Morgan, HE orcid.org/0000-0002-9259-5237, Turnbull, WB orcid.org/0000-0002-7352-0360 and Webb, ME orcid.org/0000-0003-3574-4686 (2022) Challenges in the use of sortase and other peptide ligases for site-specific protein modification. Chemical Society Reviews. ISSN 0306-0012
Abstract
Site-specific protein modification is a widely-used biochemical tool. However, there are many challenges associated with the development of protein modification techniques, in particular, achieving site-specificity, reaction efficiency and versatility. The engineering of peptide ligases and their substrates has been used to address these challenges. This review will focus on sortase, peptidyl asparaginyl ligases (PALs) and variants of subtilisin; detailing how their inherent specificity has been utilised for site-specific protein modification. The review will explore how the engineering of these enzymes and substrates has led to increased reaction efficiency mainly due to enhanced catalytic activity and reduction of reversibility. It will also describe how engineering peptide ligases to broaden their substrate scope is opening up new opportunities to expand the biochemical toolkit, particularly through the development of techniques to conjugate multiple substrates site-specifically onto a protein using orthogonal peptide ligases.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Royal Society of Chemistry 2022. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 May 2022 13:35 |
Last Modified: | 10 May 2022 13:35 |
Status: | Published online |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/d0cs01148g |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:186613 |