Abstract
Protein L-Isoaspartate O-Methyltransferase (PCMT1): A Key Player of Spontaneously Arisen Protein Damage Repair
Highlights
Methylation of aspartic acid residues was first described in the literature in erythrocytes as a possible step of repairing aged membrane proteins [1]
It has been previously shown that Protein L-isoaspartate O-methyltransferase (PCMT1, or alternatively called PIMT) can rapidly convert L-isoaspartyl sites to -carboxyl-O-methyl esters in vivo, which at physiological pH and temperature undergo spontaneous demethylation and give rise to the L-succinimide intermediate [4]
The methylation of isoAsp residues by PCMT1 is suggested to act in targeting aged proteins for proteosomal degradation [5]
Summary
Proteins undergo spontaneous non-enzymatic chemical modifications due to the exposure to e.g. oxidative reagents. The cell copes with the accumulation of such damaged proteins by proteosomal degradation. Aged or damaged proteins can be enzymatically repaired. Protein L-isoaspartate O-methyltransferase (PCMT1) catalyzes the methylation of isoAspartate (isoAsp) residues that spontaneously arise as a result of protein aging and facilitates their restoration to the normal state.PCMT1 plays a significant role in maintenance of protein homeostasis as well as in cellular function and integrity by acting on a wide variety of substrates
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