EPM2A dimer dephosphorylates phosphoglycogen-GYG1
EPM2A:PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramer + H2O → EPM2A:PPP1R3C:glycogen-GYG1:GYS1-a tetramer + Pi
- Reactome
- R-HSA-3781018
- Compartment
- cytosol
- Rhea
- RHEA:10685
Inputs
- EPM2A:PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramerR-HSA-3780999, cytosol
- H2OCHEBI:15377, H2O, cytosol
Outputs
- EPM2A:PPP1R3C:glycogen-GYG1:GYS1-a tetramerR-HSA-3781000, cytosol
- PiCHEBI:43474, HO4P, cytosol
Catalysed by
- carbohydrate phosphatase activity of EPM2A:PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramer [cytosol]
Literature
- Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease Mol. Cell, 2015
- Dimeric quaternary structure of human laforin J. Biol. Chem., 2015
- Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo Proc. Natl. Acad. Sci. U.S.A., 2007