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Efficient N‐Terminal Labeling of Proteins by Use of Sortase
Author(s) -
Williamson Daniel J.,
Fascione Martin A.,
Webb Michael E.,
Turnbull W. Bruce
Publication year - 2012
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.201204538
Subject(s) - sortase , terminal (telecommunication) , sortase a , chemistry , computer science , biochemistry , bacterial protein , computer network , gene
“Sorting out” N‐terminal labeling : The reversibility of transpeptidase reactions makes protein N‐terminal labeling challenging. Depsipeptide substrates for sortase A release alcohol by‐products, which are poor nucleophiles for the reverse reaction, during ligation. Proteins with an unhindered N‐terminal glycine residue can be labeled efficiently with only a minimal excess of the labeling reagent (see scheme).