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Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential

ADP-glucose pyrophosphorylase (AGPase) is the first rate limiting enzyme of starch biosynthesis pathway and has been exploited as the target for greater starch yield in several plants. The structure-function analysis and substrate binding specificity of AGPase have provided enormous potential for un...

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Autores principales: Sarma, Kishore, Sen, Priyabrata, Barooah, Madhumita, Choudhury, Manabendra D., Roychoudhury, Shubhadeep, Modi, Mahendra K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167649/
https://www.ncbi.nlm.nih.gov/pubmed/25276800
http://dx.doi.org/10.1155/2014/583606
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author Sarma, Kishore
Sen, Priyabrata
Barooah, Madhumita
Choudhury, Manabendra D.
Roychoudhury, Shubhadeep
Modi, Mahendra K.
author_facet Sarma, Kishore
Sen, Priyabrata
Barooah, Madhumita
Choudhury, Manabendra D.
Roychoudhury, Shubhadeep
Modi, Mahendra K.
author_sort Sarma, Kishore
collection PubMed
description ADP-glucose pyrophosphorylase (AGPase) is the first rate limiting enzyme of starch biosynthesis pathway and has been exploited as the target for greater starch yield in several plants. The structure-function analysis and substrate binding specificity of AGPase have provided enormous potential for understanding the role of specific amino acid or motifs responsible for allosteric regulation and catalytic mechanisms, which facilitate the engineering of AGPases. We report the three-dimensional structure, substrate, and inhibitor binding specificity of AGPase small subunit from different monocot and dicot crop plants. Both monocot and dicot subunits were found to exploit similar interactions with the substrate and inhibitor molecule as in the case of their closest homologue potato tuber AGPase small subunit. Comparative sequence and structural analysis followed by molecular docking and electrostatic surface potential analysis reveal that rearrangements of secondary structure elements, substrate, and inhibitor binding residues are strongly conserved and follow common folding pattern and orientation within monocot and dicot displaying a similar mode of allosteric regulation and catalytic mechanism. The results from this study along with site-directed mutagenesis complemented by molecular dynamics simulation will shed more light on increasing the starch content of crop plants to ensure the food security worldwide.
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spelling pubmed-41676492014-09-28 Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential Sarma, Kishore Sen, Priyabrata Barooah, Madhumita Choudhury, Manabendra D. Roychoudhury, Shubhadeep Modi, Mahendra K. Biomed Res Int Research Article ADP-glucose pyrophosphorylase (AGPase) is the first rate limiting enzyme of starch biosynthesis pathway and has been exploited as the target for greater starch yield in several plants. The structure-function analysis and substrate binding specificity of AGPase have provided enormous potential for understanding the role of specific amino acid or motifs responsible for allosteric regulation and catalytic mechanisms, which facilitate the engineering of AGPases. We report the three-dimensional structure, substrate, and inhibitor binding specificity of AGPase small subunit from different monocot and dicot crop plants. Both monocot and dicot subunits were found to exploit similar interactions with the substrate and inhibitor molecule as in the case of their closest homologue potato tuber AGPase small subunit. Comparative sequence and structural analysis followed by molecular docking and electrostatic surface potential analysis reveal that rearrangements of secondary structure elements, substrate, and inhibitor binding residues are strongly conserved and follow common folding pattern and orientation within monocot and dicot displaying a similar mode of allosteric regulation and catalytic mechanism. The results from this study along with site-directed mutagenesis complemented by molecular dynamics simulation will shed more light on increasing the starch content of crop plants to ensure the food security worldwide. Hindawi Publishing Corporation 2014 2014-09-02 /pmc/articles/PMC4167649/ /pubmed/25276800 http://dx.doi.org/10.1155/2014/583606 Text en Copyright © 2014 Kishore Sarma et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Sarma, Kishore
Sen, Priyabrata
Barooah, Madhumita
Choudhury, Manabendra D.
Roychoudhury, Shubhadeep
Modi, Mahendra K.
Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title_full Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title_fullStr Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title_full_unstemmed Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title_short Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
title_sort structural comparison, substrate specificity, and inhibitor binding of agpase small subunit from monocot and dicot: present insight and future potential
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167649/
https://www.ncbi.nlm.nih.gov/pubmed/25276800
http://dx.doi.org/10.1155/2014/583606
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