title: The design of protein-based catalysts using semisynthetic methods.
abstract: The combination of site-directed mutagenesis and chemical modification has resulted in the preparation of protein conjugates with new and useful properties. Proteins modified with metal-chelating groups are proving useful for mapping tertiary and quaternary interactions using the technique of affinity cleavage. The attachment of cofactors, including pyridoxal and pyridoxamine, has resulted in the preparation of semisynthetic transaminases that display enzyme-like properties, including enantioselectivity, substrate specificity and reaction-rate acceleration.
authors.affiliation: Department of Chemistry, University of Minnesota, Minneapolis 55455, USA. distefan@chem.umn.edu
authors.forename: M D
authors.initials: MD
authors.lastname: Distefano
authors.forename: H
authors.initials: H
authors.lastname: Kuang
authors.forename: D
authors.initials: D
authors.lastname: Qi
authors.forename: A
authors.initials: A
authors.lastname: Mazhary
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D003067:Coenzymes / Q000138:chemical synthesis / Q000737:chemistry; D017076:Computer-Aided Design; D004798:Enzymes / Q000138:chemical synthesis* / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D015202:Protein Engineering; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D003067:Coenzymes; D004798:Enzymes; D011506:Proteins