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Publication Abstract from PubMed

Debranching is a critical step in the mobilization of the important energy store glycogen. In eukaryotes, including fungi and animals, the highly conserved glycogen-debranching enzyme (GDE) debranches glycogen by a glucanotransferase (GT) reaction followed by a glucosidase (GC) reaction. Previous work indicated that these reactions are catalyzed by two active sites located more than 50 A apart and provided insights into their catalytic mechanisms and substrate recognition. Here, five crystal structures of GDE in complex with oligosaccharides with 4-9 glucose residues are presented. The data suggest that the glycogen main chain plays a critical role in binding to the GT and GC active sites of GDE and that a minimum of five main-chain residues are required for optimal binding.

Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.,Shen M, Gong X, Xiang S Acta Crystallogr F Struct Biol Commun. 2021 Nov 1;77(Pt 11):420-426. doi:, 10.1107/S2053230X21010918. Epub 2021 Oct 29. PMID:34726181^[1]

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