Isoaspartic acid (isoaspartate, isoaspartyl, β-aspartate) is an aspartic acid residue isomeric to the typical α peptide linkage. It is a β-amino acid, with the side chain carboxyl moved to the backbone. Such a change is caused by a chemical reaction in which the nitrogen atom on the N+1 following peptide bond (in black at top right of Figure 1) nucleophilically attacks the γ-carbon of the side chain of an asparagine or aspartic acid residue, forming a succinimide intermediate (in red). Hydrolysis of the intermediate results in two products, either aspartic acid (in black at left) or isoaspartic acid, which is a β-amino acid (in green at bottom right).  The reaction also results in the deamidation of the asparagine residue. Racemization may occur leading to the formation of D-aminoacids.