title: Enantioselective artificial metalloenzymes based on a bovine pancreatic polypeptide scaffold.
abstract: Site creation: Enantioselective artificial metalloenzymes have been created by grafting a new active site onto bovine pancreatic polypeptide through the introduction of an amino acid capable of coordinating a copper(II) ion. This hybrid catalyst gave good enantioselectivities in the Diels-Alder and Michael addition reactions in water (see scheme) and displayed a very high substrate selectivity.
authors: Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors: David
authors: D
authors: Coquière
authors: Jeffrey
authors: J
authors: Bos
authors: Joris
authors: J
authors: Beld
authors: Gerard
authors: G
authors: Roelfes
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D002417:Cattle; D003300:Copper / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010191:Pancreatic Polypeptide / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D008667:Metalloproteins; D010191:Pancreatic Polypeptide; D003300:Copper