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Methyl-Coenzyme M Reductase and Its Post-translational Modifications
The methyl-coenzyme M reductase (MCR) is a central enzyme in anaerobic microbial methane metabolism, which consists of methanogenesis and anaerobic oxidation of methane (AOM). MCR catalyzes the final step of methanogenesis and the first step of AOM to achieve the production and oxidation of methane,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7581889/ https://www.ncbi.nlm.nih.gov/pubmed/33162960 http://dx.doi.org/10.3389/fmicb.2020.578356 |
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author | Chen, Hao Gan, Qinglei Fan, Chenguang |
author_facet | Chen, Hao Gan, Qinglei Fan, Chenguang |
author_sort | Chen, Hao |
collection | PubMed |
description | The methyl-coenzyme M reductase (MCR) is a central enzyme in anaerobic microbial methane metabolism, which consists of methanogenesis and anaerobic oxidation of methane (AOM). MCR catalyzes the final step of methanogenesis and the first step of AOM to achieve the production and oxidation of methane, respectively. Besides a unique nickel tetrahydrocorphinoid (coenzyme F430), MCR also features several unusual post-translational modifications (PTMs), which are assumed to play important roles in regulating MCR functions. However, only few studies have been implemented on MCR PTMs. Therefore, to recapitulate current knowledge and prospect future studies, this review summarizes and discusses studies on MCR and its PTMs. |
format | Online Article Text |
id | pubmed-7581889 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-75818892020-11-05 Methyl-Coenzyme M Reductase and Its Post-translational Modifications Chen, Hao Gan, Qinglei Fan, Chenguang Front Microbiol Microbiology The methyl-coenzyme M reductase (MCR) is a central enzyme in anaerobic microbial methane metabolism, which consists of methanogenesis and anaerobic oxidation of methane (AOM). MCR catalyzes the final step of methanogenesis and the first step of AOM to achieve the production and oxidation of methane, respectively. Besides a unique nickel tetrahydrocorphinoid (coenzyme F430), MCR also features several unusual post-translational modifications (PTMs), which are assumed to play important roles in regulating MCR functions. However, only few studies have been implemented on MCR PTMs. Therefore, to recapitulate current knowledge and prospect future studies, this review summarizes and discusses studies on MCR and its PTMs. Frontiers Media S.A. 2020-10-09 /pmc/articles/PMC7581889/ /pubmed/33162960 http://dx.doi.org/10.3389/fmicb.2020.578356 Text en Copyright © 2020 Chen, Gan and Fan. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Chen, Hao Gan, Qinglei Fan, Chenguang Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title | Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title_full | Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title_fullStr | Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title_full_unstemmed | Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title_short | Methyl-Coenzyme M Reductase and Its Post-translational Modifications |
title_sort | methyl-coenzyme m reductase and its post-translational modifications |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7581889/ https://www.ncbi.nlm.nih.gov/pubmed/33162960 http://dx.doi.org/10.3389/fmicb.2020.578356 |
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