Related Experiment Video
Updated: May 29, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Radical SAM Enzyme WprB Catalyzes Uniform Cross-Link Topology between Trp-C5 and Arg-Cγ on the Precursor Peptide
Abujunaid Habib Khan1, Jabal Rahmat Haedar1, Vic Kiselov1
1Latvian Institute of Organic Synthesis, Aizkraukles Street 21, LV-1006 Riga, Latvia.
Abstract:
Cross-link containing products from ribosomally synthesized and post-translationally modified peptides (RiPPs) are generated by radical SAM enzymes (rSAM). Here, we bioinformatically expanded rSAM enzymes based on the known families StrB, NxxcB, WgkB, RrrB, TqqB and GggB. Through in vivo functional studies in E. coli, the newly identified enzyme WprB from Xenorhabdus sp. psl was found to catalyze formation of a cross-link between Trp-C5 and Arg-Cγ at three WPR motifs on the precursor peptide WprA. This represents the first report of this type of cross-link by rSAM enzymes.
More Related Videos
Related Concept Videos
Radical Chain-Growth Polymerization: Mechanism
tRNA Activation
Tail-anchoring of Proteins in the ER Membrane
Radical Reactivity: Overview
Protein Folding Quality Check in the RER
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...

