ArticlePLoS computational biology2009
Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Evaluation of ADP Glucose Pyrophosphorylase Subunit Interaction in Wheat by Binding Free Energy Calculations.Molecular biotechnology · 2026Article
- Structure and mechanism of the heterotetrameric ADP-glucose pyrophosphorylase essential for starch synthesis in plants.Science advances · 2026Article
- Expression and interaction of AGPase subunits reveal functional enzyme complexes in barley.Frontiers in plant science · 2025Article
- Genome-wide association analysis and transgenic characterization for amylose content regulating gene in tuber of Dioscorea zingiberensis.BMC plant biology · 2024Article
- A critical inter-subunit interaction for the transmission of the allosteric signal in the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase.Protein science : a publication of the Protein Society · 2023Article
- Exploiting AGPase genes and encoded proteins to prioritize development of optimum engineered strains in microalgae towards sustainable biofuel production.World journal of microbiology & biotechnology · 2023Article
- Structure, function, and evolution of plant ADP-glucose pyrophosphorylase.Plant molecular biology · 2022Review
- Phosphorylation of ADP-Glucose Pyrophosphorylase During Wheat Seeds Development.Frontiers in plant science · 2020Article
- Mechanism Underlying Heat Stability of the Rice Endosperm Cytosolic ADP-Glucose Pyrophosphorylase.Frontiers in plant science · 2019Article
- Upregulated Lipid Biosynthesis at the Expense of Starch Production in Potato (Frontiers in plant science · 2019Article
- Isolation and characterization of cDNAs and genomic DNAs encoding ADP-glucose pyrophosphorylase large and small subunits from sweet potato.Molecular genetics and genomics : MGG · 2016Article
- Structural comparison, substrate specificity, and inhibitor binding of AGPase small subunit from monocot and dicot: present insight and future potential.BioMed research international · 2014Article
- Insight into the 3D structure of ADP-glucose pyrophosphorylase from rice (Oryza sativa L.).Journal of molecular modeling · 2013Article
- Accelerated evolution and coevolution drove the evolutionary history of AGPase sub-units during angiosperm radiation.Annals of botany · 2012Article
- Insights of interaction between small and large subunits of ADP-glucose pyrophosphorylase from bread wheat (Triticum aestivum L.).Bioinformation · 2011Article
- Drug discovery using chemical systems biology: weak inhibition of multiple kinases may contribute to the anti-cancer effect of nelfinavir.PLoS computational biology · 2011Article
- Molecular recognition of H3/H4 histone tails by the tudor domains of JMJD2A: a comparative molecular dynamics simulations study.PloS one · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-glucose pyrophosphorylase (AGPase), a key allosteric enzyme involved in higher plant starch biosynthesis, is composed of pairs of large (LS) and small subunits (SS). Current evidence indicates that the two subunit types play distinct roles in enzyme function. Recently the heterotetrameric structure of potato AGPase has been modeled. In the current study, we have applied the molecular mechanics generalized born surface area (MM-GBSA) method and identified critical amino acids of the potato AGPase LS and SS subunits that interact with each other during the native heterotetrameric structure formation. We have further shown the role of the LS amino acids in subunit-subunit interaction by yeast two-hybrid, bacterial complementation assay and native gel. Comparison of the computational results with the experiments has indicated that the backbone energy contribution (rather than the side chain energies) of the interface residues is more important in identifying critical residues. We have found that lateral interaction of the LS-SS is much stronger than the longitudinal one, and it is mainly mediated by hydrophobic interactions. This study will not only enhance our understanding of the interaction between the SS and the LS of AGPase, but will also enable us to engineer proteins to obtain better assembled variants of AGPase which can be used for the improvement of plant yield.
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