Research Mentor(s)

John Antos

Affiliated Department

Chemistry

Sort Order

18

Start Date

19-5-2016 12:00 PM

End Date

19-5-2016 3:00 PM

Keywords

Sortase, nucleophile, transpeptidation, ligation, CRF, peptide

Document Type

Event

Abstract

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

Included in

Chemistry Commons

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May 19th, 12:00 PM May 19th, 3:00 PM

Evaluating Nucleophile and Substrate Specificities of Sortase A Homologs for Orthogonal Reactivity

Chemistry

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.

 

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