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Structural comparison, substrate specificity, and inhibitor binding of AGPase small subunit from monocot and dicot: present insight and future potential.
- Source :
-
BioMed research international [Biomed Res Int] 2014; Vol. 2014, pp. 583606. Date of Electronic Publication: 2014 Sep 02. - Publication Year :
- 2014
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Molecular Docking Simulation
Molecular Sequence Data
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Alignment
Sequence Analysis, Protein
Static Electricity
Structural Homology, Protein
Substrate Specificity drug effects
Enzyme Inhibitors pharmacology
Glucose-1-Phosphate Adenylyltransferase antagonists & inhibitors
Glucose-1-Phosphate Adenylyltransferase chemistry
Magnoliopsida enzymology
Poaceae enzymology
Protein Subunits antagonists & inhibitors
Protein Subunits chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 2314-6141
- Volume :
- 2014
- Database :
- MEDLINE
- Journal :
- BioMed research international
- Publication Type :
- Academic Journal
- Accession number :
- 25276800
- Full Text :
- https://doi.org/10.1155/2014/583606