ReviewCellular and molecular life sciences : CMLS2016
α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.
Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 90 citations in OpenAlex.
- Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Integrative profiling of oral fungal communities acrossAnnals of medicine · 2026Article
- Flavonoids and chalcones as selective α-glucosidase inhibitors: from enzymatic screening to validation using the human enzyme.RSC medicinal chemistry · 2026Article
- SuFEx-Enabled Reprogramming of Flavonoids for Selective α-Glucosidase Covalent Inhibition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structure-Function Relationships in Polysaccharide-Iron Complexes: Molecular Characterization, Acid-Stress Release Stability, and Gastrointestinal Tolerability.Pharmaceutics · 2026Article
- Sex-Specific Regulation of Glycemic Homeostasis by Theabrownin from Pu-erh Tea.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Preliminary Investigation on Salivary Enzymes of Massese Sheep.Animals : an open access journal from MDPI · 2026Article
- Functional Analysis of Amino Acid Residues Responsible for Substrate Specificity of GH13_17 α‑Glucosidase fromACS omega · 2026Article
- An enzymatic-metabolic sensing axis in taste cells detects glucose-yielding carbohydrates.bioRxiv : the preprint server for biology · 2026Article
- Comparative genomics of different haplotypes in Ditylenchus destructor provides insights into their host preferences.Communications biology · 2026Article
- Genomes of NBMC genomics · 2026Article
- Preparation of sea cucumber collagen hydrolysate and its inhibitory effect on α-glucosidases.Food chemistry: X · 2026Article
- α-Glucosidase-driven metabolism as a potential therapeutic vulnerability inFrontiers in microbiology · 2026Review
- Molecular Docking, Phytochemical Screening and Evaluation of Balliospermum montanum Roots for its Antihyperlipidemic Potential.Cell biochemistry and biophysics · 2025Article
- Recognition-induced destabilization: controlled release from molecularly imprinted chitosan nanoparticlesRSC advances · 2025Article
- Spatiotemporal Profiling of Starch-Degrading Enzymes in Nong-Flavor Daqu: Molecular Markers for Quantitative Quality Evaluation.Foods (Basel, Switzerland) · 2025Article
- Pathophysiology of the Neutropenia of GSDIb and G6PC3 Deficiency: Origin, Metabolism and Elimination of 1,5-Anhydroglucitol.Journal of inherited metabolic disease · 2025Review
- Introduction of new quinolone-2-thio-acetamide-propane hydrazide-benzimidazole derivatives as new α-glucosidase and α-amylase inhibitors.Scientific reports · 2025Article
- A computational study on effect of Cymbopogon citratu and Juniperus virginiana against Spodoptera litura.Scientific reports · 2025Article
- Establishing an itaconic acid production process with Ustilago species on the low-cost substrate starch.FEMS yeast research · 2024Article
Corrections and comments
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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
α-Glucosidases (AGases) and α-1,4-glucan lyases (GLases) catalyze the degradation of α-glucosidic linkages at the non-reducing ends of substrates to release α-glucose and anhydrofructose, respectively. The AGases belong to glycoside hydrolase (GH) families 13 and 31, and the GLases belong to GH31 and share the same structural fold with GH31 AGases. GH13 and GH31 AGases show diverse functions upon the hydrolysis of substrates, having linkage specificities and size preferences, as well as upon transglucosylation, forming specific α-glucosidic linkages. The crystal structures of both enzymes were determined using free and ligand-bound forms, which enabled us to understand the important structural elements responsible for the diverse functions. A series of mutational approaches revealed features of the structural elements. In particular, amino-acid residues in plus subsites are of significance, because they regulate transglucosylation, which is used in the production of industrially valuable oligosaccharides. The recently solved three-dimensional structure of GLase from red seaweed revealed the amino-acid residues essential for lyase activity and the strict recognition of the α-(1 → 4)-glucosidic substrate linkage. The former was introduced to the GH31 AGase, and the resultant mutant displayed GLase activity. GH13 and GH31 AGases hydrate anhydrofructose to produce glucose, suggesting that AGases are involved in the catabolic pathway used to salvage unutilized anhydrofructose.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.