Glycogen debranching enzyme: Difference between revisions

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[[File:Hypothesized substraight binding ___location.png|thumb|center|Hypothesized sidechain binding sites|600px]]
 
The structure of the ''Candida glabrata'' GDE has been reported.<ref>{{cite journal | vauthors = Zhai L, Feng L, Xia L, Yin H, Xiang S | title = Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations | journal = Nature Communications | volume = 7 | pagesarticle-number = 11229 | date = April 2016 | pmid = 27088557 | pmc = 4837477 | doi = 10.1038/ncomms11229 | bibcode = 2016NatCo...711229Z }}</ref> The structure revealed that distinct domains in GDE encode the glucanotransferase and glucosidase activities. Their catalyses are similar to that of alpha-amylase and glucoamylase, respectively. Their active sites are selective towards the respective substrates, ensuring proper activation of GDE. Besides the active sites GDE have additional binding sites for glycogen, which are important for its recruitment to glycogen. Mapping the disease-causing mutations onto the GDE structure provided insights into glycogen storage disease type III.
 
== Genetic ___location ==