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Activity‐Based Protein Profiling (ABPP) of Oxidoreductases
Over the last two decades, activity‐based protein profiling (ABPP) has been established as a tremendously useful proteomic tool for measuring the activity of proteins in their cellular context, annotating the function of uncharacterized proteins, and investigating the target profile of small‐molecul...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7894341/ https://www.ncbi.nlm.nih.gov/pubmed/32881211 http://dx.doi.org/10.1002/cbic.202000542 |
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author | Fuerst, Rita Breinbauer, Rolf |
author_facet | Fuerst, Rita Breinbauer, Rolf |
author_sort | Fuerst, Rita |
collection | PubMed |
description | Over the last two decades, activity‐based protein profiling (ABPP) has been established as a tremendously useful proteomic tool for measuring the activity of proteins in their cellular context, annotating the function of uncharacterized proteins, and investigating the target profile of small‐molecule inhibitors. Unlike hydrolases and other enzyme classes, which exhibit a characteristic nucleophilic residue, oxidoreductases have received much less attention in ABPP. In this minireview, the state of the art of ABPP of oxidoreductases is described and the scope and limitations of the existing approaches are discussed. It is noted that several ABPP probes have been described for various oxidases, but none so far for a reductase, which gives rise to opportunities for future research. |
format | Online Article Text |
id | pubmed-7894341 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-78943412021-03-02 Activity‐Based Protein Profiling (ABPP) of Oxidoreductases Fuerst, Rita Breinbauer, Rolf Chembiochem Minireviews Over the last two decades, activity‐based protein profiling (ABPP) has been established as a tremendously useful proteomic tool for measuring the activity of proteins in their cellular context, annotating the function of uncharacterized proteins, and investigating the target profile of small‐molecule inhibitors. Unlike hydrolases and other enzyme classes, which exhibit a characteristic nucleophilic residue, oxidoreductases have received much less attention in ABPP. In this minireview, the state of the art of ABPP of oxidoreductases is described and the scope and limitations of the existing approaches are discussed. It is noted that several ABPP probes have been described for various oxidases, but none so far for a reductase, which gives rise to opportunities for future research. John Wiley and Sons Inc. 2020-10-20 2021-02-15 /pmc/articles/PMC7894341/ /pubmed/32881211 http://dx.doi.org/10.1002/cbic.202000542 Text en © 2020 The Authors. Published by Wiley-VCH GmbH This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Minireviews Fuerst, Rita Breinbauer, Rolf Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title | Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title_full | Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title_fullStr | Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title_full_unstemmed | Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title_short | Activity‐Based Protein Profiling (ABPP) of Oxidoreductases |
title_sort | activity‐based protein profiling (abpp) of oxidoreductases |
topic | Minireviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7894341/ https://www.ncbi.nlm.nih.gov/pubmed/32881211 http://dx.doi.org/10.1002/cbic.202000542 |
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