| First Author | Popp MW | Year | 2011 |
| Journal | Angew Chem Int Ed Engl | Volume | 50 |
| Issue | 22 | Pages | 5024-32 |
| PubMed ID | 21538739 | Mgi Jnum | J:172383 |
| Mgi Id | MGI:5007581 | Doi | 10.1002/anie.201008267 |
| Citation | Popp MW, et al. (2011) Making and breaking Peptide bonds: protein engineering using sortase. Angew Chem Int Ed Engl 50(22):5024-32 |
| abstractText | 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. |
