ArticleProtein science : a publication of the Protein Society2020
Structural analysis and reaction mechanism of the disproportionating enzyme (D-enzyme) from potato.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 16 citations in OpenAlex.
- The plastidial PHS1-DPE1 complex drives efficient malto-oligosaccharides synthesis in rice starch metabolism.Nature communications · 2026Article
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Toxoplasma gondii chromatin remodeler SWI/SNF controls parasite division and gene expression.Nature communications · 2025Article
- Production of Large-Ring Cyclodextrins by Amylomaltases.Molecules (Basel, Switzerland) · 2022Review
- Identification of an Amylomaltase from the Halophilic ArchaeonLife (Basel, Switzerland) · 2022Article
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77.3 Biotech · 2021Article
- Structural analysis and reaction mechanism of the disproportionating enzyme (D-enzyme) from potato.Protein science : a publication of the Protein Society · 2020Article
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7 authors at 4 institutions in 1 country.
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Abstract
Starch produced by plants is a stored form of energy and is an important dietary source of calories for humans and domestic animals. Disproportionating enzyme (D-enzyme) catalyzes intramolecular and intermolecular transglycosylation reactions of α-1, 4-glucan. D-enzyme is essential in starch metabolism in the potato. We present the crystal structures of potato D-enzyme, including two different types of complex structures: a primary Michaelis complex (substrate binding mode) for 26-meric cycloamylose (CA26) and a covalent intermediate for acarbose. Our study revealed that the acarbose and CA26 reactions catalyzed by potato D-enzyme involve the formation of a covalent intermediate with the donor substrate. HPAEC of reaction substrates and products revealed the activity of the potato D-enzyme on acarbose and CA26 as donor substrates. The structural and chromatography analyses provide insight into the mechanism of the coupling reaction of CA and glucose catalyzed by the potato D-enzyme. The enzymatic reaction mechanism does not involve residual hydrolysis. This could be particularly useful in preventing unnecessary starch degradation leading to reduced crop productivity. Optimization of this mechanism would be important for improvements of starch storage and productivity in crops.
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