ArticlePlanta2016
The plastidial starch phosphorylase from rice endosperm: catalytic properties at low temperature.
Article in Planta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 40 citations in OpenAlex.
- Starch phosphorylase acts as a pivotal scaffold connecting starch metabolism enzymes with photosystem I subunits.Plant & cell physiology · 2026Article
- Seed priming with Streptomyces griseoviridis culture filtrate: species-specific enhancement of legume germination and seedling vigor through hormonal and metabolic signaling.BMC plant biology · 2026Article
- The plastidial PHS1-DPE1 complex drives efficient malto-oligosaccharides synthesis in rice starch metabolism.Nature communications · 2026Article
- Old player, new roles: defining the role of the plastidial phosphorylase.The New phytologist · 2025Review
- Prohexadione Calcium Improves Rice Yield Under Salt Stress by Regulating Source-Sink Relationships During the Filling Period.Plants (Basel, Switzerland) · 2025Article
- Kinetic and Structural Studies of the PlastidialACS omega · 2024Article
- Initiation of B-type starch granules in wheat endosperm requires the plastidial α-glucan phosphorylase PHS1.The Plant cell · 2023Article
- Pho1 cooperates with DPE1 to control short maltooligosaccharide mobilization during starch synthesis initiation in rice endosperm.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- Article
- Comparative Study of Starch Phosphorylase Genes and Encoded Proteins in Various Monocots and Dicots with Emphasis on Maize.International journal of molecular sciences · 2022Article
- Molecular Functions and Pathways of Plastidial Starch Phosphorylase (PHO1) in Starch Metabolism: Current and Future Perspectives.International journal of molecular sciences · 2021Review
- Proteomics and Post-Translational Modifications of Starch Biosynthesis-Related Proteins in Developing Seeds of Rice.International journal of molecular sciences · 2021Review
- Mechanism Underlying Heat Stability of the Rice Endosperm Cytosolic ADP-Glucose Pyrophosphorylase.Frontiers in plant science · 2019Article
- Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development.PloS one · 2017Article
- Rice Endosperm Starch Phosphorylase (Pho1) Assembles with Disproportionating Enzyme (Dpe1) to Form a Protein Complex That Enhances Synthesis of Malto-oligosaccharides.The Journal of biological chemistry · 2016Article
- Overexpression of the Starch Phosphorylase-Like Gene (PHO3) in Lotus japonicus has a Profound Effect on the Growth of Plants and Reduction of Transitory Starch Accumulation.Frontiers in plant science · 2016Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MAIN
conclusionConsistent with its essential role in starch biosynthesis at low temperatures, the plastidial starch phosphorylase from rice endosperm is highly active at low temperature. Moreover, contrary to results on other higher plant phosphorylases, the L80 peptide, a domain unique to plant phosphorylases and not present in orthologous phosphorylases from other organisms, is not involved in enzyme catalysis. Starch phosphorylase (Pho) is an essential enzyme in starch synthesis in developing rice endosperm as the enzyme plays a critical role in both the early and maturation phases of starch granule formation especially at low temperature. In this study, we demonstrated that the rice Pho1 maintains substantial enzyme activity at low temperature (<20 °C) and its substrate affinities for branched α-glucans and glucose-1-phosphate were significantly increased at the lower reaction temperatures. Under sub-saturating substrate conditions, OsPho1 displayed higher catalytic activities at 18 °C than at optimal 36 °C, supporting the prominent role of the enzyme in starch synthesis at low temperature. Removal of the highly charged 80-amino acid sequence L80 peptide, a region found exclusively in the plastidial Pho1 of higher plants, did not significantly alter the catalytic and regulatory properties of OsPho1 but did affect heat stability. Our kinetic results support the low temperature biosynthetic role of OsPho1 in rice endosperm and indicate that its L80 region is unlikely to have a direct enzymatic role but provides stability of the enzyme under heat stress.
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