SIRT5 and cancer: The removal of protein Kmal and Ksuc, the negatively charged acidic acyl groups, is mainly dependent on SIRT5, which is closely related to some diseases of cancer and neurodegenerative diseases.65–67 According to the crystal binding structure of succinyl-Lys peptide and SIRT5, researchers found that tyrosine 102 and arginine 105 are the special residues of SIRT5, in the deep end of substrate-binding pocket, which forms hydrogen bonds and ionic bonds with the carboxyl group of the succinyl lysine substrate.