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Asparaginyl Ligases: New Enzymes for the Protein Engineer's Toolbox
Author(s) -
Rehm Fabian B. H.,
Tyler Tristan J.,
Xie Jing,
Yap Kuok,
Durek Thomas,
Craik David J.
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100071
Subject(s) - protein engineering , enzyme , biochemistry , tripeptide , toolbox , protein design , protein function , chemistry , protein structure , computational biology , biology , peptide , computer science , gene , programming language
Enzyme‐catalysed site‐specific protein modifications enable the precision manufacture of conjugates for the study of protein function and/or for therapeutic or diagnostic applications. Asparaginyl ligases are a class of highly efficient transpeptidases with the capacity to modify proteins bearing only a tripeptide recognition motif. Herein, we review the types of protein modification that are accessible using these enzymes, including N‐ and C‐terminal protein labelling, head‐to‐tail cyclisation, and protein‐protein conjugation. We describe the progress that has been made to engineer highly efficient ligases as well as efforts to chemically manipulate the enzyme reaction to favour product formation. These enzymes are powerful additions to the protein engineer‘s toolbox.