Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants.
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Sociedade Brasileira de Genética
2013
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oai:scielo:S1415-475720130002000132013-12-10Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutasesRamana Gopavajhula,V.Viswanatha Chaitanya,K.Akbar Ali Khan,P.Shaik,Jilani P.Narasimha Reddy,P.Alanazi,Mohammad amino acid analysis model evaluation molecular modeling phylogenetic analysis superoxide dismutase (SOD) Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants.info:eu-repo/semantics/openAccessSociedade Brasileira de GenéticaGenetics and Molecular Biology v.36 n.2 20132013-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000200013en10.1590/S1415-47572013005000023 |
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Ramana Gopavajhula,V. Viswanatha Chaitanya,K. Akbar Ali Khan,P. Shaik,Jilani P. Narasimha Reddy,P. Alanazi,Mohammad |
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Ramana Gopavajhula,V. Viswanatha Chaitanya,K. Akbar Ali Khan,P. Shaik,Jilani P. Narasimha Reddy,P. Alanazi,Mohammad Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
author_facet |
Ramana Gopavajhula,V. Viswanatha Chaitanya,K. Akbar Ali Khan,P. Shaik,Jilani P. Narasimha Reddy,P. Alanazi,Mohammad |
author_sort |
Ramana Gopavajhula,V. |
title |
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
title_short |
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
title_full |
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
title_fullStr |
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
title_full_unstemmed |
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases |
title_sort |
modeling and analysis of soybean (glycine max. l) cu/zn, mn and fe superoxide dismutases |
description |
Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants. |
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Sociedade Brasileira de Genética |
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2013 |
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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000200013 |
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