Enzyme design by chemical modification of protein scaffolds

Citation
Cm. Tann et al., Enzyme design by chemical modification of protein scaffolds, CURR OP C B, 5(6), 2001, pp. 696-704
Citations number
65
Categorie Soggetti
Biochemistry & Biophysics
Journal title
CURRENT OPINION IN CHEMICAL BIOLOGY
ISSN journal
13675931 → ACNP
Volume
5
Issue
6
Year of publication
2001
Pages
696 - 704
Database
ISI
SICI code
1367-5931(200112)5:6<696:EDBCMO>2.0.ZU;2-1
Abstract
Covalent modification methods allow an almost unlimited range of functional ity to be introduced into proteins. In concert with genetic techniques, che mical strategies have had significant impact in the field of enzyme design. Major recent developments include introducing catalytic activity into inac tive proteins, modifying the selectivity and/or reactivity of existing enzy mes and designing novel enzyme-based biosensors. New chemical methods promi se 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.