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Making and Breaking Peptide Bonds: Protein Engineering Using Sortase
Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a r...
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Published in: | Angewandte Chemie International Edition 2011-05, Vol.50 (22), p.5024-5032 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry‐based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications.
It takes all sortases: Enzymatic formation of a peptide bond using the sortase A transpeptidase (SrtA) provides a convenient and mild means for engineering proteins to contain nongenetically templated modifications. Myriad applications are possible, from producing homogeneous post‐translational modification mimics, assembling protein domains, to anchoring proteins to solid surfaces. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201008267 |