Sandbox Reserved 338

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{{STRUCTURE_2vnc | PDB=2vnc | SCENE=Sandbox_Reserved_338/2vnc/1}}
{{STRUCTURE_2vnc | PDB=2vnc | SCENE=Sandbox_Reserved_338/2vnc/1}}
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A debranching enzyme is responsible for the breakdown of glycogen <ref name="Woo"> PMID:18703518 </ref>. There are two main groups of debranching enzymes, and they are separated according to their activity <ref name="Woo" />. The first group, consisting of [[pullulanase]] and isoamylases which only possess one function α-1,6-glycosidase activity <ref name="Woo" />. Whereas the second group consists of glycogen debranching enzymes which possess two functions, both α-1,6-glycosidase and α-1,4-transferase activity <ref name="Woo" />.
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A debranching enzyme is responsible for the breakdown of glycogen <ref name="Woo"> PMID:18703518 </ref>. There are two main groups of debranching enzymes, and they are separated according to their activity <ref name="Woo" />. The first group, consisting of [http://wikipedia.org/pullulanase pullulanase] and isoamylases which only possess one function α-1,6-glycosidase activity <ref name="Woo" />. Whereas the second group consists of glycogen debranching enzymes which possess two functions, both α-1,6-glycosidase and α-1,4-transferase activity <ref name="Woo" />.

Revision as of 19:11, 15 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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PDB ID 2vnc

Drag the structure with the mouse to rotate
2vnc, resolution 3.00Å ()
Related: 2vuy, 2vr5, 2vnb
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



A debranching enzyme is responsible for the breakdown of glycogen [1]. There are two main groups of debranching enzymes, and they are separated according to their activity [1]. The first group, consisting of pullulanase and isoamylases which only possess one function α-1,6-glycosidase activity [1]. Whereas the second group consists of glycogen debranching enzymes which possess two functions, both α-1,6-glycosidase and α-1,4-transferase activity [1].



References

  1. ↑ 1.0 1.1 1.2 1.3 Woo EJ, Lee S, Cha H, Park JT, Yoon SM, Song HN, Park KH. Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus. J Biol Chem. 2008 Oct 17;283(42):28641-8. Epub 2008 Aug 14. PMID:18703518 doi:10.1074/jbc.M802560200
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