title: Enzyme design by chemical modification of protein scaffolds.
abstract: Covalent modification methods allow an almost unlimited range of functionality to be introduced into proteins. In concert with genetic techniques, chemical strategies have had significant impact in the field of enzyme design. Major recent developments include introducing catalytic activity into inactive proteins, modifying the selectivity and/or reactivity of existing enzymes and designing novel enzyme-based biosensors. New chemical methods promise to further increase the range of functionality that can be incorporated into proteins. These results suggest that semi-synthetic methods will play a key role in the development of future biocatalysts.
authors.affiliation: Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
authors.forename: C M
authors.initials: CM
authors.lastname: Tann
authors.forename: D
authors.initials: D
authors.lastname: Qi
authors.forename: M D
authors.initials: MD
authors.lastname: Distefano
mesh_terms: D000595:Amino Acid Sequence; D015374:Biosensing Techniques; D015195:Drug Design; D004798:Enzymes / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D013379:Substrate Specificity
chemical_list: D004798:Enzymes