Discovery and biochemical characterization of the D-aspartyl endopeptidase activity of the serine protease LACTB.

ABSTRACT: Nonenzymatic D-isomerization of aspartic acid in proteins has been observed in lesions associated with age-related diseases, including cataracts and Alzheimer's disease. Given that D-isomerization of Asp disrupts the physiological conformation of proteins, it has been postulated that D-isomerization of Asp in proteins is a key factor in the pathogenesis of age-related diseases. D-Aspartyl endopeptidase (DAEP) activity, which cleaves proteins at the carboxy terminus of D-Asp and potentially induces degradation of abnormal proteins with D-isomerized Asp, has been observed in mitochondrial fractions of mammalian tissues. However, the specific proteins responsible for mammalian DAEP activity remain unknown. In this study, we identified mitochondrial serine β-lactamase-like protein (LACTB) as t

SUBMITTER: Ito G 

PROVIDER: S-EPMC12148432 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature