Ontology highlight
ABSTRACT:
SUBMITTER: Moller MS
PROVIDER: S-EPMC3433187 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Møller Marie Sofie MS Abou Hachem Maher M Svensson Birte B Henriksen Anette A
Acta crystallographica. Section F, Structural biology and crystallization communications 20120829 Pt 9
Barley limit dextrinase (HvLD) 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 HvLD 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 HvLD in complex with the competitive inhibitors α-cyclodextrin and β-cyclodextrin solved to 2.5 and 2.1 Å resolution, respectively ...[more]