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The structure–function relationships and physiological roles of MnSOD mutants

In this review, we focus on understanding the structure–function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that various amino acids play to maintain enzyme quaternary structure or the active site structure, catalytic potential and metal homeosta...

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Detalles Bibliográficos
Autor principal: Bonetta Valentino, Rosalin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9208312/
https://www.ncbi.nlm.nih.gov/pubmed/35662317
http://dx.doi.org/10.1042/BSR20220202
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author Bonetta Valentino, Rosalin
author_facet Bonetta Valentino, Rosalin
author_sort Bonetta Valentino, Rosalin
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description In this review, we focus on understanding the structure–function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that various amino acids play to maintain enzyme quaternary structure or the active site structure, catalytic potential and metal homeostasis in MnSOD, which is essential to maintain enzyme activity. We also observe how polymorphisms of MnSOD are linked to pathologies and how post-translational modifications affect the antioxidant properties of MnSOD. Understanding how modified forms of MnSOD may act as tumor promoters or suppressors by altering the redox status in the body, ultimately aid in generating novel therapies that exploit the therapeutic potential of mutant MnSODs or pave the way for the development of synthetic SOD mimics.
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spelling pubmed-92083122022-07-08 The structure–function relationships and physiological roles of MnSOD mutants Bonetta Valentino, Rosalin Biosci Rep Structural Biology In this review, we focus on understanding the structure–function relationships of numerous manganese superoxide dismutase (MnSOD) mutants to investigate the role that various amino acids play to maintain enzyme quaternary structure or the active site structure, catalytic potential and metal homeostasis in MnSOD, which is essential to maintain enzyme activity. We also observe how polymorphisms of MnSOD are linked to pathologies and how post-translational modifications affect the antioxidant properties of MnSOD. Understanding how modified forms of MnSOD may act as tumor promoters or suppressors by altering the redox status in the body, ultimately aid in generating novel therapies that exploit the therapeutic potential of mutant MnSODs or pave the way for the development of synthetic SOD mimics. Portland Press Ltd. 2022-06-17 /pmc/articles/PMC9208312/ /pubmed/35662317 http://dx.doi.org/10.1042/BSR20220202 Text en © 2022 The Author(s). https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Structural Biology
Bonetta Valentino, Rosalin
The structure–function relationships and physiological roles of MnSOD mutants
title The structure–function relationships and physiological roles of MnSOD mutants
title_full The structure–function relationships and physiological roles of MnSOD mutants
title_fullStr The structure–function relationships and physiological roles of MnSOD mutants
title_full_unstemmed The structure–function relationships and physiological roles of MnSOD mutants
title_short The structure–function relationships and physiological roles of MnSOD mutants
title_sort structure–function relationships and physiological roles of mnsod mutants
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9208312/
https://www.ncbi.nlm.nih.gov/pubmed/35662317
http://dx.doi.org/10.1042/BSR20220202
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