title: Structural biology of starch-degrading enzymes and their regulation.
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.
authors.affiliation: Enzyme 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.
authors.forename: Marie Sofie
authors.initials: MS
authors.lastname: Møller
authors.affiliation: Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark. Electronic address: bis@bio.dtu.dk.
authors.forename: Birte
authors.initials: B
authors.lastname: Svensson
mesh_terms: D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D013213:Starch / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes; D013213:Starch