Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
Publication: Research - peer-review › Journal article – Annual report year: 2012
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. 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.
| Original language | English |
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| Journal | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online |
| Publication date | 2012 |
| Volume | 68 |
| Journal number | Pt 9 |
| Pages | 1008-1012 |
| ISSN | 1744-3091 |
| DOIs | |
| State | Published |
| Citations | Web of Science® Times Cited: 0 |
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ID: 10854400