S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate α-methyl ester
protein-L-isoaspartate O-methyltransferase; protein-β-aspartate O-methyltransferase; D-aspartyl/L-isoaspartyl methyltransferase; L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase; protein (D-aspartate) methyltransferase; protein D-aspartate methyltransferase; protein L-isoaspartate methyltransferase; protein L-isoaspartyl methyltransferase; protein O-methyltransferase (L-isoaspartate); L-aspartyl/L-isoaspartyl protein methyltransferase
Aswad, D.W. and Johnson, B.A. The unusual substrate-specificity of eukaryotic protein carboxyl methyltransferases. Trends Biochem. Sci.12 (1987) 155–158.
Clarke, S. Protein carboxyl methyltransferases: two distinct classes of enzymes. Annu. Rev. Biochem.54 (1985) 479–506. [PMID: 3896126]
Kim, S. and Paik, W.K. Purification and properties of protein methylase II. J. Biol. Chem.245 (1970) 1806–1813. [PMID: 5438363]
Ota, I.M., Ding, L. and Clarke, S. Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase. J. Biol. Chem.262 (1987) 8522–8531. [PMID: 3597386]
[EC 22.214.171.124 created 1984, modified 1989 (EC 126.96.36.199 created 1972, modified 1983, modified 1989, part incorporated 1992)]