ArticlePlant physiology2009
Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme.
Article in Plant physiology, 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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17 citing papers in PubMed, 48 citations in OpenAlex.
- A plastidic starch biosynthetic pathway defines columella-specific carbon metabolism in rice root tips.Frontiers in plant science · 2026Article
- 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
- Genome-Wide Identification of DOF Gene Family and the Mechanism Dissection ofInternational journal of molecular sciences · 2022Article
- Genetic and genomic analysis of the seed-filling process in maize based on a logistic model.Heredity · 2020Article
- Phosphorylation of ADP-Glucose Pyrophosphorylase During Wheat Seeds Development.Frontiers in plant science · 2020Article
- Evolutionary, structural and expression analysis of core genes involved in starch synthesis.Scientific reports · 2018Article
- Resurrecting the Regulatory Properties of theFrontiers in plant science · 2018Article
- Enhancement of Heat Stability and Kinetic Parameters of the Maize Endosperm ADP-Glucose Pyrophosphorylase by Mutagenesis of Amino Acids in the Small Subunit With High B Factors.Frontiers in plant science · 2018Article
- APlant direct · 2017Article
- Mapping of quantitative trait loci for tuber starch and leaf sucrose contents in diploid potato.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016Article
- Lineage-Specific Evolutionary Histories and Regulation of Major Starch Metabolism Genes during Banana Ripening.Frontiers in plant science · 2016Article
- AGPase: its role in crop productivity with emphasis on heat tolerance in cereals.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2015Review
- 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
- Contrasted patterns of selection since maize domestication on duplicated genes encoding a starch pathway enzyme.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2011Article
- Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase.Plant physiology · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-glucose pyrophosphorylase (AGPase) catalyzes a rate-limiting step in glycogen and starch synthesis in bacteria and plants, respectively. Plant AGPase consists of two large and two small subunits that were derived by gene duplication. AGPase large subunits have functionally diverged, leading to different kinetic and allosteric properties. Amino acid changes that could account for these differences were identified previously by evolutionary analysis. In this study, these large subunit residues were mapped onto a modeled structure of the maize (Zea mays) endosperm enzyme. Surprisingly, of 29 amino acids identified via evolutionary considerations, 17 were located at subunit interfaces. Fourteen of the 29 amino acids were mutagenized in the maize endosperm large subunit (SHRUNKEN-2 [SH2]), and resulting variants were expressed in Escherichia coli with the maize endosperm small subunit (BT2). Comparisons of the amount of glycogen produced in E. coli, and the kinetic and allosteric properties of the variants with wild-type SH2/BT2, indicate that 11 variants differ from the wild type in enzyme properties or in vivo glycogen level. More interestingly, six of nine residues located at subunit interfaces exhibit altered allosteric properties. These results indicate that the interfaces between the large and small subunits are important for the allosteric properties of AGPase, and changes at these interfaces contribute to AGPase functional specialization. Our results also demonstrate that evolutionary analysis can greatly facilitate enzyme structure-function analyses.
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