| EC |
2.1.1.77 |
| Accepted name: |
protein-L-isoaspartate(D-aspartate) O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate α-methyl ester |
| Other name(s): |
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 |
| Systematic name: |
S-adenosyl-L-methionine:protein-L-isoaspartate O-methyltransferase |
| Comments: |
D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105638-50-4 |
| References: |
| 1. |
Aswad, D.W. and Johnson, B.A. The unusual substrate-specificity of eukaryotic protein carboxyl methyltransferases. Trends Biochem. Sci. 12 (1987) 155–158. |
| 2. |
Clarke, S. Protein carboxyl methyltransferases: two distinct classes of enzymes. Annu. Rev. Biochem. 54 (1985) 479–506. [DOI] [PMID: 3896126] |
| 3. |
Kim, S. and Paik, W.K. Purification and properties of protein methylase II. J. Biol. Chem. 245 (1970) 1806–1813. [PMID: 5438363] |
| 4. |
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] |
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| [EC 2.1.1.77 created 1984, modified 1989 (EC 2.1.1.24 created 1972, modified 1983, modified 1989, part incorporated 1992)] |
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