蛋白質におけるアスパラギン酸の異性化

抄録

Aspartic acid in protein isomerizes autocatalytically to isoaspartate via succinimide intermediate in vitro and in vivo. We have determined the crystal structures of Ustilago sphaerogena ribonuclease U₂ with an isoaspartate residue and hen egg-white lysozymes with a succinimide intermediate and with an isoaspartate residue at 1.8 Å resolution. These crystal structures reveal that the isomerizations of aspartic acids induce structural changes on proteins, which result in modifying the function and physical properties of the proteins.