ArticlePlant physiology2006
The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 77 citations in OpenAlex.
- Old player, new roles: defining the role of the plastidial phosphorylase.The New phytologist · 2025Review
- A Starch Phosphorylase, ZmPHOH, Improves Photosynthetic Recovery from Short-Term Cold Exposure in Maize.International journal of molecular sciences · 2025Article
- Kinetic and Structural Studies of the PlastidialACS omega · 2024Article
- Cytosolic disproportionating enzyme2 is essential for pollen germination and pollen tube elongation in rice.Plant physiology · 2023Article
- Article
- Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022Review
- Energy-Saving LED Light Affects the Efficiency of the Photosynthetic Apparatus and Carbohydrate Content inBiology · 2021Article
- Functional relationships of three NFU proteins in the biogenesis of chloroplastic iron-sulfur clusters.Plant direct · 2021Article
- Transitory Starch Metabolism in Guard Cells: Unique Features for a Unique Function.Plant physiology · 2017Review
- An Organelle RNA Recognition Motif Protein Is Required for Photosystem II SubunitPlant physiology · 2017Article
- A Nitrogen-Fixing Subunit Essential for Accumulating 4Fe-4S-Containing Photosystem I Core Proteins.Plant physiology · 2016Article
- 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
- The plastidial starch phosphorylase from rice endosperm: catalytic properties at low temperature.Planta · 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
- Analysis of Loss-of-Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate-Derived Amino Acid Contents.Plant physiology · 2015Article
- The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.Journal of bacteriology · 2015Article
- Article
- Sequence variation, differential expression, and divergent evolution in starch-related genes among accessions of Arabidopsis thaliana.Plant molecular biology · 2015Article
- 2-Deoxy-2-fluoro-d-glucose metabolism in Arabidopsis thaliana.Frontiers in plant science · 2015Article
- Loss of cytosolic phosphoglucose isomerase affects carbohydrate metabolism in leaves and is essential for fertility of Arabidopsis.Plant physiology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transitory starch of leaves is broken down hydrolytically, making maltose the predominant form of carbon exported from chloroplasts at night. Maltose metabolism in the cytoplasm of Escherichia coli requires amylomaltase (MalQ) and maltodextrin phosphorylase (MalP). Possible orthologs of MalQ and MalP in the cytosol of Arabidopsis (Arabidopsis thaliana) were proposed as disproportionating enzyme (DPE2, At2g40840) and alpha-glucan phosphorylase (AtPHS2, At3g46970). In this article, we measured the activities of recombinant DPE2 and AtPHS2 proteins with various substrates; we show that maltose and a highly branched, soluble heteroglycan (SHG) are excellent substrates for DPE2 and propose that a SHG is the in vivo substrate for DPE2 and AtPHS2. In E. coli, MalQ and MalP preferentially use smaller maltodextrins (G(3)-G(7)) and we suggest that MalQ and DPE2 have similar, but nonidentical, roles in maltose metabolism. To study this, we complemented a MalQ(-) E. coli strain with DPE2 and found that the rescue was not complete. To investigate the role of AtPHS2 in maltose metabolism, we characterized a T-DNA insertion line of the AtPHS2 gene. The nighttime maltose level increased 4 times in the Atphs2-1 mutant. The comparison of maltose metabolism in Arabidopsis with that in E. coli and the comparison of the maltose level in plants lacking DPE2 or AtPHS2 indicate that an alternative route to metabolize the glucan residues in SHG exists. Other plant species also contain SHG, DPE2, and alpha-glucan phosphorylase, so this pathway for maltose metabolism may be widespread among plants.
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