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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...

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Detalles Bibliográficos
Autores principales: Fuerst, Rita, Breinbauer, Rolf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
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.
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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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