Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy

S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega-dimethyl-L-arginine-forming)

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine (overall reaction) [RN:R11219];
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine [RN:R11216];
(1b) S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine [RN:R11217]

R11216 R11217 R11219
Reaction

S-adenosyl-L-methionine [CPD:C00019];
[protein]-L-arginine [CPD:C00613];
[protein]-Nomega-methyl-L-arginine [CPD:C04143]

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 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.

EC 2.1.1.319 created 2015