Thomas Tørring

This study identifies an essential follower peptide for triculamin biosynthesis and shows its role in enzyme-substrate complex formation and substrate promiscuity.

This study reconstitutes the APD biosynthesis pathway in E. coli to identify the PKS machinery responsible for warhead formation.

This study reports the first NMR structure of a class V lasso peptide, gelatinamin A, and characterizes its biosynthesis and antibiotic properties.

This study identifies the biosynthesis of triculamin, a lasso peptide with antimycobacterial activity, and shows its convergent evolution across bacterial phyla.

The paper uses LanM enzymes and leader peptides to modify D-Ala in GLP-1 and GLP-2 in E. coli, showing how precursor design affects modification patterns.