Journal
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 34
Volume 34, Issue -, Pages 163-188Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-cellbio-100617-062527
Keywords
transpeptidases; sortase A; nucleophile; protein engineering; cell surface labeling
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIAID NIH HHS [R01 AI087879] Funding Source: Medline
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Molecular biologists and chemists alike have long sought to modify proteins with substituents that cannot be installed by standard or even advanced genetic approaches. We here describe the use of transpeptidases to achieve these goals. Living systems encode a variety of transpeptidases and peptide ligases that allow for the enzyme-catalyzed formation of peptide bonds, and protein engineers have used directed evolution to enhance these enzymes for biological applications. We focus primarily on the transpeptidase sortase A, which has become popular over the past few years for its ability to perform a remarkably wide variety of protein modifications, both in vitro and in living cells.
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