EC - Protein-L-isoaspartate(D-aspartate) O-methyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
protein-L-isoaspartate(D-aspartate) O-methyltransferase
Other names:
D-aspartyl/L-isoaspartyl methyltransferase
L-aspartyl/L-isoaspartyl protein methyltransferase
L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase
protein (D-aspartate) methyltransferase
protein O-methyltransferase (L-isoaspartate)
protein D-aspartate methyltransferase
protein L-isoaspartate methyltransferase
protein L-isoaspartyl methyltransferase
protein β-aspartate O-methyltransferase
protein-L-isoaspartate O-methyltransferase
L-isoaspartyl protein carboxyl methyltransferase
Systematic name:
S-adenosyl-L-methionine:protein-L-isoaspartate O-methyltransferase



D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00985
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004719
CAS Registry Number: 105638-50-4
UniProtKB/Swiss-Prot: (332) [show] [UniProt]


  1. Aswad, D.W. and Johnson, B.A.
    The unusual substrate-specificity of eukaryotic protein carboxyl methyltransferases.
    Trends Biochem. Sci. 12: 155-158 (1987).
  2. Clarke, S.
    Protein carboxyl methyltransferases: two distinct classes of enzymes.
    Annu. Rev. Biochem. 54: 479-506 (1985). [PMID: 3896126]
  3. Kim, S. and Paik, W.K.
    Purification and properties of protein methylase II.
    J. Biol. Chem. 245: 1806-1813 (1970). [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: 8522-8531 (1987). [PMID: 3597386]

[EC created 1984, modified 1989 (EC created 1972, modified 1983, modified 1989, part incorporated 1992)]