Enzymatic Modification Of Amino Acids And Their Products

The inventors report the structural characterization of BesD, a recently discovered radical halogenase from the FeII/-ketogluturate family that chlorinates the free amino acid lysine. They also identify and characterize additional halogenases that produce mono- and di-chlorinated as well as brominated and azidated amino acids. The substrate selectivity of this new family of radical halogenases takes advantage of the central role of amino acids in metabolism and enables engineering biosynthetic pathways to afford a wide variety of compound classes, such as heterocycles, diamines, -keto acids, and peptides. Craig Kennedy craig.kennedy@berkeley.edu

Related Blog

Smart, interactive desk

Get ready to take your space management game to the next level with the University of Glasgow’s innovative project! By combining the

Mechanical Hamstring™

University of Delaware Technology Overview This device was created to allow athletes who suffer a hamstring strain to return to the field

Join Our Newsletter

                                                   Receive Innovation Updates, New Listing Highlights And More