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Making and Breaking Peptide Bonds: Protein Engineering Using Sortase
Author(s) -
Popp Maximilian WeiLin,
Ploegh Hidde L.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201008267
Subject(s) - sortase , sortase a , protein engineering , peptide bond , peptide , structural biology , posttranslational modification , chemistry , enzyme , computational biology , biochemistry , nanotechnology , combinatorial chemistry , bacterial protein , biology , materials science , gene
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.