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Overview on Peroxiredoxin
Peroxiredoxins (Prxs) are a very large and highly conserved family of peroxidases that reduce peroxides, with a conserved cysteine residue, designated the “peroxidatic” Cys (C(P)) serving as the site of oxidation by peroxides (Hall et al., 2011; Rhee et al., 2012). Peroxides oxidize the C(P)-SH to c...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Korean Society for Molecular and Cellular Biology
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4749868/ https://www.ncbi.nlm.nih.gov/pubmed/26831451 http://dx.doi.org/10.14348/molcells.2016.2368 |
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author | Rhee, Sue Goo |
author_facet | Rhee, Sue Goo |
author_sort | Rhee, Sue Goo |
collection | PubMed |
description | Peroxiredoxins (Prxs) are a very large and highly conserved family of peroxidases that reduce peroxides, with a conserved cysteine residue, designated the “peroxidatic” Cys (C(P)) serving as the site of oxidation by peroxides (Hall et al., 2011; Rhee et al., 2012). Peroxides oxidize the C(P)-SH to cysteine sulfenic acid (C(P)–SOH), which then reacts with another cysteine residue, named the “resolving” Cys (C(R)) to form a disulfide that is subsequently reduced by an appropriate electron donor to complete a catalytic cycle. This overview summarizes the status of studies on Prxs and relates the following 10 minireviews. |
format | Online Article Text |
id | pubmed-4749868 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Korean Society for Molecular and Cellular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-47498682016-02-25 Overview on Peroxiredoxin Rhee, Sue Goo Mol Cells Overview Peroxiredoxins (Prxs) are a very large and highly conserved family of peroxidases that reduce peroxides, with a conserved cysteine residue, designated the “peroxidatic” Cys (C(P)) serving as the site of oxidation by peroxides (Hall et al., 2011; Rhee et al., 2012). Peroxides oxidize the C(P)-SH to cysteine sulfenic acid (C(P)–SOH), which then reacts with another cysteine residue, named the “resolving” Cys (C(R)) to form a disulfide that is subsequently reduced by an appropriate electron donor to complete a catalytic cycle. This overview summarizes the status of studies on Prxs and relates the following 10 minireviews. Korean Society for Molecular and Cellular Biology 2016-01-31 2016-01-27 /pmc/articles/PMC4749868/ /pubmed/26831451 http://dx.doi.org/10.14348/molcells.2016.2368 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Overview Rhee, Sue Goo Overview on Peroxiredoxin |
title | Overview on Peroxiredoxin |
title_full | Overview on Peroxiredoxin |
title_fullStr | Overview on Peroxiredoxin |
title_full_unstemmed | Overview on Peroxiredoxin |
title_short | Overview on Peroxiredoxin |
title_sort | overview on peroxiredoxin |
topic | Overview |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4749868/ https://www.ncbi.nlm.nih.gov/pubmed/26831451 http://dx.doi.org/10.14348/molcells.2016.2368 |
work_keys_str_mv | AT rheesuegoo overviewonperoxiredoxin |