Journal
BIOCHEMISTRY
Volume 46, Issue 18, Pages 5283-5292Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi700468t
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Funding
- NIGMS NIH HHS [R01 GM041574, GM-41574] Funding Source: Medline
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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.
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