ArticlePlant physiology2005
Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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112 citing papers in PubMed, 272 citations in OpenAlex.
- Solving the Insoluble: Regulation of α-Polyglucan Solubility and Functionality in Nature.Molecules (Basel, Switzerland) · 2026Review
- Understanding and modifying starch metabolism to limit yield losses in field-grown cassava.Plant physiology · 2026Article
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Identification of pivotal genes associated with sugar and organic acid metabolism during Prunus Mume fruit ripening via metabolomic and transcriptomic analyses.BMC plant biology · 2025Article
- Regulatory role of calcium sulfide in ripening delay of postharvest bananas.Food chemistry. Molecular sciences · 2025Article
- Functional Characterization of Arabidopsis α-Amylase3 (AMY3): Amylose Specificity and Structural Insights into Its Duplex Carbohydrate-Binding Module.bioRxiv : the preprint server for biology · 2025Article
- Covalently linked phosphate monoesters on alpha-polyglucans reduce substrate affinity of branching enzymes.Carbohydrate polymers · 2025Article
- Simultaneous Repression of GLUCAN WATER DIKINASE 1 and STARCH BRANCHING ENZYME 1 in Potato Tubers Leads to Starch With Increased Amylose and Novel Industrial Properties.Biotechnology journal · 2025Article
- The Pseudoenzyme β-Amylase9 From Arabidopsis Activates α-Amylase3: A Possible Mechanism to Promote Stress-Induced Starch Degradation.Proteins · 2025Article
- Genome-wide identification of the AcBAM family in kiwifruit (Actinidia chinensis cv. Hongyang) and the expression profiling analysis of AcBAMs reveal their role in starch metabolism.BMC plant biology · 2025Article
- Identification of Novel Inhibitors of Starch Excess 4 (SEX4).Life (Basel, Switzerland) · 2024Article
- TgLaforin, a glucan phosphatase, reveals the dynamic role of storage polysaccharides inbioRxiv : the preprint server for biology · 2024Article
- The pseudoenzyme β-amylase9 from Arabidopsis binds to and enhances the activity of α-amylase3: A possible mechanism to promote stress-induced starch degradation.bioRxiv : the preprint server for biology · 2024Article
- Starch phosphorylation-A needle in a haystack.Plant methods · 2024Article
- The end game(s) of photosynthetic carbon metabolism.Plant physiology · 2024Review
- Allelic variation in the autotetraploid potato: genes involved in starch and steroidal glycoalkaloid metabolism as a case study.BMC genomics · 2024Article
- Transcriptomic analysis of potato (Solanum tuberosum L.) tuber development reveals new insights into starch biosynthesis.PloS one · 2024Article
- The LIKE SEX FOUR 1-malate dehydrogenase complex functions as a scaffold to recruit β-amylase to promote starch degradation.The Plant cell · 2023Article
- Assessing the impacts of genetic defects on starch metabolism inJournal of the Royal Society, Interface · 2023Article
- Gradual Analytics of Starch-Interacting Proteins Revealed the Involvement of Starch-Phosphorylating Enzymes during Synthesis of Storage Starch in Potato (Molecules (Basel, Switzerland) · 2023Article
52 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phosphorylation of amylopectin by the glucan, water dikinase (GWD; EC 2.7.9.4) is an essential step within starch metabolism. This is indicated by the starch excess phenotype of GWD-deficient plants, such as the sex1-3 mutant of Arabidopsis (Arabidopsis thaliana). To identify starch-related enzymes that rely on glucan-bound phosphate, we studied the binding of proteins extracted from Arabidopsis wild-type leaves to either phosphorylated or nonphosphorylated starch granules. Granules prepared from the sex1-3 mutant were prephosphorylated in vitro using recombinant potato (Solanum tuberosum) GWD. As a control, the unmodified, phosphate free granules were used. An as-yet uncharacterized protein was identified that preferentially binds to the phosphorylated starch. The C-terminal part of this protein exhibits similarity to that of GWD. The novel protein phosphorylates starch granules, but only following prephosphorylation with GWD. The enzyme transfers the beta-P of ATP to the phosphoglucan, whereas the gamma-P is released as orthophosphate. Therefore, the novel protein is designated as phosphoglucan, water dikinase (PWD). Unlike GWD that phosphorylates preferentially the C6 position of the glucose units, PWD phosphorylates predominantly (or exclusively) the C3 position. Western-blot analysis of protoplast and chloroplast fractions from Arabidopsis leaves reveals a plastidic location of PWD. Binding of PWD to starch granules strongly increases during net starch breakdown. Transgenic Arabidopsis plants in which the expression of PWD was reduced by either RNAi or a T-DNA insertion exhibit a starch excess phenotype. Thus, in Arabidopsis leaves starch turnover requires a close collaboration of PWD and GWD.
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