Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.

摘要: A protein-derived cofactor is a catalytic or redox-active site in protein that formed by post-translational modification of one more amino acid residues. These modifications are irreversible and endow the modified residues with new functional properties. This Perspective focuses on following advances this area have occurred during recent years. The biosynthesis tryptophan tryptophylquinone catalyzed diheme enzyme, MauG. bis-FeIV redox state hemes performs three two-electron oxidations specific Trp via long-range electron transfer. In contrast, flavoenzyme catalyzes cysteine (CTQ) present newly discovered family CTQ-dependent oxidases. Another carbonyl cofactor, pyruvoyl found classes decarboxylases reductases, an apparently autocatalytic cleavage precursor at N-terminus product. I...