Reversal of protein chemical aging by enzymatic deglycation | Nature Communications

Advanced glycation end products (AGEs) in proteins, a hallmark of aging, are considered irreversible. Here, authors report the development of CMLase - an enzyme that specifically oxidizes Nε-carboxymethyl-lysine (CML) and restores the native lysine residues in vitro and in human tissue samples.

Download PDF Subjects Biotechnology Glycobiology Glycosylation Oxidoreductases Protein design Abstract The accumulation of advanced glycation end products (AGEs) in long-lived proteins is a hallmark of mammalian aging and implicated as a driver of metabolic dysfunction. Among these adducts, N ε -carboxymethyl-lysine (CML) is particularly abundant in aging tissues, where it modifies proteins and acts as a ligand for the receptor for advanced glycation end products (RAGE), thereby perpetuating chronic inflammation and oxidative stress. While endogenous detoxification systems exist for reactive p

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