N-Terminal Protein Modification by Substrate-Activated Reverse Proteolysis (pages 3024–3028)
Dr. Sandra Liebscher, Dr. Michael Schöpfel, Dr. Tobias Aumüller, Ariunkhur Sharkhuukhen, Dr. Andreas Pech, Dr. Eva Höss, Dr. Christoph Parthier, Dr. Günther Jahreis, Prof. Dr. Milton T. Stubbs and Prof. Dr. Frank Bordusa
Article first published online: 12 FEB 2014 | DOI: 10.1002/anie.201307736
Trypsiligase catalyzes the selective modification of proteins with the substrate-mimetic 4-guanidino phenyl ester (OGp). Modification proceeds with quantitative product yields under native (aqueous) conditions. The variant possesses a disordered zymogen-like activation domain, effectively suppressing the hydrolysis reaction, which is converted to an active conformation in the presence of appropriate substrates.