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Structure, Oligomerization and Activity Modulation in N-Ribohydrolases
Enzymes catalyzing the hydrolysis of the N-glycosidic bond in nucleosides and other ribosides (N-ribohydrolases, NHs) with diverse substrate specificities are found in all kingdoms of life. While the overall NH fold is highly conserved, limited substitutions and insertions can account for difference...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8910321/ https://www.ncbi.nlm.nih.gov/pubmed/35269719 http://dx.doi.org/10.3390/ijms23052576 |
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author | Degano, Massimo |
author_facet | Degano, Massimo |
author_sort | Degano, Massimo |
collection | PubMed |
description | Enzymes catalyzing the hydrolysis of the N-glycosidic bond in nucleosides and other ribosides (N-ribohydrolases, NHs) with diverse substrate specificities are found in all kingdoms of life. While the overall NH fold is highly conserved, limited substitutions and insertions can account for differences in substrate selection, catalytic efficiency, and distinct structural features. The NH structural module is also employed in monomeric proteins devoid of enzymatic activity with different physiological roles. The homo-oligomeric quaternary structure of active NHs parallels the different catalytic strategies used by each isozyme, while providing a buttressing effect to maintain the active site geometry and allow the conformational changes required for catalysis. The unique features of the NH catalytic strategy and structure make these proteins attractive targets for diverse therapeutic goals in different diseases. |
format | Online Article Text |
id | pubmed-8910321 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89103212022-03-11 Structure, Oligomerization and Activity Modulation in N-Ribohydrolases Degano, Massimo Int J Mol Sci Review Enzymes catalyzing the hydrolysis of the N-glycosidic bond in nucleosides and other ribosides (N-ribohydrolases, NHs) with diverse substrate specificities are found in all kingdoms of life. While the overall NH fold is highly conserved, limited substitutions and insertions can account for differences in substrate selection, catalytic efficiency, and distinct structural features. The NH structural module is also employed in monomeric proteins devoid of enzymatic activity with different physiological roles. The homo-oligomeric quaternary structure of active NHs parallels the different catalytic strategies used by each isozyme, while providing a buttressing effect to maintain the active site geometry and allow the conformational changes required for catalysis. The unique features of the NH catalytic strategy and structure make these proteins attractive targets for diverse therapeutic goals in different diseases. MDPI 2022-02-25 /pmc/articles/PMC8910321/ /pubmed/35269719 http://dx.doi.org/10.3390/ijms23052576 Text en © 2022 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Degano, Massimo Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title | Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title_full | Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title_fullStr | Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title_full_unstemmed | Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title_short | Structure, Oligomerization and Activity Modulation in N-Ribohydrolases |
title_sort | structure, oligomerization and activity modulation in n-ribohydrolases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8910321/ https://www.ncbi.nlm.nih.gov/pubmed/35269719 http://dx.doi.org/10.3390/ijms23052576 |
work_keys_str_mv | AT deganomassimo structureoligomerizationandactivitymodulationinnribohydrolases |