{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Morgan HE"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["2341-2347"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9782347"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(12)"],"pubmed_abstract":["<i>Staphylococcus aureus</i> sortase A is a transpeptidase that has been extensively exploited for site-specific modification of proteins and was originally used to attach a labeling reagent containing an LPXTG recognition sequence to a protein or peptide with an N-terminal glycine. Sortase mutants with other recognition sequences have also been reported, but in all cases, the reversibility of the transpeptidation reaction limits the efficiency of sortase-mediated labeling reactions. For the wildtype sortase, depsipeptide substrates, in which the scissile peptide bond is replaced with an ester, allow effectively irreversible sortase-mediated labeling as the alcohol byproduct is a poor competing nucleophile. In this paper, the use of depsipeptide substrates for evolved sortase variants is r"],"journal":["Bioconjugate chemistry"],"pubmed_title":["Combined Application of Orthogonal Sortases and Depsipeptide Substrates for Dual Protein Labeling."],"pmcid":["PMC9782347"],"funding_grant_id":["BB/R005540/1","BB/M011151/1"],"pubmed_authors":["Morgan HE","Webb ME","Kaminski TP","Arnott ZLP","Turnbull WB"],"additional_accession":[]},"is_claimable":false,"name":"Combined Application of Orthogonal Sortases and Depsipeptide Substrates for Dual Protein Labeling.","description":"<i>Staphylococcus aureus</i> sortase A is a transpeptidase that has been extensively exploited for site-specific modification of proteins and was originally used to attach a labeling reagent containing an LPXTG recognition sequence to a protein or peptide with an N-terminal glycine. Sortase mutants with other recognition sequences have also been reported, but in all cases, the reversibility of the transpeptidation reaction limits the efficiency of sortase-mediated labeling reactions. For the wildtype sortase, depsipeptide substrates, in which the scissile peptide bond is replaced with an ester, allow effectively irreversible sortase-mediated labeling as the alcohol byproduct is a poor competing nucleophile. In this paper, the use of depsipeptide substrates for evolved sortase variants is r","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-04T07:59:58.215Z","creation":"2025-04-04T07:59:58.215Z"},"accession":"S-EPMC9782347","cross_references":{"pubmed":["36356167"],"doi":["10.1021/acs.bioconjchem.2c00411"]}}