Research Mentor(s)
Antos, John M.
Description
Enzymes have become an attractive option for protein modification chemistry due to the remarkable site-specificity they afford. Of particular interest is sortase A from taphylococcus aureus (SrtAaur), which has garnered attention for its ability to install a variety of non-natural modifications to a conserved oligopeptide substrate. In addition to SrtAaur it has become apparent that sortase A homologs exist in other bacterial strains, each of which is potentially a novel catalyst for protein engineering. Previous work has demonstrated that eight representative sortase A homologs exhibit unique specificities for synthetic peptide substrates, capable of identifying characteristic combinations of amino acids in the “sorting motif.” Presented here is a nucleophile profile of the most promiscuous sortase A homolog investigated, that from Streptococcus pneumoniae (SrtApneu). Exhibiting unique specificities, this SrtA variant may enable unique protein modification chemistry.
Document Type
Event
Start Date
19-5-2016 12:00 PM
End Date
19-5-2016 3:00 PM
Department
Chemistry
Genre/Form
student projects; posters
Subjects – Topical (LCSH)
Enzymes--Analysis; Protein engineering
Type
Image
Keywords
Sortase, nucleophile, transpeptidation, ligation, CRF, peptide
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this documentation for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.
Language
English
Format
application/pdf
Included in
Evaluating Nucleophile and Substrate Specificities of Sortase A Homologs for Orthogonal Reactivity
Enzymes have become an attractive option for protein modification chemistry due to the remarkable site-specificity they afford. Of particular interest is sortase A from taphylococcus aureus (SrtAaur), which has garnered attention for its ability to install a variety of non-natural modifications to a conserved oligopeptide substrate. In addition to SrtAaur it has become apparent that sortase A homologs exist in other bacterial strains, each of which is potentially a novel catalyst for protein engineering. Previous work has demonstrated that eight representative sortase A homologs exhibit unique specificities for synthetic peptide substrates, capable of identifying characteristic combinations of amino acids in the “sorting motif.” Presented here is a nucleophile profile of the most promiscuous sortase A homolog investigated, that from Streptococcus pneumoniae (SrtApneu). Exhibiting unique specificities, this SrtA variant may enable unique protein modification chemistry.
Comments
Outstanding Poster Award Recipient