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On the diversity of F(420) ‐dependent oxidoreductases: A sequence‐ and structure‐based classification
The F(420) deazaflavin cofactor is an intriguing molecule as it structurally resembles the canonical flavin cofactor, although behaves as a nicotinamide cofactor due to its obligate hydride‐transfer reactivity and similar low redox potential. Since its discovery, numerous enzymes relying on it have...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8518648/ https://www.ncbi.nlm.nih.gov/pubmed/34216160 http://dx.doi.org/10.1002/prot.26170 |
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author | Mascotti, María Laura Juri Ayub, Maximiliano Fraaije, Marco W. |
author_facet | Mascotti, María Laura Juri Ayub, Maximiliano Fraaije, Marco W. |
author_sort | Mascotti, María Laura |
collection | PubMed |
description | The F(420) deazaflavin cofactor is an intriguing molecule as it structurally resembles the canonical flavin cofactor, although behaves as a nicotinamide cofactor due to its obligate hydride‐transfer reactivity and similar low redox potential. Since its discovery, numerous enzymes relying on it have been described. The known deazaflavoproteins are taxonomically restricted to Archaea and Bacteria. The biochemistry of the deazaflavoenzymes is diverse and they exhibit great structural variability. In this study a thorough sequence and structural homology evolutionary analysis was performed in order to generate an overarching classification of the F(420)‐dependent oxidoreductases. Five different deazaflavoenzyme Classes (I–V) are described according to their structural folds as follows: Class I encompassing the TIM‐barrel F(420)‐dependent enzymes; Class II including the Rossmann fold F(420)‐dependent enzymes; Class III comprising the β‐roll F(420)‐dependent enzymes; Class IV which exclusively gathers the SH3 barrel F(420)‐dependent enzymes and Class V including the three layer ββα sandwich F(420)‐dependent enzymes. This classification provides a framework for the identification and biochemical characterization of novel deazaflavoenzymes. |
format | Online Article Text |
id | pubmed-8518648 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-85186482021-10-21 On the diversity of F(420) ‐dependent oxidoreductases: A sequence‐ and structure‐based classification Mascotti, María Laura Juri Ayub, Maximiliano Fraaije, Marco W. Proteins Research Articles The F(420) deazaflavin cofactor is an intriguing molecule as it structurally resembles the canonical flavin cofactor, although behaves as a nicotinamide cofactor due to its obligate hydride‐transfer reactivity and similar low redox potential. Since its discovery, numerous enzymes relying on it have been described. The known deazaflavoproteins are taxonomically restricted to Archaea and Bacteria. The biochemistry of the deazaflavoenzymes is diverse and they exhibit great structural variability. In this study a thorough sequence and structural homology evolutionary analysis was performed in order to generate an overarching classification of the F(420)‐dependent oxidoreductases. Five different deazaflavoenzyme Classes (I–V) are described according to their structural folds as follows: Class I encompassing the TIM‐barrel F(420)‐dependent enzymes; Class II including the Rossmann fold F(420)‐dependent enzymes; Class III comprising the β‐roll F(420)‐dependent enzymes; Class IV which exclusively gathers the SH3 barrel F(420)‐dependent enzymes and Class V including the three layer ββα sandwich F(420)‐dependent enzymes. This classification provides a framework for the identification and biochemical characterization of novel deazaflavoenzymes. John Wiley & Sons, Inc. 2021-07-16 2021-11 /pmc/articles/PMC8518648/ /pubmed/34216160 http://dx.doi.org/10.1002/prot.26170 Text en © 2021 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Research Articles Mascotti, María Laura Juri Ayub, Maximiliano Fraaije, Marco W. On the diversity of F(420) ‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title | On the diversity of F(420)
‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title_full | On the diversity of F(420)
‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title_fullStr | On the diversity of F(420)
‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title_full_unstemmed | On the diversity of F(420)
‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title_short | On the diversity of F(420)
‐dependent oxidoreductases: A sequence‐ and structure‐based classification |
title_sort | on the diversity of f(420)
‐dependent oxidoreductases: a sequence‐ and structure‐based classification |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8518648/ https://www.ncbi.nlm.nih.gov/pubmed/34216160 http://dx.doi.org/10.1002/prot.26170 |
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