ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Boosting secretion of starch-converting enzymes from Priestia koreensis HL12 and its application in non-thermal cassava pulp saccharification process for maltooligosaccharides synthesis.Bioresources and bioprocessing · 2025Article
- BoGH13ACellular and molecular life sciences : CMLS · 2023Article
- Interplay of starch debranching enzyme and its inhibitor is mediated by Redox-Activated SPL transcription factor.Computational and structural biotechnology journal · 2022Article
- Understanding Thermostability Factors of Barley Limit Dextrinase by Molecular Dynamics Simulations.Frontiers in molecular biosciences · 2020Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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