase
Reaction: 2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine (overall reaction)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
(1b) S-adenosyl-L-methionine + [protein]-Nω-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine
Other name(s): PRMT1 (gene name); PRMT2 (gene name); PRMT3 (gene name); PRMT4 (gene name); PRMT6 (gene name); PRMT8 (gene name); RMT1 (gene name); CARM1 (gene name)
Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω-dimethyl-L-arginine-forming)
Comments: This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues [1]. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells [2]. cf. EC, type II protein arginine methyltransferase, EC, type III protein arginine methyltransferase, and EC, type IV protein arginine methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Gary, J.D. and Clarke, S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 61 (1998) 65–131. [PMID: 9752719]
2.  Tang, J., Gary, J.D., Clarke, S. and Herschman, H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273 (1998) 16935–16945. [DOI] [PMID: 9642256]
3.  Tang, J., Frankel, A., Cook, R.J., Kim, S., Paik, W.K., Williams, K.R., Clarke, S. and Herschman, H.R. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J. Biol. Chem. 275 (2000) 7723–7730. [DOI] [PMID: 10713084]
4.  Frankel, A., Yadav, N., Lee, J., Branscombe, T.L., Clarke, S. and Bedford, M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 (2002) 3537–3543. [DOI] [PMID: 11724789]
[EC created 2015]

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