Making and breaking peptide bonds: protein engineering using sortase

Angew Chem Int Ed Engl. 2011 May 23;50(22):5024-32. doi: 10.1002/anie.201008267. Epub 2011 Apr 27.


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.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Aminoacyltransferases / chemistry
  • Aminoacyltransferases / genetics
  • Aminoacyltransferases / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • Protein Engineering*
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Staphylococcus aureus / enzymology


  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases