title: Sortagging: a robust and efficient chemoenzymatic ligation strategy.
abstract: Bioorthogonal, chemoselective ligation methods are an essential part of the tools utilized to investigate biochemical pathways. Specifically enzymatic approaches are valuable methods in this context due to the inherent specificity of the deployed enzymes and the mild conditions of the modification reactions. One of the most common strategies is based on the transpeptidation catalyzed by sortase A derived from Staphylococcus aureus. The procedure is well established and a wide variety of applications have been published to date. Here, implementations of sortase A, which range from protein labeling using fluorescence dyes and the preparation of cyclic proteins to the modification of entire cells, are summarized. Furthermore, there is a focus on the optimization approaches established to solve the drawbacks of sortase-mediated transpeptidation.
authors: Bielefeld University, Department of Chemistry, Organic and Bioorganic Chemistry (OCIII), Universitätsstrasse 25, 33615 Bielefeld (Germany). Markus.Ritzefeld@gmx.de.
authors: Markus
authors: M
authors: Ritzefeld
mesh_terms: D019881:Aminoacyltransferases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D015394:Molecular Structure; D011506:Proteins / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases
keywords: chemical biology; enzymes; peptides; protein engineering; protein modification