At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology.
- Author(s): Latham, John A
- Barr, Ian
- Klinman, Judith P
- et al.
Published Web Locationhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5633103/
Radical S-adenosylmethionine (RS) enzymology has emerged as a major biochemical strategy for the homolytic cleavage of unactivated C-H bonds. At the same time, the post-translational modification of ribosomally synthesized peptides is a rapidly expanding area of investigation. We discuss the functional cross-section of these two disciplines, highlighting the recently uncovered importance of protein-protein interactions, especially between the peptide substrate and its chaperone, which functions either as a stand-alone protein or as an N-terminal fusion to the respective RS enzyme. The need for further work on this class of enzymes is emphasized, given the poorly understood roles performed by multiple, auxiliary iron-sulfur clusters and the paucity of protein X-ray structural data.
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