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Publication Abstract from PubMed

Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 A resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of HvLD in complex with the competitive inhibitors alpha-cyclodextrin and beta-cyclodextrin solved to 2.5 and 2.1 A resolution, respectively. However, three loops in the N-terminal domain that are shown here to resemble carbohydrate-binding module family 21 were traceable and were included in the present HvLD structure but were too flexible to be traced and included in the structures of the two HvLD-inhibitor complexes.

Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.,Moller MS, Abou Hachem M, Svensson B, Henriksen A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep;68(Pt 9):1008-12. Epub, 2012 Aug 29. PMID:22949184^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.