Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues. These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 184.108.40.206) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.
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Protein Aliases: L-isoaspartyl protein carboxyl methyltransferase; PIMT; protein carboxyl methyltransferase; Protein L-isoaspartyl/D-aspartyl methyltransferase; Protein-beta-aspartate methyltransferase; Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Gene Aliases: C79501; PCM; PCMT1; PIMT