Enzyme design by chemical modification of protein scaffolds

Cheng Min Tann, Dongfeng Qi, Mark D. Distefano

Research output: Contribution to journalReview articlepeer-review

34 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)696-704
Number of pages9
JournalCurrent opinion in chemical biology
Volume5
Issue number6
DOIs
StatePublished - Dec 1 2001

Bibliographical note

Funding Information:
We thank the Minnesota Supercomputing Institute for providing facilities for molecular modeling and the National Science Foundation (CHE9807495) for their financial support. MDD also thanks the members of the Protein Engineering group at Genentech Inc. for providing a stimulating scientific environment while on sabbatical leave there when this article was written.

Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.

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