ArticleThe Journal of biological chemistry2010
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 232 citations in OpenAlex.
- Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Computer-Aided Drug Design for Type 2 Diabetes-Related Enzymes: Polarizable and Nonpolarizable Simulations of Enzyme-Inhibitor Complexes.Journal of chemical information and modeling · 2026Article
- Vincoside Lactam from EdibleFoods (Basel, Switzerland) · 2026Article
- SuFEx-Enabled Reprogramming of Flavonoids for Selective α-Glucosidase Covalent Inhibition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Chemical Constituents and Biological Potentials of Teucrium scordium subsp. scordioides Extracts: In Vitro Experimental and In Silico Perspectives.ChemistryOpen · 2026Article
- Novel α-amylolyzates derived from enzymatically synthesized α-glucans using diverse glycogen branching enzymes decelerate glucose release by modulation of intestinal α-glucosidases.NPJ science of food · 2026Article
- A Comprehensive Review on Copper Oxide Nanoparticles: Physicochemical Parameters, Pharmacological Potential and Pathophysiological Effects.International journal of nanomedicine · 2026Review
- α-Glucosidase-driven metabolism as a potential therapeutic vulnerability inFrontiers in microbiology · 2026Review
- Exploring Small-Molecule Inhibitors of Glucosidase II: Advances, Challenges, and Therapeutic Potential in Cancer and Viral Infection.International journal of molecular sciences · 2025Review
- Optimization and semi-continuous fermentation of gluco-oligosaccharide production withFood science and biotechnology · 2025Article
- Click Reaction Inspired Enzyme Inhibitors in Diabetes Care: An Update in the Field of Chronic Metabolic Disorder.Current pharmaceutical design · 2025Review
- Discovery of potent inhibitors from traditional rice varieties targeting α-amylase: A computational approach andJournal of biosciences · 2025Article
- Antidiabetic Potential ofScientifica · 2025Article
- Unlocking nature's antidiabetic potential: computer-aided discovery of α-amylase and α-glucosidase inhibitors inIn silico pharmacology · 2025Article
- Review
- Discovery of novel flavonoid derivatives as potential dual inhibitors against α-glucosidase and α-amylase: virtual screening, synthesis, and biological evaluation.Molecular diversity · 2024Article
- Potential anti-obesity effect of saponin metabolites from adzuki beans: A computational approach.Food science & nutrition · 2024Article
- Mutations in Glycosyltransferases and Glycosidases: Implications for Associated Diseases.Biomolecules · 2024Article
- Synthesis and Biological Evaluation of New Dihydrofuro[3,2-Molecules (Basel, Switzerland) · 2024Article
- Theoretical Studies for the Discovery of Potential Sucrase-Isomaltase Inhibitors from Maize Silk Phytochemicals: An Approach to Treatment of Type 2 Diabetes.Molecules (Basel, Switzerland) · 2023Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 5 institutions in 3 countries.
Funding
Abstract
Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products. MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides. Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution. Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
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