Joint urethanase publication of several biochemistry groups in Angewandte Chemie Int. Ed. now published

We have determined the first crystal structure of an urethanase (UMG-SP-1), identified highly flexible loop regions comprising active site residues and we targeted a total of 20 potential hot spots by site-saturation mutagenesis. This lead to 3- and 8-fold improved activity against otherwise highly stable N-aryl urethane and amide bonds, respectively. Furthermore, we demonstrated the release of the corresponding monomers from a thermoplastic polyester-PU and a PA (nylon 6) by the activity of the urethanases after short incubation times. Read more in our just accepted publication in Angew. Chem. Int. Ed., see here.