Open AccessStructure of the starch‐debranching enzyme barley limit dextrinase reveals homology of the N‐terminal domain to CBM21
Author(s) -
Møller Marie Sofie,
Abou Hachem Maher,
Svensson Birte,
Henriksen Anette
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112031004
Subject(s) - starch , glycogen debranching enzyme , terminal (telecommunication) , limit (mathematics) , homology (biology) , domain (mathematical analysis) , enzyme , chemistry , materials science , biochemistry , mathematics , computer science , amino acid , mathematical analysis , glycogen synthase , telecommunications
Barley limit dextrinase ( Hv LD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses α‐1,6‐glucosidic linkages in limit dextrins derived from amylopectin. The structure of Hv LD was solved and refined to 1.9 Å resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of Hv LD in complex with the competitive inhibitors α‐cyclodextrin and β‐cyclodextrin solved to 2.5 and 2.1 Å 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 Hv LD structure but were too flexible to be traced and included in the structures of the two Hv LD–inhibitor complexes.