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Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential
Joint Authors
Sarma, Kishore
Sen, Priyabrata
Barooah, Madhumita
Choudhury, Manabendra D.
Roychoudhury, Shubhadeep
Modi, Mahendra K.
Source
Issue
Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-20, 20 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2014-09-02
Country of Publication
Egypt
No. of Pages
20
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Sarma, Kishore& Sen, Priyabrata& Barooah, Madhumita& Choudhury, Manabendra D.& Roychoudhury, Shubhadeep& Modi, Mahendra K.. 2014. Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential. BioMed Research International،Vol. 2014, no. 2014, pp.1-20.
https://search.emarefa.net/detail/BIM-1016378
Modern Language Association (MLA)
Sarma, Kishore…[et al.]. Structural Comparison, Substrate Specificity, and Inhibitor Binding of AGPase Small Subunit from Monocot and Dicot: Present Insight and Future Potential. BioMed Research International No. 2014 (2014), pp.1-20.
https://search.emarefa.net/detail/BIM-1016378
American Medical Association (AMA)
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. BioMed Research International. 2014. Vol. 2014, no. 2014, pp.1-20.
https://search.emarefa.net/detail/BIM-1016378
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1016378