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Updated: Mar 17, 2026

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
Published on: September 20, 2016
Structural biology of starch-degrading enzymes and their regulation
Marie Sofie Møller1, Birte Svensson2
1Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark; Center for Molecular Protein Science, Department of Chemistry, Lund University, 221 00 Lund, Sweden.
Abstract:
Starch is a major energy source for all domains of life. Recent advances in structures of starch-degrading enzymes encompass the substrate complex of starch debranching enzyme, the function of surface binding sites in plant isoamylase, details on individual steps in the mechanism of plant disproportionating enzyme and a self-stabilised conformation of amylose accommodated in the active site of plant α-glucosidase. Important inhibitor complexes include a flavonol glycoside, montbretin A, binding at the active site of human pancreatic α-amylase and barley limit dextrinase inhibitor binding to the debranching enzyme, limit dextrinase using a new binding mode for cereal protein inhibitors.
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