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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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Detalles Bibliográficos
Autor principal: Degano, Massimo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
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.
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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
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