Protein-Derived Cofactors. Expanding the Scope of Post-Translational Modifications

• Published in: Biochemistry (Easton) Vol. 46; no. 18; pp. 5283 - 5292
• Main Author: Davidson, Victor L
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 08-05-2007
• Subjects: Animals; Bacterial Proteins - biosynthesis; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Coenzymes - biosynthesis; Coenzymes - chemistry; Coenzymes - genetics; Coenzymes - metabolism; Hemeproteins - biosynthesis; Hemeproteins - chemistry; Hemeproteins - genetics; Hemeproteins - metabolism; Oxidation-Reduction; Plant Proteins - biosynthesis; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - metabolism; Protein Processing, Post-Translational - genetics
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi700468t

Recent advances in enzymology, structural biology, and protein chemistry have extended the scope of the field of cofactor-dependent enzyme catalysis. It has been documented that catalytic and redox-active prosthetic groups may be derived from post-translational modification of amino acid residues of proteins. These protein-derived cofactors typically arise from the oxygenation of aromatic residues, covalent cross-linking of amino acid residues, or cyclization or cleavage of internal amino acid residues. In some cases, the post-translation modification is a self-processing event, whereas in others, another processing enzyme is required. The characterization of protein-derived cofactors and their mechanisms of biogenesis introduce a new dimension to our current views about protein evolution and protein structure−function relationships.