Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases

Sophie Bozonnet, Birgit Christine Bønsager, B. Kramhoft, H. Mori, Maher Abou Hachem, Martin Willemoes, M.T. Jensen, Kenji Fukuda, P.K. Nielsen, N. Juge, N. Aghajari, S. Tranier, X. Robert, R. Haser, Birte Svensson

    Research output: Contribution to journalJournal articleResearchpeer-review


    This review on barley alpha-amylases 1 (AMY1) and 2 (AMY2) addresses rational mutations at distal subsites to the catalytic site, polysaccharide hydrolysis, and interactions with proteinaceous inhibitors. Subsite mapping of barley alpha-amylases revealed 6 glycone and 4 aglycone substrate subsites. Moreover, two maltooligosaccharide surface binding sites have been identified. Engineering of outer subsites -6 and +4 alters action patterns and relative specificities. Thus, compared to wild-type, Y105A AMY1 (subsite -6) shows 140%, 15%, and
    Original languageEnglish
    Pages (from-to)27-36
    Publication statusPublished - 2005


    • isozyme chimeras
    • amylopectin
    • proteinaceous inhibitors
    • degree of multiple attack
    • barley alpha-amylase
    • secondary binding sites
    • subsite mutants


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