Specific recognition of altered polypeptides by widely distributed methyltransferases.
Protein carboxyl methyltransferase activity has been detected in extracts prepared from bacterial cells (Salmonella typhimurium), amphibian (Xenopus laevis) oocytes, and transformed mammalian cell lines. This activity appears to specifically recognize altered aspartyl residues based on the observation that the synthetic peptide L-Val-L-Tyr-L-Pro-L-isoAsp-Gly-L-Ala is a good methyl-accepting substrate for the methyltransferase activity, but that the corresponding peptide containing a normal L-aspartyl residue is not. These activities are similar to those of the previously described human erythrocyte and bovine brain enzymes which catalyze the formation of polypeptide D-aspartyl beta-methyl esters and L-isoaspartyl alpha-methyl esters. The wide distribution of these enzymatic activites suggest that the methylation of atypical proteins is an essential function in cells.
D000818:Animals; D004912:Erythrocytes / Q000201:enzymology; D005260:Female; D006801:Humans; D008780:Methyltransferases / Q000032:analysis*; D010455:Peptides / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology; D014982:Xenopus laevis
D010455:Peptides; D008780:Methyltransferases